|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
78-800 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 951.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 78 ASLAWL-GTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 156
Cdd:TIGR00958 1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 157 KPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGshptAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGN 231
Cdd:TIGR00958 72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 232 PVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 311
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 312 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 391
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 392 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 471
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 472 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 551
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAV 711
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 712 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLME 791
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*....
gi 1168024061 792 KKGCYWAMV 800
Cdd:TIGR00958 703 DQGCYKHLV 711
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
260-538 |
2.66e-166 |
|
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: 482.36 E-value: 2.66e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024061 500 SSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
261-802 |
3.12e-138 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 224055 [Multi-domain] Cd Length: 567 Bit Score: 420.68 E-value: 3.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 261 EMAIPFFTGRLTDWILQDgsADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:COG1132 30 SLLLPLLIGRIIDALLAD--LGELLELLLLLLLLALLGGVLRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 341 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 420
Cdd:COG1132 108 SGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 421 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 500
Cdd:COG1132 188 GELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 501 SGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLhLEGLVQFQDVSFAYPNRPdvLV 580
Cdd:COG1132 268 VGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPEVEDPPDPLKD-TIGSIEFENVSFSYPGKK--PV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIA 660
Cdd:COG1132 345 LKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 661 YGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQ 740
Cdd:COG1132 425 LGRPD-ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEAL 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024061 741 VEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:COG1132 504 IQDALKKLLKG--RTTLIIAHRLSTIKNADRIIVLDNGRIVERGTHEELLAKGGLYARLYQA 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
552-780 |
6.70e-136 |
|
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: 401.85 E-value: 6.70e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAV 711
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024061 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
262-797 |
3.59e-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: 339.20 E-value: 3.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 262 MAIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGD---GIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQ 337
Cdd:COG2274 171 LATPLFSQIVIDKVLPDASRST----LTVLAIGLLLAALFEALLRllrTYLIAHLGkRLDLELSGRFFRHLLRLPLSYFE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 338 QNQTGNIMSRVTEDTSTLSDSLSENLSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVR 417
Cdd:COG2274 247 KRSVGEIISRVRELEQIREFLTGSILTLII-DLLFALIFLAVMFLYSWKLTLIVLAAIPLNVLITLIFQP---LLRRKTR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 418 ESLAKSSQVA---IEALSAMPTVRSFANEEGEAQKFREKLQE-IKTLNQKEAVAYAVNSWTTSISGmLLKVGILYIGGQL 493
Cdd:COG2274 323 KLIEESAEQQsflVETIKGIETVKALAAEPRFRSQWDNRLAKqVNIGFKTEKLALILNTIKSLLQQ-LSSVLILWFGAIL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 494 VTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAY 572
Cdd:COG2274 402 VLEGELTLGQLVAFNMLAGYFISPITRLSQLWTDFQQAKVALERLGDILDTPPeQEGDKTLIHLPKLQGEIEFENVSFRY 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 573 PNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFG 652
Cdd:COG2274 482 GPD-DPPVLEDLSLEIPPGEKVAIVGRSGSGKSTLLKLLLGLYKPQQGRILLDGVDLNDIDLASLRRQVGYVLQDPFLFS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 653 RSLQENIAYGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSA 732
Cdd:COG2274 561 GSIRENIALGNPE-ATDEEIIEAAQLAGAHEFIENLPMGYDTPVGEGGANLSGGQRQRLALARALLSKPKILLLDEATSA 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024061 733 LDANSQLQVEQLLyeSPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYW 797
Cdd:COG2274 640 LDPETEAIILQNL--LQILQGRTVIIIAHRLSTIRSADRIIVLDQGKIVEQGSHEELLAQGGLYA 702
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
320-796 |
3.68e-105 |
|
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: 335.13 E-value: 3.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 320 LQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLF 399
Cdd:TIGR02204 93 IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 400 LLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklQEIKTLNQKEAVAYAVNSWTTSISG 479
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFG---GAVEKAYEAARQRIRTRALLTAIVI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 480 MLL---KVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTP--RCPPSGLL 554
Cdd:TIGR02204 250 VLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 555 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH 634
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 635 RYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVA 712
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYG---RPdaTDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
....
gi 1168024061 793 KGCY 796
Cdd:TIGR02204 565 GGLY 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
563-802 |
2.76e-98 |
|
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: 304.85 E-value: 2.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 643 AVGQEPQVFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPC 722
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 723 VLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
260-538 |
1.13e-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: 294.84 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024061 500 SSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
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 ... |
260-538 |
1.54e-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: 273.28 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024061 500 SSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
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 ... |
260-538 |
1.12e-76 |
|
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: 249.92 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024061 500 SSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18784 251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
561-794 |
2.62e-74 |
|
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: 241.36 E-value: 2.62e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 561 GLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 641 VAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRK 720
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024061 721 PCVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:cd03254 158 PKILILDEATSNIDTET----EKLIQEALEKLMkgRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
563-797 |
4.08e-74 |
|
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: 240.98 E-value: 4.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 643 AVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPC 722
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024061 723 VLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYW 797
Cdd:cd03251 159 ILILDEATSALDTES----ERLVQAALERLMknRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
314-796 |
4.99e-71 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 244.16 E-value: 4.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 314 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 389
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 390 VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 469
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 470 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 548
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 549 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP 628
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 629 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQ 708
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQ 788
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
....*...
gi 1168024061 789 LMEKKGCY 796
Cdd:PRK11176 565 LLAQNGVY 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
323-802 |
1.62e-70 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 242.94 E-value: 1.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 323 EVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLS----DSLSENLSLFLWYLVrglcLLGIMLWGSVSLTMVTLVTLPLL 398
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVV----LLPLALFMNWRLSLVLVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 399 FLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklqeiKTLNQKEAVAYAVNSW----- 473
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALR------DIADNLLAAQMPVLSWwalas 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 474 -TTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPS 551
Cdd:PRK13657 244 vLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPdVRDPP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:PRK13657 324 GAIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQ 709
Cdd:PRK13657 402 VTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
490
....*....|...
gi 1168024061 790 MEKKGCYWAMVQA 802
Cdd:PRK13657 557 VARGGRFAALLRA 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
563-802 |
4.57e-69 |
|
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: 227.50 E-value: 4.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 642 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKP 721
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 722 CVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:cd03253 157 PILLLDEATSALDTHT----EREIQAALRDVSkgRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
...
gi 1168024061 800 VQA 802
Cdd:cd03253 233 WKA 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
563-801 |
4.68e-67 |
|
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: 222.36 E-value: 4.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 642 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKP 721
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 722 CVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
418-799 |
1.45e-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: 229.55 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 418 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISGMLLKVgILYIGGQLVTS 496
Cdd:COG5265 116 NADSDANAKAIDSLLNFETVKYFGNEEYEAVRYDHALETYEKAAIKVHVSLLVlNFGQTAIFSTGLRV-MMTMSALGVEE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 497 GAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDR------TPRCPPsglLTPLHLeGLVQFQDVSF 570
Cdd:COG5265 195 GQLTVGDLVNVNALLFQLSIPLNFLGFSYREIRQALTDMEKMFDLLDVeaevsdAPDAPP---LWPVRL-GAVAFINVSF 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 571 AY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ 649
Cdd:COG5265 271 AYdPRRP---ILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSITIDGQDIRDVTQQSLRRAIGIVPQDTV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 650 VFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDA 729
Cdd:COG5265 348 LFNDTIAYNIKYGRP-DATAEEVGAAAEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVAIARTILKNPPILILDEA 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 730 TSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:COG5265 427 TSALDTHTEQAIQAALREV--SAGRTTLVIAHRLSTIIDADEIIVLDNGRIVERGTHEELLAAGGLYAEM 494
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
563-778 |
8.36e-66 |
|
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: 216.48 E-value: 8.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 643 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQQQAVALARALIRKPC 722
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024061 723 VLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGG 778
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
431-802 |
8.76e-66 |
|
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: 229.07 E-value: 8.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 431 LSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeAVAYAVNS-----WTTSISGMLlkvGILYIGGQLVTSGAVSSGNLV 505
Cdd:COG4988 186 LRGLETLRAFGRTEATEERIRKDSEDFRKATMS-VLRIAFLSsavleFFAYLSIAL---VAVYIGFRLLGEGDLTLFAGL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 506 TFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLE--GLVQFQDVSFAYPNRPdvLVLQG 583
Cdd:COG4988 262 FVLILAPEFFQPLRDLGSFFHAAAAGEAAADKLFTLLESPVATPGSGEKAEVANEppIEISLENLSFRYPDGK--PALSD 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGl 663
Cdd:COG4988 340 LNLTIKAGQLTALVGASGAGKSTLLNLLLGFLAPTQGEIRVNGIDLRDLSPEAWRKQISWVSQNPYLFAGTIRENILLA- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 664 TQKPTMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQ 743
Cdd:COG4988 419 RPDASDEEIIAALDQAGLLEFVPK-PDGLDTVIGEGGAGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQ 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024061 744 LLYESPERysRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:COG4988 498 ALQELAKQ--KTVLVITHRLEDAADADRIVVLDNGRLVEQGTHEELSEKQGLYANLLKQ 554
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
561-780 |
7.11e-61 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 204.75 E-value: 7.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 561 GLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 641 VAAVGQEPQVFGRSLQENIAYGLtQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRK 720
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 721 PCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
445-801 |
1.62e-60 |
|
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: 1.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 445 GEAQKFREKL-QEIKTLNQKEAVAYAVNSWTTSIsgMLLKVGILYIGGQLVTSGAVSSGNL-----VTFVLYQMQFTQAL 518
Cdd:COG4987 215 GAEDAYRTALeATEASWLKAQRKQARFTGLSDAI--LLLIAGLLVIGLLLWMAAQVGAGALaqpgaALALLVIFAALEAF 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 519 EVLLSIYP-RVQKAVGSSEKIFEYLDRTPRCPPSGLLTPlHLEGLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALV 597
Cdd:COG4987 293 EPLAPGAFqHLGQVIASARRLNDILDQKPEVTFPDEQTA-TTGQALELRNVSFTYPGQQ-TKALKNFNLTLAQGEKVAIL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 598 GPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygLTQKP--TMEEITAA 675
Cdd:COG4987 371 GRSGSGKSTLLQLLAGAWDPQQGSITLNGVEIASLDEQALRETISVLTQRVHLFSGTLRDNL---RLANPdaSDEELWAA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 676 AVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRS 755
Cdd:COG4987 448 LQQVGLEKLLESAPDGLNTWLGEGGRRLSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLALLFEHAE--GKT 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1168024061 756 VLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:COG4987 526 LLMVTHRLRGLERMDRIIVLDNGKIIEEGTHAELLANNGRYKRLYQ 571
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
293-801 |
7.78e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 213.43 E-value: 7.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 293 ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDslsenlslfLWYLV- 371
Cdd:PRK10790 73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---------LYVTVv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 372 ----RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV----QVRESLAKSSQVAIEALSAMPTVRSFANE 443
Cdd:PRK10790 144 atvlRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 444 egeaQKFREKLQEIKTLNqkeavaYAVNSWTTSISGMLLK-----------VGILYIGGqLVTSGAVSSGNLVTFVLYQM 512
Cdd:PRK10790 224 ----ARFGERMGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 513 QFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRtPRCPPSGLLTPLHlEGLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGE 592
Cdd:PRK10790 293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 593 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltQKPTMEEI 672
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 673 TAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRY 752
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--RE 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1168024061 753 SRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:PRK10790 525 HTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
260-518 |
8.41e-60 |
|
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: 204.03 E-value: 8.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 337
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 338 QNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 417
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 418 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 497
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 1168024061 498 AVSSGNLVTFVLYQMQFTQAL 518
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
335-802 |
4.74e-59 |
|
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: 213.83 E-value: 4.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 335 FFQQNQTGNIMSRVTeDTSTLSDSL-SENLSLFL--WYLVrglcLLGIML-WGSVSLTMVTLVTLPLLFLLPKKVGKWYQ 410
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 411 LLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQK----FREKLQEIKTLNQKEAVAYAVNSWTTSIsgmlLKVGI 486
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLI----LNVVI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 487 LYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQF 565
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 566 QDVSFAYP-NRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAV 644
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 645 GQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVL 724
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024061 725 ILDDATSALDANSQLQ-VEQLLYESperySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:TIGR01193 634 ILDESTSNLDTITEKKiVNNLLNLQ----DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-799 |
2.22e-51 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 189.15 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 330 RQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIM-LWGSVSLTMVTLVTLPLLFLLPKKVGKw 408
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGD- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 409 yqllevQVRESLaKSSQVAI--------EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSIS-G 479
Cdd:PRK10789 160 ------QLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAiG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 480 M--LLKVGilyiGGQ-LVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPpSGLLTP 556
Cdd:PRK10789 233 ManLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 557 LHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 636
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 637 LHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALA 714
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*
gi 1168024061 795 CYWAM 799
Cdd:PRK10789 542 WYRDM 546
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
480-792 |
4.01e-50 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 480 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 558
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPsRDPAMPLPEP-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 559 lEGLVQFQDVSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:TIGR01842 314 -EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 639 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALI 718
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024061 719 RKPCVLILDDATSALDAnsqlQVEQLLYE---SPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDE----EGEQALANaikALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
445-801 |
3.31e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 183.10 E-value: 3.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 445 GEAQKFREKL--QEIKTLNQKEAVAyavnswttSISGM----------LLKVGILYIGGQLVTSGAVSSGNLVTFVLYQM 512
Cdd:PRK11160 217 GAEDRYRQQLeqTEQQWLAAQRRQA--------NLTGLsqalmilangLTVVLMLWLAAGGVGGNAQPGALIALFVFAAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 513 QftqALEVLLSI---YPRVQKAVGSSEKIFEYLDRTP--RCPPSGLLTPLHleGLVQFQDVSFAYPNRPDvLVLQGLTFT 587
Cdd:PRK11160 289 A---AFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 588 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKp 667
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 668 TMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYE 747
Cdd:PRK11160 442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1168024061 748 SPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:PRK11160 521 HAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
480-792 |
8.08e-46 |
|
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: 173.23 E-value: 8.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 480 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 558
Cdd:COG4618 254 MALQSAVLGLGAWLVIKGEITPGMMIAGSILSGRALAPIDLAIANWKQFVAARQSYKRLNELLAELPaAAERMPLPAP-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 559 lEGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:COG4618 332 -QGALSVERLTAAPPGQKKP-ILKGISFALQAGEALGIIGPSGSGKSTLARLLVGIWPPTSGSVRLDGADLRQWDREQLG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 639 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALI 718
Cdd:COG4618 410 RHIGYLPQDVELFDGTIAENIAR-FGEEADPEKVIEAARLAGVHELILRLPQGYDTRIGEGGATLSGGQRQRIALARALY 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024061 719 RKPCVLILDDATSALDANSqlqvEQLLYE---SPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:COG4618 489 GDPFLVVLDEPNSNLDSEG----EAALAAailAAKARGGTVVVIAHRPSALASVDKILVLQDGRIAAFGPREEVLAK 561
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
514-799 |
8.18e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.49 E-value: 8.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 514 FTQALEVLLSIYPRVQKAVGSSEKIFEYLDrTPRCPPSGLLTPLHLEGLVQF--QDVSfaypnrpdVLVLQG------LT 585
Cdd:PRK11174 300 FYQPLRDLGTFYHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIeaEDLE--------ILSPDGktlagpLN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 586 FTLRPGEVTALVGPNGSGKST-VAALLQNL-YQptgGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGl 663
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 664 tqKPTM--EEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSqlqv 741
Cdd:PRK11174 447 --NPDAsdEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS---- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 742 EQLLYESPERYSRS--VLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:PRK11174 521 EQLVMQALNAASRRqtTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
318-763 |
1.04e-45 |
|
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: 172.16 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 318 SHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 382
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvivpagvalvvGAAAVAAIAVLSVPAALILAAGLLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 383 GSVSLTMVTLvtlpllfllpkKVGKWYQLLEVQVRESLAkssQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 462
Cdd:TIGR02868 166 AGFVAPLVSL-----------RAARAAEQALARLRGELA---AQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 463 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKIFEYL 542
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 543 DRTPRCP----PSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 618
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLE-LRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 619 GGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 696
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024061 697 GEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHL 763
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
260-538 |
1.49e-45 |
|
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: 164.82 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024061 500 SSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
581-731 |
1.09e-44 |
|
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: 157.42 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQENI 659
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024061 660 AYGLtqkpTMEEITAAAVKSGAHSFISGLPQGY--DTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATS 731
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
562-782 |
1.77e-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: 156.90 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 562 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEHRYL 637
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 638 HRQVAAVGQEPQ-----VF--GRSLQENI-AYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQLSGG 706
Cdd:cd03257 81 RKEIQMVFQDPMsslnpRMtiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPH-----------ELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024061 707 QQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIRE 782
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
262-538 |
3.05e-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: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 262 MAIPFFTGRLTDWILQ-DGSADTFTRNLT-----LMSILTIASA-------VLEFVGDGIYNNtmghvhshLQGEVFGAV 328
Cdd:cd18573 13 MSVPFAIGKLIDVASKeSGDIEIFGLSLKtfalaLLGVFVVGAAanfgrvyLLRIAGERIVAR--------LRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 329 LRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKW 408
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 409 YQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILY 488
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168024061 489 IGGQLVTSGAVSSGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
561-785 |
3.16e-43 |
|
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: 156.11 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 561 GLVQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 640 QVAAVGQEPQVFGRSLQENIAygltqkP----TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALAR 715
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT 785
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
293-801 |
1.65e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.90 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 293 ILTIASAVleFVGDGI---YNNTMGH-VHSHLQGEVFGAVLRQETEFFQQ--NQTGNIMSRVTEDTSTLSDSLSENLSLF 366
Cdd:PTZ00265 872 ILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 367 LWYLVRGL---------C-LLGIMLWGSVSLTM----VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAI-EAL 431
Cdd:PTZ00265 950 THFIVLFLvsmvmsfyfCpIVAAVLTGTYFIFMrvfaIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIqEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 432 SAMPTVRSFANEE------GEAQKFREKLQEIKTLnqkeavayaVNS--WTTSISGMLLKVGILY-IGGQLVTSGAVSSG 502
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTL---------VNSmlWGFSQSAQLFINSFAYwFGSFLIRRGTILVD 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 503 NLVTfVLYQMQFTQALE-VLLSIYPRVQKAVGSSEKIFEYLDRTP----------RCPPSGLLtplhlEGLVQFQDVSFA 571
Cdd:PTZ00265 1101 DFMK-SLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSnidvrdnggiRIKNKNDI-----KGKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 572 YPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY------------QPTG-------------------- 619
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 620 ----------------------GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAV 677
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 678 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQQQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVL 757
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1168024061 758 LITQHLSLVEQADHILFLE-----GGAIREGGTHQQLME-KKGCYWAMVQ 801
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
564-778 |
1.94e-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: 147.61 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 564 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 643
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 644 VGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQQQAV 711
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024061 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGG 778
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
563-778 |
5.96e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 146.08 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 563 VQFQDVSFAYPNRPDV--LVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQPTGgqllldgkplpqyeHRYLHR 639
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 640 QVAAVGQEPQVFGRSLQENIAYGltqKPTMEE-----ITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQQQAVALA 714
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFG---KPFDEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024061 715 RALIRKPCVLILDDATSALDAnsqlQVEQLLYES----PERYSRSVLLITQHLSLVEQADHILFLEGG 778
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
562-789 |
1.39e-39 |
|
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: 146.94 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:COG1120 2 MLEVENLSFGYGGKP---ILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASLSPKELAKKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 642 AAVGQEPQV-FGRSLQENIAYGLTQKPTM---------EEITAAAVKSGAHSFIsglpqgyDTEVGEagsqLSGGQQQAV 711
Cdd:COG1120 79 AYVPQSPSApFGLTVYELVLLGRYPHLGLfgrpskedeEIVEEALELLGLEHLA-------DRPVDE----LSGGERQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI-REGGTHQQL 789
Cdd:COG1120 148 LIARALAQETPILLLDEPTSHLDIAHQIEVLELLRDLNREKGLTVVMVLHDLNLAARyADHLILLKDGKIvAQGTPEEVL 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
261-538 |
1.46e-39 |
|
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: 148.08 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 261 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 341 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 420
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 421 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 500
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1168024061 501 SGNLVTFVLYQMQFTQALEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd07346 255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
562-792 |
2.13e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 224054 [Multi-domain] Cd Length: 293 Bit Score: 147.45 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 562 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQV 641
Cdd:COG1131 4 VIEVRNLTKKYGG--DKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVK-EPAKVRRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 642 AAVGQEPQVFGR-SLQENI-----AYGLTQKPTMEEITAAAvksgahsFISGLPQGYDTEVgeagSQLSGGQQQAVALAR 715
Cdd:COG1131 81 GYVPQEPSLYPElTVRENLeffarLYGLSKEEAEERIEELL-------ELFGLEDKANKKV----RTLSGGMKQRLSIAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024061 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 792
Cdd:COG1131 150 ALLHDPELLILDEPTSGLDPESRREIWELLRELAKEGGVTILLSTHILEEAEElCDRVIILNDGKIIAEGTPEELKEK 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
562-793 |
2.17e-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: 145.86 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 562 LVQFQDVSFAYPNRpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYLHRQ 640
Cdd:COG1122 3 MIEAENLSFRYPGR--KAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTsSEKSLLELRQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024061 641 VAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVgeagSQLSGGQQQAVALARALI 718
Cdd:COG1122 81 VGLVFQNPddQLFGPTVEDEVAFGLENLGLPREEIEERVAEALELV--GLEELLDRPP----FNLSGGQKQRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024061 719 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKK 793
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 ... |
563-782 |
1.18e-38 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subuni |
