|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-740 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 962.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 18 ASLAWL-GTVLLFLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 96
Cdd:TIGR00958 1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 97 EPLAAALGLALPVLALFRELISWGAPGSADSTRLLHWGshpsAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGD 171
Cdd:TIGR00958 72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 172 SVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 251
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 252 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 331
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 332 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 411
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 412 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 491
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*....
gi 2468698279 732 KKGCYWAMV 740
Cdd:TIGR00958 703 DQGCYKHLV 711
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
200-478 |
1.05e-165 |
|
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: 478.89 E-value: 1.05e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
201-742 |
1.77e-136 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 224055 [Multi-domain] Cd Length: 567 Bit Score: 414.52 E-value: 1.77e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDgsADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:COG1132 30 SLLLPLLIGRIIDALLAD--LGELLELLLLLLLLALLGGVLRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:COG1132 108 SGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:COG1132 188 GELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLhLEGLVQFQDVSFAYPNRPdvLV 520
Cdd:COG1132 268 VGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPEVEDPPDPLKD-TIGSIEFENVSFSYPGKK--PV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIA 600
Cdd:COG1132 345 LKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQ 680
Cdd:COG1132 425 LGRPD-ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEAL 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 681 VEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG1132 504 IQDALKK--LLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGTHEELLAKGGLYARLYQA 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
492-720 |
1.56e-135 |
|
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: 399.15 E-value: 1.56e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
260-736 |
3.03e-106 |
|
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: 336.29 E-value: 3.03e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 260 LQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLF 339
Cdd:TIGR02204 93 IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 340 LLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklQEIKTLNQKEAVAYAVNSWTTSISG 419
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFG---GAVEKAYEAARQRIRTRALLTAIVI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLL---KVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP--RCPPSGLL 494
Cdd:TIGR02204 250 VLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH 574
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVA 652
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYG---RPdaTDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLyesPELYS-RSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQAL---ETLMKgRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
....*
gi 2468698279 732 KKGCY 736
Cdd:TIGR02204 564 KGGLY 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
202-737 |
4.66e-105 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 225183 [Multi-domain] Cd Length: 709 Bit Score: 336.89 E-value: 4.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGD---GIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:COG2274 171 LATPLFSQIVIDKVLPDASRST----LTVLAIGLLLAALFEALLRllrTYLIAHLGkRLDLELSGRFFRHLLRLPLSYFE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVR 357
Cdd:COG2274 247 KRSVGEIISRVRELEQIREFLTGSILTLII-DLLFALIFLAVMFLYSWKLTLIVLAAIPLNVLITLIFQP---LLRRKTR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVA---IEALSAMPTVRSFANEEGEAQKFREKLQE-IKTLNQKEAVAYAVNSWTTSISGmLLKVGILYIGGQL 433
Cdd:COG2274 323 KLIEESAEQQsflVETIKGIETVKALAAEPRFRSQWDNRLAKqVNIGFKTEKLALILNTIKSLLQQ-LSSVLILWFGAIL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAY 512
Cdd:COG2274 402 VLEGELTLGQLVAFNMLAGYFISPITRLSQLWTDFQQAKVALERLGDILDTPPeQEGDKTLIHLPKLQGEIEFENVSFRY 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 513 PNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:COG2274 482 GPD-DPPVLEDLSLEIPPGEKVAIVGRSGSGKSTLLKLLLGLYKPQQGRILLDGVDLNDIDLASLRRQVGYVLQDPFLFS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG2274 561 GSIRENIALGNPE-ATDEEIIEAAQLAGAHEFIENLPMGYDTPVGEGGANLSGGQRQRLALARALLSKPKILLLDEATSA 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 673 LDANSQLQVEQLLyeSPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYW 737
Cdd:COG2274 640 LDPETEAIILQNL--LQILQGRTVIIIAHRLSTIRSADRIIVLDQGKIVEQGSHEELLAQGGLYA 702
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
503-742 |
2.40e-99 |
|
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: 306.00 E-value: 2.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
205-736 |
1.49e-96 |
|
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: 310.50 E-value: 1.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 205 PFFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLE----FVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:TIGR02203 31 STLAALLKP-LLDDGFGGRDRSVLWWVPLVVIGLAVLRgicsFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:TIGR02203 110 TGTLLSRITFDSEQVASAATDAFIV----LVREtltvIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:TIGR02203 186 QNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPLHLEGLVQFQDVSFAYPNRp 516
Cdd:TIGR02203 266 GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 677 SQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR02203 504 SERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
200-478 |
2.78e-93 |
|
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: 292.14 E-value: 2.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
200-478 |
7.31e-85 |
|
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: 270.20 E-value: 7.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
200-478 |
5.82e-77 |
|
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: 249.54 E-value: 5.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18784 251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
503-737 |
3.20e-76 |
|
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: 245.60 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYW 737
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
501-734 |
9.41e-76 |
|
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: 244.06 E-value: 9.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
226-736 |
1.12e-75 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 258.13 E-value: 1.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 226 RNLTLMSILTIAS---AVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQ----ETEFFQQNQTGNITSRVTEdTSTLSDS 298
Cdd:TIGR01846 173 RGLSTLSVLALAMlavAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHllglPLGYFESRRVGDTVARVRE-LEQIRNF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 299 LSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVRESLAKSSQVA---IEALSAMP 375
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP---ILRKRVEDKFERSAAATsflVESVTGIE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 376 TVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFT 455
Cdd:TIGR01846 329 TIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVT 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 456 QAVEVLLSIYPRVQKAVGSSEKIFEYLDrTPRCP-PSGLLTPLHLEGLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEV 533
Cdd:TIGR01846 409 QPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPrSAGLAALPELRGAITFENIRFRYaPDSPEVL--SNLNLDIKPGEF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 534 TALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEIT 613
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 614 AAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElyS 693
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--G 642
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2468698279 694 RSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
254-736 |
3.19e-71 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 243.39 E-value: 3.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 254 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 329
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 330 VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 409
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 410 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 488
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 489 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP 568
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQR 648
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQ 728
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
....*...
gi 2468698279 729 LMEKKGCY 736
Cdd:PRK11176 565 LLAQNGVY 572
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
503-742 |
6.65e-70 |
|
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: 228.65 E-value: 6.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSqlqvEQLLYESPE--LYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:cd03253 157 PILLLDEATSALDTHT----EREIQAALRdvSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
...
gi 2468698279 740 VQA 742
Cdd:cd03253 233 WKA 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
175-742 |
3.27e-69 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 237.94 E-value: 3.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 175 RLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWIlqdgsadtfTRNLTLMSILTIasavleFVGDGIYNnTMG 254
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAI---------SGKGDIFPLLAA------WAGFGLFN-IIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 255 HV----------HSHLQG---EVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLS----DSLSENLSLFLWYLVrglcLL 317
Cdd:PRK13657 73 GVlvarhadrlaHRRRLAvltEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVV----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 318 GIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklqei 397
Cdd:PRK13657 149 PLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALR------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 398 KTLNQKEAVAYAVNSW------TTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:PRK13657 223 DIADNLLAAQMPVLSWwalasvLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 472 VGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAAL 550
Cdd:PRK13657 303 APKLEEFFEVEDAVPdVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 551 LQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGL 628
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 629 PQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ 708
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN 535
|
570 580 590
....*....|....*....|....*....|....
gi 2468698279 709 ADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
503-741 |
5.68e-69 |
|
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: 226.60 E-value: 5.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
503-718 |
4.99e-67 |
|
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: 218.79 E-value: 4.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
358-739 |
3.87e-66 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227590 [Multi-domain] Cd Length: 497 Bit Score: 227.24 E-value: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISGMLLKVgILYIGGQLVTS 436
Cdd:COG5265 116 NADSDANAKAIDSLLNFETVKYFGNEEYEAVRYDHALETYEKAAIKVHVSLLVlNFGQTAIFSTGLRV-MMTMSALGVEE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDR------TPRCPPsglLTPLHLeGLVQFQDVSF 510
Cdd:COG5265 195 GQLTVGDLVNVNALLFQLSIPLNFLGFSYREIRQALTDMEKMFDLLDVeaevsdAPDAPP---LWPVRL-GAVAFINVSF 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 511 AY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ 589
Cdd:COG5265 271 AYdPRRP---ILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSITIDGQDIRDVTQQSLRRAIGIVPQDTV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 VFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:COG5265 348 LFNDTIAYNIKYGRP-DATAEEVGAAAEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVAIARTILKNPPILILDEA 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 670 TSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:COG5265 427 TSALDTHTEQAIQAALREVSA--GRTTLVIAHRLSTIIDADEIIVLDNGRIVERGTHEELLAAGGLYAEM 494
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
371-742 |
5.15e-65 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227321 [Multi-domain] Cd Length: 559 Bit Score: 225.99 E-value: 5.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 371 LSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeAVAYAVNS-----WTTSISGMLlkvGILYIGGQLVTSGAVSSGNLV 445
Cdd:COG4988 186 LRGLETLRAFGRTEATEERIRKDSEDFRKATMS-VLRIAFLSsavleFFAYLSIAL---VAVYIGFRLLGEGDLTLFAGL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 446 TFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLE--GLVQFQDVSFAYPNRPdvLVLQG 523
Cdd:COG4988 262 FVLILAPEFFQPLRDLGSFFHAAAAGEAAADKLFTLLESPVATPGSGEKAEVANEppIEISLENLSFRYPDGK--PALSD 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGl 603
Cdd:COG4988 340 LNLTIKAGQLTALVGASGAGKSTLLNLLLGFLAPTQGEIRVNGIDLRDLSPEAWRKQISWVSQNPYLFAGTIRENILLA- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 604 TQKPTMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQ 683
Cdd:COG4988 419 RPDASDEEIIAALDQAGLLEFVPK-PDGLDTVIGEGGAGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQ 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 684 LLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG4988 498 ALQELAK--QKTVLVITHRLEDAADADRIVVLDNGRLVEQGTHEELSEKQGLYANLLKQ 554
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
501-720 |
9.47e-63 |
|
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: 208.98 E-value: 9.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGRSLQENIAYGLtQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
385-741 |
7.09e-61 |
|
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: 227320 [Multi-domain] Cd Length: 573 Bit Score: 214.89 E-value: 7.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 385 GEAQKFREKL-QEIKTLNQKEAVAYAVNSWTTSIsgMLLKVGILYIGGQLVTSGAVSSGNL-----VTFVLYQMQFTQAV 458
Cdd:COG4987 215 GAEDAYRTALeATEASWLKAQRKQARFTGLSDAI--LLLIAGLLVIGLLLWMAAQVGAGALaqpgaALALLVIFAALEAF 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 459 EVLLSIYP-RVQKAVGSSEKIFEYLDRTPRCPPSGLLTPlHLEGLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALV 537
Cdd:COG4987 293 EPLAPGAFqHLGQVIASARRLNDILDQKPEVTFPDEQTA-TTGQALELRNVSFTYPGQQ-TKALKNFNLTLAQGEKVAIL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 538 GPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygLTQKP--TMEEITAA 615
Cdd:COG4987 371 GRSGSGKSTLLQLLAGAWDPQQGSITLNGVEIASLDEQALRETISVLTQRVHLFSGTLRDNL---RLANPdaSDEELWAA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 616 AVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRS 695
Cdd:COG4987 448 LQQVGLEKLLESAPDGLNTWLGEGGRRLSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLALLFE--HAEGKT 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2468698279 696 VLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:COG4987 526 LLMVTHRLRGLERMDRIIVLDNGKIIEEGTHAELLANNGRYKRLYQ 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-742 |
5.91e-60 |
|
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: 215.37 E-value: 5.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTeDTSTLSDSL-SENLSLFL--WYLVrglcLLGIML-WGSVSLTMVTLVTLPLLFLLPKKVGKWYQ 350
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 351 LLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQK----FREKLQEIKTLNQKEAVAYAVNSWTTSIsgmlLKVGI 426
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLI----LNVVI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 427 LYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQF 505
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYP-NRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAV 584
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 585 GQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 665 ILDDATSALDANSQLQ-VEQLLYespeLYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:TIGR01193 634 ILDESTSNLDTITEKKiVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
233-741 |
4.78e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.34 E-value: 4.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDslsenlslfLWYLV- 311
Cdd:PRK10790 73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---------LYVTVv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 312 ----RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV----QVRESLAKSSQVAIEALSAMPTVRSFANE 383
Cdd:PRK10790 144 atvlRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 384 egeaQKFREKLQEIKTLNqkeavaYAVNSWTTSISGMLLK-----------VGILYIGGqLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK10790 224 ----ARFGERMGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 453 QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRtPRCPPSGLLTPLHlEGLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGE 532
Cdd:PRK10790 293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 533 VTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltQKPTMEEI 612
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 613 TAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyesPELY 692
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL---AAVR 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 693 SRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK10790 524 EHTTLVVIAHrLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
200-458 |
2.04e-58 |
|
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: 395537 [Multi-domain] Cd Length: 274 Bit Score: 199.41 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAV 458
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
471-715 |
9.90e-54 |
|
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: 194.04 E-value: 9.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 471 AVGSSEKIFEYLDRTPR-CPPSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAA 549
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRpLAGKAPVTAAPASSLE-FSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 550 LLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLP 629
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 630 QGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPELYS--RSVLLITQHLSLVE 707
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEALRALAqgRTVLLVTHRLALAA 521
|
....*...
gi 2468698279 708 QADHILFL 715
Cdd:TIGR02857 522 LADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
420-732 |
4.44e-52 |
|
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: 189.87 E-value: 4.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 498
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPsRDPAMPLPEP-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 lEGLVQFQDVSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:TIGR01842 314 -EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDAnsqlQVEQLLYE---SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDE----EGEQALANaikALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
270-739 |
4.56e-51 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 187.61 E-value: 4.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 RQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIM-LWGSVSLTMVTLVTLPLLFLLPKKVGKw 348
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGD- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 yqllevQVRESLaKSSQVAI--------EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSIS-G 419
Cdd:PRK10789 160 ------QLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAiG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 M--LLKVGilyiGGQ-LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPpSGLLTP 496
Cdd:PRK10789 233 ManLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRY 576
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*
gi 2468698279 735 CYWAM 739
Cdd:PRK10789 542 WYRDM 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
385-741 |
4.07e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 181.95 E-value: 4.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 385 GEAQKFREKL--QEIKTLNQKEAVAyavnswttSISGM----------LLKVGILYIGGQLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK11160 217 GAEDRYRQQLeqTEQQWLAAQRRQA--------NLTGLsqalmilangLTVVLMLWLAAGGVGGNAQPGALIALFVFAAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 453 QftqAVEVLLSI---YPRVQKAVGSSEKIFEYLDRTP--RCPPSGLLTPLHleGLVQFQDVSFAYPNRPDvLVLQGLTFT 527
Cdd:PRK11160 289 A---AFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 528 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKp 607
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 608 TMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYE 687
Cdd:PRK11160 442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 688 SPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK11160 521 HAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
420-732 |
1.74e-47 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 226969 [Multi-domain] Cd Length: 580 Bit Score: 177.47 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 498
Cdd:COG4618 254 MALQSAVLGLGAWLVIKGEITPGMMIAGSILSGRALAPIDLAIANWKQFVAARQSYKRLNELLAELPaAAERMPLPAP-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 lEGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:COG4618 332 -QGALSVERLTAAPPGQKKP-ILKGISFALQAGEALGIIGPSGSGKSTLARLLVGIWPPTSGSVRLDGADLRQWDREQLG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:COG4618 410 RHIGYLPQDVELFDGTIAENIAR-FGEEADPEKVIEAARLAGVHELILRLPQGYDTRIGEGGATLSGGQRQRIALARALY 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDANSqlqvEQLLYES-PELYSR--SVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG4618 489 GDPFLVVLDEPNSNLDSEG----EAALAAAiLAAKARggTVVVIAHRPSALASVDKILVLQDGRIAAFGPREEVLAK 561
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
258-703 |
1.48e-46 |
|
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: 173.70 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 258 SHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 322
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvivpagvalvvGAAAVAAIAVLSVPAALILAAGLLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 323 GSVSLTMVTLvtlpllfllpkKVGKWYQLLEVQVRESLAkssQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 402
Cdd:TIGR02868 166 AGFVAPLVSL-----------RAARAAEQALARLRGELA---AQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 403 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 483 DRTPRCP----PSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLE-LRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 636
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHL 703
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
200-478 |
1.97e-46 |
|
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: 167.13 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
469-739 |
9.16e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 172.72 E-value: 9.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 469 QKAVGSSEKIFEYLDrTPRCPPSGLLTPLHLEGLVQF--QDVSfaypnrpdVLVLQG------LTFTLRPGEVTALVGPN 540
Cdd:PRK11174 315 AQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIeaEDLE--------ILSPDGktlagpLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 541 GSGKST-VAALLQNLyqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKPTM--EEITAAAV 617
Cdd:PRK11174 386 GAGKTSlLNALLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQALE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVL 697
Cdd:PRK11174 461 NAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTL 538
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2468698279 698 LITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:PRK11174 539 MVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
521-671 |
2.20e-45 |
|
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 as in CFTR, or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 158.97 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQENI 599
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 600 AYGLtqkpTMEEITAAAVKSGAHSFISGLPQGY--DTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
501-725 |
4.70e-45 |
|
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: 160.74 E-value: 4.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENIAygltqkP----TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALAR 655
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
202-478 |
2.55e-43 |
|
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: 158.45 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQ-DGSADTFTRNLT-----LMSILTIASA-------VLEFVGDGIYNNtmghvhshLQGEVFGAV 268
Cdd:cd18573 13 MSVPFAIGKLIDVASKeSGDIEIFGLSLKtfalaLLGVFVVGAAanfgrvyLLRIAGERIVAR--------LRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 269 LRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKW 348
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 YQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILY 428
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
502-722 |
5.24e-43 |
|
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: 155.36 E-value: 5.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYL 577
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQ-----VF--GRSLQENI-AYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQLSGG 646
Cdd:cd03257 81 RKEIQMVFQDPMsslnpRMtiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPH-----------ELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIRE 722
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
233-741 |
1.38e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.13 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVleFVGDGI---YNNTMGH-VHSHLQGEVFGAVLRQETEFFQQ--NQTGNITSRVTEDTSTLSDSLSENLSLF 306
Cdd:PTZ00265 872 ILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 307 LWYLVRGL---------C-LLGIMLWGSVSLTM----VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAI-EAL 371
Cdd:PTZ00265 950 THFIVLFLvsmvmsfyfCpIVAAVLTGTYFIFMrvfaIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIqEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 372 SAMPTVRSFANEE------GEAQKFREKLQEIKTLnqkeavayaVNS--WTTSISGMLLKVGILY-IGGQLVTSGAVSSG 442
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTL---------VNSmlWGFSQSAQLFINSFAYwFGSFLIRRGTILVD 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 443 NLVTfVLYQMQFTQAVE-VLLSIYPRVQKAVGSSEKIFEYLDRTP----------RCPPSGLLtplhlEGLVQFQDVSFA 511
Cdd:PTZ00265 1101 DFMK-SLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSnidvrdnggiRIKNKNDI-----KGKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 512 YPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ----------------------------------- 556
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 557 -------------------PTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAV 617
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVL 697
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 698 LITQHLSLVEQADHILFLE-----GGTIREGGTHQQLME-KKGCYWAMVQ 741
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
503-719 |
9.02e-41 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 148.39 E-value: 9.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDV--LVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLyQPTEGQLlldgkplpqyehrYLHR 579
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENIAYGltqKPTMEE-----ITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFG---KPFDEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 655 RALIRKPCVLILDDATSALDAnsqlQVEQLLYES----PELYSRSVLLITQHLSLVEQADHILFLEGGT 719
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
504-719 |
2.36e-40 |
|
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: 147.23 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQRQAV 651
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGT 719
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
502-732 |
6.08e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 224054 [Multi-domain] Cd Length: 293 Bit Score: 148.99 E-value: 6.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQV 581
Cdd:COG1131 4 VIEVRNLTKKYGG--DKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVK-EPAKVRRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENI-----AYGLTQKPTMEEITAAAvksgahsFISGLPQGYDTEVgeagSQLSGGQRQAVALAR 655
Cdd:COG1131 81 GYVPQEPSLYPElTVRENLeffarLYGLSKEEAEERIEELL-------ELFGLEDKANKKV----RTLSGGMKQRLSIAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG1131 150 ALLHDPELLILDEPTSGLDPESRREIWELLRELAKEGGVTILLSTHILEEAEElCDRVIILNDGKIIAEGTPEELKEK 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
502-729 |
9.43e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 224045 [Multi-domain] Cd Length: 258 Bit Score: 147.32 E-value: 9.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG1120 2 MLEVENLSFGYGGKP---ILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASLSPKELAKKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQV-FGRSLQENIAYGLTQKPTM---------EEITAAAVKSGAHSFIsglpqgyDTEVGEagsqLSGGQRQAV 651
Cdd:COG1120 79 AYVPQSPSApFGLTVYELVLLGRYPHLGLfgrpskedeEIVEEALELLGLEHLA-------DRPVDE----LSGGERQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI-REGGTHQQL 729
Cdd:COG1120 148 LIARALAQETPILLLDEPTSHLDIAHQIEVLELLRDLNREKGLTVVMVLHDLNLAARyADHLILLKDGKIvAQGTPEEVL 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
502-733 |
1.84e-39 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 224047 [Multi-domain] Cd Length: 235 Bit Score: 145.48 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYLHRQ 580
Cdd:COG1122 3 MIEAENLSFRYPGR--KAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTsSEKSLLELRQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:COG1122 81 VGLVFQNPddQLFGPTVEDEVAFGLENLGLPREEIEERVAEALELV--GLEELLDRPP----FNLSGGQKQRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:COG1122 155 MGPEILLLDEPTAGLDPKGRRELLELLKKLKEEGGKTIIIVTHDLELVLEyADRVVVLDDGKILADGDPAEIFNDA 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
503-722 |
1.26e-38 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 142.61 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNR-PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyehryLHRQV 581
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFG-RSLQENIAYGLtqkpTMEEITAAAVKSGAHSFISglpqgydtEVGEAG------SQLSGGQRQAVALA 654
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL----ELQGVPKAEARERAEELLE--------LVGLSGfenaypHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqHlSLVEQ---ADHILFLEG--GTIRE 722
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVT-H-DIDEAvflADRVVVLSArpGRIVA 214
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
201-478 |
1.70e-38 |
|
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: 144.62 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd07346 255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
503-724 |
2.06e-38 |
|
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: 140.53 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRyLHRQVA 582
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeaGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGG 724
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
506-720 |
2.09e-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: 140.65 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVg 585
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 qePQVfgrslqeniaygltqkptMEEITAAAVksgAHSFIsglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03214 79 --PQA------------------LELLGLAHL---ADRPF---------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
504-720 |
1.90e-37 |
|
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: 137.73 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCV 663
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 664 LILDDATSALDansqLQVEQLLYE---SPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03246 118 LVLDEPNSHLD----VEGERALNQaiaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
255-746 |
2.03e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 151.28 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 255 HVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLF---LWYLVRGLCLLG----IMLWGSVSL 327
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQLLSTFALIGtvstISLWAIMPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 328 TMVTLVTLPllfllpkkvgkWYQLLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFaneegeaqKFREKLQEIKTLNQK 403
Cdd:PLN03232 1060 LILFYAAYL-----------YYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY--------KAYDRMAKINGKSMD 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 404 EAVAYAV-----NSWTT----SISGMLL----KVGILYIGGQLVTSGAVSSGNLVtfVLYQMQFTQAVEVLLSIYPRVQK 470
Cdd:PLN03232 1121 NNIRFTLantssNRWLTirleTLGGVMIwltaTFAVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAEN 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 471 AVGSSEKIFEYLDRTPRC--------PPSGLltplHLEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNG 541
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEAtaiiennrPVSGW----PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTG 1272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 542 SGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITA----AAV 617
Cdd:PLN03232 1273 AGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDAdlweALE 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVL 697
Cdd:PLN03232 1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTML 1424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 698 LITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG-CYWAMVQA--PADA 746
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHStgPANA 1476
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
503-729 |
5.51e-37 |
|
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: 138.47 E-value: 5.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTEGQLLLDGKPL--PQYEHR 575
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKsgahsfISGLPQgydtEVGE--AGSQLSGGQR 648
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALR------KAALWD----EVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGGTIREGG 724
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNM---QQAarvaDRTAFLLNGRLVEFG 222
|
....*
gi 2468698279 725 THQQL 729
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
504-719 |
6.59e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.45 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VgqepqvfgrslqeniaygltqkptmeeitaaavksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCV 663
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQA-DHILFLEGGT 719
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
202-478 |
1.14e-36 |
|
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: 139.69 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFT-RNLTLMSILTIasaVLEFVGDGIYN-------NTMGH-VHSHLQGEVFGAVLRQE 272
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEaLRALNQAVLIL---LGVVLIGSIATflrswlfTLAGErVVARLRKRLFSAIIAQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 273 TEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18780 90 IAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQ 432
Cdd:cd18780 170 SKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGR 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2468698279 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18780 250 LVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-740 |
1.41e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 148.64 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 369 EALSAMPTVRSFANEEGEAQKFR--EKLQEIKTL--NQKEAVAYAVnswttsISGMLL---KVGILYiGGQLVTSGAVSS 441
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNlsEKLYSKYILkaNFMESLHIGM------INGFILasyAFGFWY-GTRIIISDLSNQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 442 --------GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYP 513
Cdd:PTZ00265 314 qpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYD 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL-DGKPLPQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGLTQKPTME--------------------------------------------------------EITAAA 616
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 617 VKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSV 696
Cdd:PTZ00265 554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 697 LLITQHLSLVEQADHILFL-----------------------------------------------EGGTIREGGTHQQL 729
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDAL 713
|
490
....*....|..
gi 2468698279 730 ME-KKGCYWAMV 740
Cdd:PTZ00265 714 MKnKNGIYYTMI 725
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-731 |
1.58e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 224049 [Multi-domain] Cd Length: 252 Bit Score: 137.78 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHR 579
Cdd:COG1124 3 LLSVRNLSIVYGGGKFAFhALNNVSLEIERGETLGIVGESGSGKSTLARLLAGLEKPSSGSILLDGKPLAPKKRaKAFYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAavksgaHSFisGLPQGYDTEvgeAGSQLSGGQRQAVA 652
Cdd:COG1124 83 PVQMVFQDPysslnprRTVGRILSEPLRPHGLSKSQQRIAELL------DQV--GLPPSFLDR---RPHELSGGQRQRIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1124 152 IARALIPEPKLLILDEPTSALDVSVQAQILNLLLELKKERGLTYLFISHDLALVEHmCDRIAVMDNGQIVEIGPTEELLS 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
268-741 |
3.97e-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: 147.01 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 268 VLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGK 347
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF----VQR 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 348 WYQLLEVQVR--ESLAKSSQVA--IEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKEAVAYAV-NSWttsisgmlL 422
Cdd:TIGR00957 1124 FYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVaNRW--------L 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 423 KVGILYIGGQLVTSGAV---------SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP---- 489
Cdd:TIGR00957 1192 AVRLECVGNCIVLFAALfavisrhslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiq 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 ----PSGLLTplhlEGLVQFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL 564
Cdd:TIGR00957 1272 etapPSGWPP----RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 643
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES--PELYSRSVLLITQHLSLVEQADHILFLEGGTIR 721
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVD----LETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
490 500
....*....|....*....|
gi 2468698279 722 EGGTHQQLMEKKGCYWAMVQ 741
Cdd:TIGR00957 1499 EFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
202-478 |
9.62e-36 |
|
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: 136.84 E-value: 9.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSS 441
Cdd:cd18576 173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 2468698279 442 GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18576 253 GDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
503-733 |
8.92e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 133.32 E-value: 8.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-KPLPQYEHRYLHRQV 581
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALA 654
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvprEEMRKRVDEALKLvGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
503-720 |
1.01e-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: 129.83 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhRQVA 582
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspelYS---RSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRE----LKkegKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
484-731 |
1.60e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224048 [Multi-domain] Cd Length: 539 Bit Score: 138.86 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 484 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPD--------VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY 555
Cdd:COG1123 262 GDEKIIRLPRRGPLRAEPLLSVRNLSKRYGSRKGlfvrergeVKAVDDVSFDLREGETLGLVGESGSGKSTLARILAGLL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 556 QPTEGQLLLDGKPLPQYEHRY--LHRQVAAVGQEPQVF---GRSLQENIA-----YGLTQKPTMEEITAAAVKsgahsfI 625
Cdd:COG1123 342 PPSSGSIIFDGQDLDLTGGELrrLRRRIQMVFQDPYSSlnpRMTVGDILAeplriHGGGSGAERRARVAELLE------L 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 626 SGLPQGYdtevgeAGS---QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQH 702
Cdd:COG1123 416 VGLPPEF------LDRyphELSGGQRQRVAIARALALEPKLLILDEPVSALDVSVQAQVLNLLKDLQEELGLTYLFISHD 489
|
250 260 270
....*....|....*....|....*....|
gi 2468698279 703 LSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1123 490 LAVVRYiADRVAVMYDGRIVEEGPTEKVFE 519
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
502-725 |
3.08e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224058 [Multi-domain] Cd Length: 339 Bit Score: 133.91 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNR--PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRY 576
Cdd:COG1135 1 MIELENVSKTFGQTgtGTVTALDDVSLEIPKGEIFGIIGYSGAGKSTLLRLINLLERPTSGSVFVDGQdltALSEAELRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFG-RSLQENIAYGL-TQKPTMEEItAAAVKSGAHsfISGLPqgydtevGEAG---SQLSGGQRQAV 651
Cdd:COG1135 81 LRQKIGMIFQHFNLLSsRTVFENVAFPLeLAGVPKAEI-KQRVAELLE--LVGLS-------DKADrypAQLSGGQKQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:COG1135 151 AIARALANNPKILLCDEATSALDPETTQSILELLKDINRELGLTIVLITHEMEVVKRiCDRVAVLDQGRLVEEGT 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
503-720 |
9.75e-34 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; 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. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. 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: 128.76 E-value: 9.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YL 577
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVFGR-SLQENIAYGL----TQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVgeagSQLSGGQRQAVA 652
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagVPKKERRERAEELLER------VGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport ... |
501-725 |
1.87e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism];
Pssm-ID: 226361 [Multi-domain] Cd Length: 352 Bit Score: 132.02 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhryl 577
Cdd:COG3842 4 PALEIRNVSKSFG---DFTAVDDISLDIKKGEFVTLLGPSGCGKTTLLRMIAGFEQPSSGEILLDGEDitdVPPEK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 hRQVAAVGQEPQVFG-RSLQENIAYGL--TQKPTMEEITAAAVKsgAHSFIsGLPQGYDTEVgeagSQLSGGQRQAVALA 654
Cdd:COG3842 77 -RPIGMVFQSYALFPhMTVEENVAFGLkvRKKLKKAEIKARVEE--ALELV-GLEGFADRKP----HQLSGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDAN--SQLQVEQLlyespELYSR---SVLLITQH----LSLveqADHILFLEGGTIREGGT 725
Cdd:COG3842 149 RALVPEPKVLLLDEPLSALDAKlrEQMRKELK-----ELQRElgiTFVYVTHDqeeaLAM---SDRIAVMNDGRIEQVGT 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
502-722 |
6.36e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224041 [Multi-domain] Cd Length: 248 Bit Score: 127.29 E-value: 6.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYehrylHRQV 581
Cdd:COG1116 3 LLEIEGVSKSFGGVE---VLEDINLSVEKGEFVAILGPSGCGKSTLLRLIAGLEKPTSGEVLLDGRPVTGP-----GPDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFG-RSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQRQA 650
Cdd:COG1116 75 GYVFQEDALLPwLTVLDNVALGLELrgksKAEARERAKELLE----------------LVGLAGfedkypHQLSGGMRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqHlSLVEQ---ADHILFLEG--GTIRE 722
Cdd:COG1116 139 VAIARALATRPKLLLLDEPFGALDALTREELQDELLRLWEETRKTVLLVT-H-DVDEAvylADRVVVLSNrpGRIGE 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
503-720 |
1.50e-32 |
|
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: 125.32 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVF-GRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03259 73 NIGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgLEGLLNRYP-------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
502-722 |
1.64e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224059 [Multi-domain] Cd Length: 226 Bit Score: 125.31 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH-- 578
Cdd:COG1136 1 MIELKNVSKIYGLGGeKVEALKDVNLEIEAGEFVAIVGPSGSGKSTLLNLLGGLDKPTSGEVLINGKDLTKLSEKELAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 -RQvaAVGQEPQVFG----RSLQENIAYGLT-----QKPTMEEITAAAVKSG-AHSFISGLPqgydtevgeagSQLSGGQ 647
Cdd:COG1136 81 rRK--KIGFVFQNFNllpdLTVLENVELPLLiagksAGRRKRAAEELLEVLGlEDRLLKKKP-----------SELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:COG1136 148 QQRVAIARALINNPKIILADEPTGNLDSKTAKEVLELLRELNKERGKTIIMVTHDPELAKYADRVIELKDGKIEE 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
503-719 |
2.92e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 123.07 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE--HRYLHRQ 580
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVF-GRSLQENIAYGltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIR 659
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGT 719
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
500-731 |
5.60e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENigvpREEMVERVDQALRQvGMEDFLNREP-----------HRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
503-732 |
6.56e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 226359 [Multi-domain] Cd Length: 338 Bit Score: 126.99 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQyehrylH 578
Cdd:COG3839 4 LELKNVRKSFGS---FEVLKDVNLDIEDGEFVVLLGPSGCGKSTLLRMIAGLEEPTSGEILIDGRDVtdlpPE------K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVK-----SGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:COG3839 75 RGIAMVFQNYALYPHmTVYENIAFGLKLRGVPKAEIDKRVKevaklLGLEHLLNRKP-----------LQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQhlSLVEQ---ADHILFLEGGTIREGGTHQQL 729
Cdd:COG3839 144 LARALVRKPKVFLLDEPLSNLDAKLRVLMRSEIKKLHERLGTTTIYVTH--DQVEAmtlADRIVVMNDGRIQQVGTPLEL 221
|
...
gi 2468698279 730 MEK 732
Cdd:COG3839 222 YER 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
502-727 |
9.40e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224046 [Multi-domain] Cd Length: 254 Bit Score: 124.26 E-value: 9.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyeHRYLHRqv 581
Cdd:COG1121 4 MIEVENLTVSYGNRP---VLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRK--RRKRLR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aaVGQEPQvfgrslQENIAYGLtqkP-TMEEItaaaVKSGAHS---FISGLPQGYDTEVGEA----G---------SQLS 644
Cdd:COG1121 77 --IGYVPQ------KSSVDRSF---PiTVKDV----VLLGRYGkkgWFRRLNKKDKEKVDEAlervGmedlrdrqiGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREG 723
Cdd:COG1121 142 GGQKQRVLLARALAQNPDLLLLDEPFTGVDVAGQKEIYDLLKELRQ-EGKTVLMVTHDLGLVMAyFDRVICLNRHLIASG 220
|
....
gi 2468698279 724 GTHQ 727
Cdd:COG1121 221 PPEE 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
516-732 |
9.90e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224043 [Multi-domain] Cd Length: 345 Bit Score: 126.70 E-value: 9.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH-RQVAAVGQEPQVFGR- 593
Cdd:COG1118 13 GAFGALDDISLDIKSGELVALLGPSGAGKSTLLRIIAGLETPDAGRIRLNGRVLFDVSNLAVRdRKVGFVFQHYALFPHm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGLTQKPTMEEitAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:COG1118 93 TVADNIAFGLKVRKERPS--EAEIRARVEELLrlvqlEGLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG1118 164 PFGALDAKVRKELRRWLRKLHDRLGVTTVFVTHDQEEAlELADRVVVLNQGRIEQVGPPDEVYDH 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
503-723 |
7.33e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEP--QVFGRSLQENIAYGLTQK----PTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALAR 655
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvppKKMKDiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL-FLEGGTIREG 723
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIvFSEGKLIAQG 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
502-725 |
7.35e-31 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 121.15 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEHRYL 577
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVF-GRSLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE--------VGEAG------SQ 642
Cdd:cd03258 81 RRRIGMIFQHFNLLsSRTVFENVALPLE--------------------IAGVPKAEIEErvlellelVGLEDkadaypAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
....
gi 2468698279 722 EGGT 725
Cdd:cd03258 221 EEGT 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
503-729 |
2.00e-30 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 119.91 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP---QYEHRYLHR 579
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPQGYDTEVGEagsqLSGGQRQA 650
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREivleklEAV---------GLRGAEDLYPAE----LSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
503-732 |
2.73e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 119.75 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARA 656
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYE-SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
502-729 |
2.85e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224051 [Multi-domain] Cd Length: 240 Bit Score: 119.53 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHRQ 580
Cdd:COG1126 2 MIEIKNLSKSFG---DKEVLKGISLSVEKGEVVVIIGPSGSGKSTLLRCLNGLEEPDSGSITVDGEDVGDKKDiLKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFG-RSLQENIAYGL--TQKPTMEEITAAAVK--------SGAHSFisglPqgydtevgeagSQLSGGQRQ 649
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPvkVKKLSKAEAREKALEllekvglaDKADAY----P-----------AQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG1126 144 RVAIARALAMDPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMIIVTHEMGFAREvADRVIFMDQGKIIEEGPPEE 222
|
.
gi 2468698279 729 L 729
Cdd:COG1126 223 F 223
|
|
| FtsE |
COG2884 |
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome ... |
502-727 |
3.43e-30 |
|
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225438 [Multi-domain] Cd Length: 223 Bit Score: 118.86 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLH 578
Cdd:COG2884 1 MIRFENVSKAYPGGR--EALRDVSFHIPKGEFVFLTGPSGAGKSTLLKLIYGEERPTRGKILVNGHDLSRLKGReipFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVF-GRSLQENIAYGL---------TQKPTMEEITAAAVKSGAHSFisglPqgydtevgeagSQLSGGQR 648
Cdd:COG2884 79 RQIGVVFQDFRLLpDRTVYENVALPLrvigkppreIRRRVSEVLDLVGLKHKARAL----P-----------SQLSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADH-ILFLEGGTIREGGTHQ 727
Cdd:COG2884 144 QRVAIARAIVNQPAVLLADEPTGNLDPDLSWEIMRLFEEINRL-GTTVLMATHDLELVNRMRHrVLALEDGRLVRDESRG 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
504-723 |
1.03e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.86 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehRYLHRQVAA 583
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQV---FGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsglpqgydTEVGEAG------SQLSGGQRQAVALA 654
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAL--------ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREG 723
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEyFDRVLLLNRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-720 |
1.26e-29 |
|
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: 116.59 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhRQVAAVGQ 586
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCV 663
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
502-685 |
2.25e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 224053 [Multi-domain] Cd Length: 500 Bit Score: 122.62 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YLHRQ 580
Cdd:COG1129 8 LLELRGISKSFG---GVKALDGVSLTVRPGEVHALLGENGAGKSTLMKILSGVYPPDSGEILIDGKPVAFSSPRdALAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENI--------AYGLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEagsqLSGGQRQAV 651
Cdd:COG1129 85 IATVHQELSLVPNlSVAENIflgreptrRFGLIDRKAMRRRARELLAR------LGLDIDPDTLVGD----LSIAQRQMV 154
|
170 180 190
....*....|....*....|....*....|....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANsqlQVEQLL 685
Cdd:COG1129 155 EIARALSFDARVLILDEPTAALTVK---ETERLF 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
508-732 |
3.30e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224048 [Multi-domain] Cd Length: 539 Bit Score: 122.68 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL----YQPTEGQLLLDGKP---LPQYEHRYLH-R 579
Cdd:COG1123 13 VEFATDGGR-VPAVRDVSFEVEPGEILGIVGESGSGKSTLALALMGLlpegGRITSGEVILDGRDllgLSEREMRKLRgK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP-------QVFGRSLQEniAYGLTQKPTMEEITAAAVKSGAhsfISGLPQgyDTEVGEAGSQLSGGQRQAVA 652
Cdd:COG1123 92 RIAMIFQDPmtslnpvMTIGDQIRE--ALRLHGKGSRAEARKRAVELLE---QVGLPD--PERRDRYPHQLSGGMRQRVM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1123 165 IAMALALKPKLLIADEPTTALDVTTQAQILDLLKDLQRELGMAVLFITHDLGVVAElADRVVVMYKGEIVETGPTEEILS 244
|
.
gi 2468698279 732 K 732
Cdd:COG1123 245 N 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
503-732 |
4.47e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 224042 [Multi-domain] Cd Length: 253 Bit Score: 116.49 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTEGQLLLDGKPLpqYEH 574
Cdd:COG1117 8 IEVRDLNLYYG---DKHALKDINLDIPKNKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEVLLDGKNI--YDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RY----LHRQVAAVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKSGAhsfisgLpqgYDtEV----GEAGSQ 642
Cdd:COG1117 80 KVdvveLRRRVGMVFQKPNPFPMSIYDNVAYGLrlhgIKDKELDEIVESSLKKAA------L---WD-EVkdrlHKSALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGG 718
Cdd:COG1117 150 LSGGQQQRLCIARALAVKPEVLLMDEPTSALDPISTLKIEELITELKKKY--TIVIVTHNM---QQAarvsDYTAFFYLG 224
|
250
....*....|....
gi 2468698279 719 TIREGGTHQQLMEK 732
Cdd:COG1117 225 ELVEFGPTDKIFTN 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
500-732 |
7.23e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYpNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13648 5 NSIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK--PT--MEEITAAAVKS-GAHSFISGLPQGydtevgeagsqLSGGQRQAVA 652
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHavPYdeMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
503-730 |
1.72e-28 |
|
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: 114.32 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL----VPKLLKWPKEKIRERADELLAlvGLdPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
503-732 |
2.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVA 652
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRDVLADvGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
500-729 |
4.46e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226967 [Multi-domain] Cd Length: 268 Bit Score: 113.85 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNR------PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY- 572
Cdd:COG4608 2 EPLLEVKNLKKYFPVGkgfgkkRYVKAVDGVSFSIKEGETLGLVGESGCGKSTLGRLILGLEEPTSGEILFEGKDITKLs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 ---EHRYLHRQVAAVGQEPQVFGRslqeniaygltqkptmeeitaaavksgahsfisglpqgYDtevgeagSQLSGGQRQ 649
Cdd:COG4608 82 keeRRERVLELLEKVGLPEEFLYR--------------------------------------YP-------HELSGGQRQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG4608 117 RIGIARALALNPKLIVADEPVSALDVSVQAQILNLLKDLQEELGLTYLFISHDLSVVRYiSDRIAVMYLGKIVEIGPTEE 196
|
.
gi 2468698279 729 L 729
Cdd:COG4608 197 V 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
503-732 |
4.91e-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: 112.72 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqLEGYANRKP-------SQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 658 IRKPCVLILDDATSALDAnsQLQvEQLLYESPELYSR---SVLLITqH-----LSLveqADHILFLEGGTIREGGTHQQL 729
Cdd:cd03300 146 VNEPKVLLLDEPLGALDL--KLR-KDMQLELKRLQKElgiTFVFVT-HdqeeaLTM---SDRIAVMNKGKIQQIGTPEEI 218
|
...
gi 2468698279 730 MEK 732
Cdd:cd03300 219 YEE 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
502-725 |
6.04e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 6.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHRYL---H 578
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-LTQKPTMEEI----TAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLI--TQHLSLVE-QADHILFLEGGTIREGGT 725
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLY---DLNKEGITIIisTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ... |
502-731 |
9.15e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 223487 [Multi-domain] Cd Length: 237 Bit Score: 112.18 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQ 580
Cdd:COG0410 3 MLEVENLSAGYGKIQ---ALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFDGEDITGLPpHERARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaAAVKSGAHSFISGLPQGYD------TEVGEAGSQLSGGQRQAVAL 653
Cdd:COG0410 80 IAYVPEGRRIFPRlTVEENLLLG------------AYARRDKEAQERDLEEVYElfprlkERRNQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALdanSQLQVEQLLYESPELYSR---SVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:COG0410 148 ARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIKELRKEggmTILLVEQNARFAlEIADRGYVLENGRIVLSGTAAEL 224
|
..
gi 2468698279 730 ME 731
Cdd:COG0410 225 LA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
501-725 |
1.32e-27 |
|
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: 110.96 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAavksgahsfisglpqgydTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
520-731 |
1.37e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 111.37 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFGR-SLQE 597
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NI---AYGLTQ---KPTMEEItaaavksgahsfisglpqgYD------TEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03224 95 NLllgAYARRRakrKARLERV-------------------YElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 666 LDDATSALdanSQLQVEQLLYESPELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:cd03224 156 LDEPSEGL---APKIVEEIFEAIRELRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
506-730 |
1.43e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFisglpqgydtevgeAGS---QLSGGQRQAVALARA 656
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 657 LIR------KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228
|
.
gi 2468698279 730 M 730
Cdd:PRK13548 229 L 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
503-720 |
1.60e-27 |
|
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: 110.70 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ--YEHRYLHRQ 580
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAAV----KSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIkvKGMSKAEAEERALelleKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 654 ARALIRKPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
499-720 |
1.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
526-724 |
2.20e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 110.46 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----------PQyehrylHRQVAAVGQEPQV 590
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQ------QRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGR-SLQENIAYGLTQKPTMEE-ITAAAVKSGAHsfISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03297 87 FPHlNVRENLAFGLKRKRNREDrISVDELLDLLG--LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
504-720 |
2.43e-27 |
|
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: 111.12 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH---RQ 580
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaaavKSGAHSFISGLPQGYDTE-----------VGEAG------SQ 642
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSG---------------RLGRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-746 |
2.75e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 119.07 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 266 GAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFL---WYLVRGLCLLGIM----LWGSVSLTMVTLVTLPll 338
Cdd:PLN03130 994 GSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLFYGAYL-- 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 339 fllpkkvgkWYQLL--EVQVRESLAKSSQVAI--EALSAMPTVRsfaneegeAQKFREKLQEIKTLNQKEAVAYAV---- 410
Cdd:PLN03130 1072 ---------YYQSTarEVKRLDSITRSPVYAQfgEALNGLSTIR--------AYKAYDRMAEINGRSMDNNIRFTLvnms 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 411 -NSWTT----SISG-MLLKVGILYIGGQLVTSGAVSSGNLVTFVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLD 483
Cdd:PLN03130 1135 sNRWLAirleTLGGlMIWLTASFAVMQNGRAENQAAFASTMGLLLsYALNITSLLTAVLRLASLAENSLNAVERVGTYID 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 484 RTPRCP--------PSGLLTplhlEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL 554
Cdd:PLN03130 1215 LPSEAPlviennrpPPGWPS----SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI 1288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 555 YQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITAAAVKS--GAH--SFISGLPQ 630
Cdd:PLN03130 1289 VELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlkDVIRRNSL 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 631 GYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQAD 710
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIIDCD 1440
|
490 500 510
....*....|....*....|....*....|....*....
gi 2468698279 711 HILFLEGGTIREGGTHQQLMEKKGCYWA-MVQA--PADA 746
Cdd:PLN03130 1441 RILVLDAGRVVEFDTPENLLSNEGSAFSkMVQStgAANA 1479
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
502-725 |
3.24e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 224050 [Multi-domain] Cd Length: 309 Bit Score: 112.78 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG1125 1 MIEFENVSKRYGNKK---AVDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILIDGEDISDLDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVGEAGSQLSGGQRQAVALARAL 657
Cdd:COG1125 78 GYVIQQIGLFpHLTVAENIAT----VPKLLGWDKERIKKRADELLDlvGLdPSEY---ADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqH-----LSLveqADHILFLEGGTIREGGT 725
Cdd:COG1125 151 AADPPILLMDEPFGALDPITRKQLQEEIKELQKELGKTIVFVT-HdideaLKL---ADRIAVMDAGEIVQYDT 219
|
|
| FetA |
COG4619 |
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism] ... |
502-700 |
4.74e-27 |
|
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226970 [Multi-domain] Cd Length: 223 Bit Score: 109.56 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG4619 3 LLELKQVGYLAGDAK---ILNNISLSVRAGEFIAITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDVSTLKPEAYRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsfiSGLPqgyDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:COG4619 80 SYCAQTPALFGDTVEDNLifPWQIRNRRPDRAAALDLLAR------FALP---DSILTKNITELSGGEKQRIALIRNLQF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:COG4619 151 MPKILLLDEITSALDESNKRNIEEMIHRYVREQNVAVLWIT 191
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-478 |
6.54e-27 |
|
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: 111.41 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPF--FTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVhSHLQG-----EVFGAVLRQETE 274
Cdd:cd18577 18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTIT-GERQArrirkRYLKALLRQDIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18577 97 WFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18577 177 KEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLV 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18577 257 RDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MlaF |
COG1127 |
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ... |
502-729 |
7.21e-27 |
|
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224052 [Multi-domain] Cd Length: 263 Bit Score: 110.38 E-value: 7.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHR 579
Cdd:COG1127 8 LIEVRGVTKSFGDRV---ILDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEILIDGEDIPQLseEELYEIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 -QVAAVGQEPQVFGR-SLQENIAYGLTQ-----KPTMEEITAAAVKSgahsfiSGLPqgydtevGEAG----SQLSGGQR 648
Cdd:COG1127 85 kRMGVLFQQGALFSSlTVFENVAFPLREhtklpESLIRELVLMKLEL------VGLR-------GAAAdlypSELSGGMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:COG1127 152 KRVALARAIALDPELLFLDEPTSGLDPISAGVIDELIRELNDALGLTVIMVTHDLdSLLTIADRVAVLADGKVIAEGTPE 231
|
..
gi 2468698279 728 QL 729
Cdd:COG1127 232 EL 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism]; |
507-734 |
8.19e-27 |
|
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];
Pssm-ID: 226360 [Multi-domain] Cd Length: 231 Bit Score: 109.36 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlvlqgLTFTLR--PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhRQV 581
Cdd:COG3840 6 DVRFSYGHLP-------MRFDLTvpAGEIVAILGPSGAGKSTLLNLIAGFETPASGEILINGVDhtaSPPAE-----RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAYGLtqKPTM-------EEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:COG3840 74 SMLFQENNLFAHlTVAQNIGLGL--SPGLklnaeqrEKVEAAAAQVGLAGFLKRLP-----------GELSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG3840 141 ARCLVREQPILLLDEPFSALDPALRAEMLALVSQLCDERKMTLLMVTHHPEDAARiADRVVFLDNGRIAAQGSTQELLSG 220
|
..
gi 2468698279 733 KG 734
Cdd:COG3840 221 KA 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
490-731 |
1.65e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226641 [Multi-domain] Cd Length: 534 Bit Score: 114.29 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPLHLEG--LVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 558
Cdd:COG4172 262 PSGDPPPLPEDApvLLEVEDLRVWFPIKGGFLrrtvdhlrAVDGISLTLRRGQTLGLVGESGSGKSTLGlALLRLI--PS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQY---EHRYLHRQVAAVGQEPqvFG-----RSLQENIAYGL---TQKPTMEEI---TAAAVKSgahsf 624
Cdd:COG4172 340 QGEIRFDGQDIDGLsrkEMRPLRRRMQVVFQDP--YGslsprMTVGQIIEEGLrvhEPKLSAAERdqrVIEALEE----- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 625 iSGLPQG----YDTEvgeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:COG4172 413 -VGLDPAtrnrYPHE-------FSGGQRQRIAIARALILKPELILLDEPTSALDRSVQAQVLDLLRDLQQKHGLSYLFIS 484
|
250 260 270
....*....|....*....|....*....|..
gi 2468698279 701 QHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4172 485 HDLAVVRAlCHRVIVMRDGKIVEQGPTEAVFA 516
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
499-729 |
2.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.44 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVK-SGAHSFISGLPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
502-729 |
2.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--GLEELRD----RVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
203-478 |
3.80e-26 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 109.05 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFFQQ 278
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEA----LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRvvrdLRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 279 NQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRE 358
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 359 SLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGA 438
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2468698279 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18552 253 LTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
503-675 |
5.46e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 106.18 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhR 579
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELLqIEHLLDRKP-------KQLSGGQRQRVALGRAI 145
|
170
....*....|....*...
gi 2468698279 658 IRKPCVLILDDATSALDA 675
Cdd:cd03301 146 VREPKVFLMDEPLSNLDA 163
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-734 |
9.42e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.06 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSWTTSISGMLLKV---GIL-YIGGQLVTSGAVS 440
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVQTVRddelSWFRKAQLLSAFNSFILNSIPVLVTVvsfGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 441 SGNL---VTFVLYQMQ--FTQAVEVLLSIyPRVQKAVGSSEKIFeyldrtprcppsgLLTPLHLEGL--VQFQDVSFAYP 513
Cdd:PLN03130 560 SLSLfavLRFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-------------LPNPPLEPGLpaISIKNGYFSWD 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFG 592
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFN 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGLTQKPTMEEiTAAAVKSGAHSfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 673 LDANSQLQV-EQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTH----------QQLMEKKG 734
Cdd:PLN03130 771 LDAHVGRQVfDKCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYeelsnngplfQKLMENAG 841
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
502-722 |
9.43e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.95 E-value: 9.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK10247 7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPqgyDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLE--GGTIRE 722
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQphAGEMQE 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
502-722 |
1.63e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.69 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPN------RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--- 572
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHRQVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQ 642
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnprKTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 2468698279 722 E 722
Cdd:PRK10419 232 E 232
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
203-478 |
1.65e-25 |
|
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: 107.13 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSAdtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK 362
Cdd:cd18551 94 DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 363 SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSG 442
Cdd:cd18551 174 LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVG 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 2468698279 443 NLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18551 254 TLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-720 |
2.00e-25 |
|
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: 102.89 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPqyehrylhrqvaavgqepqvfGRSL 595
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLtqkptmeeitaAAVksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03216 70 RDARRAGI-----------AMV-----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2468698279 676 NsqlQVEQLLYESPELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03216 116 A---EVERLFKVIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-725 |
2.03e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 223521 [Multi-domain] Cd Length: 316 Bit Score: 107.66 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TEGQLLLDGKPL----PQ 571
Cdd:COG0444 1 LLEVKNLSVSFPTDAgVVKAVDGVSFELKKGEILGIVGESGSGKSVLAkAIMGLLPKPnariVGGEILFDGKDLlslsEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQvfgRSLqeNIAYgltqkpTMEEITAAAVKsgAHSFISGLPQGYDT------EVG--EAGS-- 641
Cdd:COG0444 81 ELRKIRGKEIAMIFQDPM---TSL--NPVM------TIGDQIAEVLR--LHGKGLSKKEAKERaielleLVGipDPERrl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 -----QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL 715
Cdd:COG0444 148 ksyphELSGGMRQRVMIAMALALNPKLLIADEPTTALDVTVQAQILDLLKELQREKGTALILITHDLGVVAEiADRVAVM 227
|
250
....*....|
gi 2468698279 716 EGGTIREGGT 725
Cdd:COG0444 228 YAGRIVEEGP 237
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
202-478 |
2.27e-25 |
|
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: 106.75 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdGIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQ-GYLAEKASQkVAYDLRNDLYDHLQRLSFSFHDKAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLG----IMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18542 95 TGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIipfiALFSYVFFKKVRPAFE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 evQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN-SWTTSISGMLLkVGILYIGG 431
Cdd:cd18542 169 --EIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYwPLMDFLSGLQI-VLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ... |
518-720 |
2.58e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 223488 [Multi-domain] Cd Length: 250 Bit Score: 105.35 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVF----- 591
Cdd:COG0411 17 LTAVNDVSLEVRPGEIVGLIGPNGAGKTTLFNLITGFYKPSSGTVIFRGRDITGLPpHRIARLGIARTFQITRLFpgltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 ------GRSLQENIAYGLTQKPTMEEITAAAVKsgAHSFIS--GLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCV 663
Cdd:COG0411 97 lenvavGAHARLGLSGLLGRPRARKEEREARER--ARELLEfvGLGELADRPAGN----LSYGQQRRLEIARALATQPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:COG0411 171 LLLDEPAAGLNPEETEELAELIRELRDRGGVTILLIEHDMKLVMGlADRIVVLNYGEV 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms]; |
499-729 |
2.99e-25 |
|
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
Pssm-ID: 226637 [Multi-domain] Cd Length: 267 Bit Score: 105.67 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVL------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY 572
Cdd:COG4167 1 IETLLEVRNLSKTFRYRTGLFrrqtveAVKPVSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEILINDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHRQVAAVGQEP-------QVFGRSLQE--NIAYGLTQKPTMEEI--TAAAVksgahsfisGLpqgYDTEVGEAGS 641
Cdd:COG4167 81 DYSFRSKRIRMIFQDPntslnprLRIGQILDFplRLNTDLEPEQRRKQIfeTLRMV---------GL---LPDHANYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL-EGGT 719
Cdd:COG4167 149 MLAPGQKQRVALARALILRPKIIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMIKHiSDQVLVMhEGEV 228
|
250
....*....|
gi 2468698279 720 IREGGTHQQL 729
Cdd:COG4167 229 VERGSTADVL 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
515-736 |
4.50e-25 |
|
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: 111.96 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLyQPTEGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGR 593
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-------------SVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYG--LTQKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:TIGR00957 714 SLRENILFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 672 ALDANsqlqVEQLLYES---PE--LYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR00957 790 AVDAH----VGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_FtsE_transporter |
cd03292 |
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic ... |
503-720 |
4.59e-25 |
|
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 103.64 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLHR 579
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVF-GRSLQENIAYGL--TQKPTME---EITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFALevTGVPPREirkRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQADH-ILFLEGGTI 720
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
502-729 |
5.07e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226641 [Multi-domain] Cd Length: 534 Bit Score: 109.67 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPT----EGQLLLDGKPLPQYEHR 575
Cdd:COG4172 6 LLSIRNLSVAFhQEGGTVEAVKGISFDIEAGETLALVGESGSGKSvTALSILGLLPSPAaahpSGSILFDGEDLLAASER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHR----QVAAVGQEPQV-------FGRSLQENIA--YGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgea 639
Cdd:COG4172 86 QLRGvrgnKIGMIFQEPMTslnplhtIGKQLAEVLRlhRGLSRAAARARALELLELVGipePEKRLDAYPH--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:COG4172 157 --ELSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKELQAELGMAILFITHDLGIVRKfADRVYVMQHG 234
|
250
....*....|.
gi 2468698279 719 TIREGGTHQQL 729
Cdd:COG4172 235 EIVETGTTETL 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
500-733 |
5.44e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTEGQLLLDGKPL-- 569
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 570 PQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKsGAHSFISGLPQGYDTEVGeagsqLS 644
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVLDEAVEKSLK-GASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQADHI-----LFLEGGT 719
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSM---QQASRIsdrtgFFLDGDL 225
|
250
....*....|....
gi 2468698279 720 IREGGTHQQLMEKK 733
Cdd:PRK14239 226 IEYNDTKQMFMNPK 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
502-731 |
9.80e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHRYLHR 579
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQkptmeeiTAAAVKSGAHSFISGLPqgydTEVGEAG------SQLSGGQRQAVA 652
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLR-------VRGASKEEAEKQARELL----AKVGLAErahhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQ---LQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
...
gi 2468698279 729 LME 731
Cdd:PRK09493 223 LIK 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
496-731 |
9.92e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.10 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 496 PLHLEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR 575
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQE-PQVFGRSLQENIA------------YGLTQKPTMEE-ITAAAVKSGAHSFIsglpqgydtevgeagS 641
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEaISLVGLKPLAHRLV---------------D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
250
....*....|.
gi 2468698279 721 REGGTHQQLME 731
Cdd:PRK10575 227 IAQGTPAELMR 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
490-729 |
1.21e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPL--HLEGLVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 558
Cdd:PRK15134 261 PSGDPVPLpePASPLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQYEHRYL---HRQVAAVGQEPQvfgRSL------QENIAYGLT-QKPTMeeiTAAAVKSgahSFISGL 628
Cdd:PRK15134 339 QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN---SSLnprlnvLQIIEEGLRvHQPTL---SAAQREQ---QVIAVM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 629 pqgydTEVG-------EAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQ 701
Cdd:PRK15134 410 -----EEVGldpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
250 260
....*....|....*....|....*....
gi 2468698279 702 HLSLVEQADH-ILFLEGGTIREGGTHQQL 729
Cdd:PRK15134 485 DLHVVRALCHqVIVLRQGEVVEQGDCERV 513
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
203-478 |
2.39e-24 |
|
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: 103.72 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdgIYN-NTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR--FYLvSWLGeRVVADLRKAVFAHLLRLSPSFFETTR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd18575 92 TGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:cd18575 172 ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMS 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18575 252 AGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
506-730 |
2.52e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.78 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYG----------LTQKPtmEEITAAAVKsgahsfisglpqgyDTEVGEAG----SQLSGGQRQA 650
Cdd:PRK11231 83 QHHLTpEGITVRELVAYGrspwlslwgrLSAED--NARVNQAME--------------QTRINHLAdrrlTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLITQhLSLVEQA----DHILFLEGGTIREGGTH 726
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR---ELNTQGKTVVTV-LHDLNQAsrycDHLVVLANGHVMAQGTP 222
|
....
gi 2468698279 727 QQLM 730
Cdd:PRK11231 223 EEVM 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
520-728 |
2.92e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226929 [Multi-domain] Cd Length: 259 Bit Score: 102.82 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQV-FGRSLQEN 598
Cdd:COG4559 16 LLDGVSLDLRPGEVLAILGPNGAGKSTLLKALSGELSPDSGEVTLNGVPLNSWPPEELARHRAVLPQNSSLaFPFTVQEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYGL------TQKPTMEEITAAAVksgAHSFISGLPQGYDTEvgeagsqLSGGQRQAVALARAL------IRKPCVLIL 666
Cdd:COG4559 96 VQMGRiphrsgREPEEDERIAAQAL---AATDLSGLAGRDYRT-------LSGGEQQRVQLARVLaqlwppVPSGRWLFL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 667 DDATSALDANSQLQVEQLLYespELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG4559 166 DEPTSALDIAHQHHTLRLAR---QLAREggAVLAVLHDLNLAAQyADRIVLLHQGRVIASGSPQD 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
503-729 |
4.21e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 101.04 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqYEHRYLHRQVa 582
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQvfGRSL------QENIAY-----GLTQKPTMEEITAAAVKsgahsfiSGLPQGYDTEVGeagsQLSGGQRQAV 651
Cdd:cd03263 77 -LGYCPQ--FDALfdeltvREHLRFyarlkGLPKSEIKEEVELLLRV-------LGLTDKANKRAR----TLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
520-729 |
4.59e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.40 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 674 DANSQLQVEQLLYE-SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK10851 168 DAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
503-720 |
5.32e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 100.65 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLVLqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLpQGYDTEVGEagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV--GL-AGLEKRLPG---ELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
497-723 |
8.72e-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: 100.59 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVqfqdVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY-EHR 575
Cdd:cd03219 1 LEVRGLT----KRFG-----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEPQVFGR-SLQENIA--------YGLTQKPTMEEITAAAVKsgAHSFIS--GLPQGYDTEVGEagsqLS 644
Cdd:cd03219 72 IARLGIGRTFQIPRLFPElTVLENVMvaaqartgSGLLLARARREEREARER--AEELLErvGLADLADRPAGE----LS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGT-IRE 722
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRVTVLDQGRvIAE 224
|
.
gi 2468698279 723 G 723
Cdd:cd03219 225 G 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
507-724 |
9.13e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQV-FGRSLQENIAYG----LTQKPTMEEITAAAVKSGAHSfiSGLPQGYDTEVgeagSQLSGGQRQAVALARALIRKP 661
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMER--TGVAQFADRPV----TSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
201-478 |
1.32e-23 |
|
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: 101.70 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYN---NTMG-HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18544 15 ELLGPLLIKRAIDDYIVPGQGDL--QGLLLLALLYLGLLLLSFLLQYLQTyllQKLGqRIIYDLRRDLFSHIQRLPLSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18544 93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVlpllLLATYLFRKKSRKAYR-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 evQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGG 431
Cdd:cd18544 171 --EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18544 248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
502-734 |
2.02e-23 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 226927 [Multi-domain] Cd Length: 245 Bit Score: 99.80 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQV 581
Cdd:COG4555 1 MLEVTDLTKSYG--SKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFV-RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAY-----GLTQKpTMEEITAAAVKSgahsfiSGLPQGYDTEVGEagsqLSGGQRQAVALAR 655
Cdd:COG4555 78 GVLFGERGLYARlTARENLKYfarlnGLSRK-EIKARIAELSKR------LQLLEYLDRRVGE----FSTGMKQKVAIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG4555 147 ALVHDPSILVLDEPTSGLDIRTRRKFHDFIKQLKN-EGRAVIFSSHIMQEVEAlCDRVIVLHKGEVVLEGSIEALDARTV 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
515-725 |
2.12e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEP------ 588
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 -----QVFGRSLQENIAygLTQKPTMEEITAAAVKSGAhsfisgLPQgydtEVGEAGSQLSGGQRQAVALARALIRKPCV 663
Cdd:PRK15112 103 rqrisQILDFPLRLNTD--LEPEQREKQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
203-478 |
3.89e-23 |
|
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: 100.17 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSA------DTFTRNLTLMSILTIASAVLEFvgdgIYNNTMGHVhshlqgeVFGAV--LRQETE 274
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSY----LQNRLMARV-------SQRTVydLRKDLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 ---------FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKV 345
Cdd:cd18547 86 eklqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 346 GKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkV 424
Cdd:cd18547 166 AKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-V 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18547 245 LVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
515-712 |
3.91e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.19 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLV--LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP- 588
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 ------QVFGRSLQENIAYGltqkptmEEITAAAVKSGAHSFIS--GL-PQGYDtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11308 103 gslnprKKVGQILEEPLLIN-------TSLSAAERREKALAMMAkvGLrPEHYD----RYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEqadHI 712
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVE---HI 221
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
518-729 |
4.01e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226643 [Multi-domain] Cd Length: 386 Bit Score: 102.07 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYLHR-QVAAVGQEpqvFG- 592
Cdd:COG4175 41 VVGVNDASLDVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTRGEILVDGKdiaKLSAAELRELRRkKISMVFQS---FAl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevgeagsQLSGGQRQAVALARALIRK 660
Cdd:COG4175 118 lphRTVLENVAFGLEvqgvpkaerEERALEALELVGLEGYADKYPN---------------ELSGGMQQRVGLARALAND 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 661 PCVLILDDATSALDA--NSQLQvEQLLYESPELySRSVLLITQHLslvEQA----DHILFLEGGTIREGGTHQQL 729
Cdd:COG4175 183 PDILLMDEAFSALDPliRTEMQ-DELLELQAKL-KKTIVFITHDL---DEAlrigDRIAIMKDGEIVQVGTPEEI 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
369-734 |
4.58e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.44 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSW---TTSISGMLLKVGI-LYIGGQLVTSGAVS 440
Cdd:PLN03232 484 EILASMDTVKCYAWE----KSFESRIQGIRneelSWFRKAQLLSAFNSFilnSIPVVVTLVSFGVfVLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 441 SGNLVTFVLYQMQ-----FTQAVEVLLSIyPRVQKAVGSSEKIfeyLDRTPRCPPSgllTPLhleglVQFQDVSFAYPNR 515
Cdd:PLN03232 560 SLSLFAVLRSPLNmlpnlLSQVVNANVSL-QRIEELLLSEERI---LAQNPPLQPG---APA-----ISIKNGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTEGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGRS 594
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIAYGLTQKPtmeEITAAAVKSGAHSFISGLPQGYD-TEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PLN03232 695 VRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 674 DANSQLQVeqllYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT----------HQQLMEKKG 734
Cdd:PLN03232 772 DAHVAHQV----FDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTfaelsksgslFKKLMENAG 841
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
518-722 |
6.52e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226647 [Multi-domain] Cd Length: 228 Bit Score: 97.86 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH----RYLHRQVAAVGQEPQVFGR 593
Cdd:COG4181 23 LSILKGVELVVKRGETVAIVGPSGSGKSTLLAVLAGLDDPSSGEVRLLGQPLHKLDEdaraALRARHVGFVFQSFHLIPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENIAYGLTqkptMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG4181 103 lTALENVALPLE----LRGESSADSRAGAKALLEAV--GLGKRLTHYPAQLSGGEQQRVALARAFAGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 673 LDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:COG4181 177 LDRATGDKIADLLFALNRERGTTLVLVTHDPQLAARCDRQLRLRSGRLVE 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
201-478 |
7.26e-23 |
|
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: 99.51 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFF 276
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERitadLRRDLYEHLQRLSLSFF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18563 95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEI----KTLNQKEAVAYAVNSWTTSISGMLlkvgILYIGGQ 432
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELldanIRAEKLWATFFPLLTFLTSLGTLI----VWYFGGR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2468698279 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18563 251 QVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
525-674 |
7.95e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyEHRYL---HRQVAAVGQEPQVFGR-SLQENIA 600
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGL--------TQKPTMEEItaaAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK10771 94 LGLnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
..
gi 2468698279 673 LD 674
Cdd:PRK10771 160 LD 161
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
487-742 |
8.21e-23 |
|
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: 98.44 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 487 RCPPSGLLTplhLEGLVQFQDVSFAYPN--RPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL 564
Cdd:cd03288 7 GSSNSGLVG---LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsFISGLPQGYDTEVGEAGSQ 642
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdpECKCTDDRLWEALEIAQLKN----MVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
250 260
....*....|....*....|.
gi 2468698279 723 GGTHQQLMEKK-GCYWAMVQA 742
Cdd:cd03288 235 CDTPENLLAQEdGVFASLVRT 255
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-729 |
9.03e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-----LLDG-KPLPQYEH--RYLHRQVAAVGQEPQVF 591
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 -GRSLQENIAYG--LTQKPTMEEITAAAVKSGAHSFISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11264 98 pHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 669 ATSALDANSQLQV----EQLLYEspelySRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK11264 171 PTSALDPELVGEVlntiRQLAQE-----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-733 |
1.19e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 223562 [Multi-domain] Cd Length: 530 Bit Score: 102.33 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP----LPQYEHRYL 577
Cdd:COG0488 3 MITLENLSLAYGDRP---LLENVSLTLNPGERIGLVGRNGAGKSTLLKILAGELEPDSGEVTRPKGLrvgyLSQEPPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQV-----AAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS---------GLPQgYDTEVGEagsqL 643
Cdd:COG0488 80 EKTVldyviEGFGELRELLAELEEAYALLADPDDELLAELEALLEELDGWTLEAraeeallglGFPD-EDRPVSS----L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT--QHLsLVEQADHILFLEGGTIR 721
Cdd:COG0488 155 SGGWRRRVALARALLEEPDLLLLDEPTNHLDLESIEWLEDYLKR----YPGTVIVVShdRYF-LDNVATHILELDRGKLT 229
|
250
....*....|...
gi 2468698279 722 E-GGTHQQLMEKK 733
Cdd:COG0488 230 PyKGNYSSYLEQK 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
502-730 |
1.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHRQ 580
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYG---LTQKPT--MEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPIeiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
520-732 |
1.43e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.02 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhRQVAAVGQEPQVFGR-SL 595
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDTevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLgIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 675 ANSQLQVEQLLYESPELYSRSVLLITQhlSLVEQ---ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTH--DFEEAwalADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
518-746 |
1.59e-22 |
|
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: 97.71 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYL----HRQVAAVGQEpqvFG- 592
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQS---FAl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevgeagsQLSGGQRQAVALARALIRK 660
Cdd:cd03294 114 lphRTVLENVAFGLEvqgvpraerEERAAEALELVGLEGWEHKYPD---------------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDA--NSQLQvEQLLYESPELySRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQLmekkgcyw 737
Cdd:cd03294 179 PDILLMDEAFSALDPliRREMQ-DELLRLQAEL-QKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI-------- 248
|
....*....
gi 2468698279 738 amVQAPADA 746
Cdd:cd03294 249 --LTNPAND 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-735 |
2.56e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRqva 582
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQ---------------VFGRSlqeniaYGLTQKptmeeiTAAAVKSGAHSFiSGLPQGYDTEVGEagsqLSGGQ 647
Cdd:PRK13537 82 -VGVVPQfdnldpdftvrenllVFGRY------FGLSAA------AARALVPPLLEF-AKLENKADAKVGE----LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPE--LYSRSVLLITQHlsLVEQA----DHILFLEGG-TI 720
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWERLRslLARGKTILLTTH--FMEEAerlcDRLCVIEEGrKI 217
|
250
....*....|....*
gi 2468698279 721 REGGTHQQLMEKKGC 735
Cdd:PRK13537 218 AEGAPHALIESEIGC 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
489-735 |
2.79e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 489 PPSGLLTPLHLEglvqFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP 568
Cdd:PRK13536 32 SIPGSMSTVAID----LAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQyEHRYLHRQVAAVGQ----EPQVfgrSLQEN-IAYGLTQKPTMEEItaAAVKSGAHSFiSGLPQGYDTEVgeagSQL 643
Cdd:PRK13536 105 VPA-RARLARARIGVVPQfdnlDLEF---TVRENlLVFGRYFGMSTREI--EAVIPSLLEF-ARLESKADARV----SDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQlqveQLLYESpelySRSVL------LITQHlsLVEQA----DHIL 713
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR----HLIWER----LRSLLargktiLLTTH--FMEEAerlcDRLC 243
|
250 260
....*....|....*....|...
gi 2468698279 714 FLEGG-TIREGGTHQQLMEKKGC 735
Cdd:PRK13536 244 VLEAGrKIAEGRPHALIDEHIGC 266
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
503-731 |
3.33e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqNLYQPTEGQLLLDGKP--LPQ--YEHRY-- 576
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVefFNQniYERRVnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 --LHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQRQ 649
Cdd:PRK14258 84 nrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGgthqQ 728
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGNENRIG----Q 233
|
...
gi 2468698279 729 LME 731
Cdd:PRK14258 234 LVE 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
520-723 |
3.34e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 94.93 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPLPQYEHRylhRQVAAVGQEPQVFGR-SLQ 596
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYgltqkptmeeitAAAVKSgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:cd03213 101 ETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 677 SQLQVEQLLYESPELySRSVLLITQHLS--LVEQADHILFL-EGGTIREG 723
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLsQGRVIYFG 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-734 |
5.85e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 223562 [Multi-domain] Cd Length: 530 Bit Score: 100.40 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLPQYehrYLHRQV 581
Cdd:COG0488 321 VLEFENVSKGYDGGR--LLLKDLSFRIDRGDRIAIVGPNGAGKSTLLKLLAGELGPLSGTVKV-GETVKIG---YFDQHR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEpqvfgRSLQENIAYGLTQKPTMEeitaaaVKSGAHSFisGLPQgydTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:COG0488 395 DELDPD-----KTVLEELSEGFPDGDEQE------VRAYLGRF--GFTG---EDQEKPVGVLSGGEKARLLLAKLLLQPP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG0488 459 NLLLLDEPTNHLDIESLEALEEALLD----FEGTVLLVSHDRYFLDRvATRIWLVEDKVEEFEGGYEDYLEQKK 528
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
520-676 |
7.69e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyEHRYL-HRQVAAVGQEPQVFGR-SLQE 597
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIqQRDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGY-DtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK11432 98 NVGYGLkMLGVPKEERKQRVKEALELVDLAGFEDRYvD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
.
gi 2468698279 676 N 676
Cdd:PRK11432 170 N 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
502-733 |
9.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHR---YLH 578
Cdd:PRK13636 5 ILKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGahsfISGLPQgydtevgEAGSQLSGGQRQAV 651
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVE-QADHILFL-EGGTIREGGTHQQL 729
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMkEGRVILQGNPKEVF 230
|
....
gi 2468698279 730 MEKK 733
Cdd:PRK13636 231 AEKE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
503-724 |
1.24e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.44 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlPQYEHRYLhRQVA 582
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEAL-RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFG-RSLQENI-----AYGLTQKPTMEEITaaavksgahsfISGLPQGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:cd03268 76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLD-----------VVGLKDSAKKKVK----GFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
508-721 |
1.27e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226905 [Multi-domain] Cd Length: 259 Bit Score: 94.82 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHrylhrqvAAVG 585
Cdd:COG4525 9 LSLSYEGKP-RSALEDVSLTIASGELVVVLGPSGCGKTTLLNLIAGFVTPSRGSIQLNGRRIegPGAER-------GVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQVFG-RSLQENIAYGLtQKPTMEEITAAAVksgAHSFISglpqgydtEVGEAGS------QLSGGQRQAVALARALI 658
Cdd:COG4525 81 QNEALLPwLNVIDNVAFGL-QLRGIEKAQRREI---AHQMLA--------LVGLEGAehkyiwQLSGGMRQRVGIARALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIR 721
Cdd:COG4525 149 VEPQLLLLDEPFGALDALTREQMQELLLDLWQETGKQVLLITHDIeEALFLATRLVVLSPGPGR 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
502-682 |
1.36e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.33 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQV 581
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaaavksgahsfisglpqgydTEVGEA-------------GSQLSGG 646
Cdd:PRK09452 89 NTVFQSYALFPHmTVFENVAFGLrMQKTPAAEIT--------------------PRVMEAlrmvqleefaqrkPHQLSGG 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDAN--SQLQVE 682
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKlrKQMQNE 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
499-731 |
1.77e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PT---EGQLLLDGKPL--PQ 571
Cdd:PRK14243 7 TETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYG---LTQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQR 648
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGGTIREGG 724
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM---QQAarvsDMTAFFNVELTEGGG 232
|
....*..
gi 2468698279 725 THQQLME 731
Cdd:PRK14243 233 RYGYLVE 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
485-742 |
1.84e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 100.24 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 485 TPRCPPSGLLTPLHLEGLVqFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLL 563
Cdd:PTZ00243 1292 EPASPTSAAPHPVQAGSLV-FEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 564 LDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtmEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 643
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLIL-DDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250 260
....*....|....*....|.
gi 2468698279 723 GGTHQQL-MEKKGCYWAMVQA 742
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEA 1545
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
503-724 |
3.18e-21 |
|
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: 92.64 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEhRYLHRQVA 582
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGeagsQLSGGQRQAVALARALIR 659
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY----IAWLKGIPSKEVKARVDEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
202-455 |
4.00e-21 |
|
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: 94.40 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDwILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYNNT-MG---HVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18541 16 LLIPRIIGRAID-ALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLiFGasrRIEYDLRNDLFAHLLTLSPSFYQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:cd18541 93 KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISGMLLKVG---ILYIGGQLV 434
Cdd:cd18541 173 EAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR---VDALFFPLIGLLIGLSfliVLWYGGRLV 249
|
250 260
....*....|....*....|.
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFT 455
Cdd:cd18541 250 IRGTITLGDLVAFNSYLGMLI 270
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
507-729 |
4.30e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.57 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAY-----GLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYplkshGIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLyesPELYSRSVLLITQH--LSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLI---TELKNEIAIVIVSHnpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
504-732 |
5.62e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224057 [Multi-domain] Cd Length: 249 Bit Score: 92.68 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEhrylhrqvAA 583
Cdd:COG1134 26 RLKGLAKGGRKVAEFWALKDISFEIYKGERVGIIGHNGAGKSTLLKLIAGIYKPTSGKVKVTGKVAPLIE--------LG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRslqENIA-----YGLTQKPT---MEEITAAAvksgahsfisglpqgydtEVGEAGSQ----LSGGQRQAV 651
Cdd:COG1134 98 AGFDPELTGR---ENIYlrgliLGLTRKEIdekVDEIIEFA------------------ELGDFIDQpvktYSSGMYARL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQA-DHILFLEGGTIREGGTHQQLM 730
Cdd:COG1134 157 AFSVATHVEPDILLLDEVLAVGDAAFQEKCLERLNELVE-KNKTIVLVSHDLGAIKQYcDRAIWLEHGQIRMEGSPEEVI 235
|
..
gi 2468698279 731 EK 732
Cdd:COG1134 236 PA 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
509-734 |
9.11e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226952 [Multi-domain] Cd Length: 325 Bit Score: 93.99 E-value: 9.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKpLPQYEHRYLHRQVAAVgqep 588
Cdd:COG4586 28 HFFHRKERSIEAVQDISFEIPKGEIVGFLGANGAGKSTTLKMLTGLLLPTSGKVRVNGK-DPFRRREEYLRSIGLV---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 qvFGRSLQenIAYGLTQKPTME------EITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:COG4586 103 --MGQKLQ--LWWDLPALDSLEvlkliyEIPDDEFAERLDFLTEIL--DLEGFLKWPVRKLSLGQRMRAELAAALLHPPK 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG4586 177 VLFLDEPTVGLDVNAQANIREFLKEYNEERQATVLLTTHIFDDIATlCDRVLLIDQGQLVFDGTLAQLQEQFG 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
503-719 |
1.00e-20 |
|
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: 89.04 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqva 582
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 avgqepqvfgrslqENIAYgltqkptmeeitaaavksgahsFisglpqgydtevgeagSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03221 63 --------------VKIGY----------------------F----------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYEspelYSRSVLLITQHLSLVEQ-ADHILFLEGGT 719
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-724 |
1.22e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSLQENIAYGL-------TQKPTMEEITAAAVKSGahsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCV 663
Cdd:PRK14247 95 PNLSIFENVALGLklnrlvkSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
519-719 |
1.55e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.59 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LP-----------QYEHRYLHRQVAA- 583
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPghqiarmgvvrTFQHVRLFREMTVi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 ----VGQEpqvfgRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLpqgydTEVG--EAGSqLSGGQRQAVALARA 656
Cdd:PRK11300 99 enllVAQH-----QQLKTGLFSGLLKTPAFRRAESEALDRAATWLeRVGL-----LEHAnrQAGN-LAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGT 719
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGT 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
502-724 |
1.73e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.50 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQ 580
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAY-----GLtqKPTmeEITaAAVKSGAHSFisGLPQGYDTEVGEagsqLSGGQRQAVALA 654
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYfaglyGL--KGD--ELT-ARLEELADRL--GMEELLDRRVGG----FSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
500-725 |
1.74e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.07 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPD---VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRY 576
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAA-VGQEP--QVFGRSLQENIAYG---LTQKPtmEEITA----AAVKSGAHSFISGLPQgydtevgeagsQLSGG 646
Cdd:PRK13633 82 DIRNKAGmVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
524-685 |
1.88e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL---PQYEhrylhRQVAAVGQEPQVFGR-SLQENI 599
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQ-----RPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGLTQ-KPTMEEITA--AAVKSGAH--SFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:PRK11607 113 AFGLKQdKLPKAEIASrvNEMLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170
....*....|....*
gi 2468698279 675 AN----SQLQVEQLL 685
Cdd:PRK11607 182 KKlrdrMQLEVVDIL 196
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
503-685 |
1.88e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226164 [Multi-domain] Cd Length: 258 Bit Score: 91.55 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYLHR 579
Cdd:COG3638 4 IEVKNLSKTYPG--GHQALKDVNLEINQGEMVAIIGPSGAGKSTLLRSLNGLVDPTSGEILFNGVqitKLKGKELRKLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYG-LTQKPTMeeitaaavksgaHSFIsGLP------QGYD--TEVG------EAGSQL 643
Cdd:COG3638 82 DIGMIFQQFNLVPRlSVLENVLLGrLGYTSTW------------RSLF-GLFskedkaQALDalERVGildkayQRASTL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLL 685
Cdd:COG3638 149 SGGQQQRVAIARALVQQPKIILADEPVASLDPESAKKVMDIL 190
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
502-723 |
1.94e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLH 578
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQAL--QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVF-GRSLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:PRK10908 79 RQIGMIFQDHHLLmDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLSLVEQADH-ILFLEGGTIREG 723
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE----FNRvgvTVLMATHDIGLISRRSYrMLTLSDGHLHGG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
503-725 |
1.99e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.33 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY---EHRYLH 578
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEpqvF----GRSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLPQGYDTevgeAGSQLSGGQRQAVA 652
Cdd:PRK11153 82 RQIGMIFQH---FnllsSRTVFDNVALPLE----LAGTPKAEIKARVTELLElvGLSDKADR----YPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
503-721 |
2.52e-20 |
|
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: 90.03 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHRylHRqva 582
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR--NR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQVFG----RSLQENIAY-----GLTQKPTMEEITAAAVKSGahsfISglpqGYDTEVGEagsQLSGGQRQAVAL 653
Cdd:cd03269 72 -IGYLPEERGlypkMKVIDQLVYlaqlkGLKKEEARRRIDEWLERLE----LS----EYANKRVE---ELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
502-732 |
2.85e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL----LLDGKPLPQYEHR 575
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKSgahsfisglpQGYDTEVGEAGS-QLSGGQR 648
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLEM----------VGLADEFWEKSPfELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPS 229
|
....*
gi 2468698279 728 QLMEK 732
Cdd:PRK13643 230 DVFQE 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
202-478 |
3.19e-20 |
|
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: 91.76 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHV------------HSHLQGEVFGavl 269
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGD----LSGLLIIALLFLALNLVNWVASRLRIYLMAKVgqrilydlrqdlFSHLQKLSFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 rqeteFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKV 345
Cdd:cd18545 90 -----FFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVlpllVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 346 GKWYQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSW---TTSISGML 421
Cdd:cd18545 165 RKAWQ----RVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR---AVRLNALfwpLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 422 LKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-478 |
4.26e-20 |
|
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: 91.39 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEfVGDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLG-VVQTYLSARIGqGVMYDLRVQLYAHLQRMSLAFFTRTR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTED--------TSTLSDSLSENLSLFLwylvrglcLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18550 95 TGEIQSRLNNDvggaqsvvTGTLTSVVSNVVTLVA--------TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSA--MPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAyavNSWTTSISGMLLKVG---IL 427
Cdd:cd18550 167 TREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALA---GRWFFAALGLFTAIGpalVY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 428 YIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18550 244 WVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion ... |
502-725 |
4.70e-20 |
|
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 224044 [Multi-domain] Cd Length: 257 Bit Score: 90.45 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGkplpqyeHRYLHRQV 581
Cdd:COG1119 31 LIELKNVSVRRNGKK---ILGDLSWQVNPGEHWAIVGPNGAGKTTLLSLLTGEHPPSSGDVTLLG-------RRFGKGET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aavgqepqvfGRSLQENIAY-----GLTQKP--TMEEItaaaVKSGAHSFISGLPQGYD----------TEVGEAGS--- 641
Cdd:COG1119 101 ----------IFELRKRIGLvsselHERFRVreTVRDV----VLSGFFASIGIYQEDLTaedlaaaqwlLELLGAKHlad 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 ----QLSGGQRQAVALARALIRKPCVLILDDATSALD--ANSQLqVEQLLYESPELYSRSVLLITQHlslVEQA----DH 711
Cdd:COG1119 167 rpfgSLSQGEQRRVLIARALVKDPELLILDEPAQGLDliAREQL-LNRLEELAASPGAPALLFVTHH---AEEIppcfTH 242
|
250
....*....|....
gi 2468698279 712 ILFLEGGTIREGGT 725
Cdd:COG1119 243 RLLLKEGEVVAQGK 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
507-681 |
5.35e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHR---YLHRQVAA 583
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSgAHSFISGlpQGYDTEVGEAgsqLSGGQRQAVALARALIRKP 661
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDA--QHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
|
170 180
....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQV 681
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQM 175
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
509-720 |
5.52e-20 |
|
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: 89.70 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKpLPqYEHR--YLHRQVAAVGQ 586
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VP-WKRRkkFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVF-------GRSLQENIaYGLTQ---KPTMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARA 656
Cdd:cd03267 103 KTQLWwdlpvidSFYLLAAI-YDLPParfKKRLDELSELL----------DLEELLDTPV----RQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
499-724 |
8.48e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSR--SVLLITQHLSL-VEQADHILFL-EGGTIREGG 724
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD---RLHNQgkTVIVATHDVDLaAEWADQVIVLkEGRVLAEGD 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
503-720 |
1.25e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.48 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTEGQLLLDGKPLpqyeHRYL 577
Cdd:cd03234 4 LPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR----KPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVFGRSL--QENIAYGLTQKptMEEITAAAVKSgAHSFISGLPQGYDTEVGEAG-SQLSGGQRQAVALA 654
Cdd:cd03234 79 FQKCVAYVRQDDILLPGLtvRETLTYTAILR--LPRKSSDAIRK-KRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR--SVLLITQHL---SLVEQADHILFLEGGTI 720
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQ----LARrnRIVILTIHQprsDLFRLFDRILLLSSGEI 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
495-720 |
1.26e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGlvqfqdVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY-- 572
Cdd:PRK11247 11 TPLLLNA------VSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHrqvaavgQEPQVFG-RSLQENIAYGLTQ--KPTMEEITAAAvksgahsfisglpqGYDTEVGEAGSQLSGGQRQ 649
Cdd:PRK11247 82 DTRLMF-------QDARLLPwKKVIDNVGLGLKGqwRDAALQALAAV--------------GLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
502-720 |
1.49e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQYEHR-- 575
Cdd:PRK15439 11 LLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 -YLhrqvaaVGQEPQVF-GRSLQENIAYGLTQKP-TMEEITAAAVKSGAHsfisglpqgYDTEVgEAGSqLSGGQRQAVA 652
Cdd:PRK15439 88 iYL------VPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS-SAGS-LEVADRQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 653 LARALIRKPCVLILDDATSALdanSQLQVEQLLYESPELYSRSV--LLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
505-733 |
1.91e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 505 FQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP----QYEHRYLH 578
Cdd:PRK13634 5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYDTEvgeAGSQLSGGQRQAVALA 654
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG----PMNFGVSEEDAKQKAREMIElvGLPEELLAR---SPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
495-724 |
2.03e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.59 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEh 574
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 rylhrqvAAVGQEPQVFGRslqENIA-----YGLTQK---PTMEEItaaavksgaHSFiSGLPQGYDTEVGEagsqLSGG 646
Cdd:cd03220 91 -------LGGGFNPELTGR---ENIYlngrlLGLSRKeidEKIDEI---------IEF-SELGDFIDLPVKT----YSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
206-487 |
4.26e-19 |
|
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: 88.66 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 206 FFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHL----QGEVFGAVLRQETEFFQQ--N 279
Cdd:cd18578 30 ILFSKLIS-VFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLtrrlRKLAFRAILRQDIAWFDDpeN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLGI-MLWGSVS---LTMVTLVTLPLLFLLPKKVGKWYQLLEVQ 355
Cdd:cd18578 109 STGALTSRLSTDASDVRGLVGDRLGL----ILQAIVTLVAgLIIAFVYgwkLALVGLATVPLLLLAGYLRMRLLSGFEEK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 356 VRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISgMLLKVGILYIGGQLV 434
Cdd:cd18578 185 NKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgFGLSQSLT-FFAYALAFWYGGRLV 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTfVLYQMQFT-QAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPR 487
Cdd:cd18578 264 ANGEYTFEQFFI-VFMALIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
520-731 |
4.39e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226961 [Multi-domain] Cd Length: 256 Bit Score: 87.48 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 586
Cdd:COG4598 21 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSAGSIRVNGeeirlkrdkdgqlKPADKRQLQRLRTRLGMVFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFG-RSLQENI------AYGLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIR 659
Cdd:COG4598 101 HFNLWShMTVLENVieapvhVLGVSKAEAIERAEKYLAKVGIAEKADAYP-----------AHLSGGQQQRVAIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 660 KPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4598 170 EPEVMLFDEPTSALDpelVGEVLKVMQDLAEE----GRTMVVVTHEMGFARDvSSHVIFLHQGKIEEEGPPEQVFG 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
516-719 |
4.40e-19 |
|
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: 86.62 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLL-------LDGKPLPQYEHRYlhrQVAAVGQEP 588
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRY---SVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVFGRSLQENIAYGltqKPTMEEITAAAVKSGA-HSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:cd03290 89 WLLNATVEENITFG---SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 668 DATSALDAN-----SQLQVEQLLYESpelySRSVLLITQHLSLVEQADHILFLEGGT 719
Cdd:cd03290 166 DPFSALDIHlsdhlMQEGILKFLQDD----KRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
484-731 |
5.46e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.53 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 484 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNrpdvlvlqgltftlrpGEVTALVGPNGSGKSTvaaLLQNL---YQPTEG 560
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSLlsqFEISEG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 561 QLLLDgkplpqyehrylhRQVAAVGQEPQVFGRSLQENIaygLTQKPTMEEITAAAVK-SGAHSFISGLPQGYDTEVGEA 639
Cdd:PTZ00243 716 RVWAE-------------RSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVRvSQLEADLAQLGGGLETEIGEK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 GSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN-SQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGA--LAGKTRVLATHQVHVVPRADYVVALGDG 857
|
250
....*....|...
gi 2468698279 719 TIREGGTHQQLME 731
Cdd:PTZ00243 858 RVEFSGSSADFMR 870
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
502-700 |
9.46e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEhrylhR 579
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAaVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKsgahsfisglpqgydtEVGEAGS------QLSGGQRQ 649
Cdd:PRK11248 73 GVV-FQNEGLLPWRNVQDNVAFGLqlagVEKMQRLEIAHQMLK----------------KVGLEGAekryiwQLSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
503-733 |
1.20e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPN-RP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQYEHRY 576
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAVAL 653
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 2468698279 733 K 733
Cdd:PRK13646 237 K 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
514-723 |
1.35e-18 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 226617 [Multi-domain] Cd Length: 209 Bit Score: 85.04 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR 593
Cdd:COG4133 11 ERGERTLFSDLSFTLNAGEALQITGPNGAGKTTLLRILAGLLRPDAGEVYWQGEPIQNVRESY-HQALLYLGHQPGIKTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENIAY--GLTQKPTMEEITAAAVKSGAHSFIsglpqgyDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:COG4133 90 lTALENLHFwqRFHGSGNAATIWEALAQVGLAGLE-------DLPVG----QLSAGQQRRVALARLWLSPAPLWILDEPF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 671 SALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREG 723
Cdd:COG4133 159 TALDKEGVALLTALMAA--HAAQGGIVLLTTHQPLPIASAQIRRLDLTATKAT 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
512-731 |
1.65e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 512 YPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQV 590
Cdd:cd03218 10 YGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYdtevgeaGSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03218 87 FRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 669 ATSALDANSQLQVEQLLYespELYSRSV-LLITQH-----LSLVEQAdHILFleGGTIREGGTHQQLME 731
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIK---ILKDRGIgVLITDHnvretLSITDRA-YIIY--EGKVLAEGTPEEIAA 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
517-729 |
2.08e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 84.73 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQVAAVGQEPQVfGRSLQ 596
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 --ENIA-----YGLTQKPTMEEITAAAvksgahSFIsglpqgydtEVGEAGSQL----SGGQRQAVALARALIRKPCVLI 665
Cdd:cd03265 90 gwENLYiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
515-685 |
3.52e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY--GLTQKPTMEEITAAAVKsgahsfisglpqgydteVGEAG------SQLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK13538 90 TALENLRFyqRLHGPGDDEALWEALAQ-----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|
gi 2468698279 666 LDDATSALDANSQLQVEQLL 685
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALL 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
515-678 |
3.94e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YL-HRQvaavGQEPQ 589
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 VfgrSLQENIA-----YGltQKPTMEEITAAAVKSGAhsfISGLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK13539 88 L---TVAENLEfwaafLG--GEELDIAAALEAVGLAP---LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....
gi 2468698279 665 ILDDATSALDANSQ 678
Cdd:PRK13539 150 ILDEPTAALDAAAV 163
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
520-685 |
4.30e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 I----AYGLTQKPTMEEITAAAvksgahsfisGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:TIGR01189 94 LhfwaAIHGGAQRTIEDALAAV----------GLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|.
gi 2468698279 675 ANSQLQVEQLL 685
Cdd:TIGR01189 160 KAGVALLAGLL 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
502-729 |
5.20e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TEGQLLLDGKPLPQYEHR 575
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgea 639
Cdd:PRK15134 85 TLRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYPH--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:PRK15134 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 2468698279 719 TIREGGTHQQL 729
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
515-712 |
7.52e-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: 82.54 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY--GLTQKPTMEEITAAAVKSGAHSFISGlpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03231 89 SVLENLRFwhADHSDEQVEEALARVGLNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468698279 672 ALDANSQLQVEQLLyeSPELYSRSVLLITQHLSLVEQADHI 712
Cdd:cd03231 155 ALDKAGVARFAEAM--AGHCARGGMVVLTTHQDLGLSEAGA 193
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
503-675 |
1.13e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.28 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQE----PQVfgrSLQENIAYGL----TQKPTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:PRK11650 80 MVFQNyalyPHM---SVRENMAYGLkirgMPKAEIEErVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAM 145
|
170 180
....*....|....*....|..
gi 2468698279 654 ARALIRKPCVLILDDATSALDA 675
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-731 |
1.14e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQLLLDGKPL--PQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 R-SLQENIAYGL------TQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK14267 99 HlTIYDNVAIGVklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-478 |
1.34e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 83.74 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQD-GSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG---------HVHSHLQgevfgavlRQE 272
Cdd:cd18778 17 VPPWLIRELVDLVTIGsKSLGLLLGLALLLLGAYLLRALLNFL-RIYLNHVAEqkvvadlrsDLYDKLQ--------RLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 273 TEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKE----AVAYAVNSWTTSIsGMLLkvgILY 428
Cdd:cd18778 168 YRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAmklwAIFHPLMEFLTSL-GTVL---VLG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18778 244 FGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| YufO |
COG3845 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-718 |
2.24e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226364 [Multi-domain] Cd Length: 501 Bit Score: 85.67 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PqyehrylhRQVAAVG-----Q 586
Cdd:COG3845 15 PGVVANDDVSLSVKKGEIHALLGENGAGKSTLMKILFGLYQPDSGEIRVDGKEVriksP--------RDAIRLGigmvhQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVL 664
Cdd:COG3845 87 HFMLVPTlTVAENIILGLePSKGGLIDRRQARARIKELSERYGLPVDPDAKVAD----LSVGEQQRVEILKALYRGARLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 665 ILDDATSALdanSQLQVEQLLYESPELYS--RSVLLITQHLSLV-EQADHILFLEGG 718
Cdd:COG3845 163 ILDEPTAVL---TPQEADELFEILRRLAAegKTIIFITHKLKEVmAIADRVTVLRRG 216
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
520-687 |
2.99e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYG-LTQKPTM-------EEITAAAVKSGAHSFISGlpQGYDTevgeagsqLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:PRK10253 102 VARGrYPHQPLFtrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170
....*....|....*..
gi 2468698279 671 SALDANSQLQVEQLLYE 687
Cdd:PRK10253 172 TWLDISHQIDLLELLSE 188
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
520-729 |
3.12e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YLHRQVAAVGQepqvFGRSL 595
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 Q-----ENIAYGL---TQKPtmeeitaAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11629 100 PdftalENVAMPLligKKKP-------AEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 668 DATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILfleggTIREGGTHQQL 729
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-----EMRDGRLTAEL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
516-684 |
4.02e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlpqyeHRY------LHRQVAAVGQEPQ 589
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 -VFGRSLQENIAYGltQKPT-MEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11288 90 lVPEMTVAENLYLG--QLPHkGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170
....*....|....*..
gi 2468698279 668 DATSALdanSQLQVEQL 684
Cdd:PRK11288 166 EPTSSL---SAREIEQL 179
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
520-720 |
4.67e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 224026 [Multi-domain] Cd Length: 263 Bit Score: 81.60 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHrqVAAVGQEPQ--VFGR-S 594
Cdd:COG1101 21 ALNGLSLEIAEGDFVTVIGSNGAGKSTLLNAIAGDLKPTSGQILIDGVDVTKKsvAKRANL--LARVFQDPLagTAPElT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIAYGLtQKPTMEEITAAAVKSGAHSF---ISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:COG1101 99 IEENLALAE-SRGKKRGLSSALNERRRSSFrerLARLGLGLENRLSDRIGLLSGGQRQALSLLMATLHPPKILLLDEHTA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 672 ALDANSQLQVEQLLYESPELYSRSVLLITQHLslvEQA----DHILFLEGGTI 720
Cdd:COG1101 178 ALDPKTAEFVMELTAKIVEEHKLTTLMVTHNM---EDAldygNRLIMLHSGKI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
520-731 |
7.49e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224060 [Multi-domain] Cd Length: 243 Bit Score: 80.71 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQyeHRYLHRQVAAVGQEPQVFGR-SL 595
Cdd:COG1137 19 VVNDVSLEVNSGEIVGLLGPNGAGKTTTFYMIVGLVRPDSGKILLDDEditKLPM--HKRARLGIGYLPQEASIFRKlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGL--TQKPTMEEITAAAVKSGAHSF-ISGLpqgydteVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG1137 97 EDNIMAVLeiREKDLKKAERKEELDALLEEFhITHL-------RDSKAYSLSGGERRRVEIARALAANPKFILLDEPFAG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 673 LDANSQLQVEQLLyesPELYSRSV-LLITQH-----LSLVEQAdHILFleGGTIREGGTHQQLME 731
Cdd:COG1137 170 VDPIAVIDIQRII---KHLKDRGIgVLITDHnvretLDICDRA-YIIS--DGKVLAEGSPEEIVN 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
503-725 |
7.70e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHRYLH 578
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHsfISGLPqgYDTEVGEAGSQLSGGQRQAVALARA 656
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMN--IVGLD--YEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 657 LIRKPCVLILDDATSALDANSQlqvEQLLYESPEL---YSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGR---DEILNKIKELhkeYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
503-718 |
9.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRPdvLVLQGLT---FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYL 577
Cdd:PRK13641 3 IKFENVDYIYsPGTP--MEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 ---HRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAV 651
Cdd:PRK13641 81 kklRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLSLV-EQADHILFLEGG 718
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD----YQKaghTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
525-730 |
1.12e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY---EHRYLHRQ-VAAVGQEPQVFGR-SLQENI 599
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGL-----TQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:PRK10070 128 AFGMelagiNAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 675 ANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
503-717 |
1.59e-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: 77.58 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVA 582
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYgltqkPTMEEitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 663 VLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:cd03223 112 FVFLDEATSALDE----ESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
520-736 |
1.72e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223473 [Multi-domain] Cd Length: 251 Bit Score: 79.93 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGKP---LPQYEHrylhrqvAAVG-----QEP- 588
Cdd:COG0396 19 ILKGVNLTVKEGEVHAIMGPNGSGKSTLAYTIMGHpkYEVTEGEILFDGEDileLSPDER-------ARAGiflafQYPv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVFGRSLQENIAYGLTQKPTMEEITAAA---VKSGAHSFisGLPQGY-DTEVGEAgsqLSGGQRQAVALARALIRKPCVL 664
Cdd:COG0396 92 EIPGVTNSDFLRAAMNARRGARGILPEFikeLKEKAELL--GLDEEFlERYVNEG---FSGGEKKRNEILQLLLLEPKLA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 665 ILDDATSALDANSQLQVEQLL--YESPElysRSVLLITQHLSLVE--QADHILFLEGGTI-REGGTHQQLMEKKGCY 736
Cdd:COG0396 167 ILDEPDSGLDIDALKIVAEGInaLREEG---RGVLIITHYQRLLDyiKPDKVHVLYDGRIvKSGDPELAEELEEKGY 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-715 |
1.79e-16 |
|
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: 79.43 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEhrylhRQVaaVGQEPQVFG-RSLQE 597
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItePGPD-----RMV--VFQNYSLLPwLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGLTQ-KPTMEEITAAAVKSgAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVE-EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468698279 677 SQLQVEQLLYESPELYSRSVLLITQHLslveqaDHILFL 715
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDV------DEALLL 181
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
265-449 |
2.15e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 80.28 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 265 FGAVLRQETEFFQQNQTGNITSRVTEDT----STLSDSLSENLSLFLwyLVRGLC--LLGImlwgSVSLTMVTLVTLPLL 338
Cdd:cd18574 82 FSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVT--QTVGCVvsLYLI----SPKLTLLLLVIVPVV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 339 FLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-----Nsw 413
Cdd:cd18574 156 VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIfqglsN-- 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 2468698279 414 tTSISGMLLkvGILYIGGQLVTSGAVSSGNLVTFVL 449
Cdd:cd18574 234 -LALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
500-729 |
2.63e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQD--VSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQLLLDGKPLPQYEH 574
Cdd:PRK09473 10 DALLDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RYLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAA--AVK-SGAHSFISGLPQgydtevge 638
Cdd:PRK09473 89 KELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEESVRMldAVKmPEARKRMKMYPH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 639 agsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:PRK09473 161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYA 237
|
250
....*....|..
gi 2468698279 718 GTIREGGTHQQL 729
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
503-733 |
3.75e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.40 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY----EHRY 576
Cdd:PRK13649 3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkP-----TMEEITAAAVKSGAHSFISglpqgyDTEVGEAGSQLSGGQRQ 649
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPELYSRSVLLITqHL--SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVT-HLmdDVANYADFVYVLEKGKLVLSGKPK 230
|
250
....*....|..
gi 2468698279 728 Q------LMEKK 733
Cdd:PRK13649 231 DifqdvdFLEEK 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
515-729 |
4.72e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehRYLHRQV------------- 581
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRQVielseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 ------AAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPQgydtevgeags 641
Cdd:PRK10261 101 vrgadmAMIFQEPMtslnpVFtvGEQIAESIR--LHQGASREEAMVEAKRmldqvriPEAQTILSRYPH----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 2468698279 721 REGGTHQQL 729
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
201-470 |
5.32e-16 |
|
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: 79.03 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGiYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTY-WGHVMGaRIETDMRRDLFEHLQKLSFSFFDNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDsLS----ENLslflwyLVRGLCLLG---IMLWGSVSLTMVTLVT----LPLLFLLPKKVGKW 348
Cdd:cd18549 97 KTGQLMSRITNDLFDISE-LAhhgpEDL------FISIITIIGsfiILLTINVPLTLIVFALlplmIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 YQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGM---LLKV 424
Cdd:cd18549 170 FR----RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK---AYKAMAYFFSGMNFftnLLNL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQK 470
Cdd:cd18549 242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
503-717 |
6.89e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 226646 [Multi-domain] Cd Length: 604 Bit Score: 81.59 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLvLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVA 582
Cdd:COG4178 393 ITLENLSLRTPDG-QTL-LSELNFEVRPGERLLITGESGAGKTSLLRALAGLWPWGSGRI-----------SMPADSALL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAY-GLTQKPTMEEITAAAVKSGAHSFISGLpqgydTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:COG4178 460 FLPQRPYLPQGTLREALCYpNAAPDFSDAELVAVLHKVGLGDLAERL-----DEEDRWDRVLSGGEQQRLAFARLLLHKP 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:COG4178 535 KWVFLDEATSALDEETEDRLYQLLKE--ELPDATVISVGHRPTLWNFHSRQLELLD 588
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
520-720 |
7.45e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 75.93 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFG----RS 594
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKREGlvldLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIAygltqkptmeeitaaavksgahsfisglpqgydtevgeAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03215 95 VAENIA--------------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468698279 675 ANSQLQVEQLLYESPElYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:cd03215 137 VGAKAEIYRLIRELAD-AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-733 |
1.18e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEG-----QLLLDGKPLPQYEHRY-LHRQVAAVGQEPQVFGR 593
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 674 DANSQLQVEQLLYESPElySRSVLLITQHLSlveQADHI-----LFLEGGTIREGGTHQQLMEKK 733
Cdd:PRK14271 195 DPTTTEKIEEFIRSLAD--RLTVIIVTHNLA---QAARIsdraaLFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
505-722 |
1.36e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.40 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 505 FQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQ-VAA 583
Cdd:PRK10522 325 LRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKlFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRSLqeniaygltqKPTMEEITAAAVKsgahSFISGLPQGYDTEVGE---AGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10522 402 VFTDFHLFDQLL----------GPEGKPANPALVE----KWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 661 PCVLILDDAtsALDANSQLQVE---QLLyesPELYS--RSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PRK10522 468 RDILLLDEW--AADQDPHFRREfyqVLL---PLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
502-720 |
1.83e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhrq 580
Cdd:PRK10535 4 LLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 vAAVGQEPqvFGRSLQEniaYGLTQKPTME---EITA-------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQA 650
Cdd:PRK10535 81 -AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAvyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
202-471 |
2.55e-15 |
|
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: 77.10 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYI-RSYLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTeDTSTLSDSLSEN-LSLFLWYLVrGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQllevQ 355
Cdd:cd18570 98 TGEIISRFN-DANKIREAISSTtISLFLDLLM-VIISGIILFFYNWKLFLITLLIiplyILIILLFNKPFKKKNR----E 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 356 VRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVT 435
Cdd:cd18570 172 VMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVI 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 2468698279 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:cd18570 252 KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
501-713 |
2.72e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 226620 [Multi-domain] Cd Length: 213 Bit Score: 75.25 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT---EGQLLLDGKPLPQY-EHRy 576
Cdd:COG4136 1 GMLCLKNVSLRLPGS---CLLANVNFTIAKGEIVTLMGPSGCGKSTLLSWMIGALAGQfscTGELWLNEQRLDMLpAAQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lhRQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEE----ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:COG4136 77 --RQIGILFQDALLFPHlSVGQNLLFALPATLKGNArrnaANAALERSGLDGAFHQDPA-----------TLSGGQRARV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:COG4136 144 ALLRALLAQPKALLLDEPFSRLDVALRDQFRQWVFSEVRAAGIPTVQVTHDLQDVPAGSRVI 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
520-733 |
2.91e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 226635 [Multi-domain] Cd Length: 242 Bit Score: 76.03 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH------RYLHRQVAAVGQEPQVFGR 593
Cdd:COG4161 17 ALFDITLDCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkaiRDLRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENI------AYGLTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCVLIL 666
Cdd:COG4161 97 lTVQENLieapcrVLGLSKDQALARAEKLLKRLRLKPYADRYPL-----------HLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVlLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:COG4161 166 DEPTAALDPEITAQIVSIIKELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDASCFTEPQ 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
520-730 |
3.71e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENI------AYGLTQKPTMEEitaaAVKSGAHSFISGLPQGydtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 660 KPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10619 170 EPEVLLFDEPTSALDpelVGEVLRIMQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
502-715 |
3.79e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK09544 4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAvgqePQVFGRSLQeniaygLTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:PRK09544 81 TL----PLTVNRFLR------LRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFL 715
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
251-730 |
4.06e-15 |
|
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: 79.95 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 251 NTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSenLSLF----LWYLVRG-LCLLGIMLWGSV 325
Cdd:TIGR01271 951 HTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP--LTLFdfiqLTLIVLGaIFVVSVLQPYIF 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 326 SLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSsqvAIEALSAMPTVRSFANeegeaQKFREKLQEiKTLNQKEA 405
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH---LITSLKGLWTIRAFGR-----QSYFETLFH-KALNLHTA 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 406 VAYAvnsWTTSISGMLLKVGILY-----------IGGQLVTSGAVssGNLVTFVLYQMQFTQAVeVLLSIypRVQKAVGS 474
Cdd:TIGR01271 1100 NWFL---YLSTLRWFQMRIDIIFvfffiavtfiaIGTNQDGEGEV--GIILTLAMNILSTLQWA-VNSSI--DVDGLMRS 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 475 SEKIFEYLDRTPRCP-PSGLLTPLHL-----------------EGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTAL 536
Cdd:TIGR01271 1172 VSRVFKFIDLPQEEPrPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGL 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 537 VGPNGSGKSTV-AALLQNLyqPTEGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSLQENI-AYgltQKPTMEE 611
Cdd:TIGR01271 1251 LGRTGSGKSTLlSALLRLL--STEGEIQIDGV---SWNSVTLQTWRKAFGVIPQkvfIFSGTFRKNLdPY---EQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 612 ITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpel 691
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS--- 1399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2468698279 692 YSRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:TIGR01271 1400 FSNCTVILSEHrVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
521-723 |
4.12e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 227019 [Multi-domain] Cd Length: 249 Bit Score: 75.83 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK----PLPqyEHRYLHRQVAAVGQEPQVF-GRSL 595
Cdd:COG4674 21 LNDLSFSVDPGELRVLIGPNGAGKTTLMDVITGKTRPQEGEVLFDGDtdltKLP--EHRIARAGIGRKFQKPTVFeNLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQ--GYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:COG4674 99 RENLELALNRDKSVFASLFARLRAEERRRIDELLAtiGLGDERDRLAALLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 674 DANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFL-EGGTIREG 723
Cdd:COG4674 179 TDAETEKTAELLKSLAG--KHSILVVEHDMGFVREiADKVTVLhEGSVLAEG 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
516-724 |
4.14e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTEGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVF 591
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 GRSLQENIAYGL-----TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK10418 92 FNPLHTMHTHARetclaLGKPADDATLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
520-727 |
4.37e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.44 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------KPLPQyEHRYLHRQVAAVGQepqvfg 592
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDK-AIRELRRNVGMVFQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 rslQENIAYGLTqkpTMEEITAAAVKsgahsfISGLPQgyDTEVGEAGS----------------QLSGGQRQAVALARA 656
Cdd:PRK11124 90 ---QYNLWPHLT---VQQNLIEAPCR------VLGLSK--DQALARAEKllerlrlkpyadrfplHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVlLITQHLSLVEQ-ADHILFLEGGTIREGGTHQ 727
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
431-731 |
4.58e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 431 GQLVTSGAVSSgnlvTFVLYQMQFTQAvevLLSIYPRVQKAVGSS-EKIFEYL---DRTPRCPPSGLLTPLHLEGLVQFQ 506
Cdd:PRK10261 245 GEAVETGSVEQ----IFHAPQHPYTRA---LLAAVPQLGAMKGLDyPRRFPLIsleHPAKQEPPIEQDTVVDGEPILQVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHR 575
Cdd:PRK10261 318 NLVTRFPLRSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEP-------QVFGRSLQENI-AYGLTQKPTMEEITAAAVKSgahsfISGLPQgydtEVGEAGSQLSGGQ 647
Cdd:PRK10261 398 ALRRDIQFIFQDPyasldprQTVGDSIMEPLrVHGLLPGKAAAARVAWLLER-----VGLLPE----HAWRYPHEFSGGQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADH---ILFLegGTIREGG 724
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvaVMYL--GQIVEIG 546
|
....*..
gi 2468698279 725 THQQLME 731
Cdd:PRK10261 547 PRRAVFE 553
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
520-722 |
4.59e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHRqVAAVGQEPQVF----GR 593
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLR-AKHVGFVFQSFmlipTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK10584 104 NALENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
520-733 |
5.71e-15 |
|
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: 79.18 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGLTqkptMEEITAAAVKSGAH--SFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:TIGR01271 508 IFGLS----YDEYRYTSVIKACQleEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 678 qLQVEQLLYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:TIGR01271 581 -VVTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
260-722 |
6.86e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 226968 [Multi-domain] Cd Length: 546 Bit Score: 78.30 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 260 LQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSL------------FLWYL---VRGLCLLGIML--W 322
Cdd:COG4615 83 LRSEFIKKILDTPLERIERLGSARLLAGLTSDVRNISFAFSRLPELvqaiiltlgsaaYLAYLspkMFLLTVVWIVVtiW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 323 GSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLakssqvaieaLSAMPTVRSFANE-EGEAQKFREKLQEIKTLN 401
Cdd:COG4615 163 GGFVLMARVYKHMAAARETEDKLQNDYQTILEGRKELT----------LNRERAEYVHNNLyIPDAQEYRHHIIRANTFH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 402 QkeavayAVNSWTTSIsgMLLKVGI-LYIGGQLvtsGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIfE 480
Cdd:COG4615 233 L------LAVNWSNIM--LLGLIGLvFWLALSL---GWASTNVAATIVLVLLFLRTPLLSAVGILPTLLTAQVAFNKI-A 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 481 YLDRTPrcPPSGLLTPLHLEGL--VQFQDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:COG4615 301 KLELAP--YKADFPRPQAFPDWktLELRNVRFAYQ--DNAFHVGPINLTIKRGELVFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPL-PQYEHRYlhRQV-AAVGQEPQVFGRSLqeniayGLTQKPTMEEITAaavksgahsFISGLPQGYDTEV 636
Cdd:COG4615 377 SGEILLDGKPVsAEQLEDY--RKLfSAVFSDYHLFDQLL------GPEGKASPQLIEK---------WLQRLELAHKTSL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GE---AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:COG4615 440 NDgrfSNLKLSTGQKKRLALLLALLEERDILVLDEWAADQDPAFRREFYQVLLPLLKEQGKTIFAISHDDHYFIHADRLL 519
|
....*....
gi 2468698279 714 FLEGGTIRE 722
Cdd:COG4615 520 EMRNGQLSE 528
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-684 |
6.94e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFGR- 593
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYG--LTQK---------PTMEEITAAAVKsgahsfISGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPC 662
Cdd:PRK09700 96 TVLENLYIGrhLTKKvcgvniidwREMRVRAAMMLL------RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180
....*....|....*....|..
gi 2468698279 663 VLILDDATSALdanSQLQVEQL 684
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYL 184
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
520-733 |
7.05e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQ---LLLDGKPLPQYEH---------------------R 575
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYdteVGEAGSQLSGGQRQAV 651
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY---LQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYS--RSVLLITQHL-SLVEQADHILFL-EGGTIREGGTHQ 727
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD---NLNKqgKTIILVTHDLdNVLEWTKRTIFFkDGKIIKDGDTYD 251
|
....*.
gi 2468698279 728 QLMEKK 733
Cdd:PRK13651 252 ILSDNK 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
520-735 |
1.68e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.56 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGK---PLPQYEhrylhrqvaavgqepqvfgRS 594
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEE-------------------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQeniayGLT---QKPtmEEITAAAVKsgahSFISGLPQGydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03217 76 RL-----GIFlafQYP--PEIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 672 ALDANS----QLQVEQLLYEspelySRSVLLITQHLSLVE--QADHILFLEGGTIREGGTHQ--QLMEKKGC 735
Cdd:cd03217 134 GLDIDAlrlvAEVINKLREE-----GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
523-729 |
1.80e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 523 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPQVfgrSLQ--- 596
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLA---SLNprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ---ENIAYGL-TQKPTM------EEITAAAVKSGahsFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK15079 116 tigEIIAEPLrTYHPKLsrqevkDRVKAMMLKVG---LLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
509-718 |
2.83e-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: 72.30 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL---YQPTEGQLLLDGKPLPQYEHRYlHRQVAAVG 585
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEpqvfgrslQENIAYgLTQKPTMEeitaAAVKSGAHSFISGlpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03233 90 EE--------DVHFPT-LTVRETLD----FALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 666 LDDATSALDANSQLQVEQLLYE-SPELYSRSVLLITQ-HLSLVEQADHILFLEGG 718
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTmADVLKTTTFVSLYQaSDEIYDLFDKVLVLYEG 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
520-729 |
3.22e-14 |
|
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: 73.74 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGLT--QKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:cd03291 119 IFGVSydEYRYKSVVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 678 qLQVEQLLYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:cd03291 192 -VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
526-724 |
3.89e-14 |
|
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226628 [Multi-domain] Cd Length: 352 Bit Score: 74.30 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-------HRylhRQVAAVGQEPQVFGR-SLQE 597
Cdd:COG4148 19 FTLPARGITALFGPSGSGKTSLINMIAGLTRPDEGRIELNGRVLVDAEkgiflppEK---RRIGYVFQDARLFPHyTVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGL--TQKPTMEEITAAAvksGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:COG4148 96 NLRYGMwkSMRAQFDQLVALL---GIEHLLDRYP-----------GTLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 676 NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:COG4148 162 PRKREILPYLERLRDEINIPILYVSHSLDEVLRlADRVVVLENGKVKASG 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-685 |
4.24e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPT---EGQLLLDGKPLPQYEHRYLHRQ-VAAVGQE---- 587
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQElalv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 588 PQVfgrSLQENIAYGltqkptmEEITA------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK13549 95 KEL---SVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180
....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANsqlQVEQLL 685
Cdd:PRK13549 163 RLLILDEPTASLTES---ETAVLL 183
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
502-731 |
8.90e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226963 [Multi-domain] Cd Length: 252 Bit Score: 71.95 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG4604 1 MITIENVSKSYGTKV---VLDDVSLDIPKGGITSIIGPNGAGKSTLLSMMSRLLKKDSGEITIDGLELTSTPSKELAKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQV-----------FGRslqeniaYGLTQ-KPTME--EITAAAVKsgaHSFISGLPQGYDTEvgeagsqLSGGQ 647
Cdd:COG4604 78 SILKQENHInsrltvrdlvgFGR-------FPYSQgRLTKEdrRIINEAIE---YLHLEDLSDRYLDE-------LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTH 726
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQIMKILRRLADELGKTIVVVLHDINFASCySDHIVALKNGKVVKQGSP 220
|
....*
gi 2468698279 727 QQLME 731
Cdd:COG4604 221 DEIIQ 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
520-747 |
1.30e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTE-------GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSLQENIAYGltQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARAL---------IRKP 661
Cdd:PRK13547 96 FAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK---KGCYW 737
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPahiARCYG 253
|
250
....*....|...
gi 2468698279 738 ---AMVQAPADAP 747
Cdd:PRK13547 254 favRLVDAGDGVP 266
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
520-733 |
1.73e-13 |
|
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: 71.42 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTEGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSL 595
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGV---SWNSVPLQKWRKAFGVIPQkvfIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03289 94 RKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 675 ANSQLQVEQLLYESpelYSRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:cd03289 171 PITYQVIRKTLKQA---FADCTVILSEHrIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
507-732 |
2.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ-----YEHRYLHR 579
Cdd:PRK13645 11 NVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGltqkptmeEITAAAVKSGAHSFIS------GLPQGYdteVGEAGSQLSGGQRQAV 651
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFG--------PVNLGENKQEAYKKVPellklvQLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL-EGGTIREGG----- 724
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMhEGKVISIGSpfeif 239
|
....*...
gi 2468698279 725 THQQLMEK 732
Cdd:PRK13645 240 SNQELLTK 247
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ... |
517-718 |
2.14e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226631 [Multi-domain] Cd Length: 300 Bit Score: 71.62 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyehrylhRQVAAVGQEPQvfgrslq 596
Cdd:COG4152 14 DKKAVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLSQ-------EIKNRIGYLPE------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 eniAYGLTQKPTMEEITAaavksgahsFISGLpQGYDT--------------EVGEAGS----QLSGGQRQAVALARALI 658
Cdd:COG4152 80 ---ERGLYPKMTVEDQLK---------YLAEL-KGMPKaeiqkklqawlerlEIVGKKTkkikELSKGNQQKIQFISAVI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:COG4152 147 HEPELLILDEPFSGLDPVNVELLKDAIFELKE-EGATIIFSSHRMEHVEElCDRLLMLKKG 206
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
202-478 |
5.00e-13 |
|
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: 70.53 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQD--GSADTFTRNLTLMS-----ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETE 274
Cdd:cd18554 16 LLLPLILKYIVDDVIQGssLTLDEKVYKLFTIIgimffIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQ--EIKTLNQKEAVAYAVNSWTTSIS-GMLLKVGilyIGG 431
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKTFSAVNTITDlAPLLVIG---FAA 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
503-724 |
6.77e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhR 579
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQE----PQVfgrSLQENIAYGLT-QKPTMEEI-----TAAAVKSGAHsFISGLPQGydtevgeagsqLSGGQRQ 649
Cdd:PRK11000 76 GVGMVFQSyalyPHL---SVAENMSFGLKlAGAKKEEInqrvnQVAEVLQLAH-LLDRKPKA-----------LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDAnsQLQVeQLLYESPELYSR--SVLLITQHlSLVEQ---ADHILFLEGGTIREGG 724
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDA--ALRV-QMRIEISRLHKRlgRTMIYVTH-DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms]; |
518-731 |
7.54e-13 |
|
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
Pssm-ID: 226639 [Multi-domain] Cd Length: 330 Bit Score: 70.26 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP----TEGQLLLDGKPL----PQYEHRYLHRQVAAVGQEPQ 589
Cdd:COG4170 20 VKAVDRVSMTLNEGEIRGLVGESGSGKSLIAKAICGVNKDnwrvTADRMRFDDIDLlrlsPRERRKLVGHNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 V-------FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFISglpQGYDTEVGEagsqlsgGQRQAV 651
Cdd:COG4170 100 ScldpserVGRQLIQNIPawtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDIM---RSYPYELTE-------GECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:COG4170 168 MIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLSRLNQNSNTTILLISHDLqMISQWADKINVLYCGQTVESAPSEELV 247
|
.
gi 2468698279 731 E 731
Cdd:COG4170 248 T 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
506-700 |
9.68e-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: 71.12 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQllldGKPLPQYEHRYLHrqvaavg 585
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----ARPQPGIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQ------VFG----------RSLQE----NIAYG---------LTQKPTMEEITAAAvksGAHSFISGL-------- 628
Cdd:TIGR03719 75 QEPQldptktVREnveegvaeikDALDRfneiSAKYAepdadfdklAAEQAELQEIIDAA---DAWDLDSQLeiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 629 -PQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT 700
Cdd:TIGR03719 152 cPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVT 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
517-725 |
1.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------------LLDGKPLPQYEHRY--LHRQ 580
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhELITNPYSKKIKNFkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLPQGYD-TEVGEAGsqLSGGQRQAVALARAL 657
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGT 725
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
502-713 |
1.25e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQ 580
Cdd:PRK11614 5 MLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYG--LTQKPTMEEITAAAVKSgahsfisgLPQGYDTEVGEAGSqLSGGQRQAVALARAL 657
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGgfFAERDQFQERIKWVYEL--------FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 658 IRKPCVLILDDATSAL---------DANSQLQ--------VEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLapiiiqqifDTIEQLReqgmtiflVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
515-729 |
1.38e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPT----EGQLLLDGKPLpqyEHRYLHRQVAAVgQEPQV 590
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPI---DAKEMRAISAYV-QQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSL--QENIAYGLTQKptMEEITAAAVKSGAHSFI---SGLPQGYDTEVGEAGSQ--LSGGQRQAVALARALIRKPCV 663
Cdd:TIGR00955 110 FIPTLtvREHLMFQAHLR--MPRRVTKKEKRERVDEVlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQL 729
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism]; |
521-730 |
1.58e-12 |
|
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism];
Pssm-ID: 226622 [Multi-domain] Cd Length: 248 Bit Score: 67.95 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQepqvfgrslQENia 600
Cdd:COG4138 15 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGSGSIQFAGQPLEAWSATELARHRAYLSQ---------QQT-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 yGLTQKPTMEEIT---AAAVKSGAHSFISGLpQGYDTEVGEAGSQLSGGQRQAVALARALIR-----KPC--VLILDDAT 670
Cdd:COG4138 83 -PPFAMPVWHYLTlhqPDKTRTELLNDVAGA-LALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpdaNPAgqLLLLDEPM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 671 SALDANSQLQVEQLLYESPElYSRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:COG4138 161 NSLDVAQQSALDRLLSALCQ-QGLAIVMSSHDLNhTLRHAHRAWLLKRGKLLASGRREEVL 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
524-730 |
2.04e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENIAYG 602
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 603 LTQKPTMEEItAAAVKSGAHSFisglpqGYDTEVGEAGSQLSGGQRQAVALARALIR-----KP--CVLILDDATSALDA 675
Cdd:PRK03695 94 QPDKTRTEAV-ASALNEVAEAL------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 676 NSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK03695 167 AQQAALDRLLSELCQQ-GIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
500-731 |
2.23e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAY--PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-LLDG-------KPL 569
Cdd:TIGR03269 277 EPIIKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewvdmtKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 570 PQYEHRyLHRQVAAVGQEPQVFG-RSLQENiaygLTQKPTMEEITAAAVKSGAHSFISGlpqGYDTEVGEA-----GSQL 643
Cdd:TIGR03269 357 PDGRGR-AKRYIGILHQEYDLYPhRTVLDN----LTEAIGLELPDELARMKAVITLKMV---GFDEEKAEEildkyPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIRE 722
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVK 508
|
....*....
gi 2468698279 723 GGTHQQLME 731
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
427-717 |
2.60e-12 |
|
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: 70.16 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 427 LYIGGQLVTSGAVSSGNLVTfVLYQMQ----FTQAVEVLLSIYPRVQK------AVGSSEKIFEYLDRTPRCPPSGLLtp 496
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLML-AGRDMTrlagFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVSFAYPNRpDVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLdgKPLPQyehry 576
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--KPAKG----- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lhrQVAAVGQEPQVFGRSLQENIAY----------GLTQKpTMEEITaAAVKSGahsFISGLPQGYDTeVGEAGSQLSGG 646
Cdd:TIGR00954 516 ---KLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDK-DLEQIL-DNVQLT---HILEREGGWSA-VQDWMDVLSGG 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALdansQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
233-478 |
2.85e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 68.31 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDgIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLV 311
Cdd:cd18564 62 GIALLRGLASYAGT-YLTALVGqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 312 RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFR 391
Cdd:cd18564 141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 392 EklQEIKTLnQKEAVAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRV 468
Cdd:cd18564 221 R--ENRKSL-RAGLRAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRI 297
|
250
....*....|
gi 2468698279 469 QKAVGSSEKI 478
Cdd:cd18564 298 AKASASAERV 307
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-732 |
2.89e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.83 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGKPLPQYEhrYLHRQvAAVGQEPQVFGRS 594
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCG--YVERP-SKVGEPCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIA--YGLTQKptmeeITAAAVKSGAHSF----------------ISGLPQ-GYDTE--VGEA-------------- 639
Cdd:TIGR03269 89 LEPEEVdfWNLSDK-----LRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEGKeaVGRAvdliemvqlshrit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 --GSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSvLLITQHLSLV--EQADHILFL 715
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS-MVLTSHWPEVieDLSDKAIWL 242
|
250
....*....|....*..
gi 2468698279 716 EGGTIREGGTHQQLMEK 732
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
230-478 |
5.94e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 67.21 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 230 LMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWY 309
Cdd:cd18565 59 LTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 310 LVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQ 388
Cdd:cd18565 139 VVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNARLE-NNLSGIAVIKAFTAEDFERE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 389 KFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAV------SSGNLVTFVLYQMQFTQAVE 459
Cdd:cd18565 218 RVADASEEYRDANWR---AIRLRAAFFPVIRLVAGAGfvaTFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLT 294
|
250
....*....|....*....
gi 2468698279 460 VLLSIYPRVQKAVGSSEKI 478
Cdd:cd18565 295 RLGDLIDQYQRAMASAKRV 313
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
530-702 |
8.60e-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: 63.55 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 530 PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLldgkplpqyehrylhrqvaavgqepqvfgrslqeniaygltqkptm 609
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 610 eeitaaaVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ-----LQVEQL 684
Cdd:smart00382 35 -------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRL 107
|
170
....*....|....*...
gi 2468698279 685 LYESPELYSRSVLLITQH 702
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
201-478 |
1.20e-11 |
|
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: 65.97 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMG----HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18543 15 GLAIPLLTRRAIDGPIAHGD----RSALWPLVLLLLALGVAEAVLSFLRRYLAGrlslGVEHDLRTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18543 91 DRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:cd18543 170 QDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVAN 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18543 250 GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
517-675 |
2.02e-11 |
|
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: 66.77 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQE-PQVFG 592
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQElTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGltqkptmEEITA-------AAVKSGAHSFISGLpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:TIGR02633 93 LSVAENIFLG-------NEITLpggrmayNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170
....*....|
gi 2468698279 666 LDDATSALDA 675
Cdd:TIGR02633 165 LDEPSSSLTE 174
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
202-478 |
2.02e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 65.59 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDgIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18546 16 LAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQT-RLTGRTGErLLYDLRLRVFAHLQRLSLDFHERET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLwylVRGLCLLGI---MLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQLLEV--- 354
Cdd:cd18546 95 SGRIMTRMTSDIDALSELLQTGLVQLV---VSLLTLVGIavvLLVLDPRLALVALAALPPLAL----ATRWFRRRSSray 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 -QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 433
Cdd:cd18546 168 rRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18546 248 VAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
483-731 |
3.46e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 224053 [Multi-domain] Cd Length: 500 Bit Score: 66.38 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 483 DRTPRCPPSGLLTP-LHLEGL---VQFQDVSFaypnrpdvlvlqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:COG1129 249 DLFPEPPEEGIGEPvLEVRNLsggGKVRDVSF----------------TVRAGEILGIAGLVGAGRTELARALFGARPAS 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQY-EHRYLHRQVAAVGQEPQ----VFGRSLQENIAYG-LTQKPTMEEITAAAVKSGAHSFISGL---P 629
Cdd:COG1129 313 SGEILLDGKPVRIRsPRDAIKAGIAYVPEDRKseglVLDMSIAENITLAsLRRFSRRGLIDRRKERALAERYIRRLrikT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 630 QGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLS-L 705
Cdd:COG1129 393 PSPEQPIGT----LSGGNQQKVVLARWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE----LAAegkAILMISSELPeL 464
|
250 260 270
....*....|....*....|....*....|.
gi 2468698279 706 VEQADHILFLEGGTI-----REGGTHQQLME 731
Cdd:COG1129 465 LGLSDRILVMREGRIvgeldREEATEEAIMA 495
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
203-478 |
3.59e-11 |
|
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: 64.50 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18568 100 DIITRFQE-NQKIRRFLTRSaLTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEegeaQKFREKLQE--IKTLNQ--KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:cd18568 178 EQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNTrfRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18568 254 QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| YufO |
COG3845 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
502-720 |
5.06e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 226364 [Multi-domain] Cd Length: 501 Bit Score: 65.64 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSfAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ- 580
Cdd:COG3845 257 VLEVEDLS-VKDRRG-VTAVKDVSFEVRAGEIVGIAGVAGNGQSELVEAISGLRKPASGRILLNGKDVLGRLSPRERRRl 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 -VAAVGQEPQ----VFGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgahsfisglpqgYDTEVGEAGS--- 641
Cdd:COG3845 335 gLAYVPEDRHghglVLDLSLAENLVlgrhdkkpfsrGGFLDRRAIRKFARELIEE------------FDVRAPSPDApar 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelySRS----VLLITQHL-SLVEQADHILFLE 716
Cdd:COG3845 403 SLSGGNQQKLILARELARRPDLLIAAQPTRGLDVGAIEFIHERLLE-----LRDagkaVLLISEDLdEILELSDRIAVIY 477
|
....
gi 2468698279 717 GGTI 720
Cdd:COG3845 478 EGRI 481
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
500-668 |
6.64e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 ---------QVAAVGQEPQVFgrslqENIAYGL---TQKP-------TMEEITAAAVKSGAHSfisgLPqgydtevgeag 640
Cdd:PRK11831 82 vrkrmsmlfQSGALFTDMNVF-----DNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKL----MP----------- 141
|
170 180
....*....|....*....|....*...
gi 2468698279 641 SQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
225-478 |
6.95e-11 |
|
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: 64.22 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 225 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLS 304
Cdd:cd18558 59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 305 LFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPkkvGKWYQLLEVQV---RESLAKSSQVAIEALSAMPTVRSFA 381
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSA---VVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 382 NEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL 461
Cdd:cd18558 216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQ 295
|
250
....*....|....*..
gi 2468698279 462 LSIYPRVQKAVGSSEKI 478
Cdd:cd18558 296 VPSIEAFANARGAAYHI 312
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
506-702 |
8.67e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK-----PLpqyeHRYLHRQ 580
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGLTQKptmEEITAAAVKSGAHSFISGLPQGYDTEvgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVlLITQH 702
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGV-LITDH 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
642-725 |
1.95e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*
gi 2468698279 721 REGGT 725
Cdd:PRK11022 233 VETGK 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
524-725 |
2.44e-10 |
|
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: 64.26 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--------------PQYEHRYLHRQVAavgqEPQ 589
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmcPQHNILFHHLTVA----EHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 VFGRSLQeniayGLTQKPTMEEITAAAVKSGAHSfisglpqgydtEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR01257 1025 LFYAQLK-----GRSWEEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 670 TSALDANSQLQVEQLL--YESpelySRSVLLITQHLSLVE-QADHILFLEGGTIREGGT 725
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLlkYRS----GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
506-700 |
2.57e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGqlllDGKPLPQYEHRYLHrqvaavg 585
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYGLTQKP----------------------------TMEEITAAAvksGAHSFIS---------G 627
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGVAEVKaaldrfneiyaayaepdadfdalaaeqgELQEIIDAA---DAWDLDSqleiamdalR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 628 LPQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT 700
Cdd:PRK11819 154 CPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVT 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
495-682 |
2.61e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 227118 [Multi-domain] Cd Length: 235 Bit Score: 61.29 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQfqdvSFAYPNRPDVL--VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL----DGKP 568
Cdd:COG4778 3 TPLNVSNVSK----TFTLHQQGGVRlpVLRNVSLSVNAGECVVLHGPSGSGKSTLLRSLYANYLPDEGQILVrhegEWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQYEHRYL----HRQVAAVGQepqvFGRSLQENIAYGLTQKPTMEE-ITAAAVKSGAHSFISGLpqgydtEVGE----- 638
Cdd:COG4778 79 LVTAEPREVlevrRTTIGYVSQ----FLRVIPRVSALDVVAEPLLARgVPREVARAKAADLLTRL------NLPErlwsl 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468698279 639 AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQVE 682
Cdd:COG4778 149 APATFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAtNRAVVVE 193
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
203-478 |
3.81e-10 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 61.75 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQ-LLEVQVRESl 360
Cdd:cd18588 100 DTVARVRE-LESIRQFLTGSaLTLVL-DLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRrRLEEKFQRG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLK---VGILYIGGQLVTSG 437
Cdd:cd18588 177 AENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK---TANLSNLASQIVQLIQKlttLAILWFGAYLVMDG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18588 254 ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
517-737 |
4.47e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.74 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPLPQYE--HRylhrqvAAVG-----QE 587
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpdER------ARAGlflafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 588 P-QVFGRSLQENIAYGLT---QKPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQ--LSGGQRQAVALARALIRKP 661
Cdd:TIGR01978 86 PeEIPGVSNLEFLRSALNarrSARGEEPLDLLDFEKLLKEKLALL--DMDEEFLNRSVNegFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANS-QLQVEQL-LYESPElysRSVLLITQHLSLVE--QADHILFLEGGTI-REGGTHqqLM---EKK 733
Cdd:TIGR01978 164 KLAILDEIDSGLDIDAlKIVAEGInRLREPD---RSFLIITHYQRLLNyiKPDYVHVLLDGRIvKSGDVE--LAkelEAK 238
|
....
gi 2468698279 734 GCYW 737
Cdd:TIGR01978 239 GYDW 242
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
502-703 |
5.22e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehrylhrqv 581
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------------ 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQEN-IAYGLTQKPTMEEitaaaVKSGAH--SF-ISG---LPQGYdtevgeagsQLSGGQRQAVALA 654
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSNpLLYMMRCFPGVPE-----QKLRAHlgSFgVTGnlaLQPMY---------TLSGGQKSRVAFA 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSqlqVEQLLyESPELYSRSVLLIT--QHL 703
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDA---VEALI-QGLVLFQGGVLMVShdEHL 686
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-673 |
5.67e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLvqfqDVSFaypnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRy 576
Cdd:PRK10762 5 LQLKGI----DKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lHRQVAAVG---QE----PQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGEagsqLSGGQ 647
Cdd:PRK10762 75 -SSQEAGIGiihQElnliPQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGE 146
|
170 180
....*....|....*....|....*.
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
503-718 |
5.98e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.18 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----EGQLLLDGKPLPQyehrY 576
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFGrslqeniayGLTQKPTMEeitaaavksgahsfISGLPQGydtevgeagsqLSGGQRQAVALARA 656
Cdd:cd03232 77 FQRSTGYVEQQDVHSP---------NLTVREALR--------------FSALLRG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLL-ITQ-HLSLVEQADHILFLEGG 718
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCtIHQpSASIFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
527-681 |
6.20e-10 |
|
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: 60.11 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL---PQY-EHRY-------LHRQVAAVGQEPQvfgrsL 595
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYiKADYegtvrdlLSSITKDFYTHPY-----F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAygltqKPTMEEitaaavksgahsfisglpQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03237 96 KTEIA-----KPLQIE------------------QILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
....*.
gi 2468698279 676 NSQLQV 681
Cdd:cd03237 149 EQRLMA 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
503-717 |
6.39e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLpqyehrylhrQVA 582
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVF--GRSLQENIAYGLtqkptmEEITAAAVKSGAHSFISGLP-QGYDTE--VGeagsQLSGGQRQAVALARAL 657
Cdd:TIGR03719 389 YVDQSRDALdpNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 658 IRKPCVLILDDATSALDansqlqVEQL--LYESPELYSRSVLLITqH----LSLVeqADHILFLEG 717
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD------VETLraLEEALLNFAGCAVVIS-HdrwfLDRI--ATHILAFEG 515
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
520-729 |
7.34e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT--EGQLLL-DGKPLPQyehryLHRQVAAVGQEPQVFGR-SL 595
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILAnNRKPTKQ-----ILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAY-GLTQKPtmEEITAAAVKSGAHSFIS--GLPQGYDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:PLN03211 158 RETLVFcSLLRLP--KSLTKQEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 672 ALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQA-DHILFL-EGGTIREGGTHQQL 729
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLsEGRCLFFGKGSDAM 295
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
516-684 |
7.74e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP-QYEHRYLHRQVAAVGQE-PQVFGR 593
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGltQKPT---------MEEITAAAVKSgahsfisglpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK10982 89 SVMDNMWLG--RYPTkgmfvdqdkMYRDTKAIFDE----------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180
....*....|....*....|
gi 2468698279 665 ILDDATSALdanSQLQVEQL 684
Cdd:PRK10982 157 IMDEPTSSL---TEKEVNHL 173
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
200-469 |
9.12e-10 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 60.49 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLefvgdGIYNNTMGhvhSHL-QGevFGAVLRQET----- 273
Cdd:cd18548 14 LELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIA-----GILAGYFA---AKAsQG--FGRDLRKDLfekiq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 274 ----EFFQQNQTGNITSRVTEDTSTLSDSLSenlsLFLWYLVRG--LCLLGI--MLWGSVSLTMVTLVT----LPLLFLL 341
Cdd:cd18548 84 sfsfAEIDKFGTSSLITRLTNDVTQVQNFVM----MLLRMLVRApiMLIGAIimAFRINPKLALILLVAipilALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 342 PKKVGKWYQllevQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNS-WTTSISGM 420
Cdd:cd18548 160 MKKAIPLFK----KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNpLMMLIMNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 421 LLkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL---LSIYPRVQ 469
Cdd:cd18548 236 AI-VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLsmvFVMLPRAS 286
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
507-711 |
9.44e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQ 586
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFISgLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK13540 82 RSGINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2468698279 666 LDDATSALDansQLQVEQLLYESPELYSR-SVLLITQHLSL-VEQADH 711
Cdd:PRK13540 151 LDEPLVALD---ELSLLTIITKIQEHRAKgGAVLLTSHQDLpLNKADY 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
504-715 |
1.39e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 225265 [Multi-domain] Cd Length: 593 Bit Score: 61.40 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPDVL---VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQ--------NLYQPTEGQLLLDGKPLPQY 572
Cdd:COG2401 379 EFQDILESFGVRQRVIeryVLRNLNLEIKPGDVVAVVGQSGAGKTTLLRMILgaqkgrgeEKYRPDSGKVEVPKNTVSAL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLhrqvaavgqEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLpqgydtevgeagSQLSGGQRQAVA 652
Cdd:COG2401 459 IPGEY---------EPEFGEVTILEHLRSKTGDLNAAVEILNRAGLSDAVLYRRKF------------SELSTGQKERAK 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ--ADHILFL 715
Cdd:COG2401 518 LAKLLAERPNVLLIDEFAAHLDELTAVRVARKISELAREAGITLIVVTHRPEVGNAlrPDTLILV 582
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
521-725 |
1.51e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhrqVAAVGQEPQVFGR--SLQEN 598
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAY-------GLTQKPTMEE---ITAAAVKSGAHSFisglpqgYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK15056 100 VVMmgryghmGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 669 ATSALDANSQLQVEQLLYESPElYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGT 725
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLgSVTEFCDYTVMVKGTVLASGPT 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
516-717 |
1.65e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------LLD---GKPLPQYEHRYLHRQVAAV 584
Cdd:cd03236 12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 585 gQEPQ---VFGRSLQENIAYGLTQKP---TMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:cd03236 91 -VKPQyvdLIPKAVKGKVGELLKKKDergKLDELVDQL----------ELRHVLDRNI----DQLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYlSDYIHCLYG 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-718 |
4.14e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224166 [Multi-domain] Cd Length: 591 Bit Score: 59.62 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQllLDGKPLPQYEHRYLHrqvaavGQEPQVFGRSLQENiAYGLTQK 606
Cdd:COG1245 96 TPRPGKVVGILGPNGIGKSTALKILAGELKPNLGR--YEDPPSWDEVIKRFR------GTELQNYFKKLYEG-ELRAVHK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 607 PTMEEITAAAVKSGAHSFIS---------------GLPQGYDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:COG1245 167 PQYVDLIPKVVKGKVGELLKkvdergkfdevverlGLENVLDRDV----SELSGGELQRVAIAAALLRDADVYFFDEPSS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468698279 672 ALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-AD--HILFLEGG 718
Cdd:COG1245 243 YLDIRQRLNAARVIRELAE-DGKYVIVVEHDLAVLDYlSDfvHILYGEPG 291
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-683 |
4.30e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQY-EHRYLHRQVAAVGQEPQVFGRS-LQENIAYG 602
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykPQYiKPDYDGTVEDLLRSITDDLGSSyYKSEIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 603 LtqkptmeeitaaavksgahsfisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansqlqVE 682
Cdd:PRK13409 441 L-----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VE 487
|
.
gi 2468698279 683 Q 683
Cdd:PRK13409 488 Q 488
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-747 |
5.39e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPqyehryLHRQVAAV-----------GQEPQVFGR 593
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIA---------YGLTQKPTMEEITAAavksgahSFISGL----PQGyDTEVGeagsQLSGGQRQAVALARALIRK 660
Cdd:PRK11288 347 SVADNINisarrhhlrAGCLINNRWEAENAD-------RFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQALSLAL 493
|
....*...
gi 2468698279 740 VQAPADAP 747
Cdd:PRK11288 494 PRTSAAVA 501
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
524-720 |
5.51e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YLHRQVAAVGQEPQVFGRSLQENIAY- 601
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPEDRQSSGLYLDAPLAWn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 602 ---------GLTQKPTMEeitaAAVKSGAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK15439 362 vcalthnrrGFWIKPARE----NAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2468698279 673 LDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15439 434 VDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
521-725 |
8.23e-09 |
|
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: 55.41 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVaaLLQNLYqpTEGQLLLDgKPLPQYEHrylhrqvaavgqEPQVFGRSLQENIA 600
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI-SFLPKFSR------------NKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGLtqkptmeeitaaavksgahsfisglpqGYDTeVGEAGSQLSGGQRQAVALARALIR--KPCVLILDDATSALDansQ 678
Cdd:cd03238 74 VGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLH---Q 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2468698279 679 LQVEQLLYESPELYSR--SVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03238 123 QDINQLLEVIKGLIDLgnTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
520-737 |
1.45e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPL----P------------QY--------E 573
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPedragegifmafQYpveipgvsN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 574 HRYLHRQVAAV----GQEPQ---VFGRSLQENIAygLTQKPtmEEITAAAVKSGahsfisglpqgydtevgeagsqLSGG 646
Cdd:PRK09580 96 QFFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIA--LLKMP--EDLLTRSVNVG----------------------FSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSqLQVEQLLYESPELYSRSVLLITQHLSLVE--QADHILFLEGGTIREGG 724
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSG 228
|
250
....*....|....*
gi 2468698279 725 THQ--QLMEKKGCYW 737
Cdd:PRK09580 229 DFTlvKQLEEQGYGW 243
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and ... |
524-731 |
1.77e-08 |
|
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 226592 [Multi-domain] Cd Length: 258 Bit Score: 55.91 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL---LLDGKPLPQY-----EHRYLHR-------QVAAVGQEP 588
Cdd:COG4107 25 VSFDLYPGEVLGIVGESGSGKTTLLKCISGRLTPDAGTVtyrMRDGQPRDLYtmseaERRRLLRtewgfvhQNPRDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAHSFISglpqgyDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:COG4107 105 QV---SAGGNIGerlmaigarhYG--------NIRAEAQDWLEEVEID------LDRIDDLPRTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVE-QADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4107 168 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLADRLMVMKQGQVVESGLTDRVLD 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
519-722 |
1.82e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG---------------KPLPQY------EHRYL 577
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYvidgdrEYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQepqvfgRSLQENIAyglTQKPTMEEITAAAVKSGAHSFISGLpqGYDTE-VGEAGSQLSGGQRQAVALARA 656
Cdd:PRK10636 95 EAQLHDANE------RNDGHAIA---TIHGKLDAIDAWTIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLyespELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIRE 722
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPiVDKIIHIEQQSLFE 226
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-478 |
1.99e-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: 56.33 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFV---GDGIYNNTMGH-----VHSHLQgevfgavlRQETE 274
Cdd:cd18540 20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLfirLAGKIEMGVSYdlrkkAFEHLQ--------TLSFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQ--LL 352
Cdd:cd18540 92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV----VSIYFQkkIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQvRESLAKSSQV--AI-EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYI 429
Cdd:cd18540 168 KAY-RKVRKINSRItgAFnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2468698279 430 GGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18540 247 GGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
525-730 |
2.21e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYLHRQVAAVGQEPQ----VFGRSLQENI 599
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKrdglVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AygLTQKP----TMEEITAAAVKSGAHSFISGL----PqGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:PRK10762 352 S--LTALRyfsrAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 672 ALDANSQLQVEQLL--YESPELysrSVLLITQHLSLV-EQADHILFLEGGTI-----REGGTHQQLM 730
Cdd:PRK10762 425 GVDVGAKKEIYQLInqFKAEGL---SIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
521-729 |
5.37e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK--------PLPQYEHRYLHR-------QVAAVG 585
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRRLLRtewgfvhQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAH-----SFISGLPqgydtevgeagSQLSGGQRQA 650
Cdd:PRK11701 102 LRMQV---SAGGNIGerlmavgarhYG--------DIRATAGDWLERveidaARIDDLP-----------TTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG-THQQ 728
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGlTDQV 239
|
.
gi 2468698279 729 L 729
Cdd:PRK11701 240 L 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-683 |
5.63e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224166 [Multi-domain] Cd Length: 591 Bit Score: 56.15 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQlllDGKPLPQYEHRYLhrqvaavgqEPQVFGrslqeniaygltqk 606
Cdd:COG1245 363 EIYDGEVIGILGPNGIGKTTFVKLLAGVIKPDEGS---EEDLKVSYKPQYI---------SPDYDG-------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 607 pTMEEITAAAVKSGAHS--FIS------GLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansq 678
Cdd:COG1245 417 -TVEDLLRSAIRSAFGSsyFKTeivkplNLEDLLERPVDE----LSGGELQRVAIAAALSREADLYLLDEPSAYLD---- 487
|
....*
gi 2468698279 679 lqVEQ 683
Cdd:COG1245 488 --VEQ 490
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
508-730 |
5.64e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVA----ALLQNLYQPTEGQLLLDGKPL----PQYEHRYLHR 579
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQV-------FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFIsglpqgydteVGEAGS 641
Cdd:PRK15093 90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDA----------MRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
250
....*....|
gi 2468698279 721 REGGTHQQLM 730
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
202-478 |
5.75e-08 |
|
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: 54.91 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd18782 99 GELSTRISE-LDTIRGFLTGTaLTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEgeaqKFREKLQEikTLNQ------KEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18782 177 AKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN--RYARslgegfKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18782 251 LRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
502-702 |
6.05e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAypnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhRQV 581
Cdd:PRK13543 11 LLAAHALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPqvfgrSLQENIAygltqkpTMEEITAAAVKSGAHSfiSGLPQGYDTEVGEAG------SQLSGGQRQAVALAR 655
Cdd:PRK13543 85 AYLGHLP-----GLKADLS-------TLENLHFLCGLHGRRA--KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLyeSPELYSRSVLLITQH 702
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMI--SAHLRGGGAALVTTH 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
521-677 |
7.92e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQptegqlLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRS------ 594
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSG------LITGDKSAGSHIELLGRTVQREGRLARDIRKSrantgy 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 --LQENIAYGLTqkpTMEEITAAAVKSGAH-----SFISGLPQGYD----TEVGEAG------SQLSGGQRQAVALARAL 657
Cdd:PRK09984 91 ifQQFNLVNRLS---VLENVLIGALGSTPFwrtcfSWFTREQKQRAlqalTRVGMVHfahqrvSTLSGGQQQRVAIARAL 167
|
170 180
....*....|....*....|
gi 2468698279 658 IRKPCVLILDDATSALDANS 677
Cdd:PRK09984 168 MQQAKVILADEPIASLDPES 187
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
202-458 |
1.02e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins 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. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 54.00 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADtftrNLTLMSI----LTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18567 19 LASPLYLQLVIDEVIVSGDRD----LLTVLAIgfglLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSR---VTEDTSTLSDSLSENL--SLFlwylvrGLCLLGIMLWGSVSLTMVTLVTLPLLFllpkkVGKW--YQ 350
Cdd:cd18567 95 KRHLGDIVSRfgsLDEIQQTLTTGFVEALldGLM------AILTLVMMFLYSPKLALIVLAAVALYA-----LLRLalYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 351 LLEVQVRESL---AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLqeIKTLNQKEAVAYaVNSWTTSISGMLL---KV 424
Cdd:cd18567 164 PLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLL--VDAINADIRLQR-LQILFSAANGLLFgleNI 240
|
250 260 270
....*....|....*....|....*....|....
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAV 458
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRA 274
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
528-688 |
1.24e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 528 LRPGEVTALVGPNGSGKST-VAALLQNLYQ---PTEGQLLLDGKPLPQYEHRY-----------LHRQVAAVGqEPQVFG 592
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTVG-ETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQ--ENIAYGLTQKPTMEEITAAAVKsgahsfISGLPQGYDTEVG-EAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR00956 163 ARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170
....*....|....*....
gi 2468698279 670 TSALDANSQLQVEQLLYES 688
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTS 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
502-731 |
1.42e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTEGQLLLDGKPL----PQY---- 572
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnPAQaira 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 ------EHRYLHRQVAAVGQEPQVFGRSLQE-----NIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeags 641
Cdd:TIGR02633 337 giamvpEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKT-ASPF---LPIG---------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLITQHLSLVEQ---ADHILF---- 714
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN---QLAQEGVAIIVVSSELAEVlglSDRVLVigeg 479
|
250
....*....|....*...
gi 2468698279 715 -LEGGTIREGGTHQQLME 731
Cdd:TIGR02633 480 kLKGDFVNHALTQEQVLA 497
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
517-737 |
1.74e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTEGQLLLDGKPLPQY--EHRYlHRQVAAVGQEP-QVF 591
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 GRSLQE--NIAYGLTQK----PTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAgsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:CHL00131 98 GVSNADflRLAYNSKRKfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 666 LDDATSALDANSQLQVEQ---LLYESpelySRSVLLITQHLSLVE--QADHILFLEGGTIREGGTHQ--QLMEKKGCYW 737
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEginKLMTS----ENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGDAElaKELEKKGYDW 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
533-721 |
1.77e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 533 VTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YL---HRQVAAVGQEPQVFGR-SLQENIAYGLtqKP 607
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGM--AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 608 TMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLy 686
Cdd:PRK11144 104 SMVAQFDKIVALlGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2468698279 687 espELYSRSV----LLITQHL-SLVEQADHILFLEGGTIR 721
Cdd:PRK11144 172 ---ERLAREInipiLYVSHSLdEILRLADRVVVLEQGKVK 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
461-731 |
3.90e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 461 LLSIYPRVQKAVGssEKIFEyldrtprcppsglltplhleglvqFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPN 540
Cdd:PRK13549 244 LTALYPREPHTIG--EVILE------------------------VRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 541 GSGKSTVAALLQNLYQ-PTEGQLLLDGKPL----PQY----------EHRYLHRQVA--AVGQE------PQVFGRSLqe 597
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKPVkirnPQQaiaqgiamvpEDRKRDGIVPvmGVGKNitlaalDRFTGGSR-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 nIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANS 677
Cdd:PRK13549 376 -IDDAAELKTILESIQRLKVKT-ASPE---LAIA----------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 678 QLQVEQLLYespELYSR--SVLLITQHLSLV-EQADHILFLEGGTIR-----EGGTHQQLME 731
Cdd:PRK13549 441 KYEIYKLIN---QLVQQgvAIIVISSELPEVlGLSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
506-699 |
4.58e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRpdVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqYEHRYLHRQVAAVG 585
Cdd:PRK11147 323 ENVNYQIDGK--QLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEpqvfgRSLQENIAYGltqkptMEEITAAAVKSGAHSFISGL---PQGYDTEVgeagSQLSGGQRQAVALARALIRKPC 662
Cdd:PRK11147 396 PE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSN 460
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468698279 663 VLILDDATSALDansqlqVE--QLLYESPELYSRSVLLI 699
Cdd:PRK11147 461 LLILDEPTNDLD------VEtlELLEELLDSYQGTVLLV 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
506-718 |
6.16e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPDVLV-LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQP------TEGQLLLDGKPLPQyehrylh 578
Cdd:TIGR00956 763 RNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPLDS------- 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 rqvaavgqepqvfgrSLQENIAYGLTQKPTMEEIT-------AAAVKSGAHSFIS-------------GLPQGYDTEVGE 638
Cdd:TIGR00956 833 ---------------SFQRSIGYVQQQDLHLPTSTvreslrfSAYLRQPKSVSKSekmeyveevikllEMESYADAVVGV 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 639 AGSQLSGGQRQAVALARALIRKPCVLI-LDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLS--LVEQADHILFL 715
Cdd:TIGR00956 898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLL 976
|
...
gi 2468698279 716 EGG 718
Cdd:TIGR00956 977 QKG 979
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
203-478 |
7.18e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.36 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGsadtftrNLTLMSILTIASAVLeFVGDGIYNNTMG--------HVHSHLQGEVFGAVLRQETE 274
Cdd:cd18555 20 LIPILTQYVIDNVIVPG-------NLNLLNVLGIGILIL-FLLYGLFSFLRGyiiiklqtKLDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVtEDTSTLSDSLSENLSL----FLWYLVrglcLLGIMLWGSVSLTMVTLVTLPLLFL----LPKKVg 346
Cdd:cd18555 92 FFENRSSGDLLFRA-NSNVYIRQILSNQVISliidLLLLVI----YLIYMLYYSPLLTLIVLLLGLLIVLllllTRKKI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 347 kwYQLLEVQVREsLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA-VNSWTTSISgMLLKVG 425
Cdd:cd18555 166 --KKLNQEEIVA-QTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNiLNSISSSIQ-FIAPLL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 426 ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18555 242 ILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
525-690 |
1.34e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ------PTEGQLL---------------------LDGKPLPQYEHRYL 577
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTT---FLRYMAMhaidgiPKNCQILhveqevvgddttalqcvlntdIERTQLLEEEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQvaAVGQEPQVFGRSLQENIAyGLTQKPT----------MEEITAAAVKSGAHSFISGLPQGYDTEVgEAGSQLSGGQ 647
Cdd:PLN03073 274 AQQ--RELEFETETGKGKGANKD-GVDKDAVsqrleeiykrLELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGW 349
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-735 |
2.08e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 411426 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhrqvA 582
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQE----PQVFGR------SLQENIA-----YGLTQ---KPTMEEITAAavkSGAHSFISgLPQGydtevgeagsQLS 644
Cdd:NF033858 73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPFAD-RPAG----------KLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQ----VEQLLYESPELysrSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRIRAERPGM---SVLVATAYMEEAERFDWLVAMDAGRV 215
|
250
....*....|....*
gi 2468698279 721 REGGTHQQLMEKKGC 735
Cdd:NF033858 216 LATGTPAELLARTGA 230
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
203-478 |
2.51e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 49.82 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRnLTLMSILTIA-SAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18783 20 APPIFFQIVIDKVLVHQSYSTLYV-LTIGVVIALLfEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEdTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18783 99 GVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISG---MLLKVGILYIGGQLVTSGA 438
Cdd:cd18783 178 ERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNWPQTLTGpleKLMTVGVIWVGAYLVFAGS 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2468698279 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18783 255 LTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
521-687 |
3.29e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFG------- 592
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEERRSTGiyayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 --RSLQENI-----AYGLTQKPTMEE-----ITAAAVKSGAHSfisglpqgydTEVGeagsQLSGGQRQAVALARALIRK 660
Cdd:PRK10982 344 gfNSLISNIrnyknKVGLLDNSRMKSdtqwvIDSMRVKTPGHR----------TQIG----SLSGGNQQKVIIGRWLLTQ 409
|
170 180
....*....|....*....|....*..
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYE 687
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAE 436
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
521-732 |
7.03e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVAAV--GQEPQVFGrslQEN 598
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAIsaGLSGQLTG---IEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAY-----GLTQKpTMEEITAAAVKSgahsfisglpqgydTEVGEAGSQ----LSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:PRK13546 106 IEFkmlcmGFKRK-EIKAMTPKIIEF--------------SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 670 TSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
202-481 |
7.21e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 48.27 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQ-------DGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMG-----HVHSHLqgevFGAVL 269
Cdd:cd18580 8 LLLLAFLSQFSNIWLDwwssdwsSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGlrasrRLHDKL----LRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 RQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGS--VSLTMVTLVTLPLlfllpkKVGK 347
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSpyFLIVLPPLLVVYY------LLQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 348 WYQLLEVQVR--ESLAKS---SQVAiEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKeavAY----AVNSWTTSIS 418
Cdd:cd18580 158 YYLRTSRQLRrlESESRSplySHFS-ETLSGLSTIRAFGWQERFIEENLRLLDA----SQR---AFylllAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 419 GMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQ-MQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
503-676 |
7.46e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLpqyehrylhrQVA 582
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQ-----EPQvfgRSLQENIAYGLtqkptmEEITAA--AVKS----GAHSFisglpQGYDTE--VGeagsQLSGGQRQ 649
Cdd:PRK11819 391 YVDQsrdalDPN---KTVWEEISGGL------DIIKVGnrEIPSrayvGRFNF-----KGGDQQkkVG----VLSGGERN 452
|
170 180
....*....|....*....|....*..
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDAN 676
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
502-688 |
9.66e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqptegqllldgkplpqyehrylhrqv 581
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------------------------------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aaVGQEPQ-------VFGR---------SLQENIAYgLTQKPTMEEITAAAVK----SGAHSFIsGLPQ----------- 630
Cdd:PRK10938 307 --TGDHPQgysndltLFGRrrgsgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFDSI-GIYQavsdrqqklaq 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 631 ------GYDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQ---VEQLLYES 688
Cdd:PRK10938 383 qwldilGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlNRQLVrrfVDVLISEG 451
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
525-716 |
1.00e-05 |
|
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: 47.22 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGeVTALVGPNGSGKSTV-AALLQNLY---QPTEGQLLLDGKPLPQYEHR---YLHRQVAA-----VGQEPQVFg 592
Cdd:cd03240 17 EIEFFSP-LTLIVGQNGAGKTTIiEALKYALTgelPPNSKGGAHDPKLIREGEVRaqvKLAFENANgkkytITRSLAIL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 rslqENIAY---GLTQKPTMEEITaaavksgahsfisglpqgydtevgeagsQLSGGQRQAV------ALARALIRKPCV 663
Cdd:cd03240 95 ----ENVIFchqGESNWPLLDMRG----------------------------RCSGGEKVLAsliirlALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 664 LILDDATSALDA-NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLE 716
Cdd:cd03240 143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
637-748 |
1.06e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQADHIL-FL 715
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVI 217
|
90 100 110
....*....|....*....|....*....|...
gi 2468698279 716 EGGTIREGGTHQQLMEKKGCYWAMVQaPADAPE 748
Cdd:NF000106 218 DRGRVIADGKVDELKTKVGGRTLQIR-PAHAAE 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
526-674 |
1.29e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 411426 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlpqyehrylhrqVAA--------VGQEPQVFgrSL-- 595
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP------------VDAgdiatrrrVGYMSQAF--SLyg 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 ----QENIA-----YGLTqkptmEEITAAAVKSGAHSFisGLpqgydTEVGEA-GSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:NF033858 353 eltvRQNLElharlFHLP-----AAEIAARVAEMLERF--DL-----ADVADAlPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
....*....
gi 2468698279 666 LDDATSALD 674
Cdd:NF033858 421 LDEPTSGVD 429
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
526-730 |
2.23e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------LLDGKPLPQY-EHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYGLTQKPTMEEItaaavksgAHSF-ISGLpqgydteVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK10938 104 EIIQDEVKDPARCEQL--------AQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 676 NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
268-478 |
2.43e-05 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 46.70 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 268 VLRQETEFFQQNQTGNITSRV-TEDT--STLSDSLSE---NLSLFLWYLVrglcllgIMLWGSVSLTMVTLVTLPLLFLL 341
Cdd:cd18569 85 VLRLPVEFFSQRYAGDIASRVqSNDRvaNLLSGQLATtvlNLVMAVFYAL-------LMLQYDVPLTLIGIAIALLNLLV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 342 PKKVGKWYQLL-EVQVRESlAKSSQVAIEALSAMPTVRSFANEEGeaqkFREKL--QEIKTLNQKEAVAyAVNSWTTSIS 418
Cdd:cd18569 158 LRLVSRKRVDLnRRLLQDS-GKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELG-RTNQLLGALP 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 419 GMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18569 232 TLLSALTnaaILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
517-685 |
2.96e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqpTEGQLLLDGKPlpQYEHRYLhrqVAAVGQEP------QV 590
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRI--IYEQDLI---VARLQQDPprnvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 F----------GRSLQE--NIAYGLTQKPT------MEEITAAAVKSGAHSFIS---------GLPQgyDTEVgeagSQL 643
Cdd:PRK11147 84 YdfvaegieeqAEYLKRyhDISHLVETDPSeknlneLAKLQEQLDHHNLWQLENrinevlaqlGLDP--DAAL----SSL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLL 685
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-699 |
3.31e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQ-----NL---------------YQPTEGQ----LLLDG--KPL--PQYehrylh 578
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgelipNLgdyeeepswdevlkrFRGTELQnyfkKLYNGeiKVVhkPQY------ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 rqvaaVGQEPQVFgrslqeniaygltqKPTMEEITAAAVKSGAHSFIS---GLPQGYDTEVgeagSQLSGGQRQAVALAR 655
Cdd:PRK13409 169 -----VDLIPKVF--------------KGKVRELLKKVDERGKLDEVVerlGLENILDRDI----SELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLI 699
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
637-725 |
6.76e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESpelySRSVLLITQHLSLVEQAD 710
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKTAD 899
|
90
....*....|....*..
gi 2468698279 711 HILFL--EGGTirEGGT 725
Cdd:TIGR00630 900 YIIDLgpEGGD--GGGT 914
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
531-717 |
9.81e-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: 43.71 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 531 GEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGkPLPQYEHRYLhrqvaavgqepqvfgrslqeniaygltqkptme 610
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 611 eitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*...
gi 2468698279 691 LYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
268-481 |
1.04e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.77 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 268 VLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVR-----GLCL---------LGIMLWGSVSLTMVtlv 333
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSiigtfILIIiylpwfaiaLPPLLVLYYFIANY--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 334 tlpllfllpkkvgkwYQ--LLEVQVRESLAKSSQVA--IEALSAMPTVRSFaneeGEAQKFREKLQE-IKTLNQKEAVAY 408
Cdd:cd18606 155 ---------------YRasSRELKRLESILRSFVYAnfSESLSGLSTIRAY----GAQDRFIKKNEKlIDNMNRAYFLTI 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 409 AVNSW----TTSISGML-LKVGILYIGGQLVTSGAvSSGNLVTFVLyqmQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18606 216 ANQRWlairLDLLGSLLvLIVALLCVTRRFSISPS-STGLVLSYVL---QITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
490-688 |
1.78e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPLhleglVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-LLDGKP 568
Cdd:PRK10636 305 PESLPNPL-----LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 L---PQYEHRYLHRQVAAVGQ----EPQVFGRSLQENIaygltqkptmeeitaaavksGAHSFisglpQGydTEVGEAGS 641
Cdd:PRK10636 377 LgyfAQHQLEFLRADESPLQHlarlAPQELEQKLRDYL--------------------GGFGF-----QG--DKVTEETR 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES 688
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEA 472
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
587-724 |
2.57e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGRSLQENIAYGLTQKPTMEEITAAAvksgaHSFI-SGLpqGYdTEVGEAGSQLSGGQRQAVALARALI---RKPC 662
Cdd:PRK00635 1651 EGKHFGQLLQTPIEEVAETFPFLKKIQKPL-----QALIdNGL--GY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPT 1722
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADHILFLEGGTIREGG 724
Cdd:PRK00635 1723 LFLLDEIATSLDNQQKSALLVQLRTLVSL-GHSVIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
503-560 |
2.62e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEG 560
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
233-482 |
3.01e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 43.23 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDGIYnnTMG------HVHSHLQGEVFGAVLRqeteFFQQNQTGNITSRVTEDTSTLSDSLSENLSLF 306
Cdd:cd18604 51 LISLLSVLLGTLRYLLF--FFGslrasrKLHERLLHSVLRAPLR----WLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 307 LWYLVRGLCLLG-------IMLWGSVSLTMVTLVtlpllfllpkkVGKWYqlLEVQ--VR--ESLAKS---SQVAiEALS 372
Cdd:cd18604 125 LESTLSLLVILIaivvvspAFLLPAVVLAALYVY-----------IGRLY--LRASreLKrlESVARSpilSHFG-ETLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 373 AMPTVRSFANEEgeaqKFREKLQE-IKTLNQKEAVAYAVNSW----TTSISGML-LKVGILyiggqLVTSGAVSSGnLVT 446
Cdd:cd18604 191 GLVTIRAFGAEE----RFIEEMLRrIDRYSRAFRYLWNLNRWlsvrIDLLGALFsFATAAL-----LVYGPGIDAG-LAG 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 2468698279 447 FVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:cd18604 261 FSLsFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
627-736 |
4.30e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223256 [Multi-domain] Cd Length: 935 Bit Score: 43.73 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 627 GLpqGYDTeVGEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DansqlqVEQLLYESPELYSR--SVLL 698
Cdd:COG0178 810 GL--GYIK-LGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLhfdD------IKKLLEVLHRLVDKgnTVIV 880
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2468698279 699 ITQHLSLVEQADHILFL------EGGTIREGGTHQQLMEKKGCY 736
Cdd:COG0178 881 IEHNLDVIKTADWIIDLgpeggdGGGEIVASGTPEEVAKVKASY 924
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
263-465 |
4.31e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 42.87 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 263 EVFGAVLRQETEFFQQNQTGNITS---RVTEDTSTLSDSLSENL----------SLFLWYLVrGLCLLGIMLwGSVSL-- 327
Cdd:cd18582 76 RVFRHLHSLSLRFHLSRKTGALSRaieRGTRGIEFLLRFLLFNIlptilelllvCGILWYLY-GWSYALITL-VTVALyv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 328 --TMvtlvtlpllfllpkKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 405
Cdd:cd18582 154 afTI--------------KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 406 VAYAVNSWTTSI---SGMllkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIY 465
Cdd:cd18582 220 TSLALLNIGQALiisLGL---TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
641-727 |
4.87e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 43.60 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 641 SQLSGGQRQAVALARALI-------RKPC-VLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADHI 712
Cdd:COG0419 814 KTLSGGERFLASLALRLAlsdllqgRARLeLLFLDEPFGTLDEERLEKLAEILEELLSD-GRQIIIISHVEELKERADVR 892
|
90
....*....|....*
gi 2468698279 713 LFLEggtiREGGTHQ 727
Cdd:COG0419 893 IRVK----KDGGRSR 903
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
522-551 |
2.06e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|....
gi 2468698279 522 QGLTFTLRPGEVTALVGPNGSGKST----VAALL 551
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
521-566 |
2.87e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 2.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG 566
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
636-718 |
2.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 636 VGEAGSQLSGGQRQAVALARALI---RKPCVLILDDATSALDANSqlqVEQLLY--ESPELYSRSVLLITQHLSLVEQAD 710
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD---IKALIYvlQSLTHQGHTVVIIEHNMHVVKVAD 879
|
90
....*....|
gi 2468698279 711 HILFL--EGG 718
Cdd:PRK00635 880 YVLELgpEGG 889
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
497-555 |
5.77e-03 |
|
AAA domain;
Pssm-ID: 433240 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 5.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVsfaypnrpdvlvlqglTFTLRPGeVTALVGPNGSGKST-VAALLQNLY 555
Cdd:pfam13476 1 LTIENFRSFRDQ----------------TIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
205-472 |
7.26e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 39.13 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 205 PFFTGRLTDWILQDGSADTFT--RNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18560 16 PLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEDTstlsDSLSENLSLFLWYLVRGL--CLLGIMLW---GSVSLTMVTLVTLPLLFLLPKKVGKWyqllEVQVR 357
Cdd:cd18560 96 EVVRIMDRGT----ESANTLLSYLVFYLVPTLleLIVVSVVFafhFGAWLALIVFLSVLLYGVFTIKVTEW----RTKFR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAK----SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 433
Cdd:cd18560 168 RAANKkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYR 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAV 472
Cdd:cd18560 248 VVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
362-477 |
8.86e-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: 38.66 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEiktlnqKEAVAYAVNSWTTSISG---MLLKVGIL---YIGGQLVT 435
Cdd:cd18583 174 EERSILTESLLNWETVKYFNREPYEKERYREAVKN------YQKAERKYLFSLNLLNAvqsLILTLGLLagcFLAAYQVS 247
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2468698279 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEK 477
Cdd:cd18583 248 QGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
|