|
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: 949.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 18 ASLAWL-GTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 96
Cdd:TIGR00958 1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 97 KPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGshptAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGN 171
Cdd:TIGR00958 72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 172 PVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 251
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 252 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 331
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 332 LITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 411
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 412 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 491
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 571
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAV 651
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLME 731
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*....
gi 2203400792 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 |
1.28e-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: 481.20 E-value: 1.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2203400792 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
201-742 |
5.27e-154 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 460.02 E-value: 5.27e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:COG1132 37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP-PSGLLTPLHLEGLVQFQDVSFAYPnrPDVL 519
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI 599
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAns 677
Cdd:COG1132 435 RYG---RPdaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDT-- 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 678 qlQVEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG1132 510 --ETEALIQEALERLMkgRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
492-720 |
1.82e-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: 401.46 E-value: 1.82e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 571
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAV 651
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
202-741 |
2.26e-123 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 384.96 E-value: 2.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 282 GNIMSRVTeDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:COG2274 253 GDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkVGILYIGGQLVTSGAVS 440
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVIDGQLT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQFQDVSFAYPNRpDVL 519
Cdd:COG2274 411 LGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLpRLKGDIELENVSFRYPGD-SPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI 599
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQL 679
Cdd:COG2274 570 TLGDPD-ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 680 QVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:COG2274 649 IILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
260-736 |
5.13e-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: 333.21 E-value: 5.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 260 LQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLF 339
Cdd:TIGR02204 93 IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 340 LLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklQEIKTLNQKEAVAYAVNSWTTSISG 419
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFG---GAVEKAYEAARQRIRTRALLTAIVI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 420 MLL---KVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP--RCPPSGLL 494
Cdd:TIGR02204 250 VLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH 574
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 575 RYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVA 652
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYG---RPdaTDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
....
gi 2203400792 733 KGCY 736
Cdd:TIGR02204 565 GGLY 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
503-742 |
1.69e-97 |
|
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: 301.38 E-value: 1.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 663 VLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
205-736 |
9.10e-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: 308.57 E-value: 9.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 205 PFFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLE----FVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:TIGR02203 31 STLAALLKP-LLDDGFGGRDRSVLWWVPLVVIGLAVLRgicsFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:TIGR02203 110 TGTLLSRITFDSEQVASAATDAFIV----LVREtltvIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:TIGR02203 186 QNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPLHLEGLVQFQDVSFAYPNRp 516
Cdd:TIGR02203 266 GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 677 SQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 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 |
1.47e-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: 292.91 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2203400792 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 |
1.16e-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: 272.51 E-value: 1.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2203400792 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
471-734 |
4.62e-79 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 263.93 E-value: 4.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 471 AVGSSEKIFEYLDRTPRCPPSGLLT-PLHLEGLVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAA 549
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPlPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 550 LLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQkPTMEEITAAAVKSGAHSFISGLP 629
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD-ASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 630 QGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQA 709
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 2203400792 710 DHILFLEGGAIREGGTHQQLMEKKG 734
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
258-741 |
1.16e-78 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 263.17 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 258 SHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLsdslsENLSL------------------FLWYLVR--GLCLL 317
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-----DNLYLrvllpllvallvilaavaFLAFFSPalALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 318 GIMLWGSVSLTMVtlitlpllfllpkkVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEI 397
Cdd:COG4987 163 LGLLLAGLLLPLL--------------AARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 398 KTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLyqmqFTQAV-EVLLSI---YPRVQKAVG 473
Cdd:COG4987 229 AAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVL----AALALfEALAPLpaaAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 474 SSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN 553
Cdd:COG4987 305 AARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 554 LYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQG 631
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA---RPdaTDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 632 YDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADH 711
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDR 538
|
490 500 510
....*....|....*....|....*....|
gi 2203400792 712 ILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
362-748 |
2.24e-78 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 263.22 E-value: 2.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQE-----IKT------LNQKEAVAYAVnswttsisGMllkVGILYIG 430
Cdd:COG5265 216 EANTRAVDSLLNYETVKYFGNEAREARRYDEALARyeraaVKSqtslalLNFGQALIIAL--------GL---TAMMLMA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 431 GQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHL-EGLVQFQDVS 509
Cdd:COG5265 285 AQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVgGGEVRFENVS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 510 FAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP 588
Cdd:COG5265 365 FGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 QVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLIL 666
Cdd:COG5265 442 VLFNDTIAYNIAYG---RPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 667 DDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY---WAMVQ 741
Cdd:COG5265 519 DEATSALDSRT----ERAIQAALREVArgRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYaqmWARQQ 594
|
....*..
gi 2203400792 742 APADAPE 748
Cdd:COG5265 595 EEEEAEE 601
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
200-478 |
2.98e-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: 247.61 E-value: 2.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2203400792 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18784 251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
226-736 |
1.56e-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: 1.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 226 RNLTLMSILTIAS---AVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQ----ETEFFQQNQTGNIMSRVTEdTSTLSDS 298
Cdd:TIGR01846 173 RGLSTLSVLALAMlavAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHllglPLGYFESRRVGDTVARVRE-LEQIRNF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 299 LSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKwyqLLEVQVRESLAKSSQVA---IEALSAMP 375
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP---ILRKRVEDKFERSAAATsflVESVTGIE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 376 TVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFT 455
Cdd:TIGR01846 329 TIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVT 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 456 QAVEVLLSIYPRVQKAVGSSEKIFEYLDrTPRCP-PSGLLTPLHLEGLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEV 533
Cdd:TIGR01846 409 QPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPrSAGLAALPELRGAITFENIRFRYaPDSPEVL--SNLNLDIKPGEF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 534 TALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEIT 613
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 614 AAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPEryS 693
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--G 642
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2203400792 694 RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 736
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
501-734 |
9.74e-75 |
|
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: 9.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 501 GLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 661 PCVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 734
Cdd:cd03254 158 PKILILDEATSNIDTET----EKLIQEALEKLMkgRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
503-737 |
2.51e-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: 240.60 E-value: 2.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 663 VLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYW 737
Cdd:cd03251 159 ILILDEATSALDTES----ERLVQAALERLMknRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
254-736 |
2.83e-70 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 241.08 E-value: 2.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 254 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 329
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 330 VTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 409
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 410 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 488
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 489 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP 568
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 569 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQR 648
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQ 728
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
....*...
gi 2203400792 729 LMEKKGCY 736
Cdd:PRK11176 565 LLAQNGVY 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
175-742 |
8.68e-70 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 239.86 E-value: 8.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 175 RLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWIlqdgsadtfTRNLTLMSILTIasavleFVGDGIYNnTMG 254
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAI---------SGKGDIFPLLAA------WAGFGLFN-IIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 255 HV----------HSHLQG---EVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLS----DSLSENLSLFLWYLVrglcLL 317
Cdd:PRK13657 73 GVlvarhadrlaHRRRLAvltEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVV----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 318 GIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklqei 397
Cdd:PRK13657 149 PLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALR------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 398 KTLNQKEAVAYAVNSW------TTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:PRK13657 223 DIADNLLAAQMPVLSWwalasvLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 472 VGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAAL 550
Cdd:PRK13657 303 APKLEEFFEVEDAVPdVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 551 LQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGL 628
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 629 PQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQ 708
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN 535
|
570 580 590
....*....|....*....|....*....|....
gi 2203400792 709 ADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
503-742 |
1.41e-68 |
|
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: 225.19 E-value: 1.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 662 CVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 739
Cdd:cd03253 157 PILLLDEATSALDTHT----EREIQAALRDVSkgRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
...
gi 2203400792 740 VQA 742
Cdd:cd03253 233 WKA 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
503-741 |
2.40e-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: 221.98 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 662 CVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
503-718 |
5.83e-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: 218.41 E-value: 5.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevdeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 663 VLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
501-720 |
3.00e-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: 205.13 E-value: 3.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 501 GLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGRSLQENIAYGLtQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
200-458 |
2.75e-59 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 201.72 E-value: 2.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 278 QNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 2203400792 438 AVSSGNLVTFVLYQMQFTQAV 458
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-742 |
1.04e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 211.91 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 FFQQNQTGNIMSRVTeDTSTLSDSL-SENLSLFL--WYLVrglcLLGIML-WGSVSLTMVTLITLPLLFLLPKKVGKWYQ 350
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 351 LLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQK----FREKLQEIKTLNQKEAVAYAVNSWTTSIsgmlLKVGI 426
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLI----LNVVI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 427 LYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQF 505
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYP-NRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAV 584
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 GQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 665 ILDDATSALDANSQLQ-VEQLLYESperySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:TIGR01193 634 ILDESTSNLDTITEKKiVNNLLNLQ----DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
233-741 |
4.80e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 207.65 E-value: 4.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 233 ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDslsenlslfLWYLV- 311
Cdd:PRK10790 73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---------LYVTVv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 312 ----RGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEV----QVRESLAKSSQVAIEALSAMPTVRSFANE 383
Cdd:PRK10790 144 atvlRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 384 egeaQKFREKLQEIKTLNqkeavaYAVNSWTTSISGMLLK-----------VGILYIGGqLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK10790 224 ----ARFGERMGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 453 QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRtPRCPPSGLLTPLHlEGLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGE 532
Cdd:PRK10790 293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 533 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltQKPTMEEI 612
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 613 TAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRY 692
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--RE 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2203400792 693 SRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK10790 525 HTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
358-732 |
3.88e-56 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 201.52 E-value: 3.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 358 ESLAKSSQVaIEALSAMPTVRsfaneegeaQKFREKLQEIKTLNqkeAVAYAVNSWTTSIS---GMLLKVGILYIGGQLV 434
Cdd:COG4618 198 EAALRNAEV-IEAMGMLPALR---------RRWQRANARALALQ---ARASDRAGGFSALSkflRLLLQSAVLGLGAYLV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 435 TSGAVSSGN------LVTFVLyqmqftQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPlHLEGLVQFQDV 508
Cdd:COG4618 265 IQGEITPGAmiaasiLMGRAL------APIEQAIGGWKQFVSARQAYRRLNELLAAVPA-EPERMPLP-RPKGRLSVENL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 509 SFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP 588
Cdd:COG4618 337 TVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 QVFGRSLQENIAyGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:COG4618 416 ELFDGTIAENIA-RFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 669 ATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
471-715 |
3.75e-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: 195.20 E-value: 3.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 471 AVGSSEKIFEYLDRTPR-CPPSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAA 549
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRpLAGKAPVTAAPASSLE-FSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 550 LLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLP 629
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 630 QGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVE 707
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEALRALAqgRTVLLVTHRLALAA 521
|
....*...
gi 2203400792 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 |
1.42e-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: 185.63 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 420 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 498
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPsRDPAMPLPEP-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 499 lEGLVQFQDVSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 578
Cdd:TIGR01842 314 -EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALI 658
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
270-739 |
2.69e-50 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 185.30 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 270 RQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIM-LWGSVSLTMVTLITLPLLFLLPKKVGKw 348
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGD- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 349 yqllevQVRESLaKSSQVAI--------EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSIS-G 419
Cdd:PRK10789 160 ------QLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAiG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 420 M--LLKVGilyiGGQ-LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPpSGLLTP 496
Cdd:PRK10789 233 ManLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 576
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALA 654
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 734
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*
gi 2203400792 735 CYWAM 739
Cdd:PRK10789 542 WYRDM 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
385-741 |
2.12e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 177.32 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 385 GEAQKFREKL--QEIKTLNQKEAVAyavnswttSISGM----------LLKVGILYIGGQLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK11160 217 GAEDRYRQQLeqTEQQWLAAQRRQA--------NLTGLsqalmilangLTVVLMLWLAAGGVGGNAQPGALIALFVFAAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 453 QftqAVEVLLSI---YPRVQKAVGSSEKIFEYLDRTP--RCPPSGLLTPLHleGLVQFQDVSFAYPNRPDvLVLQGLTFT 527
Cdd:PRK11160 289 A---AFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 528 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKp 607
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 608 TMEEITAAAVKSGAHSFISGlPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYE 687
Cdd:PRK11160 442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 688 SPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK11160 521 HAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
503-733 |
7.18e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.35 E-value: 7.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GahsfISGLpqgydteVDEAGSQLSGGQRQAVALAR 655
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFGPENlglpREEIRERVEEALELvG----LEHL-------ADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKK 733
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
258-703 |
2.19e-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: 173.32 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 258 SHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 322
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvivpagvalvvGAAAVAAIAVLSVPAALILAAGLLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 323 GSVSLTMVTLitlpllfllpkKVGKWYQLLEVQVRESLAkssQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 402
Cdd:TIGR02868 166 AGFVAPLVSL-----------RAARAAEQALARLRGELA---AQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 403 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 483 DRTPRCP----PSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLE-LRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 559 GGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 636
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 637 DEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHL 703
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
200-478 |
9.41e-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: 165.20 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 2203400792 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
501-725 |
3.75e-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: 161.12 E-value: 3.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 501 GLVQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGRSLQENIAygltqkP----TMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALAR 655
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT 725
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
521-671 |
7.69e-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 or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.81 E-value: 7.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQENI 599
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 600 AYGLtqkpTMEEITAAAVKSGAHSFISGLPQGY--DTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
469-739 |
1.80e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 168.87 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 469 QKAVGSSEKIFEYLDrTPRCPPSGLLTPLHLEGLVQF--QDVSfaypnrpdVLVLQG------LTFTLRPGEVTALVGPN 540
Cdd:PRK11174 315 AQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIeaEDLE--------ILSPDGktlagpLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 541 GSGKST-VAALLQNL-YQptgGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKPTM--EEITAAA 616
Cdd:PRK11174 386 GAGKTSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 617 VKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPERYSRS- 695
Cdd:PRK11174 460 ENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS----EQLVMQALNAASRRq 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2203400792 696 -VLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 739
Cdd:PRK11174 536 tTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
502-722 |
2.73e-44 |
|
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: 158.82 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEHRYL 577
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQEPQ-----VF--GRSLQE--NIAYGLTQKPTMEEITAAAVKSGahsfisGLPQGYdteVDEAGSQLSGGQR 648
Cdd:cd03257 81 RKEIQMVFQDPMsslnpRMtiGEQIAEplRIHGKLSKKEARKEAVLLLLVGV------GLPEEV---LNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIRE 722
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
202-478 |
1.85e-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: 158.83 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQ-DGSADTFTRNLT-----LMSILTIASA-------VLEFVGDGIYNNtmghvhshLQGEVFGAV 268
Cdd:cd18573 13 MSVPFAIGKLIDVASKeSGDIEIFGLSLKtfalaLLGVFVVGAAanfgrvyLLRIAGERIVAR--------LRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 269 LRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKW 348
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 349 YQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILY 428
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
504-720 |
2.40e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.74 E-value: 2.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRylhRQ 580
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppEWR---RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPQGY-DTEVDEagsqLSGGQRQAVALARA 656
Cdd:COG4619 76 VAYVPQEPALWGGTVRDNLPFPFQlreRKFDRERALELLER-----L--GLPPDIlDKPVER----LSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
502-730 |
3.00e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 156.74 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQV-FGRSLQENIAYGLT------QKPTME--EITAAAVKS-GAHSFIsglpqgyDTEVDEagsqLSGGQRQAV 651
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRYphlglfGRPSAEdrEAVEEALERtGLEHLA-------DRPVDE----LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 730
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
473-731 |
4.05e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 163.54 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 473 GSSEKIFEY---LDRTPRCPPSGLLTPLHLEG---LVQFQDVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGK 544
Cdd:COG1123 225 GPPEEILAApqaLAAVPRLGAARGRAAPAAAAaepLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 545 STVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP--QVFGR-SLQENIAYGLTQKPTMeeiTAAAVK 618
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPysSLNPRmTVGDIIAEPLRLHGLL---SRAERR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 619 SGAHSFIS--GLPQGYdteVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSV 696
Cdd:COG1123 382 ERVAELLErvGLPPDL---ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTY 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 2203400792 697 LLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:COG1123 459 LFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-731 |
2.00e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 154.58 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:COG1124 1 MLEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEP-------QVFGRSLQE--NIAYGLTQKPTMEEItAAAVksgahsfisGLPQGYdteVDEAGSQLSGGQRQAV 651
Cdd:COG1124 81 VQMVFQDPyaslhprHTVDRILAEplRIHGLPDREERIAEL-LEQV---------GLPPSF---LDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 730
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 2203400792 731 E 731
Cdd:COG1124 228 A 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
233-741 |
8.36e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 164.82 E-value: 8.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 233 ILTIASAVleFVGDGI---YNNTMGH-VHSHLQGEVFGAVLRQETEFFQQ--NQTGNIMSRVTEDTSTLSDSLSENLSLF 306
Cdd:PTZ00265 872 ILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 307 LWYLVRGL---------C-LLGIMLWGSVSLTM----VTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAI-EAL 371
Cdd:PTZ00265 950 THFIVLFLvsmvmsfyfCpIVAAVLTGTYFIFMrvfaIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIqEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 372 SAMPTVRSFANEE------GEAQKFREKLQEIKTLnqkeavayaVNS--WTTSISGMLLKVGILY-IGGQLVTSGAVSSG 442
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTL---------VNSmlWGFSQSAQLFINSFAYwFGSFLIRRGTILVD 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 443 NLVTfVLYQMQFTQAVE-VLLSIYPRVQKAVGSSEKIFEYLDRTP----------RCPPSGLLtplhlEGLVQFQDVSFA 511
Cdd:PTZ00265 1101 DFMK-SLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSnidvrdnggiRIKNKNDI-----KGKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 512 YPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY------------QPTG-------------------- 559
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 560 ----------------------GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAV 617
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 618 KSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVL 697
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 698 LITQHLSLVEQADHILFLE-----GGAIREGGTHQQLME-KKGCYWAMVQ 741
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
502-734 |
1.57e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.85 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlPQYEHRYLHRQV 581
Cdd:COG4555 1 MIEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVDEagsqLSGGQRQAVALARALIRK 660
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLL---YESPerysRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKG 734
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILralKKEG----KTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
504-718 |
2.09e-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: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKSGAhsfISGLPqgydtevDEAGSQLSGGQRQAVALARAL 657
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALELVG---LEGLR-------DRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGG 718
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
201-478 |
1.85e-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: 147.70 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 2203400792 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd07346 255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
502-731 |
4.55e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.98 E-value: 4.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGKPLPQYEHRYLH 578
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYGL-TQKPTMEEITAAAVKSGAhsfISGLPQGYDTEVDeagsQLSGGQRQAVALAR 655
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALeNLGLSRAEARARVLELLE---AVGLERRLDRYPH----QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
503-718 |
6.40e-39 |
|
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: 142.99 E-value: 6.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPDV--LVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQPTGgqllldgkplpqyeHRYLHR 579
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGRSLQENIAYGltqKPTMEE-----ITAAAVKSGahsfISGLPQGYDTEVDEAGSQLSGGQRQAVALA 654
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFG---KPFDEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 655 RALIRKPCVLILDDATSALDAnsqlQVEQLLYES----PERYSRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
503-732 |
1.05e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.67 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQVA 582
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGR-SLQENI-----AYGLTQKPTMEEITA--AAVksgahsfisGLPQGYDTEVdeagSQLSGGQRQAVALA 654
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDEllELF---------GLTDAADRKV----GTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 732
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
506-720 |
1.13e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.42 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVg 585
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 qePQVfgrslqeniaygltqkptMEEITAAAVksgAHSFIsglpqgydtevdeagSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03214 79 --PQA------------------LELLGLAHL---ADRPF---------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 666 LDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
503-722 |
2.04e-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: 142.23 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNR-PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyehryLHRQV 581
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFG-RSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLpQGYdteVDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLE----LQGVPKAEARERAEELLElvGL-SGF---ENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqHlSLVEQ---ADHILFLEG--GAIRE 722
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVT-H-DIDEAvflADRVVVLSArpGRIVA 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
503-724 |
7.23e-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: 138.99 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRyLHRQVA 582
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevdeaGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 663 VLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGG 724
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
504-720 |
1.32e-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: 138.12 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevdeagsqLSGGQRQAVALARALIRKPCV 663
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 664 LILDDATSALDansqLQVEQLLYESPERYS---RSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:cd03246 118 LVLDEPNSHLD----VEGERALNQAIAALKaagATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
504-718 |
1.37e-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: 137.76 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VgqepqvfgrslqeniaygltqkptmeeitaaavksgahsfisglpqgydtevdeagSQLSGGQRQAVALARALIRKPCV 663
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 664 LILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQA-DHILFLEGG 718
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
503-729 |
4.77e-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: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTGGQLLLDGKPL--PQYEHR 575
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKsgahsfISGLPQgydtEVDE--AGSQLSGGQR 648
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALR------KAALWD----EVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQA----DHILFLEGGAIREGG 724
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNM---QQAarvaDRTAFLLNGRLVEFG 222
|
....*
gi 2203400792 725 THQQL 729
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
202-478 |
5.89e-37 |
|
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: 140.46 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFT-RNLTLMSILTIasaVLEFVGDGIYN-------NTMGH-VHSHLQGEVFGAVLRQE 272
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEaLRALNQAVLIL---LGVVLIGSIATflrswlfTLAGErVVARLRKRLFSAIIAQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 273 TEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLL 352
Cdd:cd18780 90 IAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQ 432
Cdd:cd18780 170 SKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGR 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2203400792 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18780 250 LVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
255-746 |
6.81e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 149.74 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 255 HVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLF---LWYLVRGLCLLG----IMLWGSVSL 327
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQLLSTFALIGtvstISLWAIMPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 328 TMVTLITLPllfllpkkvgkWYQLLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFaneegeaqKFREKLQEIKTLNQK 403
Cdd:PLN03232 1060 LILFYAAYL-----------YYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY--------KAYDRMAKINGKSMD 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 404 EAVAYAV-----NSWTT----SISGML--LKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAV 472
Cdd:PLN03232 1121 NNIRFTLantssNRWLTirleTLGGVMiwLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSL 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 473 GSSEKIFEYLDRTPRC--------PPSGLltplHLEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNGSG 543
Cdd:PLN03232 1201 NSVERVGNYIDLPSEAtaiiennrPVSGW----PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAG 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 544 KSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITA----AAVKS 619
Cdd:PLN03232 1275 KSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDAdlweALERA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 620 GAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLI 699
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVI 1426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 700 TQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG-CYWAMVQA--PADA 746
Cdd:PLN03232 1427 AHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHStgPANA 1476
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
202-478 |
1.25e-35 |
|
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: 136.46 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 282 GNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSS 441
Cdd:cd18576 173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 2203400792 442 GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18576 253 GDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
268-741 |
3.34e-35 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 144.32 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 268 VLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLlpkkVGK 347
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF----VQR 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 348 WYQLLEVQVR--ESLAKSSQVA--IEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKEAVAYAV-NSWttsisgmlL 422
Cdd:TIGR00957 1124 FYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVaNRW--------L 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 423 KVGILYIGGQLVTSGAV---------SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP---- 489
Cdd:TIGR00957 1192 AVRLECVGNCIVLFAALfavisrhslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiq 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 490 ----PSGLLTplhlEGLVQFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL 564
Cdd:TIGR00957 1272 etapPSGWPP----RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQL 643
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREG 723
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
490
....*....|....*...
gi 2203400792 724 GTHQQLMEKKGCYWAMVQ 741
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSMAK 1518
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
500-722 |
4.03e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyehryLH 578
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVFG-RSLQENIAYGL-TQKPTMEEITAAAVK-------SG-AHSFisglPqgydtevdeagSQLSGGQR 648
Cdd:COG1116 80 PDRGVVFQEPALLPwLTVLDNVALGLeLRGVPKAERRERAREllelvglAGfEDAY----P-----------HQLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqH-----LSLveqADHILFLEG--GAIR 721
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT-HdvdeaVFL---ADRVVVLSArpGRIV 220
|
.
gi 2203400792 722 E 722
Cdd:COG1116 221 E 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-740 |
6.39e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 143.25 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 369 EALSAMPTVRSFANEEGEAQKFR--EKLQEIKTL--NQKEAVAYAVnswttsISGMLL---KVGILYiGGQLVTSGAVSS 441
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNlsEKLYSKYILkaNFMESLHIGM------INGFILasyAFGFWY-GTRIIISDLSNQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 442 --------GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYP 513
Cdd:PTZ00265 314 qpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYD 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL-DGKPLPQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 RSLQENIAYGLTQKPTME--------------------------------------------------------EITAAA 616
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 617 VKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSV 696
Cdd:PTZ00265 554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 697 LLITQHLSLVEQADHILFL-----------------------------------------------EGGAIREGGTHQQL 729
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDAL 713
|
490
....*....|..
gi 2203400792 730 ME-KKGCYWAMV 740
Cdd:PTZ00265 714 MKnKNGIYYTMI 725
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
503-718 |
1.08e-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: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhRQVA 582
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGR-SLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevdeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 662 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
503-733 |
1.27e-34 |
|
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: 132.94 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-KPLPQYEHRYLHRQV 581
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFIsglpqgydtevDEAGSQLSGGQRQAVALA 654
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvprEEMRKRVDEALKLvGMEDFR-----------DREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKK 733
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
502-727 |
4.54e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLqNLYQPTGGQLLLDGKPLPQYEHR--YLh 578
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRRigYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 rqvaavgqePQvfgrslQENIAYGLtqkP-TMEEItaaaVKSGAHSFIsGLPQGYDTE----VDEA----G--------- 640
Cdd:COG1121 81 ---------PQ------RAEVDWDF---PiTVRDV----VLMGRYGRR-GLFRRPSRAdreaVDEAlervGledladrpi 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGA 719
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREyFDRVLLLNRGL 216
|
....*...
gi 2203400792 720 IREGGTHQ 727
Cdd:COG1121 217 VAHGPPEE 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
503-720 |
1.36e-33 |
|
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: 128.41 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVF-GRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisglpqGYDTEVDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03259 73 NIGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELV------GLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAI 720
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
503-720 |
6.05e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 126.45 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YL 577
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQEPQVFGR-SLQENIAYGL----TQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVdeagSQLSGGQRQAVA 652
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagVPKKERRERAEELLER------VGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
503-718 |
9.96e-33 |
|
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: 124.61 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE--HRYLHRQ 580
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVF-GRSLQENIAYGltqkptmeeitaaavksgahsfisglpqgydtevdeagsqLSGGQRQAVALARALIR 659
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
502-722 |
2.21e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST---VAALLQnlyQPTGGQLLLDGKPLpqyeHRYL 577
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDI----SSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAA--------VGQEPQVFGR-SLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE-VDEA----G--- 640
Cdd:COG1136 77 ERELARlrrrhigfVFQFFNLLPElTALENVALPLL--------------------LAGVSRKERRErARELlervGlgd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 ------SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILF 714
Cdd:COG1136 137 rldhrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIR 216
|
....*...
gi 2203400792 715 LEGGAIRE 722
Cdd:COG1136 217 LRDGRIVS 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
502-719 |
3.43e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 124.13 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTGGQLLLDGKPLPQYEHRYlH 578
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVFGR-SLQENIA-----YGLtqKPTMEEITAAAVKSGahsfISGLpqgydteVDEAGSQLSGGQRQAVA 652
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGL--RADREAIDEALEAVG----LAGL-------ADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRS--VLLITQHLSLVEQADHILFLEGGA 719
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELI----AAHLARggAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
500-731 |
4.05e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 4.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GAHSFIsglpqgydtevDEAGSQLSGGQRQAVA 652
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENigvpREEMVERVDQALRQvGMEDFL-----------NREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLME 731
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
502-725 |
1.93e-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: 122.69 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYL 577
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQEPQVF-GRSLQENIAYGLtqkptmeEITA---AAVKSGAHSFIS--GLpqgYDTEvDEAGSQLSGGQRQAV 651
Cdd:cd03258 81 RRRIGMIFQHFNLLsSRTVFENVALPL-------EIAGvpkAEIEERVLELLElvGL---EDKA-DAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
506-731 |
4.31e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.87 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-----PQyehrylHRQ 580
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpPR------ERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFgR--SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGL----PqgydtevdeagSQLSGGQRQAVAL 653
Cdd:COG1118 77 VGFVFQHYALF-PhmTVAENIAFGLRVRPPSKAEIRARVEELLELVqLEGLadryP-----------SQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqH-----LSLveqADHILFLEGGAIREGGTHQQ 728
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVT-HdqeeaLEL---ADRVVVMNQGRIEQVGTPDE 220
|
...
gi 2203400792 729 LME 731
Cdd:COG1118 221 VYD 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
503-723 |
5.06e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.79 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEP--QVFGRSLQENIAYGLTQK----PTMEE-ITAAAVKSGAHSFISGLPQgydtevdeagsQLSGGQRQAVALAR 655
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvppKKMKDiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHIL-FLEGGAIREG 723
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIvFSEGKLIAQG 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
503-732 |
5.88e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 121.68 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevdeagSQLSGGQRQAVALARA 656
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLIT--QHLSLvEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVThdQEEAL-EVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
504-723 |
7.76e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 7.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhrqvaa 583
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VGQEPQvfgrslQENIAYGLtqkP-TMEEItaaaVKSGAHSFIsGLPQGYDTE----VDEA----G---------SQLSG 645
Cdd:cd03235 70 IGYVPQ------RRSIDRDF---PiSVRDV----VLMGLYGHK-GLFRRLSKAdkakVDEAlervGlseladrqiGELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 646 GQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREG 723
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEyFDRVLLLNRTVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
503-729 |
8.36e-31 |
|
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: 121.07 E-value: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP---QYEHRYLHR 579
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPQgydtEVDEAGSQLSGGQRQA 650
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREivleklEAV---------GLRG----AEDLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQL 729
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-720 |
1.19e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.67 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhRQVAAVGQ 586
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSgahsfisglpQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKD----------LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 665 ILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAI 720
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
503-722 |
1.97e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.69 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLY---QPTGGQLLLDGKPLPQYEHR---Y 576
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQEPQ-VFGRSLQENIAY-----GLTQKPTMEEITAAAVKSG----AHSFIsglpqgydtevdeagSQLSGG 646
Cdd:COG2884 77 LRRRIGVVFQDFRlLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGlsdkAKALP---------------HELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRS---VLLITQHLSLVEQADH-ILFLEGGAIRE 722
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL----EEINRRgttVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
504-730 |
2.31e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.78 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRPdvlvlqgLTFTL--RPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylh 578
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVFGR-SLQENIAYGLTQ--KPTMEE---ITAAAVKSGAHSFISGLPqgydtevdeagSQLSGGQRQAVA 652
Cdd:COG3840 71 RPVSMLFQENNLFPHlTVAQNIGLGLRPglKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 653 LARALIRKPCVLILDDATSALDANsqLQVE--QLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
.
gi 2203400792 730 M 730
Cdd:COG3840 218 L 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
506-730 |
4.15e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.75 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQV-FGRSLQENIAYGLTQKPTM----EEITAAAVksgahsfisglpqgydTEVDEAG------SQLSGGQRQAVALA 654
Cdd:COG4559 82 QHSSLaFPFTVEEVVALGRAPHGSSaaqdRQIVREAL----------------ALVGLAHlagrsyQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 655 RALI-------RKPCVLILDDATSALDANSQLQVEQLLYespeRYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREG 723
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLAR----QLARrggGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
....*..
gi 2203400792 724 GTHQQLM 730
Cdd:COG4559 222 GTPEEVL 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
502-725 |
5.69e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.05 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehryl 577
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglpPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQEPQVFG-RSLQENIAYGLTQ----KPTMEEITAAAVK----SG-AHSFIsglpqgydtevdeagSQLSGGQ 647
Cdd:COG3842 76 KRNVGMVFQDYALFPhLTVAENVAFGLRMrgvpKAEIRARVAELLElvglEGlADRYP---------------HQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSALDAN--SQLQVE--QLLyespERYSRSVLLITqH-----LSLveqADHILFLEGG 718
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKlrEEMREElrRLQ----RELGITFIYVT-HdqeeaLAL---ADRIAVMNDG 212
|
....*..
gi 2203400792 719 AIREGGT 725
Cdd:COG3842 213 RIEQVGT 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
526-724 |
8.60e-29 |
|
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: 114.31 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 526 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----------PQyehrylHRQVAAVGQEPQV 590
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQ------QRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 FGR-SLQENIAYGLTQKPTMEE-ITAAAVKSGAHsfISGLPQGYDtevdeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03297 87 FPHlNVRENLAFGLKRKRNREDrISVDELLDLLG--LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 669 ATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
506-730 |
1.02e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.64 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQV-FGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFisglpqgydtevdeAGS---QLSGGQRQAVALARA 656
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIR------KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228
|
.
gi 2203400792 730 M 730
Cdd:PRK13548 229 L 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
500-731 |
1.23e-28 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 114.69 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRY 576
Cdd:COG1127 3 EPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQEPQVFGrSL--QENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPqgydtevdEAG----SQ 642
Cdd:COG1127 80 LRRRIGMLFQGGALFD-SLtvFENVAFPLREHTDLseAEIRElvleklELV---------GLP--------GAAdkmpSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIR 721
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLdSAFAIADRVAVLADGKII 221
|
250
....*....|
gi 2203400792 722 EGGTHQQLME 731
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
490-731 |
1.42e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 120.94 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 490 PSGLLTPLHLEG--LVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQnLyQPT 558
Cdd:COG4172 261 PRGDPRPVPPDAppLLEARDLKVWFPIKRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 559 GGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPqvFGrSL------QENIAYGLT-QKPTM-----EEITAAAVKSgahs 623
Cdd:COG4172 339 EGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP--FG-SLsprmtvGQIIAEGLRvHGPGLsaaerRARVAEALEE---- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 624 fiSGLPQG----YDTEvdeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLI 699
Cdd:COG4172 412 --VGLDPAarhrYPHE-------FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFI 482
|
250 260 270
....*....|....*....|....*....|...
gi 2203400792 700 TQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:COG4172 483 SHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
503-732 |
3.60e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevdeagsQLSGGQRQAVA 652
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRDVLADvGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
500-732 |
5.14e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYpNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13648 5 NSIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK--PT--MEEITAAAVKSgahsfisglPQGYDTEVDEAGSqLSGGQRQAVAL 653
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHavPYdeMHRRVSEALKQ---------VDMLERADYEPNA-LSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 732
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
497-731 |
5.61e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 115.15 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVqfqdVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYE 573
Cdd:COG0444 2 LEVRNLK----VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 574 HR----YLHRQVAAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPqgydte 635
Cdd:COG0444 77 EKelrkIRGREIQMIFQDPMtslnpVMtvGDQIAEPLR--IHGGLSKAEARERAIEllervglPDPERRLDRYP------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 636 vdeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILF 714
Cdd:COG0444 149 -----HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*..
gi 2203400792 715 LEGGAIREGGTHQQLME 731
Cdd:COG0444 224 MYAGRIVEEGPVEELFE 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
503-682 |
7.67e-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: 112.33 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHsfISGLpQGYDtevDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALD--LVQL-EGYA---NRKPSQLSGGQQQRVAIARALV 146
|
170 180
....*....|....*....|....*.
gi 2203400792 659 RKPCVLILDDATSALDAN--SQLQVE 682
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKlrKDMQLE 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
503-724 |
8.04e-28 |
|
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: 111.58 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhR 579
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisglpqGYDTEVDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQH----LSLveqADHILFLEGGAIREGG 724
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqveaMTM---ADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
502-729 |
8.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisglpqGYDTEVDEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQL 729
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
520-731 |
9.81e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 111.76 E-value: 9.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP-QYEHRYLHRQVAAVGQEPQVFGR-SLQE 597
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITgLPPHERARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 598 NI---AYGLTQ---KPTMEEItaaavksgahsfisglpqgYD------TEVDEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03224 95 NLllgAYARRRakrKARLERV-------------------YElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 666 LDDATSALdanSQLQVEQlLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:cd03224 156 LDEPSEGL---APKIVEE-IFEAIRELRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
504-720 |
1.12e-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: 112.28 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH---RQ 580
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaaavKSGAHSFISGLPQGYDTE--------VDEAG---------SQ 642
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSG---------------RLGRRSTWRSLFGLFPKEekqralaaLERVGlldkayqraDQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAI 720
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
502-725 |
1.16e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRYL---H 578
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYG-LTQKPTMEEItAAAVKSGAHSFisGLpQGYDtevDEAGSQLSGGQRQAVALAR 655
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEV-EKRVKEALKAV--GM-EGFE---NKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVE-QADHILFLEGGAIREGGT 725
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
503-730 |
1.30e-27 |
|
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: 112.01 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL----VPKLLKWPKEKIRERADELLAlvGLdPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
503-720 |
1.50e-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: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ--YEHRYLHRQ 580
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAAV----KSGAHSFISGLPqgydtevdeagSQLSGGQRQAVAL 653
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIkvKGMSKAEAEERALelleKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 654 ARALIRKPCVLILDDATSALD---ANSQLQVEQLLYESperySRSVLLITQHLSLV-EQADHILFLEGGAI 720
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
202-478 |
3.09e-27 |
|
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: 112.14 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdGIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQ-GYLAEKASQkVAYDLRNDLYDHLQRLSFSFHDKAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLG----IMLWGSVSLTMVTLIT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18542 95 TGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIipfiALFSYVFFKKVRPAFE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 evQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN-SWTTSISGMLLkVGILYIGG 431
Cdd:cd18542 169 --EIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYwPLMDFLSGLQI-VLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2203400792 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
203-478 |
3.76e-27 |
|
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: 112.13 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFFQQ 278
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEA----LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRvvrdLRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 279 NQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRE 358
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 359 SLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGA 438
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2203400792 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18552 253 LTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
499-720 |
3.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFISGLPqgydtevdeagSQLSGGQRQAV 651
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
499-729 |
4.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVK-SGAHSFISGLPqgydtevdeagSQLSGGQRQAV 651
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 729
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
502-722 |
4.81e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPN------RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--- 572
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 573 EHRYLHRQVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAhsfisGLPqgyDTEVDEAGSQLSG 645
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnprKTVREIIREPLRHLLSLDKAERLARASEMLRAV-----DLD---DSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 646 GQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIRE 722
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-746 |
5.57e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.30 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 266 GAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFL---WYLVRGLCLLGIM----LWGSVSLTMVTLITLPll 338
Cdd:PLN03130 994 GSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLFYGAYL-- 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 339 fllpkkvgkWYQLL--EVQVRESLAKSSQVAI--EALSAMPTVRsfaneegeAQKFREKLQEIKTLNQKEAVAYAV---- 410
Cdd:PLN03130 1072 ---------YYQSTarEVKRLDSITRSPVYAQfgEALNGLSTIR--------AYKAYDRMAEINGRSMDNNIRFTLvnms 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 411 -NSWttsisgmlLKVGILYIGG---QLVTSGAV----SSGNLVTF-------VLYQMQFTQAVEVLLSIYPRVQKAVGSS 475
Cdd:PLN03130 1135 sNRW--------LAIRLETLGGlmiWLTASFAVmqngRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 476 EKIFEYLDRTPRCP--------PSGLLTplhlEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKST 546
Cdd:PLN03130 1207 ERVGTYIDLPSEAPlviennrpPPGWPS----SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSS 1280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 547 VAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITAAAVKS--GAH-- 622
Cdd:PLN03130 1281 MLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlk 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 623 SFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQH 702
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHR 1432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2203400792 703 LSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWA-MVQA--PADA 746
Cdd:PLN03130 1433 LNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMVQStgAANA 1479
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
502-685 |
8.02e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PqyeHRYL 577
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsP---RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQEPQVF-GRSLQENIA-------YGLTQKPTMEEITAAAVKS-GAHsfISglPqgyDTEVdeagSQLSGGQR 648
Cdd:COG1129 78 AAGIAIIHQELNLVpNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--ID--P---DTPV----GDLSVAQQ 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANsqlQVEQLL 685
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTER---EVERLF 180
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-478 |
9.14e-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: 111.03 E-value: 9.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPF--FTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVhSHLQG-----EVFGAVLRQETE 274
Cdd:cd18577 18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTIT-GERQArrirkRYLKALLRQDIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18577 97 WFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18577 177 KEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLV 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2203400792 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18577 257 RDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
501-725 |
1.40e-26 |
|
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: 107.88 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 501 GLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAavksgahsfisglpqgydTEVDEAGSQLSGGQRQAVALARALI 658
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESperYSRSVLLITQH-LSLVEQADHILFLEGGAIREGGT 725
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREE---FTNSTILTIAHrLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
502-715 |
3.56e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK10247 7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPqgyDTEVDEAGSQLSGGQRQAVALARALI 658
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFL 715
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
203-478 |
4.82e-26 |
|
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: 108.67 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSAdtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 283 NIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAK 362
Cdd:cd18551 94 DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 363 SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSG 442
Cdd:cd18551 174 LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVG 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 2203400792 443 NLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18551 254 TLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
521-712 |
1.36e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.28 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYLHRQVAAVGQEPqvfgrslqe 597
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 598 niaYG-LTQKPTMEEITAAAVKsgahsfISGL--PQGYDTEVDEAGS--------------QLSGGQRQAVALARALIRK 660
Cdd:COG4608 105 ---YAsLNPRMTVGDIIAEPLR------IHGLasKAERRERVAELLElvglrpehadryphEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEqadHI 712
Cdd:COG4608 176 PKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVR---HI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
503-720 |
2.22e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 104.80 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR---YLHR 579
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVF-GRSLQENIAYGLtqkptmeEITAAAVKSGAHSFISGLPQ-GYDTEVDEAGSQLSGGQRQAVALARAL 657
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFAL-------EVTGVPPREIRKRVPAALELvGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADH-ILFLEGGAI 720
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
506-730 |
2.31e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQV-FGRSLQENIAYG----------LTQKPtmEEITAAAVKsgahsfisglpqgyDTEVDEAG----SQLSGGQRQA 650
Cdd:PRK11231 83 QHHLTpEGITVRELVAYGrspwlslwgrLSAED--NARVNQAME--------------QTRINHLAdrrlTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSlveQA----DHILFLEGGAIREGGTH 726
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTP 222
|
....
gi 2203400792 727 QQLM 730
Cdd:PRK11231 223 EEVM 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
502-731 |
2.55e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.17 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLHR 579
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFGR-SLQENIAYGLTQkptmeeiTAAAVKSGAHSFISGL--PQGYDTEVDEAGSQLSGGQRQAVALARA 656
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLR-------VRGASKEEAEKQARELlaKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 657 LIRKPCVLILDDATSALDANSQ---LQVEQLLYESperySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
203-478 |
3.10e-25 |
|
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: 106.41 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAV-----LEFVgdgiynNTMG-HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALasalrFYLV------SWLGeRVVADLRKAVFAHLLRLSPSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 277 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18575 88 ETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:cd18575 168 QDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2203400792 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18575 248 GRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
203-478 |
5.62e-25 |
|
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: 105.95 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSA------DTFTRNLTLMSILTIASAVLEFvgdgIYNNTMGHVhshlqgeVFGAV--LRQETE 274
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSY----LQNRLMARV-------SQRTVydLRKDLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 ---------FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKV 345
Cdd:cd18547 86 eklqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 346 GKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkV 424
Cdd:cd18547 166 AKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-V 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18547 245 LVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
503-729 |
7.81e-25 |
|
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: 103.35 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqYEHRYLHRQVa 582
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 aVGQEPQvfGRSL------QENIAY-----GLTQKPTMEEITAAAVKsgahsfiSGLPQGYDTEVdeagSQLSGGQRQAV 651
Cdd:cd03263 77 -LGYCPQ--FDALfdeltvREHLRFyarlkGLPKSEIKEEVELLLRV-------LGLTDKANKRA----RTLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
507-724 |
7.82e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 7.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EPQV-FGRSLQENIAYG----LTQKPTMEEITAAAVKSGAHSfisglpQGYDTEVDEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMER------TGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 662 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
490-729 |
9.35e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 490 PSGLLTPL--HLEGLVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 558
Cdd:PRK15134 261 PSGDPVPLpePASPLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 559 GGQLLLDGKPLPQYEHRYL---HRQVAAVGQEPQvfgRSL------QENIAYGLT-QKPTMeeiTAAAVKSgahSFISGL 628
Cdd:PRK15134 339 QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN---SSLnprlnvLQIIEEGLRvHQPTL---SAAQREQ---QVIAVM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 629 PQ-GYDTEVDEA-GSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV 706
Cdd:PRK15134 410 EEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
250 260
....*....|....*....|....
gi 2203400792 707 EQADH-ILFLEGGAIREGGTHQQL 729
Cdd:PRK15134 490 RALCHqVIVLRQGEVVEQGDCERV 513
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
503-675 |
1.01e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 106.31 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehrylH 578
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlpPK------D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVF-GRSLQENIAYGLT-QKPTMEEItAAAVKSGAHSF-ISGL----PqgydtevdeagSQLSGGQRQAV 651
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPLKlRKVPKAEI-DRRVREAAELLgLEDLldrkP-----------KQLSGGQRQRV 142
|
170 180
....*....|....*....|....
gi 2203400792 652 ALARALIRKPCVLILDDATSALDA 675
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDA 166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
503-725 |
1.09e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.93 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYLH 578
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVFG-RSLQENIAYGLtqkptmeEIT---AAAVKSGAHSFIS--GLPqgydtevDEAG---SQLSGGQRQ 649
Cdd:COG1135 82 RKIGMIFQHFNLLSsRTVAENVALPL-------EIAgvpKAEIRKRVAELLElvGLS-------DKADaypSQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
515-725 |
1.20e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.10 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP------ 588
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 -----QVFGRSLQENIAygLTQKPTMEEITAAAVKSGAhsfisgLPqgydtevDEAG---SQLSGGQRQAVALARALIRK 660
Cdd:PRK15112 103 rqrisQILDFPLRLNTD--LEPEQREKQIIETLRQVGL------LP-------DHASyypHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
518-723 |
1.45e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 103.58 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYehrylhrQVAAVG-----QEPQ 589
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPH-------RIARLGiartfQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 590 VFGR-SLQENIAYGLTqkptmeeitaAAVKSGAHSFISGLPQGYDTE-------------------VDEAGSQLSGGQRQ 649
Cdd:COG0411 90 LFPElTVLENVLVAAH----------ARLGRGLLAALLRLPRARREEreareraeellervgladrADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGA-IREG 723
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRvIAEG 235
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
201-478 |
1.50e-24 |
|
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: 104.51 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFF 276
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERitadLRRDLYEHLQRLSLSFF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 277 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18563 95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEI----KTLNQKEAVAYAVNSWTTSISGMLlkvgILYIGGQ 432
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELldanIRAEKLWATFFPLLTFLTSLGTLI----VWYFGGR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2203400792 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18563 251 QVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
201-478 |
2.15e-24 |
|
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: 104.01 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYN---NTMG-HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18544 15 ELLGPLLIKRAIDDYIVPGQGDL--QGLLLLALLYLGLLLLSFLLQYLQTyllQKLGqRIIYDLRRDLFSHIQRLPLSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 277 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLIT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18544 93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVlpllLLATYLFRKKSRKAYR-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 evQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGG 431
Cdd:cd18544 171 --EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2203400792 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18544 248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
506-718 |
2.26e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.81 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTGGQLLLDGKPL-----PQY 572
Cdd:COG1117 15 RNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILLDGEDIydpdvDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 573 EHRylhRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKSgahsfiSGLpqgYDtEV----DEAGSQL 643
Cdd:COG1117 89 ELR---RRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIVEESLRK------AAL---WD-EVkdrlKKSALGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSlveQA----DHILFLEGG 718
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQ---QAarvsDYTAFFYLG 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
497-723 |
2.45e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.13 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVqfqdVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY-EHR 575
Cdd:cd03219 1 LEVRGLT----KRFG-----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQEPQVFGR-SLQENIaygltqkptmeeITAAAVKSGAHSFISGLPQGYDTEVDEAG-------------- 640
Cdd:cd03219 72 IARLGIGRTFQIPRLFPElTVLENV------------MVAAQARTGSGLLLARARREEREARERAEellervgladladr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 --SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03219 140 paGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRVTVLDQ 218
|
....*..
gi 2203400792 718 GA-IREG 723
Cdd:cd03219 219 GRvIAEG 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
500-733 |
2.82e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGQLLLDGKPL-- 569
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 570 PQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKsGAHSFISGLPQGYDTEVDeagsqLS 644
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVLDEAVEKSLK-GASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQADHI-----LFLEGGA 719
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSM---QQASRIsdrtgFFLDGDL 225
|
250
....*....|....
gi 2203400792 720 IREGGTHQQLMEKK 733
Cdd:PRK14239 226 IEYNDTKQMFMNPK 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
496-731 |
3.12e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 496 PLHLEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR 575
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQE-PQVFGRSLQENIA------------YGLTQKPTMEE-ITAAAVKSGAHSFisglpqgydteVDeags 641
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEaISLVGLKPLAHRL-----------VD---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
250
....*....|.
gi 2203400792 721 REGGTHQQLME 731
Cdd:PRK10575 227 IAQGTPAELMR 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
502-729 |
3.63e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLHR 579
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAA------VksgahsfisGLPqgydtevDEAG---SQLSGGQ 647
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLAPIkvKKMSKAEAEERAmellerV---------GLA-------DKADaypAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSALDansqlqveqllyesPERySRSVL-----LITQHLSLV----------EQADHI 712
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALD--------------PEL-VGEVLdvmrdLAKEGMTMVvvthemgfarEVADRV 206
|
250
....*....|....*..
gi 2203400792 713 LFLEGGAIREGGTHQQL 729
Cdd:COG1126 207 VFMDGGRIVEEGPPEEF 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-720 |
4.38e-24 |
|
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: 99.43 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqyehrylhrqvaavgqepqvfGRSL 595
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENIAYGLtqkptmeeitaAAVksgahsfisglpqgydtevdeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03216 70 RDARRAGI-----------AMV-----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 676 NsqlQVEQLLyespERYSR------SVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:cd03216 116 A---EVERLF----KVIRRlraqgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-734 |
5.95e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.29 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSWTTSISGMLLKV---GIL-YIGGQLVTSGAVS 440
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVQTVRddelSWFRKAQLLSAFNSFILNSIPVLVTVvsfGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 441 SGNL---VTFVLYQMQ--FTQAVEVLLSIyPRVQKAVGSSEKIFeyldrtprcppsgLLTPLHLEGL--VQFQDVSFAYP 513
Cdd:PLN03130 560 SLSLfavLRFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-------------LPNPPLEPGLpaISIKNGYFSWD 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFG 592
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFN 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 RSLQENIAYGLTQKPTMEEiTAAAVKSGAHSfISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 673 LDANSQLQV-EQLLYESPERYSRsvLLITQHLSLVEQADHILFLEGGAIREGGTH----------QQLMEKKG 734
Cdd:PLN03130 771 LDAHVGRQVfDKCIKDELRGKTR--VLVTNQLHFLSQVDRIILVHEGMIKEEGTYeelsnngplfQKLMENAG 841
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
503-720 |
6.53e-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: 100.26 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPDVLVLqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEE-----ITAAAVKSGAHSFISGLPQgydtevdeagsQLSGGQRQAVALARA 656
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGLKLTAedrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
504-715 |
7.55e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhRQ 580
Cdd:COG4525 5 TVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGAD-----RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VaaVGQEPQVFG-RSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLpQGYDtevDEAGSQLSGGQRQAVALARAL 657
Cdd:COG4525 80 V--VFQKDALLPwLNVLDNVAFGLR----LRGVPKAERRARAEELLAlvGL-ADFA---RRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHlslVEQAdhiLFL 715
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEA---LFL 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
520-732 |
1.32e-23 |
|
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: 100.10 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhRQVAAVGQEPQVFGR-SL 595
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENIAYGLTQKPTMEEITAAAVKSGAHSFisglpqGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEML------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 676 NSQLQVEQLLYESPERYSRSVLLITQhlSLVEQ---ADHILFLEGGAIREGGTHQQLMEK 732
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTH--DFEEAwalADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
517-731 |
1.45e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 100.06 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFGR-S 594
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQENI---AYGLTQKP----TMEEItaaavksgahsfisglpqgYDT--EVDE----AGSQLSGGQRQAVALARALIRKP 661
Cdd:COG0410 95 VEENLllgAYARRDRAevraDLERV-------------------YELfpRLKErrrqRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 662 CVLILDDATSALdanSQLQVEQlLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:COG0410 156 KLLLLDEPSLGL---APLIVEE-IFEIIRRLNRegvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
485-742 |
2.77e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.40 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 485 TPRCPPSGLLTPLHLEGLVqFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLL 563
Cdd:PTZ00243 1292 EPASPTSAAPHPVQAGSLV-FEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 564 LDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtmEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQL 643
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 644 SGGQRQAVALARALIRKPCVLIL-DDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQADHILFLEGGAIRE 722
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250 260
....*....|....*....|.
gi 2203400792 723 GGTHQQL-MEKKGCYWAMVQA 742
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEA 1545
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
202-455 |
3.34e-23 |
|
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: 100.56 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDwILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYNNT-MG---HVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18541 16 LLIPRIIGRAID-ALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLiFGasrRIEYDLRNDLFAHLLTLSPSFYQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 278 QNQTGNIMSRVTEDTSTLSDSLSENlslfLWYLVRGLCL----LGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLE 353
Cdd:cd18541 93 KNRTGDLMARATNDLNAVRMALGPG----ILYLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 354 VQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISGMLLKVG---ILYIG 430
Cdd:cd18541 169 RKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR---VDALFFPLIGLLIGLSfliVLWYG 245
|
250 260
....*....|....*....|....*
gi 2203400792 431 GQLVTSGAVSSGNLVTFVLYQMQFT 455
Cdd:cd18541 246 GRLVIRGTITLGDLVAFNSYLGMLI 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
520-729 |
3.52e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 599 IAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYdtEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ 678
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAH--LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 679 LQVEQLLYESPERYS-RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 729
Cdd:PRK10851 173 KELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-729 |
3.70e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-----LLDG-KPLPQYEH--RYLHRQVAAVGQEPQVF 591
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 592 -GRSLQENIAYG--LTQKPTMEEITAAAVKSGAHSFISGLPQGYDtevdeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11264 98 pHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 669 ATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQL 729
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
525-674 |
4.33e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyEHRYL---HRQVAAVGQEPQVFGR-SLQENIA 600
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 601 YGL--------TQKPTMEEItaaAVKSGAHSFISGLPqgydtevdeagSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK10771 94 LGLnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
..
gi 2203400792 673 LD 674
Cdd:PRK10771 160 LD 161
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
515-725 |
4.78e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLV--LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP- 588
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 ------QVFGRSLQENIAYGltqkptmEEITAAAVKSGAHSFIS--GL-PQGYDtevdEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11308 103 gslnprKKVGQILEEPLLIN-------TSLSAAERREKALAMMAkvGLrPEHYD----RYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
502-733 |
4.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHR---YLH 578
Cdd:PRK13636 5 ILKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGahsfISGLPqgydtevDEAGSQLSGGQRQAV 651
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTG----IEHLK-------DKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVE-QADHILFL-EGGAIREGGTHQQL 729
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMkEGRVILQGNPKEVF 230
|
....
gi 2203400792 730 MEKK 733
Cdd:PRK13636 231 AEKE 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
502-730 |
5.37e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH-RYLHRQ 580
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEP--QVFGRSLQENIAYG---LTQKPT--MEEITAAAVKSGAHSFISGLPQgydtevdeagsQLSGGQRQAVAL 653
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPIeiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
515-736 |
5.94e-23 |
|
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: 105.03 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTGgqllldgkplpqyeHRYLHRQVAAVGQEPQVFGR 593
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAYG--LTQKPTMEEITAAAVKSGahsfISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:TIGR00957 714 SLRENILFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 672 ALDANsqlqVEQLLYES---PERY--SRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 736
Cdd:TIGR00957 790 AVDAH----VGKHIFEHvigPEGVlkNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
511-715 |
9.63e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 511 AYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVAAVGQ---E 587
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 588 PQVFGRSLQENIAYGLTQK------PTME---EITAAAVKSGAHSFiSGLPqgydteVDEagsqLSGGQRQAVALARALI 658
Cdd:NF040873 67 PDSLPLTVRDLVAMGRWARrglwrrLTRDdraAVDDALERVGLADL-AGRQ------LGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFL 715
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
520-729 |
9.90e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyEHRYL-HRQVAAVGQEPQVFGR-SLQE 597
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIqQRDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 598 NIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGYdteVDeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:PRK11432 98 NVGYGLkMLGVPKEERKQRVKEALELVDLAGFEDRY---VD----QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 677 SQLQVEQLLYESPERYSRSVLLITQHLSlvEQ---ADHILFLEGGAIREGGTHQQL 729
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQS--EAfavSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
503-731 |
1.61e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG-----GQLLLDGKPLpqYEHRY- 576
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 ---LHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSgahsfiSGLPQGYDTEVDEAGSQLSGGQR 648
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGgthq 727
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGNENRIG---- 232
|
....
gi 2203400792 728 QLME 731
Cdd:PRK14258 233 QLVE 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
518-746 |
1.71e-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: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYL----HRQVAAVGQEpqvFG- 592
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQS---FAl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevdeagsQLSGGQRQAVALARALIRK 660
Cdd:cd03294 114 lphRTVLENVAFGLEvqgvpraerEERAAEALELVGLEGWEHKYPD---------------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQLmekkgcywam 739
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI---------- 248
|
....*..
gi 2203400792 740 VQAPADA 746
Cdd:cd03294 249 LTNPAND 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
497-729 |
4.47e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 100.53 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLvqfqDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQP---TGGQLLLDGKPL--- 569
Cdd:COG4172 7 LSVEDL----SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 570 PQYEHRYLH-RQVAAVGQEPQV-------FGRSLQENIA--YGLTQKPTMEEITA--AAVksgahsfisGLPqgyDTE-- 635
Cdd:COG4172 82 SERELRRIRgNRIAMIFQEPMTslnplhtIGKQIAEVLRlhRGLSGAAARARALEllERV---------GIP---DPErr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 636 VDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILF 714
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAV 229
|
250
....*....|....*
gi 2203400792 715 LEGGAIREGGTHQQL 729
Cdd:COG4172 230 MRQGEIVEQGPTAEL 244
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
487-742 |
6.86e-22 |
|
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: 95.75 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 487 RCPPSGLLTplhLEGLVQFQDVSFAYPN--RPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL 564
Cdd:cd03288 7 GSSNSGLVG---LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsFISGLPQGYDTEVDEAGSQ 642
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdpECKCTDDRLWEALEIAQLKN----MVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIRE 722
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
250 260
....*....|....*....|.
gi 2203400792 723 GGTHQQLMEKK-GCYWAMVQA 742
Cdd:cd03288 235 CDTPENLLAQEdGVFASLVRT 255
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
489-735 |
8.67e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 489 PPSGLLTPLHLEglvqFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP 568
Cdd:PRK13536 32 SIPGSMSTVAID----LAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 569 LPQyEHRYLHRQVAAVGQ----EPQVfgrSLQEN-IAYGLTQKPTMEEItaAAVKSGAHSFiSGLPQGYDTEVdeagSQL 643
Cdd:PRK13536 105 VPA-RARLARARIGVVPQfdnlDLEF---TVRENlLVFGRYFGMSTREI--EAVIPSLLEF-ARLESKADARV----SDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQlqveQLLYESperySRSVL------LITQHlsLVEQA----DHIL 713
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR----HLIWER----LRSLLargktiLLTTH--FMEEAerlcDRLC 243
|
250 260
....*....|....*....|...
gi 2203400792 714 FLEGG-AIREGGTHQQLMEKKGC 735
Cdd:PRK13536 244 VLEAGrKIAEGRPHALIDEHIGC 266
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
502-723 |
9.86e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR---YLH 578
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQAL--QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEPQVF-GRSLQENIAY-----GLTQKPTMEEITAAAVKSGAhsfisglpqgydteVDEAGS---QLSGGQRQ 649
Cdd:PRK10908 79 RQIGMIFQDHHLLmDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGL--------------LDKAKNfpiQLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITQHLSLVEQADH-ILFLEGGAIREG 723
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLHGG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
502-722 |
1.16e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 94.42 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--EHRYLH 578
Cdd:COG4181 8 IIELRGLTKTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQvAAVGQepqVFgRSLQ--------ENIAYGLtqkptmEEITAAAVKSGAHSFIS--GLPQgydtEVDEAGSQLSGGQR 648
Cdd:COG4181 88 RA-RHVGF---VF-QSFQllptltalENVMLPL------ELAGRRDARARARALLErvGLGH----RLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 722
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
520-718 |
1.38e-21 |
|
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: 93.00 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPLPQYEHRylhRQVAAVGQEPQVFGR-SLQ 596
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAYgltqkptmeeitAAAVKSgahsfisglpqgydtevdeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:cd03213 101 ETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2203400792 677 SQLQVEQLLYESPERySRSVLLITQHLS--LVEQADHILFLEGG 718
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQG 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
503-725 |
1.43e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.79 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRYLH 578
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEpqvF----GRSLQENIAYGLTqkptmeeitaaavksgahsfISGLPQG-YDTEVDE----AG--------- 640
Cdd:PRK11153 82 RQIGMIFQH---FnllsSRTVFDNVALPLE--------------------LAGTPKAeIKARVTEllelVGlsdkadryp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGA 719
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGR 218
|
....*.
gi 2203400792 720 IREGGT 725
Cdd:PRK11153 219 LVEQGT 224
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
202-478 |
1.75e-21 |
|
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: 95.61 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHV------------HSHLQGEVFGavl 269
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGD----LSGLLIIALLFLALNLVNWVASRLRIYLMAKVgqrilydlrqdlFSHLQKLSFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 270 rqeteFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLIT----LPLLFLLPKKV 345
Cdd:cd18545 90 -----FFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVlpllVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 346 GKWYQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSW---TTSISGML 421
Cdd:cd18545 165 RKAWQ----RVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR---AVRLNALfwpLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 422 LKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
505-721 |
1.84e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 505 FQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGkplpqyehrylHRQVAAV 584
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 GQEPQVF-GRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQG-------------YDTEVDEA----G------ 640
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAelqeefealggweAEARAEEIlsglGfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 ----SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT--QHLsLVEQADHILF 714
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVShdRYF-LDRVATRILE 221
|
....*..
gi 2203400792 715 LEGGAIR 721
Cdd:COG0488 222 LDRGKLT 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
502-682 |
2.04e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.94 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQV 581
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaaavksgahsfisglpqgydTEVDEA-------------GSQLSGG 646
Cdd:PRK09452 89 NTVFQSYALFPHmTVFENVAFGLrMQKTPAAEIT--------------------PRVMEAlrmvqleefaqrkPHQLSGG 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDAN--SQLQVE 682
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKlrKQMQNE 186
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-735 |
2.40e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRqva 582
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 aVGQEPQ---------------VFGRSlqeniaYGLTQKptmeeiTAAAVKSGAHSFiSGLPQGYDTEVDEagsqLSGGQ 647
Cdd:PRK13537 82 -VGVVPQfdnldpdftvrenllVFGRY------FGLSAA------AARALVPPLLEF-AKLENKADAKVGE----LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESperySRSVL------LITQHlsLVEQA----DHILFLEG 717
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWER----LRSLLargktiLLTTH--FMEEAerlcDRLCVIEE 213
|
250
....*....|....*....
gi 2203400792 718 G-AIREGGTHQQLMEKKGC 735
Cdd:PRK13537 214 GrKIAEGAPHALIESEIGC 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
502-724 |
3.35e-21 |
|
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: 92.82 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ 580
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGR-SLQENIAY-----GLtqKPTmeEITAAavksgahsfISGLPQGYDTE--VDEAGSQLSGGQRQAVA 652
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYfaglyGL--KGD--ELTAR---------LEELADRLGMEelLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQlqveQLLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMAT----RALREFIRQLRAlgkCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
499-731 |
3.89e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.69 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 499 LEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTG---GQLLLDGKPL--PQ 571
Cdd:PRK14243 7 TETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYG---LTQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVDEAGSQLSGGQR 648
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQA----DHILFLEGGAIREGG 724
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM---QQAarvsDMTAFFNVELTEGGG 232
|
....*..
gi 2203400792 725 THQQLME 731
Cdd:PRK14243 233 RYGYLVE 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
503-724 |
4.72e-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: 91.87 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEhRYLHRQVA 582
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGR-SLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVdeagSQLSGGQRQAVALARALIR 659
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY----IAWLKGIPSKEVKARVDEVLElvNLGDRAKKKI----GSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
369-734 |
5.30e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSW---TTSISGMLLKVGI-LYIGGQLVTSGAVS 440
Cdd:PLN03232 484 EILASMDTVKCYAWE----KSFESRIQGIRneelSWFRKAQLLSAFNSFilnSIPVVVTLVSFGVfVLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 441 SGNLVTFVLYQMQ-----FTQAVEVLLSIyPRVQKAVGSSEKIfeyLDRTPRCPPSgllTPLhleglVQFQDVSFAYPNR 515
Cdd:PLN03232 560 SLSLFAVLRSPLNmlpnlLSQVVNANVSL-QRIEELLLSEERI---LAQNPPLQPG---APA-----ISIKNGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGRS 594
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQENIAYGLTQKPtmeEITAAAVKSGAHSFISGLPQGYD-TEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PLN03232 695 VRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 674 DANSQLQVeqllYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT----------HQQLMEKKG 734
Cdd:PLN03232 772 DAHVAHQV----FDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTfaelsksgslFKKLMENAG 841
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
248-580 |
5.33e-21 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 97.56 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 248 IYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVS 326
Cdd:COG4615 70 LLLTRLGQhAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 327 L-TMVTLITLPLLFLLPKKVGKWYQLLEvQVRE---SLAKSSQVAIE-----ALSAmPTVRSFANEEgeaqkFREKLQEI 397
Cdd:COG4615 149 LfLLTLVLLGLGVAGYRLLVRRARRHLR-RAREaedRLFKHFRALLEgfkelKLNR-RRRRAFFDED-----LQPTAERY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 398 KTLNQKEAVAYAVN-SWTTSIsgMLLKVG-ILYIGGQLvtsGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSS 475
Cdd:COG4615 222 RDLRIRADTIFALAnNWGNLL--FFALIGlILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 476 EKIfEYLDRTPRCPPSGLLTPLHLEGLVQFQ-----DVSFAYPNRPD--VLVLQGLTFTLRPGEVTALVGPNGSGKSTVA 548
Cdd:COG4615 297 RKI-EELELALAAAEPAAADAAAPPAPADFQtlelrGVTYRYPGEDGdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350
....*....|....*....|....*....|..
gi 2203400792 549 ALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ 580
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTA-DNREAYRQ 406
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
519-718 |
6.69e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LP-----------QYEHRYLHRQVAA- 583
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPghqiarmgvvrTFQHVRLFREMTVi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 ----VGQEpqvfgRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLpqgydTEV--DEAGSqLSGGQRQAVALARA 656
Cdd:PRK11300 99 enllVAQH-----QQLKTGLFSGLLKTPAFRRAESEALDRAATWLeRVGL-----LEHanRQAGN-LAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGG 718
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQG 230
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-478 |
7.04e-21 |
|
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: 93.70 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEfVGDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLG-VVQTYLSARIGqGVMYDLRVQLYAHLQRMSLAFFTRTR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTED--------TSTLSDSLSENLSLFLwylvrglcLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLL 352
Cdd:cd18550 95 TGEIQSRLNNDvggaqsvvTGTLTSVVSNVVTLVA--------TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 EVQVRESLAKSSQVAIEALSA--MPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISGMLLKVG---IL 427
Cdd:cd18550 167 TREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQAL---AGRWFFAALGLFTAIGpalVY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 428 YIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18550 244 WVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
500-725 |
7.27e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.23 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRPD---VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 576
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAA-VGQEP--QVFGRSLQENIAYG---LTQKPtmEEITA----AAVKSGAHSFisglpqgydteVDEAGSQLSGG 646
Cdd:PRK13633 82 DIRNKAGmVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRErvdeSLKKVGMYEY-----------RRHAPHLLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT 725
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
503-724 |
8.80e-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: 91.12 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlPQYEHRYLhRQVA 582
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEAL-RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFG-RSLQENI-----AYGLTQKPTMEEITaaavksgahsfISGLpqgyDTEVDEAGSQLSGGQRQAVALARA 656
Cdd:cd03268 76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLD-----------VVGL----KDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPErYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
507-729 |
1.03e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTGGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGR-SLQENIAY-----GLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVDEAGSQLSGGQRQAVALA 654
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYplkshGIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
502-732 |
1.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL----LLDGKPLPQYEHR 575
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfISGLPQGYdteVDEAGSQLSGGQRQ 649
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLE------MVGLADEF---WEKSPFELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQ 728
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSD 230
|
....
gi 2203400792 729 LMEK 732
Cdd:PRK13643 231 VFQE 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
517-748 |
1.19e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRylhrqvaavgqepqvfgrslq 596
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDR--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAY-----GLTQKPTMEE----------ITAAAVKSGAHSFIS--GLPQGYDTEVDEagsqLSGGQRQAVALARALIR 659
Cdd:COG4152 71 RRIGYlpeerGLYPKMKVGEqlvylarlkgLSKAEAKRRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 660 KPCVLILDDATSALDA-NSQLqVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKGCYW 737
Cdd:COG4152 147 DPELLILDEPFSGLDPvNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
250
....*....|.
gi 2203400792 738 AMVQAPADAPE 748
Cdd:COG4152 225 LRLEADGDAGW 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
502-720 |
1.40e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 91.68 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQnlyqptggqlLLDGkplpqyehrYLHrqv 581
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG---------DLP--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGR-----SLQE---NIAY---GLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTEVDEAG---------- 640
Cdd:COG1119 55 PTYGNDVRLFGErrggeDVWElrkRIGLvspALQLRFPRDETVLDVVLSGFFDSI-GLYREPTDEQRERArellellgla 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 -------SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHI 712
Cdd:COG1119 134 hladrpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHV 213
|
....*...
gi 2203400792 713 LFLEGGAI 720
Cdd:COG1119 214 LLLKDGRV 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
495-720 |
1.54e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 495 TPLHLEGlvqfqdVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY-- 572
Cdd:PRK11247 11 TPLLLNA------VSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 573 EHRYLHrqvaavgQEPQVFG-RSLQENIAYGLTQ--KPTMEEITAAAvksgahsfisglpqGYDTEVDEAGSQLSGGQRQ 649
Cdd:PRK11247 82 DTRLMF-------QDARLLPwKKVIDNVGLGLKGqwRDAALQALAAV--------------GLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAI 720
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
524-700 |
1.89e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL---PQYEhrylhRQVAAVGQEPQVFGR-SLQENI 599
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQ-----RPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLTQ-KPTMEEITA--AAVKSGAH--SFISGLPQgydtevdeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:PRK11607 113 AFGLKQdKLPKAEIASrvNEMLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190
....*....|....*....|....*....|
gi 2203400792 675 AN----SQLQVEQLLyespERYSRSVLLIT 700
Cdd:PRK11607 182 KKlrdrMQLEVVDIL----ERVGVTCVMVT 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-724 |
1.97e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.51 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 FGRSLQENIAYGL-------TQKPTMEEITAAAVKSGahsfisgLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCV 663
Cdd:PRK14247 95 PNLSIFENVALGLklnrlvkSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 664 LILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
503-721 |
2.65e-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: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRylHRqva 582
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR--NR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 aVGQEPQVFG----RSLQENIAY-----GLTQKPTMEEITAAAVKSGahsfISglpqGYDTEVDEagsQLSGGQRQAVAL 653
Cdd:cd03269 72 -IGYLPEERGlypkMKVIDQLVYlaqlkGLKKEEARRRIDEWLERLE----LS----EYANKRVE---ELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIR 721
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
502-700 |
5.99e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhR 579
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAaVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKsgahsfisglpqgydtEVDEAGS------QLSGGQRQ 649
Cdd:PRK11248 73 GVV-FQNEGLLPWRNVQDNVAFGLqlagVEKMQRLEIAHQMLK----------------KVGLEGAekryiwQLSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLIT 700
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
503-718 |
6.14e-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: 86.73 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqva 582
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 avgqepqvfgrslqENIAYgltqkptmeeitaaavksgahsFisglpqgydtevdeagSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03221 63 --------------VKIGY----------------------F----------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 663 VLILDDATSALDANSQLQVEQLLyespERYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
507-734 |
6.19e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHR---YLHRQVAA 583
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSgAHSFISGlpQGYDTEVDEAgsqLSGGQRQAVALARALIRKP 661
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDA--QHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 662 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGG------THQQLMEKKG 734
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
517-729 |
8.94e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 88.58 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQVAAVGQEPQVfGRSLQ 596
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 --ENIA-----YGLTQKPTMEEITAAAvksgahSFIsGLPQGYDTEVdeagSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:cd03265 90 gwENLYiharlYGVPGAERRERIDELL------DFV-GLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 670 TSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
499-724 |
9.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 499 LEGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGAHSFisglpqgydteVDEAGSQLSGGQRQAV 651
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDF-----------RDKPPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSL-VEQADHILFL-EGGAIREGG 724
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLaAEWADQVIVLkEGRVLAEGD 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
500-718 |
1.41e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ-----------NLYQPTGGQLLLdgkp 568
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaglwpygsgRIARPAGARVLF---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 569 LPQyeHRYLhrqvaavgqePQVfgrSLQENIAY-GLTQKPTMEEITAAAVKSGAHSFISGLpqgyDTEVDeAGSQLSGGQ 647
Cdd:COG4178 431 LPQ--RPYL----------PLG---TLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEAD-WDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
509-720 |
1.45e-19 |
|
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: 88.54 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKpLPqYEHR--YLHRQVAAVGQ 586
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VP-WKRRkkFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EPQVF-------GRSLQENIaYGLTQ---KPTMEEITaAAVKSGAhsfisglpqgydtEVDEAGSQLSGGQRQAVALARA 656
Cdd:cd03267 103 KTQLWwdlpvidSFYLLAAI-YDLPParfKKRLDELS-ELLDLEE-------------LLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
503-720 |
1.79e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.10 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTGGQLLLDGKPLpqyeHRYL 577
Cdd:cd03234 4 LPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR----KPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQ-VAAVGQepqvfgrslQENIAYGLTQKptmEEITAAAV-KSGAHSfisglPQGYDTEVDEAGS-------------- 641
Cdd:cd03234 79 FQKcVAYVRQ---------DDILLPGLTVR---ETLTYTAIlRLPRKS-----SDAIRKKRVEDVLlrdlaltriggnlv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 642 -QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLL-ITQHLS-LVEQADHILFLEGG 718
Cdd:cd03234 142 kGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILtIHQPRSdLFRLFDRILLLSSG 220
|
..
gi 2203400792 719 AI 720
Cdd:cd03234 221 EI 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
505-733 |
2.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 505 FQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP----QYEHRYLH 578
Cdd:PRK13634 5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYdteVDEAGSQLSGGQRQAVALA 654
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG----PMNFGVSEEDAKQKAREMIElvGLPEEL---LARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKK 733
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
502-720 |
2.36e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQYEHR-- 575
Cdd:PRK15439 11 LLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 -YLhrqvaaVGQEPQVF-GRSLQENIAYGLTQKP-TMEEITAAAVKSGAHsfisglpqgydTEVDEAGSQLSGGQRQAVA 652
Cdd:PRK15439 88 iYL------VPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 653 LARALIRKPCVLILDDATSALdanSQLQVEQLLYESPERYSRSV--LLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
502-722 |
3.54e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQV 581
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVF--GRSLQENIAYGltqKPTMEEITAAAVkSGAHSFiSGlpqgydTEVDEAGSQLSGGQRQAVALARALIR 659
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELRDG---APGGTEQEVRGY-LGRFLF-SG------DDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLITqH----LSLVeqADHILFLEGGAIRE 722
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVS-HdryfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
495-724 |
4.17e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEh 574
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 575 rylhrqvAAVGQEPQVFGRslqENI-----AYGLTQK---PTMEEItaaavksgaHSFiSGLPQGYDTEVdeagSQLSGG 646
Cdd:cd03220 91 -------LGGGFNPELTGR---ENIylngrLLGLSRKeidEKIDEI---------IEF-SELGDFIDLPV----KTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
526-730 |
5.65e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 89.39 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----------PqyeHRylhRQVAAVGQEPQVFG-RS 594
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflpP---HR---RRIGYVFQEARLFPhLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQENIAYGL------TQKPTMEEITAAAvksGahsfISGL----PQgydtevdeagsQLSGGQRQAVALARALIRKPCVL 664
Cdd:COG4148 94 VRGNLLYGRkrapraERRISFDEVVELL---G----IGHLldrrPA-----------TLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 665 ILDDATSALDANSQLQV----EQLlyesPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 730
Cdd:COG4148 156 LMDEPLAALDLARKAEIlpylERL----RDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
504-717 |
6.84e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQP--TGGQLLLDGK---PLPQYEhryl 577
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRrltALPAEQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 hRQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEE----ITAAAVKSGAHSFISGLPqgydtevdeagSQLSGGQRQAVA 652
Cdd:COG4136 76 -RRIGILFQDDLLFPHlSVGENLAFALPPTIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-478 |
9.03e-19 |
|
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: 87.59 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQD-GSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG---------HVHSHLQgevfgavlRQE 272
Cdd:cd18778 17 VPPWLIRELVDLVTIGsKSLGLLLGLALLLLGAYLLRALLNFL-RIYLNHVAEqkvvadlrsDLYDKLQ--------RLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 273 TEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLL 352
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKE----AVAYAVNSWTTSIsGMLLkvgILY 428
Cdd:cd18778 168 YRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAmklwAIFHPLMEFLTSL-GTVL---VLG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18778 244 FGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-709 |
1.25e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 512 YPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhRYlhRQVAAVGQE 587
Cdd:COG1101 12 NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK-RA--KYIGRVFQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 588 PQV---FGRSLQEN--IAYGLTQKPTMeeitAAAVKSGAHSFIS--------GLPQGYDTEVdeagSQLSGGQRQAVALA 654
Cdd:COG1101 89 PMMgtaPSMTIEENlaLAYRRGKRRGL----RRGLTKKRRELFRellatlglGLENRLDTKV----GLLSGGQRQALSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLslvEQA 709
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM---EQA 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
503-733 |
1.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPN-RP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQYEHRY 576
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVDEAGS-QLSGGQRQAVAL 653
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 732
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 2203400792 733 K 733
Cdd:PRK13646 237 K 237
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
206-487 |
1.56e-18 |
|
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: 87.12 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 206 FFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHL----QGEVFGAVLRQETEFFQQ--N 279
Cdd:cd18578 30 ILFSKLIS-VFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLtrrlRKLAFRAILRQDIAWFDDpeN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDSLSENLSLFL-----------------WYLvrGLCLLGIM--LWGSVSLTMvtlitlpllfl 340
Cdd:cd18578 109 STGALTSRLSTDASDVRGLVGDRLGLILqaivtlvagliiafvygWKL--ALVGLATVplLLLAGYLRM----------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 341 lpkkvgKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISg 419
Cdd:cd18578 176 ------RLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgFGLSQSLT- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 420 MLLKVGILYIGGQLVTSGAVSSGNLVTfVLYQMQFT-QAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPR 487
Cdd:cd18578 249 FFAYALAFWYGGRLVANGEYTFEQFFI-VFMALIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
515-712 |
1.63e-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: 84.47 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAY--GLTQKPTMEEITAAAvksgahsfisGLpQGYDtevDEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03231 89 SVLENLRFwhADHSDEQVEEALARV----------GL-NGFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2203400792 672 ALDANSQLQVEQLLYESPERYSRSVLliTQHLSLVEQADHI 712
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVL--TTHQDLGLSEAGA 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
502-729 |
1.82e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TGGQLLLDGKPLPQYEHR 575
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevdea 639
Cdd:PRK15134 85 TLRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYPH--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 640 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:PRK15134 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 2203400792 719 AIREGGTHQQL 729
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
520-705 |
1.88e-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: 84.33 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 599 I----AYGLTQKPTMEEITAAAvksgahsfisglpqGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:TIGR01189 94 LhfwaAIHGGAQRTIEDALAAV--------------GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|.
gi 2203400792 675 ANSQLQVEQLLYESPERysRSVLLITQHLSL 705
Cdd:TIGR01189 160 KAGVALLAGLLRAHLAR--GGIVLLTTHQDL 188
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
520-729 |
1.90e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YLHRQVAAVGQepqvFGRSL 595
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 Q-----ENIAYGL---TQKPtmeeitaAAVKSGAHSFISGLpqGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11629 100 PdftalENVAMPLligKKKP-------AEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 668 DATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILfleggAIREGGTHQQL 729
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-----EMRDGRLTAEL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
503-725 |
2.87e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.87 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLH 578
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHsfISGLPqgYDTEVDEAGSQLSGGQRQAVALARA 656
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMN--IVGLD--YEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
515-678 |
3.46e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YL-HRQvaavGQEPQ 589
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 590 VfgrSLQENIA-----YGltQKPTMEEITAAAVKSGAhsfISGLPQGYdtevdeagsqLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK13539 88 L---TVAENLEfwaafLG--GEELDIAAALEAVGLAP---LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....
gi 2203400792 665 ILDDATSALDANSQ 678
Cdd:PRK13539 150 ILDEPTAALDAAAV 163
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
512-727 |
7.72e-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: 83.36 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 512 YPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQV 590
Cdd:cd03218 10 YGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 FGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLpqgydteVDEAGSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03218 87 FRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFhITHL-------RKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 669 ATSALDANSQLQVEQLLYESPERySRSVlLITQH-----LSLVEQAdHILFlEGGAIREGGTHQ 727
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDR-GIGV-LITDHnvretLSITDRA-YIIY-EGKVLAEGTPEE 219
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
201-470 |
8.67e-18 |
|
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: 84.42 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGiYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTY-WGHVMGaRIETDMRRDLFEHLQKLSFSFFDNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 280 QTGNIMSRVTEDTSTLSDsLS----ENLslflwyLVRGLCLLG---IMLWGSVSLTMVTLI----TLPLLFLLPKKVGKW 348
Cdd:cd18549 97 KTGQLMSRITNDLFDISE-LAhhgpEDL------FISIITIIGsfiILLTINVPLTLIVFAllplMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 349 YQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGM---LLKV 424
Cdd:cd18549 170 FR----RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK---AYKAMAYFFSGMNFftnLLNL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2203400792 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQK 470
Cdd:cd18549 242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
503-675 |
8.88e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQE----PQVfgrSLQENIAYGL----TQKPTMEEITAAAVKsgahsfISGLpqgyDTEVDEAGSQLSGGQRQAVALA 654
Cdd:PRK11650 80 MVFQNyalyPHM---SVRENMAYGLkirgMPKAEIEERVAEAAR------ILEL----EPLLDRKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 2203400792 655 RALIRKPCVLILDDATSALDA 675
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
515-685 |
1.03e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAY--GLTQKPTMEEITAA--AVksgahsfisGLpQGYDtevDEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:PRK13538 90 TALENLRFyqRLHGPGDDEALWEAlaQV---------GL-AGFE---DVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170
....*....|....*.
gi 2203400792 670 TSALDANSQLQVEQLL 685
Cdd:PRK13538 157 FTAIDKQGVARLEALL 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
516-684 |
1.29e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlpqyeHRY------LHRQVAAVGQEPQ 589
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 590 -VFGRSLQENIAYGltQKPT-MEEITAAAVKSGAHSFISGLpqGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11288 90 lVPEMTVAENLYLG--QLPHkGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170
....*....|....*..
gi 2203400792 668 DATSALdanSQLQVEQL 684
Cdd:PRK11288 166 EPTSSL---SAREIEQL 179
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
503-718 |
2.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.34 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAY-PNRPdvLVLQGLT---FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYL 577
Cdd:PRK13641 3 IKFENVDYIYsPGTP--MEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 ---HRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPqgyDTEVDEAGSQLSGGQRQA 650
Cdd:PRK13641 81 kklRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKkvGLS---EDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpERYSRSVLLITQHLSLV-EQADHILFLEGG 718
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
520-720 |
2.78e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.17 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFG----RS 594
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKREGlvldLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQENIAygltqkptmeeitaaavksgahsfisglpqgydtevdeAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03215 95 VAENIA--------------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2203400792 675 ANSQLQVEQLLYESPERySRSVLLITQHLS-LVEQADHILFLEGGAI 720
Cdd:cd03215 137 VGAKAEIYRLIRELADA-GKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
516-719 |
3.05e-17 |
|
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: 81.22 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLL-------LDGKPLPQYEHRYlhrQVAAVGQEP 588
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRY---SVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 QVFGRSLQENIAYGltqKPTMEEITAAAVKSGA-HSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:cd03290 89 WLLNATVEENITFG---SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 668 DATSALDAN-SQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGA 719
Cdd:cd03290 166 DPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
515-729 |
3.24e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyehRYLHRQV------------- 581
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRQVielseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 ------AAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPQgydtevdeags 641
Cdd:PRK10261 101 vrgadmAMIFQEPMtslnpVFtvGEQIAESIR--LHQGASREEAMVEAKRmldqvriPEAQTILSRYPH----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAI 720
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 2203400792 721 REGGTHQQL 729
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
500-729 |
4.03e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQD--VSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYEH 574
Cdd:PRK09473 10 DALLDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 575 RYLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAA--AVK-SGAHSFISGLPQgydtevde 638
Cdd:PRK09473 89 KELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEESVRMldAVKmPEARKRMKMYPH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 639 agsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:PRK09473 161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYA 237
|
250
....*....|..
gi 2203400792 718 GAIREGGTHQQL 729
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
525-730 |
4.72e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRYLHRQ-VAAVGQEPQVFGR-SLQENI 599
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLtqkptmeEITAAAVKSGAHSFISGLPQ-GYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ 678
Cdd:PRK10070 128 AFGM-------ELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 679 LQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
265-449 |
4.78e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 82.21 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 265 FGAVLRQETEFFQQNQTGNIMSRVTEDT----STLSDSLSENL-----------SLFL----WYLVRGLCLLGIMLWGSV 325
Cdd:cd18574 82 FSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLrsvtqtvgcvvSLYLispkLTLLLLVIVPVVVLVGTL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 326 sltmvtlitlpllfllpkkVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 405
Cdd:cd18574 162 -------------------YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLG 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2203400792 406 VAYAV-----NswtTSISGMLLkvGILYIGGQLVTSGAVSSGNLVTFVL 449
Cdd:cd18574 223 LGIGIfqglsN---LALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-731 |
5.06e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.43 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGKPL--PQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 R-SLQENIAYGL------TQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK14267 99 HlTIYDNVAIGVklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 666 LDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 731
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
502-720 |
5.96e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhrq 580
Cdd:PRK10535 4 LLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 vAAVGQEPqvFGRSLQEniaYGLTQKPTME---EITA-------AAVKSGAHSFISGLpqGYDTEVDEAGSQLSGGQRQA 650
Cdd:PRK10535 81 -AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAvyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
520-730 |
6.14e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 599 IAYG-LTQKPTM-------EEITAAAVKSGAHSFISGlpQGYDTevdeagsqLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:PRK10253 102 VARGrYPHQPLFtrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 671 SALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
503-719 |
6.76e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.73 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVA 582
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVFGRSLQENIAYgltqkPTMEEitaaavksgahsfisglpqgydtevdeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 663 VLILDDATSALDAnsqlQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGA 719
Cdd:cd03223 112 FVFLDEATSALDE----ESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-733 |
1.30e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGG-----QLLLDGKPLPQYEHRY-LHRQVAAVGQEPQVFGR 593
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 674 DANSQLQVEQLLYESPERYsrSVLLITQHLSlveQADHI-----LFLEGGAIREGGTHQQLMEKK 733
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRL--TVIIVTHNLA---QAARIsdraaLFFDGRLVEEGPTEQLFSSPK 254
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-715 |
1.43e-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: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhRQVaaVGQEPQVFG-RSLQE 597
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItePGPD-----RMV--VFQNYSLLPwLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 598 NIAYGLTQ-KPTMEEITAAAVKSgAHSFISGLPQGYDTEVDeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVE-EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2203400792 677 SQLQVEQLLYESPERYSRSVLLITQHLslveqaDHILFL 715
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDV------DEALLL 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
484-731 |
2.08e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 484 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNrpdvlvlqgltftlrpGEVTALVGPNGSGKSTvaaLLQNLyqptggqll 563
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSL--------- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 564 ldgkpLPQYE----HRYLHRQVAAVGQEPQVFGRSLQENIaygLTQKPTMEEITAAAVK-SGAHSFISGLPQGYDTEVDE 638
Cdd:PTZ00243 707 -----LSQFEisegRVWAERSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVRvSQLEADLAQLGGGLETEIGE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 639 AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN-SQLQVEQLLYESPERYSRsvLLITQHLSLVEQADHILFLEG 717
Cdd:PTZ00243 779 KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTR--VLATHQVHVVPRADYVVALGD 856
|
250
....*....|....
gi 2203400792 718 GAIREGGTHQQLME 731
Cdd:PTZ00243 857 GRVEFSGSSADFMR 870
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
503-733 |
2.59e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY----EHRY 576
Cdd:PRK13649 3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkP-----TMEEITAAAVKSGAHSFISglpqgyDTEVDEAGSQLSGGQRQ 649
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITqHL--SLVEQADHILFLEGGAIREGGTHQ 727
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVT-HLmdDVANYADFVYVLEKGKLVLSGKPK 230
|
250
....*....|..
gi 2203400792 728 Q------LMEKK 733
Cdd:PRK13649 231 DifqdvdFLEEK 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
521-730 |
3.12e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENI 599
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLtQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVdeagSQLSGGQRQAVALARALIR-------KPCVLILDDATSA 672
Cdd:COG4138 91 ALHQ-PAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 673 LDANSQLQVEQLLYESPERySRSVLLITQHLSL-VEQADHILFLEGGAIREGGTHQQLM 730
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
516-724 |
4.39e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTGGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVF 591
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 592 GRSLQENIAYGL-----TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEvdeagsqLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK10418 92 FNPLHTMHTHARetclaLGKPADDATLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 667 DDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 724
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
520-722 |
7.20e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--EHRYLHRqVAAVGQEPQVF----GR 593
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLR-AKHVGFVFQSFmlipTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIaygltQKPTMeeITAAAVKSGAHSFISGLPQ-GYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK10584 104 NALENV-----ELPAL--LRGESSRQSRNGAKALLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 673 LDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 722
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
505-722 |
1.09e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.79 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 505 FQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ-VAA 583
Cdd:PRK10522 325 LRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKlFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 584 VGQEPQVFGRSLqeniaygltqKPTMEEITAAAVKsgahSFISGLPQGYDTEVDE---AGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10522 402 VFTDFHLFDQLL----------GPEGKPANPALVE----KWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 661 PCVLILDDAtsALDANSQLQVE--QLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 722
Cdd:PRK10522 468 RDILLLDEW--AADQDPHFRREfyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
520-727 |
1.79e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-------KPLPQyEHRYLHRQVAAVGQepqvfg 592
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDK-AIRELRRNVGMVFQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 rslQENIAYGLTqkpTMEEITAAAVKsgahsfISGLPQGYDTE--------------VDEAGSQLSGGQRQAVALARALI 658
Cdd:PRK11124 90 ---QYNLWPHLT---VQQNLIEAPCR------VLGLSKDQALAraekllerlrlkpyADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVlLITQHLSLVEQ-ADHILFLEGGAIREGGTHQ 727
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
502-715 |
1.93e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK09544 4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAvgqePQVFGRSLQenIAYGLTQK---PTMEEITAAAVksgahsfisglpqgydteVDEAGSQLSGGQRQAVALARALI 658
Cdd:PRK09544 81 TL----PLTVNRFLR--LRPGTKKEdilPALKRVQAGHL------------------IDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFL 715
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
516-685 |
2.00e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehrylhrqvAA-------V 584
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPR----------DAialgigmV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 GQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSgahsfISGLPQGYDTEVD-EAG-SQLSGGQRQAVALARALIRKP 661
Cdd:COG3845 86 HQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARAR-----IRELSERYGLDVDpDAKvEDLSVGEQQRVEILKALYRGA 160
|
170 180
....*....|....*....|....
gi 2203400792 662 CVLILDDATSALdanSQLQVEQLL 685
Cdd:COG3845 161 RILILDEPTAVL---TPQEADELF 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
251-730 |
2.62e-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: 80.34 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 251 NTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSenLSLF----LWYLVRG-LCLLGIMLWGSV 325
Cdd:TIGR01271 951 HTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP--LTLFdfiqLTLIVLGaIFVVSVLQPYIF 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 326 SLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSsqvAIEALSAMPTVRSFANeegeaQKFREKLQEiKTLNQKEA 405
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH---LITSLKGLWTIRAFGR-----QSYFETLFH-KALNLHTA 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 406 VAYAvnsWTTSISGMLLKVGILY-----------IGGQLVTSGAVssGNLVTFVLYQMQFTQAVeVLLSIypRVQKAVGS 474
Cdd:TIGR01271 1100 NWFL---YLSTLRWFQMRIDIIFvfffiavtfiaIGTNQDGEGEV--GIILTLAMNILSTLQWA-VNSSI--DVDGLMRS 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 475 SEKIFEYLDRTPRCP-PSGLLTPLHL-----------------EGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTAL 536
Cdd:TIGR01271 1172 VSRVFKFIDLPQEEPrPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGL 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 537 VGPNGSGKST-VAALLQNLyqPTGGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSLQENI-AYgltQKPTMEE 611
Cdd:TIGR01271 1251 LGRTGSGKSTlLSALLRLL--STEGEIQIDGV---SWNSVTLQTWRKAFGVIPQkvfIFSGTFRKNLdPY---EQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 612 ITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESper 691
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS--- 1399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2203400792 692 YSRSVLLITQH-LSLVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:TIGR01271 1400 FSNCTVILSEHrVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
431-731 |
2.63e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 431 GQLVTSGAVSSgnlvTFVLYQMQFTQAvevLLSIYPRVQKAVGSS-EKIFEYL---DRTPRCPPSGLLTPLHLEGLVQFQ 506
Cdd:PRK10261 245 GEAVETGSVEQ----IFHAPQHPYTRA---LLAAVPQLGAMKGLDyPRRFPLIsleHPAKQEPPIEQDTVVDGEPILQVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEHR 575
Cdd:PRK10261 318 NLVTRFPLRSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQEP-------QVFGRSLQENI-AYGLTQKPTMEEITAAAVKSgahsfISGLPQG---YDTEvdeagsqLS 644
Cdd:PRK10261 398 ALRRDIQFIFQDPyasldprQTVGDSIMEPLrVHGLLPGKAAAARVAWLLER-----VGLLPEHawrYPHE-------FS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADH---ILFLegGAIR 721
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvaVMYL--GQIV 543
|
330
....*....|
gi 2203400792 722 EGGTHQQLME 731
Cdd:PRK10261 544 EIGPRRAVFE 553
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
202-471 |
3.12e-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: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYI-RSYLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTeDTSTLSDSLSEN-LSLFLWYLVrGLCLLGIMLWGSVSLTMVTLIT----LPLLFLLPKKVGKWYQllevQ 355
Cdd:cd18570 98 TGEIISRFN-DANKIREAISSTtISLFLDLLM-VIISGIILFFYNWKLFLITLLIiplyILIILLFNKPFKKKNR----E 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 356 VRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVT 435
Cdd:cd18570 172 VMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVI 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 2203400792 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:cd18570 252 KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
520-734 |
4.03e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGKPL----PqyEHRylhrqvAAVG-----QEP 588
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelsP--DER------ARAGiflafQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 589 QVF-GRSLQE--NIAYGltqKPTMEEITAAAVKSGAHSFIS--GLPQGY-DTEVDEaGsqLSGGQRQAVALARALIRKPC 662
Cdd:COG0396 87 VEIpGVSVSNflRTALN---ARRGEELSAREFLKLLKEKMKelGLDEDFlDRYVNE-G--FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 663 VLILDDATSALDANSqLQ-----VEQLLyeSPErysRSVLLITQHLSLVE--QADHILFLEGGAI-REGGTH--QQLmEK 732
Cdd:COG0396 161 LAILDETDSGLDIDA-LRivaegVNKLR--SPD---RGILIITHYQRILDyiKPDFVHVLVDGRIvKSGGKElaLEL-EE 233
|
..
gi 2203400792 733 KG 734
Cdd:COG0396 234 EG 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
520-719 |
4.07e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 75.16 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL---YQPTGGQLLldgkplpqYEHRYlhRQVAAVGQEPQVFGRSLQ 596
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKST---LLKCIygnYLPDSGSIL--------VRHDG--GWVDLAQASPREILALRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAYgLTQ-------KPTMEEITAAAVKsgahsfisglpQGYDTEV--DEAGSQL-----------------SGGQRQA 650
Cdd:COG4778 93 RTIGY-VSQflrviprVSALDVVAEPLLE-----------RGVDREEarARARELLarlnlperlwdlppatfSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGA 719
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
506-730 |
4.57e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:COG4604 5 KNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQV-----------FGR--------------SLQENIAY-GLtqkptmEEItaaavksgAHSFIsglpqgydtevDEa 639
Cdd:COG4604 82 QENHInsrltvrelvaFGRfpyskgrltaedreIIDEAIAYlDL------EDL--------ADRYL-----------DE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 640 gsqLSGGQRQavalaRALI------RKPCVLiLDDATSALDANSQLQVEQLLYESPERYSRSVLLI-------TQHlslv 706
Cdd:COG4604 136 ---LSGGQRQ-----RAFIamvlaqDTDYVL-LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVlhdinfaSCY---- 202
|
250 260
....*....|....*....|....
gi 2203400792 707 eqADHILFLEGGAIREGGTHQQLM 730
Cdd:COG4604 203 --ADHIVAMKDGRVVAQGTPEEII 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
513-725 |
7.93e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.73 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 513 PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTGGQLLLDGKplpqyehrylhrqVAA-----V 584
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILEPTSGRVEVNGR-------------VSAllelgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 GQEPQVFGRslqENI-----AYGLTQKPT---MEEITAaavksgahsFiSGLPQGYDTEVdeagSQLSGGQRQAVALARA 656
Cdd:COG1134 98 GFHPELTGR---ENIylngrLLGLSRKEIdekFDEIVE---------F-AELGDFIDQPV----KTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 725
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-685 |
8.90e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKPLPQYEHRYLHRQ-VAAVGQE---- 587
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAgIAIIHQElalv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 588 PQVfgrSLQENIAYGltqkptmEEITA------AAVKSGAHSFISGLpqGYDTEVDEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK13549 95 KEL---SVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180
....*....|....*....|....
gi 2203400792 662 CVLILDDATSALDANsqlQVEQLL 685
Cdd:PRK13549 163 RLLILDEPTASLTES---ETAVLL 183
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
523-729 |
1.20e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.90 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 523 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPQVfgrSLQ--- 596
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLA---SLNprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ---ENIAYGL-TQKPTM------EEITAAAVKSGAhsfisgLPQgydtEVDEAGSQLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK15079 116 tigEIIAEPLrTYHPKLsrqevkDRVKAMMLKVGL------LPN----LINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 667 DDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 729
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
520-733 |
1.52e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.12 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQ---LLLDGKPLPQYEH---------------------R 575
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 576 YLHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYdteVDEAGSQLSGGQRQAV 651
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY---LQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFL-EGGAIREGGTHQQL 729
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLdNVLEWTKRTIFFkDGKIIKDGDTYDIL 253
|
....
gi 2203400792 730 MEKK 733
Cdd:PRK13651 254 SDNK 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
497-667 |
3.02e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVQfqdvsfAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYE 573
Cdd:COG1137 4 LEAENLVK------SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPMHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 574 hR------YLhrqvaavGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaAAVKSGAHSF-ISGLpqgydteVDEAGSQLS 644
Cdd:COG1137 75 -RarlgigYL-------PQEASIFRKlTVEDNILAVLeLRKLSKKERE-ERLEELLEEFgITHL-------RKSKAYSLS 138
|
170 180
....*....|....*....|...
gi 2203400792 645 GGQRQAVALARALIRKPCVLILD 667
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLD 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
515-729 |
3.48e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPTG----GQLLLDGKPLpqyEHRYLHRQVAAVgQEPQV 590
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPI---DAKEMRAISAYV-QQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 FGRSL--QENIAY--------GLTQKPTMEE----ITAAAVKSGAHSFI--SGLPQGydtevdeagsqLSGGQRQAVALA 654
Cdd:TIGR00955 110 FIPTLtvREHLMFqahlrmprRVTKKEKRERvdevLQALGLRKCANTRIgvPGRVKG-----------LSGGERKRLAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQL 729
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-684 |
3.79e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFGR- 593
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAYG--LTQK---------PTMEEITAAAVKsgahsfISGLPQGYDTEVDEagsqLSGGQRQAVALARALIRKPC 662
Cdd:PRK09700 96 TVLENLYIGrhLTKKvcgvniidwREMRVRAAMMLL------RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180
....*....|....*....|..
gi 2203400792 663 VLILDDATSALdanSQLQVEQL 684
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYL 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
520-735 |
4.22e-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: 71.40 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGK---PLPQYEhrylhrqvaavgqepqvfgRS 594
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEE-------------------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQeniayGLT---QKPtmEEITAAAVKsgahSFISGLPQGydtevdeagsqLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03217 76 RL-----GIFlafQYP--PEIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 672 ALDANSQLQVEQLLYESPERySRSVLLITQHLSLVE--QADHILFLEGGAIREGGTHQ--QLMEKKGC 735
Cdd:cd03217 134 GLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
520-730 |
4.27e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EPQVFGR-SLQENI------AYGLTQKPTMEEitaaAVKSGAHSFISGLPQGydtevdEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 660 KPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
507-732 |
8.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ-----YEHRYLHR 579
Cdd:PRK13645 11 NVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEP--QVFGRSLQENIAYGltqkptmeEITAAAVKSGAHSFIS------GLPQGYdteVDEAGSQLSGGQRQAV 651
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFG--------PVNLGENKQEAYKKVPellklvQLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFL-EGGAIREGG----- 724
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMhEGKVISIGSpfeif 239
|
....*...
gi 2203400792 725 THQQLMEK 732
Cdd:PRK13645 240 SNQELLTK 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
427-717 |
2.05e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 73.63 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 427 LYIGGQLVTSGAVSSGNLVTfVLYQMQ----FTQAVEVLLSIYPRVQK------AVGSSEKIFEYLDRTPRCPPSGLLtp 496
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLML-AGRDMTrlagFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVQFQDVSFAYPNRpDVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgKPLPQyehry 576
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT---KPAKG----- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 lhrQVAAVGQEPQVFGRSLQENIAY----------GLTQKpTMEEITAAaVKSGahsFISGLPQGYDTeVDEAGSQLSGG 646
Cdd:TIGR00954 516 ---KLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDK-DLEQILDN-VQLT---HILEREGGWSA-VQDWMDVLSGG 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALdansQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
517-725 |
2.61e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------------LLDGKPLPQYEHRY--LHRQ 580
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhELITNPYSKKIKNFkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEP--QVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLPQGYDTeVDEAGSQLSGGQRQAVALARALI 658
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSY-LERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESpERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGT 725
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
503-724 |
2.70e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhR 579
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQE----PQVfgrSLQENIAYGLT-QKPTMEEI-----TAAAVKSGAHSfisglpqgydteVDEAGSQLSGGQRQ 649
Cdd:PRK11000 76 GVGMVFQSyalyPHL---SVAENMSFGLKlAGAKKEEInqrvnQVAEVLQLAHL------------LDRKPKALSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQhlSLVEQ---ADHILFLEGGAIREGG 724
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
230-478 |
2.76e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 71.44 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 230 LMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWY 309
Cdd:cd18565 59 LTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 310 LVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQ 388
Cdd:cd18565 139 VVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNARLE-NNLSGIAVIKAFTAEDFERE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 389 KFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAV------SSGNLVTFVLYQMQFTQAVE 459
Cdd:cd18565 218 RVADASEEYRDANWR---AIRLRAAFFPVIRLVAGAGfvaTFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLT 294
|
250
....*....|....*....
gi 2203400792 460 VLLSIYPRVQKAVGSSEKI 478
Cdd:cd18565 295 RLGDLIDQYQRAMASAKRV 313
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
509-681 |
3.47e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGKPLPQYEHRYlHRQVAAVG 585
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEpqvfgrslQENIAYgLTQKPTMEeitaAAVKSGAHSFISGlpqgydtevdeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03233 90 EE--------DVHFPT-LTVRETLD----FALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLC 141
|
170
....*....|....*.
gi 2203400792 666 LDDATSALDANSQLQV 681
Cdd:cd03233 142 WDNSTRGLDSSTALEI 157
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
202-478 |
3.54e-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: 70.91 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQD--GSADTFTRNLTLMS-----ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETE 274
Cdd:cd18554 16 LLLPLILKYIVDDVIQGssLTLDEKVYKLFTIIgimffIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQ--EIKTLNQKEAVAYAVNSWTTSIS-GMLLKVGilyIGG 431
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKTFSAVNTITDlAPLLVIG---FAA 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2203400792 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
520-747 |
4.90e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV----AALLQNLYQPTG----GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 FGRSLQENIAYGltQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARAL---------IRKP 661
Cdd:PRK13547 96 FAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 662 CVLILDDATSALDANSQLQveqlLYESPERYSRS----VLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK---K 733
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHR----LLDTVRRLARDwnlgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPahiA 249
|
250
....*....|....*..
gi 2203400792 734 GCYW---AMVQAPADAP 747
Cdd:PRK13547 250 RCYGfavRLVDAGDGVP 266
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
518-732 |
5.50e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK-PLPQyEHRYLhRQVAAvgqepqVFGrslq 596
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKR-RKEFA-RRIGV------VFG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 eniaygltQK-------PTME---------EITAAAVKSGAHSFISGLPQG--YDTEVdeagSQLSGGQRQAVALARALI 658
Cdd:COG4586 103 --------QRsqlwwdlPAIDsfrllkaiyRIPDAEYKKRLDELVELLDLGelLDTPV----RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 732
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
500-731 |
9.73e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAY--PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-LLDG-------KPL 569
Cdd:TIGR03269 277 EPIIKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewvdmtKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 570 PQYEHRyLHRQVAAVGQEPQVFG-RSLQENiaygLTQKPTMEEITAAAVKSGAHSFIS-GLPQGYDTEV-DEAGSQLSGG 646
Cdd:TIGR03269 357 PDGRGR-AKRYIGILHQEYDLYPhRTVLDN----LTEAIGLELPDELARMKAVITLKMvGFDEEKAEEIlDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGT 725
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 2203400792 726 HQQLME 731
Cdd:TIGR03269 512 PEEIVE 517
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
202-478 |
9.75e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 69.44 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDgIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18546 16 LAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQT-RLTGRTGErLLYDLRLRVFAHLQRLSLDFHERET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 281 TGNIMSRVTEDTSTLSDSLSENLSLFLwylVRGLCLLGI---MLWGSVSLTMVTLITLPLLFLlpkkVGKWYQLLEV--- 354
Cdd:cd18546 95 SGRIMTRMTSDIDALSELLQTGLVQLV---VSLLTLVGIavvLLVLDPRLALVALAALPPLAL----ATRWFRRRSSray 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 355 -QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 433
Cdd:cd18546 168 rRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2203400792 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18546 248 VAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
201-478 |
9.95e-13 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 69.43 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 201 EMAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMG----HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18543 15 GLAIPLLTRRAIDGPIAHGD----RSALWPLVLLLLALGVAEAVLSFLRRYLAGrlslGVEHDLRTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 277 QQNQTGNIMSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18543 91 DRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:cd18543 170 QDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVAN 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2203400792 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18543 250 GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
506-700 |
1.05e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.12 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQllldGKPLPQYEHRYLHrqvaavg 585
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----ARPQPGIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQ------VFG----------RSLQE----NIAYG---------LTQKPTMEEITAAAvksGAHSFISGLPQGYDT-- 634
Cdd:TIGR03719 75 QEPQldptktVREnveegvaeikDALDRfneiSAKYAepdadfdklAAEQAELQEIIDAA---DAWDLDSQLEIAMDAlr 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 635 --EVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT 700
Cdd:TIGR03719 152 cpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVT 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
520-733 |
1.21e-12 |
|
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: 69.11 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTGGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSL 595
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGV---SWNSVPLQKWRKAFGVIPQkvfIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03289 94 RKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 675 ANSQLQVEQLLYESperYSRSVLLITQH-LSLVEQADHILFLEGGAIREGGTHQQLMEKK 733
Cdd:cd03289 171 PITYQVIRKTLKQA---FADCTVILSEHrIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
520-733 |
1.45e-12 |
|
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: 71.48 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLTqkptMEEITAAAVKSGAH--SFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:TIGR01271 508 IFGLS----YDEYRYTSVIKACQleEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 678 qLQVEQLLYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKK 733
Cdd:TIGR01271 581 -VVTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
233-478 |
1.55e-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: 69.08 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 233 ILTIASAVLEFVGDgIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLV 311
Cdd:cd18564 62 GIALLRGLASYAGT-YLTALVGqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 312 RGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFR 391
Cdd:cd18564 141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 392 EklQEIKTLnQKEAVAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRV 468
Cdd:cd18564 221 R--ENRKSL-RAGLRAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRI 297
|
250
....*....|
gi 2203400792 469 QKAVGSSEKI 478
Cdd:cd18564 298 AKASASAERV 307
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
524-725 |
1.57e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG----GQLLLDGKPL---PQYEHRYL-HRQVAAVGQEPQVfgrSL 595
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLqriSEKERRNLvGAEVAMIFQDPMT---SL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENIAYGLTqkpTMEEI------TAAAVKSGAHSFIS--GLPQGyDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11022 103 NPCYTVGFQ---IMEAIkvhqggNKKTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 668 DATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGT 725
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-732 |
2.41e-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: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGKPLPQYEhrYLHRQvAAVGQEPQVFGRS 594
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCG--YVERP-SKVGEPCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 595 LQENIA--YGLTQKptmeeITAAAVKSGAHSF----------------ISGLPQ-GYDTE--VDEA-------------- 639
Cdd:TIGR03269 89 LEPEEVdfWNLSDK-----LRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEGKeaVGRAvdliemvqlshrit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 640 --GSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSvLLITQHLSLV--EQADHILFL 715
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS-MVLTSHWPEVieDLSDKAIWL 242
|
250
....*....|....*..
gi 2203400792 716 EGGAIREGGTHQQLMEK 732
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
507-670 |
2.42e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRPD-----VLVLQGLT---------FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqy 572
Cdd:COG1129 240 ELEDLFPKRAAapgevVLEVEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 573 ehryLHRQVAAVGQ-----------EPQVFGRSLQENIA---------YGLTQKPTMEEITAAAVKSgahsfisgL---P 629
Cdd:COG1129 318 ----IRSPRDAIRAgiayvpedrkgEGLVLDLSIRENITlasldrlsrGGLLDRRRERALAEEYIKR--------LrikT 385
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2203400792 630 QGYDTEVdeagSQLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:COG1129 386 PSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
530-702 |
2.61e-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: 65.09 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 530 PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgkplpqyehrylhrqvaavgqepqvfgrslqeniaygltqkptm 609
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 610 eeitaaaVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ-----LQVEQL 684
Cdd:smart00382 35 -------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRL 107
|
170
....*....|....*...
gi 2203400792 685 LYESPERYSRSVLLITQH 702
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
518-732 |
4.69e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.01 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP----TGGQLLLDGKPL----PQYEHRYLHRQVAAVGQEPQ 589
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklsPRERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 590 V-------FGRSLQENI-AYGLT----QKPTMEEITAAA------VKSgaHSFI-SGLPQgydtevdeagsQLSGGQRQA 650
Cdd:COG4170 100 ScldpsakIGDQLIEAIpSWTFKgkwwQRFKWRKKRAIEllhrvgIKD--HKDImNSYPH-----------ELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQL 729
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 2203400792 730 MEK 732
Cdd:COG4170 247 LKS 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
520-729 |
5.61e-12 |
|
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: 67.19 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AYGLT--QKPTMEEITAAAVKSGahsfISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:cd03291 119 IFGVSydEYRYKSVVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 678 qLQVEQLLYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 729
Cdd:cd03291 192 -VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
502-673 |
8.56e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQ 580
Cdd:PRK11614 5 MLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGR-SLQENIAYG--LTQKPTMEEITAAAVKSgahsfisgLPQGYDTEVDEAGSqLSGGQRQAVALARAL 657
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGgfFAERDQFQERIKWVYEL--------FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170
....*....|....*.
gi 2203400792 658 IRKPCVLILDDATSAL 673
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
506-702 |
9.61e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK-----PLpqyeHRYLHRQ 580
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 581 VAAVGQEPQVFGR-SLQENIAYGLT--QKPTMEEITAAAVKSGAHSFISGLPqgydtevDEAGSQLSGGQRQAVALARAL 657
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEHLR-------DSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2203400792 658 IRKPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVlLITQH 702
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGV-LITDH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
517-675 |
1.04e-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: 67.93 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKPLPQYEHRYLHRQ-VAAVGQE-PQVF 591
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQElTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 592 GRSLQENIAYGltqkptmEEITA-------AAVKSGAHSFISGLpQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:TIGR02633 92 ELSVAENIFLG-------NEITLpggrmayNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170
....*....|.
gi 2203400792 665 ILDDATSALDA 675
Cdd:TIGR02633 164 ILDEPSSSLTE 174
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
203-478 |
3.03e-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: 64.89 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 283 NIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18568 100 DIITRFQE-NQKIRRFLTRSaLTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEegeaQKFREKLQE--IKTLNQ--KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:cd18568 178 EQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNTrfRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2203400792 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18568 254 QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
524-725 |
4.49e-11 |
|
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: 66.96 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--------------PQYEHRYLHRQVAavgqEPQ 589
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmcPQHNILFHHLTVA----EHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 590 VFGRSLQeniayGLTQKPTMEEITAAAVKSGAHSfisglpqgydtEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR01257 1025 LFYAQLK-----GRSWEEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400792 670 TSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVE-QADHILFLEGGAIREGGT 725
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
524-730 |
5.62e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENIAYG 602
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 603 LTQKPTMEEItAAAVKSGAHSFisglpqGYDTEVDEAGSQLSGGQRQAVALARALIR-----KP--CVLILDDATSALDA 675
Cdd:PRK03695 94 QPDKTRTEAV-ASALNEVAEAL------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 676 NSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK03695 167 AQQAALDRLLSELCQQ-GIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
500-668 |
5.70e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 ---------QVAAVGQEPQVFgrslqENIAYGL---TQKP-------TMEEITAAAVKSGAHSfisgLPqgydtevdeag 640
Cdd:PRK11831 82 vrkrmsmlfQSGALFTDMNVF-----DNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKL----MP----------- 141
|
170 180
....*....|....*....|....*...
gi 2203400792 641 SQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-747 |
8.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqyehryLHRQVAAV-----------GQEPQVFGR 593
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAygltqkptmeeITAAAVKSGAHSFISGlpqgyDTEVDEAGSQ-----------------LSGGQRQAVALARA 656
Cdd:PRK11288 347 SVADNIN-----------ISARRHHLRAGCLINN-----RWEAENADRFirslniktpsreqlimnLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKGC 735
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQAL 489
|
250
....*....|..
gi 2203400792 736 YWAMVQAPADAP 747
Cdd:PRK11288 490 SLALPRTSAAVA 501
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
524-720 |
1.14e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR-YLHRQVAAVGQEPQVFGRSLQENIAY- 601
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPEDRQSSGLYLDAPLAWn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 602 ---------GLTQKPTMEeitaAAVKSGAHSFIsGLPQgydTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK15439 362 vcalthnrrGFWIKPARE----NAVLERYRRAL-NIKF---NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2203400792 673 LDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 720
Cdd:PRK15439 434 VDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
520-729 |
1.30e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQyehryLHRQVAAVGQEPQVFGR-SL 595
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENIAY-GLTQKPtmEEITAAAVKSGAHSFIS--GLPQGYDTEVDEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:PLN03211 158 RETLVFcSLLRLP--KSLTKQEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 672 ALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQA-DHILFL-EGGAIREGGTHQQL 729
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLsEGRCLFFGKGSDAM 295
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
506-700 |
1.54e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGqlllDGKPLPQYEHRYLHrqvaavg 585
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQV-FGRSLQENIAYGLTQKP----------------------------TMEEITAAAvksGAHSFISGLPQGYDT-- 634
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGVAEVKaaldrfneiyaayaepdadfdalaaeqgELQEIIDAA---DAWDLDSQLEIAMDAlr 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 635 --EVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT 700
Cdd:PRK11819 154 cpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVT 217
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
203-478 |
1.72e-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: 62.52 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 283 NIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQ-LLEVQVRESl 360
Cdd:cd18588 100 DTVARVRE-LESIRQFLTGSaLTLVL-DLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRrRLEEKFQRG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLK---VGILYIGGQLVTSG 437
Cdd:cd18588 177 AENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK---TANLSNLASQIVQLIQKlttLAILWFGAYLVMDG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2203400792 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18588 254 ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
507-711 |
2.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQ 586
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFISgLPQGYdtevdeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK13540 82 RSGINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2203400792 666 LDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSL-VEQADH 711
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQE--HRAKGGAVLLTSHQDLpLNKADY 195
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
517-737 |
3.70e-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: 61.12 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPLPQYE--HRylhrqvAAVG-----QE 587
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpdER------ARAGlflafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 588 P-QVFGRSLQENIAYGLT---QKPTMEEITAAAvksgahsFISGLPQGYDT-EVDEAGSQ------LSGGQRQAVALARA 656
Cdd:TIGR01978 86 PeEIPGVSNLEFLRSALNarrSARGEEPLDLLD-------FEKLLKEKLALlDMDEEFLNrsvnegFSGGEKKRNEILQM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIRKPCVLILDDATSALDANS-QLQVEQL-LYESPErysRSVLLITQHLSLVE--QADHILFLEGGAI-REGGTHqqLM- 730
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDAlKIVAEGInRLREPD---RSFLIITHYQRLLNyiKPDYVHVLLDGRIvKSGDVE--LAk 233
|
....*....
gi 2203400792 731 --EKKGCYW 737
Cdd:TIGR01978 234 elEAKGYDW 242
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
225-478 |
3.71e-10 |
|
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: 61.91 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 225 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLS 304
Cdd:cd18558 59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 305 LFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPkkvGKWYQLLEVQV---RESLAKSSQVAIEALSAMPTVRSFA 381
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSA---VVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 382 NEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL 461
Cdd:cd18558 216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQ 295
|
250
....*....|....*..
gi 2203400792 462 LSIYPRVQKAVGSSEKI 478
Cdd:cd18558 296 VPSIEAFANARGAAYHI 312
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
520-674 |
3.72e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY--QPTGGQLLLDGKPLPQyehrylhrqvaavgqepqvfGRSLQE 597
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLID 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 598 NIAYGLTQKPTMEEITAAavksgahsfisGL--PQGYDTEVDEagsqLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:COG2401 105 AIGRKGDFKDAVELLNAV-----------GLsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
497-720 |
3.92e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVqfqdvsfaYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 576
Cdd:COG3845 258 LEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQ-VAAVGQEPQVFG----RSLQENIA-----------YGLTQKPTMEEITAAAVKSgahsfisglpqgYD---TEVD 637
Cdd:COG3845 330 RRRLgVAYIPEDRLGRGlvpdMSVAENLIlgryrrppfsrGGFLDRKAIRAFAEELIEE------------FDvrtPGPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 638 EAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLS-LVEQADHILFLE 716
Cdd:COG3845 398 TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeILALSDRIAVMY 476
|
....
gi 2203400792 717 GGAI 720
Cdd:COG3845 477 EGRI 480
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
516-719 |
4.07e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.84 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------LLD---GKPLPQYEHRYLHRQVAAV 584
Cdd:cd03236 12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 gQEPQ---VFGRSLQENIAYGLTQKP---TMEEITAAAvksgahsfisGLPQGYDTEVDeagsQLSGGQRQAVALARALI 658
Cdd:cd03236 91 -VKPQyvdLIPKAVKGKVGELLKKKDergKLDELVDQL----------ELRHVLDRNID----QLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 659 RKPCVLILDDATSALDANSQLQVEQLLYE--SPERYsrsVLLITQHLSLVEQ-AD--HILFLEGGA 719
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRElaEDDNY---VLVVEHDLAVLDYlSDyiHCLYGEPGA 218
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-478 |
4.54e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 61.34 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFV---GDGIYNNTMGH-----VHSHLQgevfgavlRQETE 274
Cdd:cd18540 20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLfirLAGKIEMGVSYdlrkkAFEHLQ--------TLSFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLlpkkVGKWYQ--LL 352
Cdd:cd18540 92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV----VSIYFQkkIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 353 EVQvRESLAKSSQV--AI-EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYI 429
Cdd:cd18540 168 KAY-RKVRKINSRItgAFnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2203400792 430 GGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18540 247 GGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
503-718 |
4.69e-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: 59.56 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----GGQLLLDGKPLPQyehrY 576
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 LHRQVAAVGQEPQVFGrslqeniayGLTQKPTMEeitaaavksgahsfISGLPQGydtevdeagsqLSGGQRQAVALARA 656
Cdd:cd03232 77 FQRSTGYVEQQDVHSP---------NLTVREALR--------------FSALLRG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLL-ITQ-HLSLVEQADHILFLEGG 718
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCtIHQpSASIFEKFDRLLLLKRG 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
519-736 |
6.35e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.49 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG---------------KPLPQY------EHRYL 577
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYvidgdrEYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQVAAVGQepqvfgRSLQENIAyglTQKPTMEEITAAAVKSGAHSFISGLpqGYDTE-VDEAGSQLSGGQRQAVALARA 656
Cdd:PRK10636 95 EAQLHDANE------RNDGHAIA---TIHGKLDAIDAWTIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 657 LIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLITQHLSLVEQ-ADHILFLEggaireggtHQQLMEKKGC 735
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPiVDKIIHIE---------QQSLFEYTGN 230
|
.
gi 2203400792 736 Y 736
Cdd:PRK10636 231 Y 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
521-729 |
6.70e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK--------PLPQYEHRYLHR-------QVAAVG 585
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRRLLRtewgfvhQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEPQVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAHSFISGlpqgydTEVDEAGSQLSGGQRQAVALAR 655
Cdd:PRK11701 102 LRMQV---SAGGNIGerlmavgarhYG--------DIRATAGDWLERVEIDA------ARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG-THQQL 729
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGlTDQVL 240
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
200-469 |
6.79e-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: 60.88 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLefvgdGIYNNTMGhvhSHL-QGevFGAVLRQET----- 273
Cdd:cd18548 14 LELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIA-----GILAGYFA---AKAsQG--FGRDLRKDLfekiq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 274 ----EFFQQNQTGNIMSRVTEDTSTLSDSLSenlsLFLWYLVRG--LCLLGI--MLWGSVSLTMVTLIT----LPLLFLL 341
Cdd:cd18548 84 sfsfAEIDKFGTSSLITRLTNDVTQVQNFVM----MLLRMLVRApiMLIGAIimAFRINPKLALILLVAipilALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 342 PKKVGKWYQllevQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNS-WTTSISGM 420
Cdd:cd18548 160 MKKAIPLFK----KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNpLMMLIMNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 421 LLkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL---LSIYPRVQ 469
Cdd:cd18548 236 AI-VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLsmvFVMLPRAS 286
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
527-681 |
6.83e-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: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL---PQY-EHRY-------LHRQVAAVGQEPQvfgrsL 595
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYiKADYegtvrdlLSSITKDFYTHPY-----F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 596 QENIAygltqKPTMEEitaaavksgahsfisglpQGYDTEVDEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03237 96 KTEIA-----KPLQIE------------------QILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
....*.
gi 2203400792 676 NSQLQV 681
Cdd:cd03237 149 EQRLMA 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
502-685 |
1.03e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyehrylhrqv 581
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------------ 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGRSLQEN-IAYGLTQKPTMEEitaaaVKSGAH--SF-ISG---LPQGYdtevdeagsQLSGGQRQAVALA 654
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSNpLLYMMRCFPGVPE-----QKLRAHlgSFgVTGnlaLQPMY---------TLSGGQKSRVAFA 639
|
170 180 190
....*....|....*....|....*....|.
gi 2203400792 655 RALIRKPCVLILDDATSALDANSqlqVEQLL 685
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDA---VEALI 667
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
516-678 |
1.28e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKP-----LPQYEHR---YLHRQVAAV 584
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkdIRDSEALgivIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 585 gqePQVfgrSLQENI-------AYGL-----TQKPTMEEItaAAVksgahsfisGLPQGYDTEVDEAGSqlsgGQRQAVA 652
Cdd:NF040905 91 ---PYL---SIAENIflgneraKRGVidwneTNRRARELL--AKV---------GLDESPDTLVTDIGV----GKQQLVE 149
|
170 180
....*....|....*....|....*..
gi 2203400792 653 LARALIRKPCVLILDDATSAL-DANSQ 678
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSA 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
503-717 |
1.35e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQVA 582
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQEPQVF--GRSLQENIAYGLtqkptmEEITAAAVKSGAHSFISGLP-QGYDTEvdEAGSQLSGGQRQAVALARALIR 659
Cdd:TIGR03719 389 YVDQSRDALdpNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQ--KKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 660 KPCVLILDDATSALDansqlqVEQL--LYESPERYSRSVLLITqH----LSLVeqADHILFLEG 717
Cdd:TIGR03719 461 GGNVLLLDEPTNDLD------VETLraLEEALLNFAGCAVVIS-HdrwfLDRI--ATHILAFEG 515
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
516-684 |
1.40e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP-QYEHRYLHRQVAAVGQE-PQVFGR 593
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 594 SLQENIAYGltQKPT---------MEEITAAAVKSgahsfisglpqgYDTEVD--EAGSQLSGGQRQAVALARALIRKPC 662
Cdd:PRK10982 89 SVMDNMWLG--RYPTkgmfvdqdkMYRDTKAIFDE------------LDIDIDprAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180
....*....|....*....|..
gi 2203400792 663 VLILDDATSALdanSQLQVEQL 684
Cdd:PRK10982 155 IVIMDEPTSSL---TEKEVNHL 173
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
520-737 |
3.72e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPL----P------------QY--------E 573
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPedragegifmafQYpveipgvsN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 574 HRYLHRQVAAV----GQEPQ---VFGRSLQENIAygLTQKPtmEEITAAAVKSGahsfisglpqgydtevdeagsqLSGG 646
Cdd:PRK09580 96 QFFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIA--LLKMP--EDLLTRSVNVG----------------------FSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 647 QRQAVALARALIRKPCVLILDDATSALDANSqLQVEQLLYESPERYSRSVLLITQHLSLVE--QADHILFLEGGAIREGG 724
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSG 228
|
250
....*....|....*
gi 2203400792 725 THQ--QLMEKKGCYW 737
Cdd:PRK09580 229 DFTlvKQLEEQGYGW 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-673 |
4.03e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLvqfqDVSFaypnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRy 576
Cdd:PRK10762 5 LQLKGI----DKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 577 lHRQVAAVG---QE----PQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVDEagsqLSGGQ 647
Cdd:PRK10762 75 -SSQEAGIGiihQElnliPQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGE 146
|
170 180
....*....|....*....|....*.
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-683 |
1.16e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQY-EHRYLHRQVAAVGQEPQVFGRS-LQENIAYG 602
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykPQYiKPDYDGTVEDLLRSITDDLGSSyYKSEIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 603 LtqkptmeeitaaavksgahsfisGLPQGYDTEVDEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansqlqVE 682
Cdd:PRK13409 441 L-----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VE 487
|
.
gi 2203400792 683 Q 683
Cdd:PRK13409 488 Q 488
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
521-725 |
1.25e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhrqVAAVGQepqvfgrslQENIA 600
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ---------SEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 601 YGLtqkPTMEEITAAAVKSGAHSFISgLPQGYDTE-VDEAGS-------------QLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK15056 91 WSF---PVLVEDVVMMGRYGHMGWLR-RAKKRDRQiVTAALArvdmvefrhrqigELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 667 DDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFLEGGAIREGGT 725
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLgSVTEFCDYTVMVKGTVLASGPT 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-681 |
2.05e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQY-EHRYlHRQVAAV--GQEPQVFGRS-LQENIA 600
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISykPQYiSPDY-DGTVEEFlrSANTDDFGSSyYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 601 YGLtqkptmeeitaaavksgahsfisGLPQGYDTEVDEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQ 680
Cdd:COG1245 441 KPL-----------------------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
.
gi 2203400792 681 V 681
Cdd:COG1245 494 V 494
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
202-458 |
2.07e-08 |
|
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: 56.32 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADtftrNLTLMSI----LTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18567 19 LASPLYLQLVIDEVIVSGDRD----LLTVLAIgfglLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 278 QNQTGNIMSR---VTEDTSTLSDSLSENL--SLFlwylvrGLCLLGIMLWGSVSLTMVTLITLPLLFllpkkVGKW--YQ 350
Cdd:cd18567 95 KRHLGDIVSRfgsLDEIQQTLTTGFVEALldGLM------AILTLVMMFLYSPKLALIVLAAVALYA-----LLRLalYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 351 LLEVQVRESL---AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLqeIKTLNQKEAVAYaVNSWTTSISGMLL---KV 424
Cdd:cd18567 164 PLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLL--VDAINADIRLQR-LQILFSAANGLLFgleNI 240
|
250 260 270
....*....|....*....|....*....|....
gi 2203400792 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAV 458
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRA 274
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
202-478 |
2.39e-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: 56.06 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 282 GNIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd18782 99 GELSTRISE-LDTIRGFLTGTaLTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 361 AKSSQVAIEALSAMPTVRSFANEEgeaqKFREKLQEikTLNQ------KEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18782 177 AKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN--RYARslgegfKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2203400792 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18782 251 LRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
525-730 |
2.42e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYLHRQVAAVGQEPQ----VFGRSLQENI 599
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKrdglVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 600 AygLTQKP----TMEEITAAAVKSGAHSFIsGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK10762 352 S--LTALRyfsrAGGSLKHADEQQAVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 676 NSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAI-----REGGTHQQLM 730
Cdd:PRK10762 429 GAKKEIYQLINQFKAE-GLSIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
508-730 |
2.54e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVA----ALLQNLYQPTGGQLLLDGKPL----PQYEHRYLHR 579
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 580 QVAAVGQEPQV-------FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFI-SGLPQgydtevdeag 640
Cdd:PRK15093 90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDAmRSFPY---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 sQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGA 719
Cdd:PRK15093 158 -ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQ 236
|
250
....*....|.
gi 2203400792 720 IREGGTHQQLM 730
Cdd:PRK15093 237 TVETAPSKELV 247
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
203-478 |
7.34e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 54.82 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGsadtftrNLTLMSILTIASAVLeFVGDGIYNNTMG--------HVHSHLQGEVFGAVLRQETE 274
Cdd:cd18555 20 LIPILTQYVIDNVIVPG-------NLNLLNVLGIGILIL-FLLYGLFSFLRGyiiiklqtKLDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 275 FFQQNQTGNIMSRVtEDTSTLSDSLSENLSL----FLWYLVrglcLLGIMLWGSVSLTMVTLITLPLLFL----LPKKVg 346
Cdd:cd18555 92 FFENRSSGDLLFRA-NSNVYIRQILSNQVISliidLLLLVI----YLIYMLYYSPLLTLIVLLLGLLIVLllllTRKKI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 347 kwYQLLEVQVREsLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA-VNSWTTSISgMLLKVG 425
Cdd:cd18555 166 --KKLNQEEIVA-QTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNiLNSISSSIQ-FIAPLL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 426 ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18555 242 ILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
517-737 |
1.55e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTGGQLLLDGKPLPQY--EHRYlHRQVAAVGQEP-QVF 591
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 592 GRSLQE--NIAYGLTQK----PTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAgsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:CHL00131 98 GVSNADflRLAYNSKRKfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400792 666 LDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVE--QADHILFLEGGAIREGGTHQ--QLMEKKGCYW 737
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGI-NKLMTSENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGDAElaKELEKKGYDW 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
533-721 |
1.56e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 533 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR-YL---HRQVAAVGQEPQVFGR-SLQENIAYGLtqKP 607
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGM--AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 608 TMEEITAAAVKS-GAHSFISGLPqgydtevdeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLy 686
Cdd:PRK11144 104 SMVAQFDKIVALlGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2203400792 687 espERYSRSV----LLITQHL-SLVEQADHILFLEGGAIR 721
Cdd:PRK11144 172 ---ERLAREInipiLYVSHSLdEILRLADRVVVLEQGKVK 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
521-725 |
1.66e-07 |
|
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: 51.94 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVaaLLQNLYqpTGGQLLLDgKPLPQYEHrylhrqvaavgqEPQVFGRSLQENIA 600
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI-SFLPKFSR------------NKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 601 YGLtqkptmeeitaaavksgahsfisglpqGYDTeVDEAGSQLSGGQRQAVALARALIR--KPCVLILDDATSALDansQ 678
Cdd:cd03238 74 VGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLH---Q 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2203400792 679 LQVEQLLyESPERY---SRSVLLITQHLSLVEQADHILFLEGGAIREGGT 725
Cdd:cd03238 123 QDINQLL-EVIKGLidlGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
506-699 |
2.51e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 506 QDVSFAYPNRpdVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqYEHRYLHRQVAAVG 585
Cdd:PRK11147 323 ENVNYQIDGK--QLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 586 QEpqvfgRSLQENIAYGltqkptMEEITAAAVKSGAHSFISGL---PQGYDTEVdeagSQLSGGQRQAVALARALIRKPC 662
Cdd:PRK11147 396 PE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSN 460
|
170 180 190
....*....|....*....|....*....|....*....
gi 2203400792 663 VLILDDATSALDansqlqVE--QLLYESPERYSRSVLLI 699
Cdd:PRK11147 461 LLILDEPTNDLD------VEtlELLEELLDSYQGTVLLV 493
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
502-674 |
4.23e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAypnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhRQV 581
Cdd:PRK13543 11 LLAAHALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVFGR-SLQENIAY--GLTQKPTMEEITAAAVksgahsfISGLPQGYDTEVdeagSQLSGGQRQAVALARALI 658
Cdd:PRK13543 85 AYLGHLPGLKADlSTLENLHFlcGLHGRRAKQMPGSALA-------IVGLAGYEDTLV----RQLSAGQKKRLALARLWL 153
|
170
....*....|....*.
gi 2203400792 659 RKPCVLILDDATSALD 674
Cdd:PRK13543 154 SPAPLWLLDEPYANLD 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
521-677 |
4.34e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY---QPTGGQLLLDGKPLpQYEHRY---LHRQVAAVG---QEPQVF 591
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTV-QREGRLardIRKSRANTGyifQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 592 GR-SLQENIAYG-LTQKPTMEEITAAAVKSGAHSFISGLPQ-GYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK09984 99 NRlSVLENVLIGaLGSTPFWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
....*....
gi 2203400792 669 ATSALDANS 677
Cdd:PRK09984 179 PIASLDPES 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
528-688 |
6.76e-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: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 528 LRPGEVTALVGPNGSGKST-VAALLQNLYQ---PTGGQLLLDGKPLPQYEHRY-----------LHRQVAAVGqEPQVFG 592
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTVG-ETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 RSLQ--ENIAYGLTQKPTMEEITAAAVKsgahsfISGLPQGYDTEV-DEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR00956 163 ARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170
....*....|....*....
gi 2203400792 670 TSALDANSQLQVEQLLYES 688
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTS 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
514-734 |
1.11e-06 |
|
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: 52.32 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 514 NRPDVLVLQGLT---------------FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--------- 569
Cdd:TIGR01257 1933 NKTDILRLNELTkvysgtsspavdrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdvhq 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 570 -----PQY----------EHRYLHRQVAAVGQEpqvfgrslqeniaygltqkpTMEEITAAAVKSgahsfisglpQGYDT 634
Cdd:TIGR01257 2013 nmgycPQFdaiddlltgrEHLYLYARLRGVPAE--------------------EIEKVANWSIQS----------LGLSL 2062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 635 EVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAnsqlQVEQLLYE---SPERYSRSVLLITQHLSLVEQ-AD 710
Cdd:TIGR01257 2063 YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP----QARRMLWNtivSIIREGRAVVLTSHSMEECEAlCT 2138
|
250 260
....*....|....*....|....
gi 2203400792 711 HILFLEGGAIREGGTHQQLMEKKG 734
Cdd:TIGR01257 2139 RLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
525-690 |
1.47e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ------PTGGQLL---------------------LDGKPLPQYEHRYL 577
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTT---FLRYMAMhaidgiPKNCQILhveqevvgddttalqcvlntdIERTQLLEEEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 578 HRQvaAVGQEPQVFGRSLQENIAyGLTQKPT----------MEEITAAAVKSGAHSFISGLPQGYDTEVdEAGSQLSGGQ 647
Cdd:PLN03073 274 AQQ--RELEFETETGKGKGANKD-GVDKDAVsqrleeiykrLELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGW 349
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2203400792 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
502-731 |
1.50e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTGGQLLLDGKPL----PQY---- 572
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnPAQaira 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 573 ------EHRYLHRQVAAVGQEPQVFGRSLQE-----NIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevdeags 641
Cdd:TIGR02633 337 giamvpEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKT-ASPF---LPIG---------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILF-----L 715
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVlGLSDRVLVigegkL 481
|
250
....*....|....*.
gi 2203400792 716 EGGAIREGGTHQQLME 731
Cdd:TIGR02633 482 KGDFVNHALTQEQVLA 497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
517-685 |
2.11e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqpTGGQLLLDGKPlpQYEHRYLhrqVAAVGQEP------QV 590
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRI--IYEQDLI---VARLQQDPprnvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 591 F----------GRSLQE--NIAYGLTQKPT------MEEITAAAVKSGAHSF---ISGLPQGYDTEVDEAGSQLSGGQRQ 649
Cdd:PRK11147 84 YdfvaegieeqAEYLKRyhDISHLVETDPSeknlneLAKLQEQLDHHNLWQLenrINEVLAQLGLDPDAALSSLSGGWLR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2203400792 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLL 685
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL 199
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
202-481 |
2.13e-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: 50.20 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 202 MAIPFFTGRLTDWILQ-------DGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMG-----HVHSHLqgevFGAVL 269
Cdd:cd18580 8 LLLLAFLSQFSNIWLDwwssdwsSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGlrasrRLHDKL----LRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 270 RQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGS--VSLTMVTLITLPLlfllpkKVGK 347
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSpyFLIVLPPLLVVYY------LLQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 348 WYQLLEVQVR--ESLAKS---SQVAiEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKeavAY----AVNSWTTSIS 418
Cdd:cd18580 158 YYLRTSRQLRrlESESRSplySHFS-ETLSGLSTIRAFGWQERFIEENLRLLDA----SQR---AFylllAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 419 GMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQ-MQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
203-478 |
2.53e-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: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 203 AIPFFTGRLTDWILQDGSADTFTRnLTLMSILTIA-SAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18783 20 APPIFFQIVIDKVLVHQSYSTLYV-LTIGVVIALLfEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 282 GNIMSRVTEdTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18783 99 GVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISG---MLLKVGILYIGGQLVTSGA 438
Cdd:cd18783 178 ERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNWPQTLTGpleKLMTVGVIWVGAYLVFAGS 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2203400792 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18783 255 LTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-735 |
2.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhrqvA 582
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQE----PQVFGR------SLQENIA-----YGLTQ---KPTMEEITAAavkSGAHSFisglpqgydteVDEAGSQLS 644
Cdd:NF033858 73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPF-----------ADRPAGKLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQ----VEQLLYESPerySRSVLLITQHLSLVEQADHILFLEGGAI 720
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRIRAERP---GMSVLVATAYMEEAERFDWLVAMDAGRV 215
|
250
....*....|....*
gi 2203400792 721 REGGTHQQLMEKKGC 735
Cdd:NF033858 216 LATGTPAELLARTGA 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
461-731 |
2.77e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 461 LLSIYPRVQKAVGssEKIFEyldrtprcppsglltplhleglvqFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPN 540
Cdd:PRK13549 244 LTALYPREPHTIG--EVILE------------------------VRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 541 GSGKSTVAALLQNLYQptG---GQLLLDGKPL----PQYEHRYlhrQVAAVGQEPQVFG----RSLQENIAYG-LTQKPT 608
Cdd:PRK13549 298 GAGRTELVQCLFGAYP--GrweGEIFIDGKPVkirnPQQAIAQ---GIAMVPEDRKRDGivpvMGVGKNITLAaLDRFTG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 609 MEEITAAAVKSGAHSFISGL------PqgydtevDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVE 682
Cdd:PRK13549 373 GSRIDDAAELKTILESIQRLkvktasP-------ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIY 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 683 QLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIR-----EGGTHQQLME 731
Cdd:PRK13549 446 KLINQLVQQ-GVAIIVISSELPEVlGLSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-719 |
5.04e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 527 TLRPGEVTALVGPNGSGKSTVAALLqnlyqptGGQLlldgKP-LPQYEHRYLHRQV--AAVGQEPQVFGRSLQENiayGL 603
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKIL-------SGEL----IPnLGDYEEEPSWDEVlkRFRGTELQNYFKKLYNG---EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 604 T--QKPTMEEITAAAVKSGAHSFIsglpqgydTEVDEAG-------------------SQLSGGQRQAVALARALIRKPC 662
Cdd:PRK13409 161 KvvHKPQYVDLIPKVFKGKVRELL--------KKVDERGkldevverlglenildrdiSELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 663 VLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQ-AD--HILFLEGGA 719
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYlADnvHIAYGEPGA 290
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
639-748 |
6.18e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 639 AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQADHIL-FLEG 717
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVIDR 219
|
90 100 110
....*....|....*....|....*....|.
gi 2203400792 718 GAIREGGTHQQLMEKKGCYWAMVQaPADAPE 748
Cdd:NF000106 220 GRVIADGKVDELKTKVGGRTLQIR-PAHAAE 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
521-718 |
7.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFG------- 592
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEERRSTGiyayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 --RSLQENI-----AYGLTQKPTMEE-----ITAAAVKSGAHSfisglpqgydTEVdeaGSqLSGGQRQAVALARALIRK 660
Cdd:PRK10982 344 gfNSLISNIrnyknKVGLLDNSRMKSdtqwvIDSMRVKTPGHR----------TQI---GS-LSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400792 661 PCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFLEGG 718
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
526-730 |
8.70e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------LLDGKPLPQY-EHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAYGLTQKPTMEEItaaavksgAHSF-ISGLpqgydteVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK10938 104 EIIQDEVKDPARCEQL--------AQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 676 NSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLM 730
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
525-716 |
8.99e-06 |
|
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: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 525 TFTLRPGeVTALVGPNGSGKSTV-AALLQNLY---QPTGGQLLLDGKPLPQYEHR---YLHRQVAA-----VGQEPQVFg 592
Cdd:cd03240 17 EIEFFSP-LTLIVGQNGAGKTTIiEALKYALTgelPPNSKGGAHDPKLIREGEVRaqvKLAFENANgkkytITRSLAIL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 593 rslqENIAY---GLTQKPTMEEITaaavksgahsfisglpqgydtevdeagsQLSGGQRQAV------ALARALIRKPCV 663
Cdd:cd03240 95 ----ENVIFchqGESNWPLLDMRG----------------------------RCSGGEKVLAsliirlALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 664 LILDDATSALDA-NSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLE 716
Cdd:cd03240 143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
502-688 |
1.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqpTGGQllldgkplPQYEHRYLHrqv 581
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDH--------PQGYSNDLT--- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 aavgqepqVFGR---------SLQENIAYgLTQKPTMEEITAAAVK----SGAHSFIsGLPQ-----------------G 631
Cdd:PRK10938 320 --------LFGRrrgsgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFDSI-GIYQavsdrqqklaqqwldilG 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 632 YDTEVDEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQ---VEQLLYES 688
Cdd:PRK10938 390 IDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlNRQLVrrfVDVLISEG 451
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
521-732 |
1.75e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVAAV--GQEPQVFGrslQEN 598
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAIsaGLSGQLTG---IEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 599 IAY-----GLTQKpTMEEITAAAVK-SGAHSFISGLPQGYdtevdeagsqlSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK13546 106 IEFkmlcmGFKRK-EIKAMTPKIIEfSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 673 LDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 732
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
268-478 |
2.05e-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: 47.09 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 268 VLRQETEFFQQNQTGNIMSRV-TEDT--STLSDSLSE---NLSLFLWYLVrglcllgIMLWGSVSLTMVTLITLPLLFLL 341
Cdd:cd18569 85 VLRLPVEFFSQRYAGDIASRVqSNDRvaNLLSGQLATtvlNLVMAVFYAL-------LMLQYDVPLTLIGIAIALLNLLV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 342 PKKVGKWYQLL-EVQVRESlAKSSQVAIEALSAMPTVRSFANEEGeaqkFREKL--QEIKTLNQKEAVAyAVNSWTTSIS 418
Cdd:cd18569 158 LRLVSRKRVDLnRRLLQDS-GKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELG-RTNQLLGALP 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 419 GMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18569 232 TLLSALTnaaILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
503-717 |
2.51e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQVA 582
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 583 AVGQ-----EPQvfgRSLQENIAYGLtqkptmEEITAA--AVKS----GAHSFisglpQGYDTEvDEAGsQLSGGQRQAV 651
Cdd:PRK11819 391 YVDQsrdalDPN---KTVWEEISGGL------DIIKVGnrEIPSrayvGRFNF-----KGGDQQ-KKVG-VLSGGERNRL 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400792 652 ALARALIRKPCVLILDDATSALDansqlqVEQL--LYESPERYSRSVLLITqH----LSLVeqADHILFLEG 717
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLD------VETLraLEEALLEFPGCAVVIS-HdrwfLDRI--ATHILAFEG 517
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
268-481 |
3.11e-05 |
|
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: 46.31 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 268 VLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVR-----GLCL---------LGIMLWGSVSLTMVtli 333
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSiigtfILIIiylpwfaiaLPPLLVLYYFIANY--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 334 tlpllfllpkkvgkwYQ--LLEVQVRESLAKSSQVA--IEALSAMPTVRSFaneeGEAQKFREKLQE-IKTLNQKEAVAY 408
Cdd:cd18606 155 ---------------YRasSRELKRLESILRSFVYAnfSESLSGLSTIRAY----GAQDRFIKKNEKlIDNMNRAYFLTI 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 409 AVNSW----TTSISGML-LKVGILYIGGQLVTSGAvSSGNLVTFVLyqmQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18606 216 ANQRWlairLDLLGSLLvLIVALLCVTRRFSISPS-STGLVLSYVL---QITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
233-482 |
3.15e-05 |
|
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: 46.69 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 233 ILTIASAVLEFVGDGIYnnTMG------HVHSHLQGEVFGAVLRqeteFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLF 306
Cdd:cd18604 51 LISLLSVLLGTLRYLLF--FFGslrasrKLHERLLHSVLRAPLR----WLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 307 LWYLVRGLCLLG-------IMLWGSVSLTMVTLItlpllfllpkkVGKWYqlLEVQ--VR--ESLAKS---SQVAiEALS 372
Cdd:cd18604 125 LESTLSLLVILIaivvvspAFLLPAVVLAALYVY-----------IGRLY--LRASreLKrlESVARSpilSHFG-ETLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 373 AMPTVRSFANEEgeaqKFREKLQE-IKTLNQKEAVAYAVNSW----TTSISGML-LKVGILyiggqLVTSGAVSSGnLVT 446
Cdd:cd18604 191 GLVTIRAFGAEE----RFIEEMLRrIDRYSRAFRYLWNLNRWlsvrIDLLGALFsFATAAL-----LVYGPGIDAG-LAG 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 2203400792 447 FVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:cd18604 261 FSLsFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
531-717 |
3.22e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 531 GEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGkPLPQYEHRYLhrqvaavgqepqvfgrslqeniaygltqkptme 610
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 611 eitaaavksgahsfisglpqgydtevdeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*...
gi 2203400792 691 RYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
522-742 |
4.61e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 522 QGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYLHRQVAAVGQ---EPQVFGR-SLQ 596
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENIAYGLTQK------------PTMEEITAAAVKSgahsfisgLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK09700 360 QNMAISRSLKdggykgamglfhEVDEQRTAENQRE--------LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 665 ILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHI-LFLEGGAIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELpEIITVCDRIaVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
643-725 |
5.46e-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: 46.93 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 643 LSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESperySRSVLLITQHLSLVEQADHILFL- 715
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKTADYIIDLg 905
|
90
....*....|.
gi 2203400792 716 -EGGAirEGGT 725
Cdd:TIGR00630 906 pEGGD--GGGT 914
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-719 |
9.11e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 527 TLRPGEVTALVGPNGSGKSTVAALLqnlyqptGGQLlldgKP-LPQYEH---------RYlhrqvaaVGQEPQVFGRSLQ 596
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKIL-------SGEL----KPnLGDYDEepswdevlkRF-------RGTELQDYFKKLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 597 ENiaygltqkptmeEITaAAVKSgahSFISGLPQGYDTEV-------DEAG-------------------SQLSGGQRQA 650
Cdd:COG1245 157 NG------------EIK-VAHKP---QYVDLIPKVFKGTVrellekvDERGkldelaeklglenildrdiSELSGGELQR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYE-SPErySRSVLLITQHLSLVEQ-AD--HILFLEGGA 719
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRElAEE--GKYVLVVEHDLAILDYlADyvHILYGEPGV 291
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
490-688 |
1.62e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 490 PSGLLTPLhleglVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-LLDGKP 568
Cdd:PRK10636 305 PESLPNPL-----LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 569 L---PQYEHRYLHRQVAAVGQ----EPQVFGRSLQENIaygltqkptmeeitaaavksGAHSFisglpQGydTEVDEAGS 641
Cdd:PRK10636 377 LgyfAQHQLEFLRADESPLQHlarlAPQELEQKLRDYL--------------------GGFGF-----QG--DKVTEETR 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2203400792 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES 688
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEA 472
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
263-465 |
1.69e-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: 44.41 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 263 EVFGAVLRQETEFFQQNQTG---NIMSRVTEDTSTLSDSLSENL----------SLFLWYLVrGLCLLGIMLwGSVSL-- 327
Cdd:cd18582 76 RVFRHLHSLSLRFHLSRKTGalsRAIERGTRGIEFLLRFLLFNIlptilelllvCGILWYLY-GWSYALITL-VTVALyv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 328 --TMvtlitlpllfllpkKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 405
Cdd:cd18582 154 afTI--------------KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400792 406 VAYAVNSWTTSI---SGMllkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIY 465
Cdd:cd18582 220 TSLALLNIGQALiisLGL---TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
643-725 |
1.99e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 643 LSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESperySRSVLLITQHLSLVEQADHILFL- 715
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK----GNTVVVIEHNLDVIKCADWIIDLg 245
|
90
....*....|.
gi 2203400792 716 -EGGAirEGGT 725
Cdd:cd03271 246 pEGGD--GGGQ 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
503-560 |
7.40e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 7.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400792 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGG 560
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
587-724 |
8.57e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 587 EPQVFGRSLQENIAYGLTQKPTMEEITAAaVKSGAHSFISGLPQGYDTevdeagSQLSGGQRQAVALARALI---RKPCV 663
Cdd:PRK00635 1651 EGKHFGQLLQTPIEEVAETFPFLKKIQKP-LQALIDNGLGYLPLGQNL------SSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400792 664 LILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGG 724
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLVQL-RTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
641-718 |
1.82e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 641 SQLSGGQRQAVALARALI---RKPCVLILDDATSALDANSqlqVEQLLY--ESPERYSRSVLLITQHLSLVEQADHILFL 715
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD---IKALIYvlQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
....*
gi 2203400792 716 --EGG 718
Cdd:PRK00635 885 gpEGG 889
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
205-472 |
1.83e-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: 41.06 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 205 PFFTGRLTDWILQDGSADTFT--RNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18560 16 PLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 283 N---IMSRVTEDTSTLsdslsenLSLFLWYLVRGL--CLLGIMLW---GSVSLTMVTLITLPLLFLLPKKVGKWyqllEV 354
Cdd:cd18560 96 EvvrIMDRGTESANTL-------LSYLVFYLVPTLleLIVVSVVFafhFGAWLALIVFLSVLLYGVFTIKVTEW----RT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 355 QVRESLAK----SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIG 430
Cdd:cd18560 165 KFRRAANKkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2203400792 431 GQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAV 472
Cdd:cd18560 245 GYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
522-551 |
1.96e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|....
gi 2203400792 522 QGLTFTLRPGEVTALVGPNGSGKST----VAALL 551
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
211-482 |
3.19e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 40.21 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 211 LTDWILQDGSADTFTRN------------LTLM-SILTIASAVLEFVGdgiYNNTMGHVHSHLqgevFGAVLRQETEFFQ 277
Cdd:cd18605 22 LSYWVSHSNNSFFNFINdsfnffltvygfLAGLnSLFTLLRAFLFAYG---GLRAARRLHNKL----LSSILFAKMSFFD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 278 QNQTGNIMSRVTEDTSTLSDSLS-------ENLSLFLWYLVrGLCLlgIMLWGSVSLTMVTLITLpllfllpkKVGKWYQ 350
Cdd:cd18605 95 KTPVGRILNRFSSDVYTIDDSLPfilnillAQLFGLLGYLV-VICY--QLPWLLLLLLPLAFIYY--------RIQRYYR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 351 LLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFANEEGEAQKFREKLqeikTLNQKEAVA-YAVNSWttsISGMLLKVG 425
Cdd:cd18605 164 ATSRELKrlNSVNLSPLYTHfsETLKGLVTIRAFRKQERFLKEYLEKL----ENNQRAQLAsQAASQW---LSIRLQLLG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400792 426 ILYIGGQLVTS------GAVSSGNLVTFVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:cd18605 237 VLIVTFVALTAvvqhffGLSIDAGLIGLALsYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
526-547 |
3.65e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 3.65e-03
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
502-716 |
4.20e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 502 LVQFQDVSFAYPNRpdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK13541 1 MLSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 582 AAVGQEPQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsglpqgydtevDEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK13541 77 HNLGLKLEM---TVFENLKFWSEIYNSAETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400792 662 CVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLE 716
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVMKAN--SGGIVLLSSHLESSIKSAQILQLD 195
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
497-555 |
6.02e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 6.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 497 LHLEGLVQFQDVsfaypnrpdvlvlqglTFTLRPGeVTALVGPNGSGKST-VAALLQNLY 555
Cdd:pfam13476 1 LTIENFRSFRDQ----------------TIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
362-477 |
7.54e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 39.05 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEiktlnqKEAVAYAVNSWTTSISG---MLLKVGIL---YIGGQLVT 435
Cdd:cd18583 174 EERSILTESLLNWETVKYFNREPYEKERYREAVKN------YQKAERKYLFSLNLLNAvqsLILTLGLLagcFLAAYQVS 247
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2203400792 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEK 477
Cdd:cd18583 248 QGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
225-321 |
7.96e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 39.23 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 225 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENls 304
Cdd:cd18601 59 DFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT-- 136
|
90
....*....|....*..
gi 2203400792 305 lFLWYLVRGLCLLGIML 321
Cdd:cd18601 137 -FLDFLQLLLQVVGVVL 152
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
211-310 |
8.17e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 39.00 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400792 211 LTDW---ILQDGSADTFTRN--LTLMSILTIASAVLEFVGDGIYnnTMGHVHS--HLQGEVFGAVLRQETEFFQQNQTGN 283
Cdd:cd18603 22 LSEWsddPALNGTQDTEQRDyrLGVYGALGLGQAIFVFLGSLAL--ALGCVRAsrNLHNKLLHNILRAPMSFFDTTPLGR 99
|
90 100
....*....|....*....|....*..
gi 2203400792 284 IMSRVTEDTSTLSDSLSENLSLFLWYL 310
Cdd:cd18603 100 ILNRFSKDIDTVDNTLPQNIRSFLNCL 126
|
|
| |
