|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
78-800 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 954.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 78 ASLAWL-GTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 156
Cdd:TIGR00958 1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 157 KPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGshptAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGN 231
Cdd:TIGR00958 72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 232 PVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 311
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 312 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 391
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 392 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 471
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 472 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 551
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 711
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLME 791
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*....
gi 1168024055 792 KKGCYWAMV 800
Cdd:TIGR00958 703 DQGCYKHLV 711
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
260-538 |
8.09e-167 |
|
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: 483.90 E-value: 8.09e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 500 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
261-802 |
5.78e-155 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 464.25 E-value: 5.78e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:COG1132 37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 420
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 421 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 500
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 501 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP-PSGLLTPLHLEGLVQFQDVSFAYPnrPDVL 579
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI 659
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAns 737
Cdd:COG1132 435 RYG---RPdaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDT-- 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 738 qlQVEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:COG1132 510 --ETEALIQEALERLMkgRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
552-780 |
1.80e-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: 403.39 E-value: 1.80e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 711
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
262-801 |
2.67e-124 |
|
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: 389.58 E-value: 2.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 341
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 342 GNIMSRVTeDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 421
Cdd:COG2274 253 GDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkVGILYIGGQLVTSGAVS 500
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVIDGQLT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 501 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQFQDVSFAYPNRpDVL 579
Cdd:COG2274 411 LGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLpRLKGDIELENVSFRYPGD-SPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI 659
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQL 739
Cdd:COG2274 570 TLGDPD-ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 740 QVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:COG2274 649 IILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
320-796 |
1.98e-105 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 335.90 E-value: 1.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 320 LQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLF 399
Cdd:TIGR02204 93 IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 400 LLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklQEIKTLNQKEAVAYAVNSWTTSISG 479
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFG---GAVEKAYEAARQRIRTRALLTAIVI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 480 MLL---KVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP--RCPPSGLL 554
Cdd:TIGR02204 250 VLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 555 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH 634
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 635 RYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVA 712
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYG---RPdaTDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
....
gi 1168024055 793 KGCY 796
Cdd:TIGR02204 565 GGLY 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
563-802 |
9.86e-99 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 306.00 E-value: 9.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 722
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 723 VLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
265-796 |
1.64e-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: 312.04 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 265 PFFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLE----FVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:TIGR02203 31 STLAALLKP-LLDDGFGGRDRSVLWWVPLVVIGLAVLRgicsFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 416
Cdd:TIGR02203 110 TGTLLSRITFDSEQVASAATDAFIV----LVREtltvIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 417 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 496
Cdd:TIGR02203 186 QNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 497 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPLHLEGLVQFQDVSFAYPNRp 576
Cdd:TIGR02203 266 GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQ 656
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 ENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 736
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 737 SQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 796
Cdd:TIGR02203 504 SERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
260-538 |
1.63e-93 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 294.45 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 500 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
260-538 |
8.58e-86 |
|
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: 274.05 E-value: 8.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 500 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
531-794 |
6.85e-80 |
|
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: 267.39 E-value: 6.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 531 AVGSSEKIFEYLDRTPRCPPSGLLT-PLHLEGLVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAA 609
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPlPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 610 LLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQkPTMEEITAAAVKSGAHSFISGLP 689
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD-ASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 690 QGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQA 769
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 1168024055 770 DHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
422-808 |
1.33e-79 |
|
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: 267.84 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQE-----IKT------LNQKEAVAYAVnswttsisGMllkVGILYIG 490
Cdd:COG5265 216 EANTRAVDSLLNYETVKYFGNEAREARRYDEALARyeraaVKSqtslalLNFGQALIIAL--------GL---TAMMLMA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 491 GQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHL-EGLVQFQDVS 569
Cdd:COG5265 285 AQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVgGGEVRFENVS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 570 FAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP 648
Cdd:COG5265 365 FGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 QVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLIL 726
Cdd:COG5265 442 VLFNDTIAYNIAYG---RPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 727 DDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY---WAMVQ 801
Cdd:COG5265 519 DEATSALDSRT----ERAIQAALREVArgRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYaqmWARQQ 594
|
....*..
gi 1168024055 802 APADAPE 808
Cdd:COG5265 595 EEEEAEE 601
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
318-801 |
9.66e-79 |
|
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: 264.71 E-value: 9.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 318 SHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 382
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNlylrvllpllvallvILAAVAFLAFFSPALALVLALGLLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 383 GSVSLTMVtlvtlpllfllpkkVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 462
Cdd:COG4987 168 AGLLLPLL--------------AARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 463 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLyqmqFTQAV-EVLLSI---YPRVQKAVGSSEKI 538
Cdd:COG4987 234 RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVL----AALALfEALAPLpaaAQHLGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 539 FEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 618
Cdd:COG4987 310 NELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 619 GGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 696
Cdd:COG4987 389 SGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA---RPdaTDEELWAALERVGLGDWLAALPDGLDTWL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 697 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLE 776
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|....*
gi 1168024055 777 GGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
260-538 |
2.84e-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: 248.77 E-value: 2.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 500 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
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 ... |
286-796 |
1.67e-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: 259.29 E-value: 1.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 286 RNLTLMSILTIAS---AVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQ----ETEFFQQNQTGNIMSRVTEdTSTLSDS 358
Cdd:TIGR01846 173 RGLSTLSVLALAMlavAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHllglPLGYFESRRVGDTVARVRE-LEQIRNF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 359 LSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVRESLAKSSQVA---IEALSAMP 435
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP---ILRKRVEDKFERSAAATsflVESVTGIE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 436 TVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFT 515
Cdd:TIGR01846 329 TIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVT 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 516 QAVEVLLSIYPRVQKAVGSSEKIFEYLDrTPRCP-PSGLLTPLHLEGLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEV 593
Cdd:TIGR01846 409 QPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPrSAGLAALPELRGAITFENIRFRYaPDSPEVL--SNLNLDIKPGEF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 594 TALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEIT 673
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 674 AAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPEryS 753
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--G 642
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1168024055 754 RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 796
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
561-794 |
2.17e-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: 244.44 E-value: 2.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 561 GLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 720
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 721 PCVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:cd03254 158 PKILILDEATSNIDTET----EKLIQEALEKLMkgRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
563-797 |
3.47e-75 |
|
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: 244.06 E-value: 3.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 722
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 723 VLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYW 797
Cdd:cd03251 159 ILILDEATSALDTES----ERLVQAALERLMknRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
314-796 |
3.14e-71 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 244.54 E-value: 3.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 314 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 389
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 390 VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 469
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 470 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 548
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 549 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP 628
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 629 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQR 708
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQ 788
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
....*...
gi 1168024055 789 LMEKKGCY 796
Cdd:PRK11176 565 LLAQNGVY 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
323-802 |
1.24e-70 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 243.33 E-value: 1.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 323 EVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLS----DSLSENLSLFLWYLVrglcLLGIMLWGSVSLTMVTLVTLPLL 398
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVV----LLPLALFMNWRLSLVLVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 399 FLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklqeiKTLNQKEAVAYAVNSW----- 473
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALR------DIADNLLAAQMPVLSWwalas 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 474 -TTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPS 551
Cdd:PRK13657 244 vLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPdVRDPP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 552 GLLTPLHLEGLVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ 631
Cdd:PRK13657 324 GAIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQ 709
Cdd:PRK13657 402 VTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
490
....*....|...
gi 1168024055 790 MEKKGCYWAMVQA 802
Cdd:PRK13657 557 VARGGRFAALLRA 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
563-802 |
1.09e-69 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 229.42 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 721
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:cd03253 157 PILLLDEATSALDTHT----EREIQAALRDVSkgRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
...
gi 1168024055 800 VQA 802
Cdd:cd03253 233 WKA 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
563-801 |
6.70e-68 |
|
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: 224.67 E-value: 6.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 721
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
563-778 |
9.84e-67 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 218.79 E-value: 9.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 722
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 723 VLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGG 778
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
561-780 |
5.62e-62 |
|
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: 207.83 E-value: 5.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 561 GLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGRSLQENIAYGLtQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 720
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
260-518 |
6.04e-60 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 204.41 E-value: 6.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 337
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 338 QNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 417
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 418 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 497
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 1168024055 498 AVSSGNLVTFVLYQMQFTQAV 518
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
293-801 |
3.53e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 211.89 E-value: 3.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 293 ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDslsenlslfLWYLV- 371
Cdd:PRK10790 73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---------LYVTVv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 372 ----RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV----QVRESLAKSSQVAIEALSAMPTVRSFANE 443
Cdd:PRK10790 144 atvlRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 444 egeaQKFREKLQEIKTLNqkeavaYAVNSWTTSISGMLLK-----------VGILYIGGqLVTSGAVSSGNLVTFVLYQM 512
Cdd:PRK10790 224 ----ARFGERMGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 513 QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRtPRCPPSGLLTPLHlEGLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGE 592
Cdd:PRK10790 293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 593 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltQKPTMEEI 672
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 673 TAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeRY 752
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--RE 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1168024055 753 SRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:PRK10790 525 HTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
335-802 |
1.44e-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: 212.29 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 FFQQNQTGNIMSRVTeDTSTLSDSL-SENLSLFL--WYLVrglcLLGIML-WGSVSLTMVTLVTLPLLFLLPKKVGKWYQ 410
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 411 LLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQK----FREKLQEIKTLNQKEAVAYAVNSWTTSIsgmlLKVGI 486
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLI----LNVVI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 487 LYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQF 565
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYP-NRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAV 644
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 GQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 724
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 725 ILDDATSALDANSQLQ-VEQLLYESperySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQA 802
Cdd:TIGR01193 634 ILDESTSNLDTITEKKiVNNLLNLQ----DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
418-792 |
2.63e-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: 203.06 E-value: 2.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 418 ESLAKSSQVaIEALSAMPTVRsfaneegeaQKFREKLQEIKTLNqkeAVAYAVNSWTTSIS---GMLLKVGILYIGGQLV 494
Cdd:COG4618 198 EAALRNAEV-IEAMGMLPALR---------RRWQRANARALALQ---ARASDRAGGFSALSkflRLLLQSAVLGLGAYLV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 495 TSGAVSSGN------LVTFVLyqmqftQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPlHLEGLVQFQDV 568
Cdd:COG4618 265 IQGEITPGAmiaasiLMGRAL------APIEQAIGGWKQFVSARQAYRRLNELLAAVPA-EPERMPLP-RPKGRLSVENL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 569 SFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP 648
Cdd:COG4618 337 TVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 QVFGRSLQENIAyGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:COG4618 416 ELFDGTIAENIA-RFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
531-775 |
2.18e-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: 196.74 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 531 AVGSSEKIFEYLDRTPR-CPPSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAA 609
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRpLAGKAPVTAAPASSLE-FSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 610 LLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLP 689
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 690 QGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPERYS--RSVLLITQHLSLVE 767
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEALRALAqgRTVLLVTHRLALAA 521
|
....*...
gi 1168024055 768 QADHILFL 775
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 ... |
480-792 |
1.96e-51 |
|
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: 188.71 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 480 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 558
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPsRDPAMPLPEP-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 559 lEGLVQFQDVSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:TIGR01842 314 -EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALI 718
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 719 RKPCVLILDDATSALDAnsqlQVEQLLYE---SPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDE----EGEQALANaikALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-799 |
2.66e-51 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 188.77 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 330 RQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIM-LWGSVSLTMVTLVTLPLLFLLPKKVGKw 408
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGD- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 409 yqllevQVRESLaKSSQVAI--------EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSIS-G 479
Cdd:PRK10789 160 ------QLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAiG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 480 M--LLKVGilyiGGQ-LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPpSGLLTP 556
Cdd:PRK10789 233 ManLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 636
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALA 714
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*
gi 1168024055 795 CYWAM 799
Cdd:PRK10789 542 WYRDM 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
445-801 |
8.17e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 181.95 E-value: 8.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 445 GEAQKFREKL--QEIKTLNQKEAVAyavnswttSISGM----------LLKVGILYIGGQLVTSGAVSSGNLVTFVLYQM 512
Cdd:PRK11160 217 GAEDRYRQQLeqTEQQWLAAQRRQA--------NLTGLsqalmilangLTVVLMLWLAAGGVGGNAQPGALIALFVFAAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 513 QftqAVEVLLSI---YPRVQKAVGSSEKIFEYLDRTP--RCPPSGLLTPLHleGLVQFQDVSFAYPNRPDvLVLQGLTFT 587
Cdd:PRK11160 289 A---AFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 588 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKp 667
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 668 TMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYE 747
Cdd:PRK11160 442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 748 SPErySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQ 801
Cdd:PRK11160 521 HAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
318-763 |
1.10e-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: 174.86 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 318 SHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 382
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvivpagvalvvGAAAVAAIAVLSVPAALILAAGLLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 383 GSVSLTMVTLvtlpllfllpkKVGKWYQLLEVQVRESLAkssQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 462
Cdd:TIGR02868 166 AGFVAPLVSL-----------RAARAAEQALARLRGELA---AQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 463 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 542
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 543 DRTPRCP----PSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 618
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLE-LRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 619 GGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 696
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 697 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERysRSVLLITQHL 763
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
563-793 |
1.80e-46 |
|
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: 165.58 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GahsfISGLpqgYDTEVgeagSQLSGGQRQAVALAR 715
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFGPENlglpREEIRERVEEALELvG----LEHL---ADRPP----HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKK 793
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
260-538 |
7.58e-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: 165.97 E-value: 7.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 419
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 420 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 499
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 500 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
529-799 |
1.15e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.11 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 529 QKAVGSSEKIFEYLDrTPRCPPSGLLTPLHLEGLVQF--QDVSfaypnrpdVLVLQG------LTFTLRPGEVTALVGPN 600
Cdd:PRK11174 315 AQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIeaEDLE--------ILSPDGktlagpLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 601 GSGKST-VAALLQNL-YQptgGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKPTM--EEITAAA 676
Cdd:PRK11174 386 GAGKTSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 677 VKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPERYSRS- 755
Cdd:PRK11174 460 ENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS----EQLVMQALNAASRRq 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1168024055 756 -VLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:PRK11174 536 tTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
581-731 |
1.00e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.81 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQENI 659
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 660 AYGLtqkpTMEEITAAAVKSGAHSFISGLPQGY--DTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
561-785 |
2.97e-44 |
|
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: 159.20 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 561 GLVQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGRSLQENIAygltqkP----TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALAR 715
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT 785
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
562-782 |
4.27e-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: 4.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEHRYL 637
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQ-----VF--GRSLQENI-AYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQLSGG 706
Cdd:cd03257 81 RKEIQMVFQDPMsslnpRMtiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPH-----------ELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIRE 782
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
262-538 |
2.60e-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: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQ-DGSADTFTRNLT-----LMSILTIASA-------VLEFVGDGIYNNtmghvhshLQGEVFGAV 328
Cdd:cd18573 13 MSVPFAIGKLIDVASKeSGDIEIFGLSLKtfalaLLGVFVVGAAanfgrvyLLRIAGERIVAR--------LRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 329 LRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKW 408
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 409 YQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILY 488
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168024055 489 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
564-780 |
7.31e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.59 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRylhRQ 640
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppEWR---RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPQGY-DTEVgeagSQLSGGQRQAVALARA 716
Cdd:COG4619 76 VAYVPQEPALWGGTVRDNLPFPFQlreRKFDRERALELLER-----L--GLPPDIlDKPV----ERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
293-801 |
1.38e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.90 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 293 ILTIASAVleFVGDGI---YNNTMGH-VHSHLQGEVFGAVLRQETEFFQQ--NQTGNIMSRVTEDTSTLSDSLSENLSLF 366
Cdd:PTZ00265 872 ILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 367 LWYLVRGL---------C-LLGIMLWGSVSLTM----VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAI-EAL 431
Cdd:PTZ00265 950 THFIVLFLvsmvmsfyfCpIVAAVLTGTYFIFMrvfaIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIqEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 432 SAMPTVRSFANEE------GEAQKFREKLQEIKTLnqkeavayaVNS--WTTSISGMLLKVGILY-IGGQLVTSGAVSSG 502
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTL---------VNSmlWGFSQSAQLFINSFAYwFGSFLIRRGTILVD 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 503 NLVTfVLYQMQFTQAVE-VLLSIYPRVQKAVGSSEKIFEYLDRTP----------RCPPSGLLtplhlEGLVQFQDVSFA 571
Cdd:PTZ00265 1101 DFMK-SLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSnidvrdnggiRIKNKNDI-----KGKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 572 YPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY------------QPTG-------------------- 619
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 620 ----------------------GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAV 677
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 678 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVL 757
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1168024055 758 LITQHLSLVEQADHILFLE-----GGAIREGGTHQQLME-KKGCYWAMVQ 801
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
562-790 |
1.63e-42 |
|
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: 155.20 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQV-FGRSLQENIAYGLT------QKPTME--EITAAAVKS-GAHSFIsglpqgyDTEVGEagsqLSGGQRQAV 711
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRYphlglfGRPSAEdrEAVEEALERtGLEHLA-------DRPVDE----LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 790
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
533-791 |
5.30e-42 |
|
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: 160.84 E-value: 5.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 533 GSSEKIFEY---LDRTPRCPPSGLLTPLHLEG---LVQFQDVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGK 604
Cdd:COG1123 225 GPPEEILAApqaLAAVPRLGAARGRAAPAAAAaepLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 605 STVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP--QVFGR-SLQENIAYGLTQKPTMeeiTAAAVK 678
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPysSLNPRmTVGDIIAEPLRLHGLL---SRAERR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 679 SGAHSFIS--GLPQGYdtevgeAG---SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYS 753
Cdd:COG1123 382 ERVAELLErvGLPPDL------ADrypHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELG 455
|
250 260 270
....*....|....*....|....*....|....*....
gi 1168024055 754 RSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:COG1123 456 LTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
562-791 |
2.19e-41 |
|
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: 151.88 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:COG1124 1 MLEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEP-------QVFGRSLQENIA-YGLTQkpTMEEITAAAVKSG-AHSFISGLPqgydtevgeagSQLSGGQRQAV 711
Cdd:COG1124 81 VQMVFQDPyaslhprHTVDRILAEPLRiHGLPD--REERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 790
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 1168024055 791 E 791
Cdd:COG1124 228 A 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
562-794 |
7.84e-41 |
|
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: 150.01 E-value: 7.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlPQYEHRYLHRQV 641
Cdd:COG4555 1 MIEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRK 720
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLL---YESPerysRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKG 794
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILralKKEG----KTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
563-778 |
1.21e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 148.00 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPDV--LVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQPTGgqllldgkplpqyeHRYLHR 639
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGRSLQENIAYGltqKPTMEE-----ITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALA 714
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFG---KPFDEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 715 RALIRKPCVLILDDATSALDAnsqlQVEQLLYES----PERYSRSVLLITQHLSLVEQADHILFLEGG 778
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
564-778 |
2.05e-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: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 643
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQRQAV 711
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGG 778
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
261-538 |
1.21e-39 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 148.47 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 420
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 421 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 500
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1168024055 501 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd07346 255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
563-782 |
5.33e-39 |
|
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: 144.15 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNR-PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyehryLHRQV 641
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFG-RSLQENIAYGLTqkptMEEITAAAVKSGAHSFISglpqgydtEVGEAG------SQLSGGQRQAVALA 714
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLE----LQGVPKAEARERAEELLE--------LVGLSGfenaypHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqHlSLVEQ---ADHILFLEG--GAIRE 782
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVT-H-DIDEAvflADRVVVLSArpGRIVA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
563-792 |
7.02e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 7.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQVA 642
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGR-SLQENI-----AYGLTQKPTMEEITA--AAVksgahsfisGLPQGYDTEVGeagsQLSGGQRQAVALA 714
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDEllELF---------GLTDAADRKVG----TLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 792
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 ... |
566-780 |
1.01e-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: 141.80 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVg 645
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 qePQVfgrslqeniaygltqkptMEEITAAAVksgAHSFIsglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLI 725
Cdd:cd03214 79 --PQA------------------LELLGLAHL---ADRPF---------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 726 LDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
562-791 |
1.11e-38 |
|
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: 151.21 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGKPLPQYEHRYLH 638
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYGL-TQKPTMEEITAAAVKSGAhsfISGLPQGYDTEVgeagSQLSGGQRQAVALAR 715
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALeNLGLSRAEARARVLELLE---AVGLERRLDRYP----HQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
563-784 |
5.01e-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: 139.76 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRyLHRQVA 642
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeaGSQLSGGQRQAVALARALIRKPC 722
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 723 VLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREGG 784
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
564-778 |
1.36e-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: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 643
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VgqepqvfgrslqeniaygltqkptmeeitaaavksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCV 723
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQA-DHILFLEGG 778
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
564-780 |
2.51e-37 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 137.73 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAA 643
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCV 723
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 724 LILDDATSALDansqLQVEQLLYESPERYS---RSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03246 118 LVLDEPNSHLD----VEGERALNQAIAALKaagATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
262-538 |
4.98e-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: 140.85 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFT-RNLTLMSILTIasaVLEFVGDGIYN-------NTMGH-VHSHLQGEVFGAVLRQE 332
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEaLRALNQAVLIL---LGVVLIGSIATflrswlfTLAGErVVARLRKRLFSAIIAQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 333 TEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 412
Cdd:cd18780 90 IAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQ 492
Cdd:cd18780 170 SKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGR 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168024055 493 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18780 250 LVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
315-806 |
5.95e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 150.51 E-value: 5.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 315 HVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLF---LWYLVRGLCLLG----IMLWGSVSL 387
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQLLSTFALIGtvstISLWAIMPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 388 TMVTLVTLPllfllpkkvgkWYQLLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFaneegeaqKFREKLQEIKTLNQK 463
Cdd:PLN03232 1060 LILFYAAYL-----------YYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY--------KAYDRMAKINGKSMD 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 464 EAVAYAV-----NSWTT----SISGMLL----KVGILYIGGQLVTSGAVSSGNLVtfVLYQMQFTQAVEVLLSIYPRVQK 530
Cdd:PLN03232 1121 NNIRFTLantssNRWLTirleTLGGVMIwltaTFAVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAEN 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 531 AVGSSEKIFEYLDRTPRC--------PPSGLltplHLEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNG 601
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEAtaiiennrPVSGW----PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTG 1272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 602 SGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITAAAVKS-- 679
Cdd:PLN03232 1273 AGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDADLWEAle 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 680 GAH--SFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVL 757
Cdd:PLN03232 1347 RAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTML 1424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 758 LITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKG-CYWAMVQA--PADA 806
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHStgPANA 1476
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
563-789 |
1.08e-36 |
|
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: 137.70 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTGGQLLLDGKPL--PQYEHR 635
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKsgahsfISGLPQgydtEVGE--AGSQLSGGQR 708
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALR------KAALWD----EVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQA----DHILFLEGGAIREGG 784
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNM---QQAarvaDRTAFLLNGRLVEFG 222
|
....*
gi 1168024055 785 THQQL 789
Cdd:cd03260 223 PTEQI 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
429-800 |
9.62e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 146.33 E-value: 9.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 429 EALSAMPTVRSFANEEGEAQKFR--EKLQEIKTL--NQKEAVAYAVnswttsISGMLL---KVGILYiGGQLVTSGAVSS 501
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNlsEKLYSKYILkaNFMESLHIGM------INGFILasyAFGFWY-GTRIIISDLSNQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 502 --------GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYP 573
Cdd:PTZ00265 314 qpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYD 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 574 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL-DGKPLPQYEHRYLHRQVAAVGQEPQVFG 652
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 RSLQENIAYGLTQKPTME--------------------------------------------------------EITAAA 676
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 677 VKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSV 756
Cdd:PTZ00265 554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 757 LLITQHLSLVEQADHILFL-----------------------------------------------EGGAIREGGTHQQL 789
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDAL 713
|
490
....*....|..
gi 1168024055 790 ME-KKGCYWAMV 800
Cdd:PTZ00265 714 MKnKNGIYYTMI 725
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
262-538 |
9.97e-36 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 136.84 E-value: 9.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 341
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 342 GNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 421
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSS 501
Cdd:cd18576 173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1168024055 502 GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18576 253 GDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
560-782 |
1.09e-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: 135.99 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyehryLH 638
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVFG-RSLQENIAYGLtqkpTMEEITAAAVKSGAHSFISglpqgydtEVGEAG------SQLSGGQRQAV 711
Cdd:COG1116 80 PDRGVVFQEPALLPwLTVLDNVALGL----ELRGVPKAERRERARELLE--------LVGLAGfedaypHQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqH-----LSLveqADHILFLEG--GAIRE 782
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT-HdvdeaVFL---ADRVVVLSArpGRIVE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-801 |
2.85e-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: 145.09 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 328 VLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGK 407
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF----VQR 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 408 WYQLLEVQVR--ESLAKSSQVA--IEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKEAVAYAV-NSWttsisgmlL 482
Cdd:TIGR00957 1124 FYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVaNRW--------L 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 483 KVGILYIGGQLVTSGAV---------SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP---- 549
Cdd:TIGR00957 1192 AVRLECVGNCIVLFAALfavisrhslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiq 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 550 ----PSGLLTplhlEGLVQFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL 624
Cdd:TIGR00957 1272 etapPSGWPP----RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 625 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 703
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIREG 783
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
490
....*....|....*...
gi 1168024055 784 GTHQQLMEKKGCYWAMVQ 801
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
563-778 |
1.23e-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: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhRQVA 642
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGR-SLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKP 721
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGG 778
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
563-793 |
3.45e-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: 131.78 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-KPLPQYEHRYLHRQV 641
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALA 714
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvprEEMRKRVDEALKLvGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKK 793
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
563-780 |
3.62e-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: 127.25 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhrylhR 639
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVF-GRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 717
Cdd:cd03259 73 NIGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgLEGLLNRYP-------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 718 IRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAI 780
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
562-787 |
5.71e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLqNLYQPTGGQLLLDGKPLPQYEHR--YLh 638
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRRigYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 rqvaavgqePQvfgrslQENIAYGLtqkP-TMEEItaaaVKSGAHSFIsGLPQGYDTE-----------VGEAG------ 700
Cdd:COG1121 81 ---------PQ------RAEVDWDF---PiTVRDV----VLMGRYGRR-GLFRRPSRAdreavdealerVGLEDladrpi 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 701 SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGA 779
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREyFDRVLLLNRGL 216
|
....*...
gi 1168024055 780 IREGGTHQ 787
Cdd:COG1121 217 VAHGPPEE 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
563-780 |
6.42e-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: 6.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YL 637
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQVFGR-SLQENIAYGL----TQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVgeagSQLSGGQRQAVA 712
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagVPKKERRERAEELLER------VGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
563-778 |
1.10e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 124.61 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE--HRYLHRQ 640
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVF-GRSLQENIAYGltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIR 719
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGG 778
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
562-782 |
3.06e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.77 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST---VAALLQnlyQPTGGQLLLDGKPLpqyeHRYL 637
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDI----SSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAA--------VGQEPQVFGR-SLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE--------VGEAG 700
Cdd:COG1136 77 ERELARlrrrhigfVFQFFNLLPElTALENVALPLL--------------------LAGVSRKERRErarellerVGLGD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 701 ------SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILF 774
Cdd:COG1136 137 rldhrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIR 216
|
....*...
gi 1168024055 775 LEGGAIRE 782
Cdd:COG1136 217 LRDGRIVS 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
560-791 |
4.24e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVA 712
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENigvpREEMVERVDQALRQvGMEDFLNREP-----------HRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLME 791
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
562-785 |
1.03e-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: 123.85 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYL 637
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQVF-GRSLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE--------VGEAG------SQ 702
Cdd:cd03258 81 RRRIGMIFQHFNLLsSRTVFENVALPLE--------------------IAGVPKAEIEErvlellelVGLEDkadaypAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 703 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIR 781
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
....
gi 1168024055 782 EGGT 785
Cdd:cd03258 221 EEGT 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
562-779 |
1.58e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.20 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTGGQLLLDGKPLPQYEHRYlH 638
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVFGR-SLQENIA-----YGLtqKPTMEEITAAAVKsgahsfiSGLPQGYDTEVGeagsQLSGGQRQAVA 712
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGL--RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRS--VLLITQHLSLVEQADHILFLEGGA 779
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELI----AAHLARggAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
563-783 |
5.72e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.79 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEP--QVFGRSLQENIAYGLTQK----PTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALAR 715
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvppKKMKDiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHIL-FLEGGAIREG 783
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIvFSEGKLIAQG 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
566-791 |
7.04e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.49 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-----PQyehrylHRQ 640
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpPR------ERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFgR--SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGL----PqgydtevgeagSQLSGGQRQAVAL 713
Cdd:COG1118 77 VGFVFQHYALF-PhmTVAENIAFGLRVRPPSKAEIRARVEELLELVqLEGLadryP-----------SQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 714 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITqH-----LSLveqADHILFLEGGAIREGGTHQQ 788
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVT-HdqeeaLEL---ADRVVVMNQGRIEQVGTPDE 220
|
...
gi 1168024055 789 LME 791
Cdd:COG1118 221 VYD 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
563-792 |
9.33e-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: 121.29 E-value: 9.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 642
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARA 716
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLIT--QHLSLvEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVThdQEEAL-EVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
567-780 |
1.49e-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: 119.28 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhRQVAAVGQ 646
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCV 723
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAI 780
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
564-783 |
3.21e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyehRYLHRQVAA 643
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VGQEPQV---FGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsglpqgydTEVGEAG------SQLSGGQRQAVALA 714
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAL--------ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREG 783
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEyFDRVLLLNRTVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
563-789 |
3.74e-30 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 119.14 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP---QYEHRYLHR 639
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPQGYDTEVGEagsqLSGGQRQA 710
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREivleklEAV---------GLRGAEDLYPAE----LSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
563-782 |
2.79e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.31 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLY---QPTGGQLLLDGKPLPQYEHR---Y 636
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQEPQ-VFGRSLQENIAY-----GLTQKPTMEEITAAAVKSG----AHSFIsglpqgydtevgeagSQLSGG 706
Cdd:COG2884 77 LRRRIGVVFQDFRlLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGlsdkAKALP---------------HELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRS---VLLITQHLSLVEQADH-ILFLEGGAIRE 782
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL----EEINRRgttVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
564-790 |
3.03e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRPdvlvlqgLTFTL--RPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylh 638
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVFGR-SLQENIAYGLTQ--KPTMEE---ITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 712
Cdd:COG3840 71 RPVSMLFQENNLFPHlTVAQNIGLGLRPglKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 713 LARALIRKPCVLILDDATSALDANsqLQVE--QLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
.
gi 1168024055 790 M 790
Cdd:COG3840 218 L 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
566-790 |
6.73e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.37 E-value: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 645
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQV-FGRSLQENIAYGLTQKPTM----EEITAAAVksgahsfisglpqgydTEVGEAG------SQLSGGQRQAVALA 714
Cdd:COG4559 82 QHSSLaFPFTVEEVVALGRAPHGSSaaqdRQIVREAL----------------ALVGLAHlagrsyQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 715 RALI-------RKPCVLILDDATSALDANSQLQVEQLLYespeRYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREG 783
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLAR----QLARrggGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
....*..
gi 1168024055 784 GTHQQLM 790
Cdd:COG4559 222 GTPEEVL 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
586-784 |
7.14e-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: 114.70 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 586 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----------PQyehrylHRQVAAVGQEPQV 650
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQ------QRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 FGR-SLQENIAYGLTQKPTMEE-ITAAAVKSGAHsfISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:cd03297 87 FPHlNVRENLAFGLKRKRNREDrISVDELLDLLG--LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
562-785 |
1.03e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehryl 637
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglpPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQVFG-RSLQENIAYGLTQ----KPTMEEITAAAVK----SG-AHSFIsglpqgydtevgeagSQLSGGQ 707
Cdd:COG3842 76 KRNVGMVFQDYALFPhLTVAENVAFGLRMrgvpKAEIRARVAELLElvglEGlADRYP---------------HQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSALDAN--SQLQVE--QLLyespERYSRSVLLITqH-----LSLveqADHILFLEGG 778
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKlrEEMREElrRLQ----RELGITFIYVT-HdqeeaLAL---ADRIAVMNDG 212
|
....*..
gi 1168024055 779 AIREGGT 785
Cdd:COG3842 213 RIEQVGT 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
566-790 |
1.42e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 645
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQV-FGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFisglpqgydtevgeAGS---QLSGGQRQAVALARA 716
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 717 LIR------KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228
|
.
gi 1168024055 790 M 790
Cdd:PRK13548 229 L 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
550-791 |
1.61e-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: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 550 PSGLLTPLHLEG--LVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQnLyQPT 618
Cdd:COG4172 261 PRGDPRPVPPDAppLLEARDLKVWFPIKRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 619 GGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPqvFGrSL------QENIAYGLT-QKPTM--EEITAAAVKSgahsfis 686
Cdd:COG4172 339 EGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP--FG-SLsprmtvGQIIAEGLRvHGPGLsaAERRARVAEA------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 687 gLpqgydTEVG-EAGS------QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLI 759
Cdd:COG4172 409 -L-----EEVGlDPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFI 482
|
250 260 270
....*....|....*....|....*....|...
gi 1168024055 760 TQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:COG4172 483 SHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
560-791 |
1.69e-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: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRY 636
Cdd:COG1127 3 EPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQEPQVFGrSL--QENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPqgydtevgEAG----SQ 702
Cdd:COG1127 80 LRRRIGMLFQGGALFD-SLtvFENVAFPLREHTDLseAEIRElvleklELV---------GLP--------GAAdkmpSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 703 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIR 781
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLdSAFAIADRVAVLADGKII 221
|
250
....*....|
gi 1168024055 782 EGGTHQQLME 791
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
563-792 |
4.03e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYEHRYLHR 639
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVA 712
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRDVLADvGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
564-780 |
5.31e-28 |
|
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: 113.05 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH---RQ 640
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaaavKSGAHSFISGLPQGYDTE-----------VGEAG------SQ 702
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSG---------------RLGRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 703 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAI 780
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
563-742 |
7.58e-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: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhrylhR 639
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 717
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqLEGYANRKP-------SQLSGGQQQRVAIARAL 145
|
170 180
....*....|....*....|....*..
gi 1168024055 718 IRKPCVLILDDATSALDAN--SQLQVE 742
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKlrKDMQLE 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
557-791 |
1.03e-27 |
|
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: 114.38 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVqfqdVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYE 633
Cdd:COG0444 2 LEVRNLK----VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 634 HR----YLHRQVAAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPqgydte 695
Cdd:COG0444 77 EKelrkIRGREIQMIFQDPMtslnpVMtvGDQIAEPLR--IHGGLSKAEARERAIEllervglPDPERRLDRYP------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 696 vgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILF 774
Cdd:COG0444 149 -----HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*..
gi 1168024055 775 LEGGAIREGGTHQQLME 791
Cdd:COG0444 224 MYAGRIVEEGPVEELFE 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
562-785 |
1.38e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRYL---H 638
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYG-LTQKPTMEEI----TAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 711
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVE-QADHILFLEGGAIREGGT 785
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
563-780 |
1.46e-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: 111.08 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ--YEHRYLHRQ 640
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAAV----KSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 713
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIkvKGMSKAEAEERALelleKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 714 ARALIRKPCVLILDDATSALD---ANSQLQVEQLLYESperySRSVLLITQHLSLV-EQADHILFLEGGAI 780
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
262-538 |
1.90e-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: 112.91 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdGIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQ-GYLAEKASQkVAYDLRNDLYDHLQRLSFSFHDKAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLG----IMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 412
Cdd:cd18542 95 TGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIipfiALFSYVFFKKVRPAFE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 evQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN-SWTTSISGMLLkVGILYIGG 491
Cdd:cd18542 169 --EIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYwPLMDFLSGLQI-VLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168024055 492 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
560-792 |
2.18e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYpNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:PRK13648 5 NSIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEP--QVFGRSLQENIAYGLTQK--PT--MEEITAAAVKS-GAHSFISGLPQGydtevgeagsqLSGGQRQAVA 712
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHavPYdeMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEK 792
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
580-791 |
2.23e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.60 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFGR-SLQE 657
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 658 NI---AYGLTQ---KPTMEEItaaavksgahsfisglpqgYD------TEVGEAGSQLSGGQRQAVALARALIRKPCVLI 725
Cdd:cd03224 95 NLllgAYARRRakrKARLERV-------------------YElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 726 LDDATSALdanSQLQVEQlLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:cd03224 156 LDEPSEGL---APKIVEE-IFEAIRELRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
263-538 |
2.50e-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: 112.52 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFFQQ 338
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEA----LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRvvrdLRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 339 NQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRE 418
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 419 SLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGA 498
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1168024055 499 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18552 253 LTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
562-745 |
3.41e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PqyeHRYL 637
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsP---RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQVF-GRSLQENIA-------YGLTQKPTMEEITAAAVKS-GAHsfISglPqgyDTEVGEagsqLSGGQR 708
Cdd:COG1129 78 AAGIAIIHQELNLVpNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--ID--P---DTPVGD----LSVAQQ 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANsqlQVEQLL 745
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTER---EVERLF 180
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
559-789 |
3.53e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 559 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVK-SGAHSFISGLPqgydtevgeagSQLSGGQRQAV 711
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
559-780 |
4.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 559 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAV 711
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
563-790 |
4.62e-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: 110.47 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVA 642
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVGEAGSQLSGGQRQAVALARALI 718
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL----VPKLLKWPKEKIRERADELLAlvGLdPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 719 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
563-784 |
5.02e-27 |
|
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: 109.65 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhR 639
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 717
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELLqIEHLLDRKP-------KQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 718 IRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQH----LSLveqADHILFLEGGAIREGG 784
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqveaMTM---ADRIAVMNDGQIQQIG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
326-806 |
5.09e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.69 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 326 GAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFL---WYLVRGLCLLGIM----LWGSVSLTMVTLVTLPll 398
Cdd:PLN03130 994 GSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLFYGAYL-- 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 399 fllpkkvgkWYQLL--EVQVRESLAKSSQVAI--EALSAMPTVRsfaneegeAQKFREKLQEIKTLNQKEAVAYAV---- 470
Cdd:PLN03130 1072 ---------YYQSTarEVKRLDSITRSPVYAQfgEALNGLSTIR--------AYKAYDRMAEINGRSMDNNIRFTLvnms 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 471 -NSWttsisgmlLKVGILYIGG---QLVTSGAV----SSGNLVTF-------VLYQMQFTQAVEVLLSIYPRVQKAVGSS 535
Cdd:PLN03130 1135 sNRW--------LAIRLETLGGlmiWLTASFAVmqngRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 536 EKIFEYLDRTPRCP--------PSGLLTplhlEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKST 606
Cdd:PLN03130 1207 ERVGTYIDLPSEAPlviennrpPPGWPS----SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSS 1280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 607 VAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITAAAVKS--GAH-- 682
Cdd:PLN03130 1281 MLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlk 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 683 SFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQH 762
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHR 1432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1168024055 763 LSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWA-MVQA--PADA 806
Cdd:PLN03130 1433 LNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMVQStgAANA 1479
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
262-538 |
5.90e-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: 111.80 E-value: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPF--FTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVhSHLQG-----EVFGAVLRQETE 334
Cdd:cd18577 18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTIT-GERQArrirkRYLKALLRQDIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGI-----------MLWGSVSLTMVTLVtlpllfllpk 403
Cdd:cd18577 97 WFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIafiyswkltlvLLATLPLIAIVGGI---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 404 kVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLK 483
Cdd:cd18577 167 -MGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 484 VGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
562-789 |
8.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.66 E-value: 8.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDtevgEAGSQLSGGQRQAVALARALIR 719
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--GLEELRD----RVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
561-785 |
1.57e-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: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 561 GLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAavksgahsfisglpqgydTEVGEAGSQLSGGQRQAVALARALI 718
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 719 RKPCVLILDDATSALDANSQLQVEQLLYESperYSRSVLLITQH-LSLVEQADHILFLEGGAIREGGT 785
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREE---FTNSTILTIAHrLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
562-782 |
1.76e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.78 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPN------RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--- 632
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 633 EHRYLHRQVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQ 702
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnprKTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 703 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIR 781
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 1168024055 782 E 782
Cdd:PRK10419 232 E 232
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
263-538 |
3.44e-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: 109.45 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSAdtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 342
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 343 NIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK 422
Cdd:cd18551 94 DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 423 SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSG 502
Cdd:cd18551 174 LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVG 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1168024055 503 NLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18551 254 TLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
562-775 |
1.98e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:PRK10247 7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPqgyDTEVGEAGSQLSGGQRQAVALARALI 718
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 719 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFL 775
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
263-538 |
2.39e-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: 107.10 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSA------DTFTRNLTLMSILTIASAVLEFvgdgIYNNTMGHVhshlqgeVFGAV--LRQETE 334
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSY----LQNRLMARV-------SQRTVydLRKDLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 ---------FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKV 405
Cdd:cd18547 86 eklqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 406 GKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkV 484
Cdd:cd18547 166 AKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-V 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 485 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18547 245 LVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
560-793 |
2.69e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.63 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGQLLLDGKPL-- 629
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 630 PQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKsGAHSFISGLPQGYDTEVGeagsqLS 704
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVLDEAVEKSLK-GASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 705 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQADHI-----LFLEGGA 779
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSM---QQASRIsdrtgFFLDGDL 225
|
250
....*....|....
gi 1168024055 780 IREGGTHQQLMEKK 793
Cdd:PRK14239 226 IEYNDTKQMFMNPK 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
562-791 |
3.48e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.17 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLHR 639
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFGR-SLQENIAYGLTQkptmeeiTAAAVKSGAHSFISGLPqgydTEVGEAG------SQLSGGQRQAVA 712
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLR-------VRGASKEEAEKQARELL----AKVGLAErahhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQ---LQVEQLLYESperySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQ 788
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
...
gi 1168024055 789 LME 791
Cdd:PRK09493 223 LIK 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
263-538 |
3.56e-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: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAV-----LEFVgdgiynNTMG-HVHSHLQGEVFGAVLRQETEFF 336
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALasalrFYLV------SWLGeRVVADLRKAVFAHLLRLSPSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 337 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 416
Cdd:cd18575 88 ETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 417 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 496
Cdd:cd18575 168 QDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1168024055 497 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18575 248 GRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
581-772 |
3.57e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.12 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYLHRQVAAVGQEPqvfgrslqe 657
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 658 niaYG-LTQKPTMEEITAAAVKsgahsfISGL--PQGYDTEVGEAGS--------------QLSGGQRQAVALARALIRK 720
Cdd:COG4608 105 ---YAsLNPRMTVGDIIAEPLR------IHGLasKAERRERVAELLElvglrpehadryphEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEqadHI 772
Cdd:COG4608 176 PKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVR---HI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
563-780 |
5.22e-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: 103.64 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR---YLHR 639
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVF-GRSLQENIAYGL--TQKPTME---EITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 713
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFALevTGVPPREirkRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 714 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADH-ILFLEGGAI 780
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
429-794 |
5.32e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.14 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 429 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSWTTSISGMLLKV---GIL-YIGGQLVTSGAVS 500
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVQTVRddelSWFRKAQLLSAFNSFILNSIPVLVTVvsfGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 501 SGNL---VTFVLYQMQ--FTQAVEVLLSIyPRVQKAVGSSEKIFeyldrtprcppsgLLTPLHLEGL--VQFQDVSFAYP 573
Cdd:PLN03130 560 SLSLfavLRFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-------------LPNPPLEPGLpaISIKNGYFSWD 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 574 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFG 652
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFN 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 RSLQENIAYGLTQKPTMEEiTAAAVKSGAHSfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 732
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 733 LDANSQLQV-EQLLYESPERYSRsvLLITQHLSLVEQADHILFLEGGAIREGGTH----------QQLMEKKG 794
Cdd:PLN03130 771 LDAHVGRQVfDKCIKDELRGKTR--VLVTNQLHFLSQVDRIILVHEGMIKEEGTYeelsnngplfQKLMENAG 841
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
563-789 |
8.86e-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: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqYEHRYLHRQVa 642
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 aVGQEPQvfGRSL------QENIAY-----GLTQKPTMEEITAAAVKsgahsfiSGLPQGYDTEVGeagsQLSGGQRQAV 711
Cdd:cd03263 77 -LGYCPQ--FDALfdeltvREHLRFyarlkGLPKSEIKEEVELLLRV-------LGLTDKANKRAR----TLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
550-789 |
1.15e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 550 PSGLLTPL--HLEGLVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 618
Cdd:PRK15134 261 PSGDPVPLpePASPLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 619 GGQLLLDGKPLPQYEHRYL---HRQVAAVGQEPQvfgRSL------QENIAYGLT-QKPTMeeiTAAAVKSgahSFISGL 688
Cdd:PRK15134 339 QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN---SSLnprlnvLQIIEEGLRvHQPTL---SAAQREQ---QVIAVM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 689 pqgydTEVG-------EAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQ 761
Cdd:PRK15134 410 -----EEVGldpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
250 260
....*....|....*....|....*....
gi 1168024055 762 HLSLVEQADH-ILFLEGGAIREGGTHQQL 789
Cdd:PRK15134 485 DLHVVRALCHqVIVLRQGEVVEQGDCERV 513
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
261-538 |
1.19e-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: 104.78 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYN---NTMG-HVHSHLQGEVFGAVLRQETEFF 336
Cdd:cd18544 15 ELLGPLLIKRAIDDYIVPGQGDL--QGLLLLALLYLGLLLLSFLLQYLQTyllQKLGqRIIYDLRRDLFSHIQRLPLSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 337 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 412
Cdd:cd18544 93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVlpllLLATYLFRKKSRKAYR-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 evQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGG 491
Cdd:cd18544 171 --EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168024055 492 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18544 248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
566-790 |
1.31e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 645
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQV-FGRSLQENIAYG----------LTQKPtmEEITAAAVKsgahsfisglpqgyDTEVGEAG----SQLSGGQRQA 710
Cdd:PRK11231 83 QHHLTpEGITVRELVAYGrspwlslwgrLSAED--NARVNQAME--------------QTRINHLAdrrlTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSlveQA----DHILFLEGGAIREGGTH 786
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTP 222
|
....
gi 1168024055 787 QQLM 790
Cdd:PRK11231 223 EEVM 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
261-538 |
1.39e-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: 104.90 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFF 336
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERitadLRRDLYEHLQRLSLSFF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 337 QQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 416
Cdd:cd18563 95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 417 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEI----KTLNQKEAVAYAVNSWTTSISGMLlkvgILYIGGQ 492
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELldanIRAEKLWATFFPLLTFLTSLGTLI----VWYFGGR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168024055 493 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18563 251 QVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
563-735 |
1.58e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.93 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehrylH 638
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlpPK------D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVF-GRSLQENIAYGLT-QKPTMEEItAAAVKSGAHSF-ISGL----PqgydtevgeagSQLSGGQRQAV 711
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPLKlRKVPKAEI-DRRVREAAELLgLEDLldrkP-----------KQLSGGQRQRV 142
|
170 180
....*....|....*....|....
gi 1168024055 712 ALARALIRKPCVLILDDATSALDA 735
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDA 166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
563-785 |
1.88e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEHRYLH 638
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVFG-RSLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE--------VGEAG------SQL 703
Cdd:COG1135 82 RKIGMIFQHFNLLSsRTVAENVALPLE--------------------IAGVPKAEIRKrvaellelVGLSDkadaypSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIRE 782
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 1168024055 783 GGT 785
Cdd:COG1135 222 QGP 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
575-785 |
2.28e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.33 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEP------ 648
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 -----QVFGRSLQENIAygLTQKPTMEEITAAAVKSGAhsfisgLPQgydtEVGEAGSQLSGGQRQAVALARALIRKPCV 723
Cdd:PRK15112 103 rqrisQILDFPLRLNTD--LEPEQREKQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 785
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
557-783 |
3.22e-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: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVqfqdVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY-EHR 635
Cdd:cd03219 1 LEVRGLT----KRFG-----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQEPQVFGR-SLQENIA--------YGLTQKPTMEEITAAAVKsgAHSFIS--GLPQGYDTEVGEagsqLS 704
Cdd:cd03219 72 IARLGIGRTFQIPRLFPElTVLENVMvaaqartgSGLLLARARREEREARER--AEELLErvGLADLADRPAGE----LS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 705 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGA-IRE 782
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRVTVLDQGRvIAE 224
|
.
gi 1168024055 783 G 783
Cdd:cd03219 225 G 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
562-789 |
3.51e-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: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLHR 639
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAAVKsgahsfisglpqgYDTEVGEAG------SQLSGGQRQA 710
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLAPIkvKKMSKAEAEERAME-------------LLERVGLADkadaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDansqlqveqllyesPERySRSVL-----LITQHLSLV----------EQADHILFL 775
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALD--------------PEL-VGEVLdvmrdLAKEGMTMVvvthemgfarEVADRVVFM 209
|
250
....*....|....
gi 1168024055 776 EGGAIREGGTHQQL 789
Cdd:COG1126 210 DGGRIVEEGPPEEF 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
578-783 |
3.90e-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: 102.42 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 578 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYehrylhrQVAAVG-----QEPQ 649
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPH-------RIARLGiartfQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 650 VFGR-SLQENIAYGLTqkptmeeitaAAVKSGAHSFISGLPQGYDTE-------------VG-------EAGSqLSGGQR 708
Cdd:COG0411 90 LFPElTVLENVLVAAH----------ARLGRGLLAALLRLPRARREEreareraeellerVGladradePAGN-LSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGA-IREG 783
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRvIAEG 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
556-791 |
4.82e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 556 PLHLEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR 635
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQE-PQVFGRSLQENIA------------YGLTQKPTMEE-ITAAAVKSGAHSFIsglpqgydtevgeagS 701
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEaISLVGLKPLAHRLV---------------D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 702 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
250
....*....|.
gi 1168024055 781 REGGTHQQLME 791
Cdd:PRK10575 227 IAQGTPAELMR 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
576-780 |
5.17e-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: 99.04 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqyehrylhrqvaavgqepqvfGRSL 655
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENIAYGLtqkptmeeitaAAVksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 735
Cdd:cd03216 70 RDARRAGI-----------AMV-----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 736 NsqlQVEQLLyespERYSR------SVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:cd03216 116 A---EVERLF----KVIRRlraqgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
575-796 |
5.88e-24 |
|
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: 108.88 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTGgqllldgkplpqyeHRYLHRQVAAVGQEPQVFGR 653
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAYG--LTQKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:TIGR00957 714 SLRENILFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 732 ALDANsqlqVEQLLYES---PERY--SRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCY 796
Cdd:TIGR00957 790 AVDAH----VGKHIFEHvigPEGVlkNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
577-791 |
9.09e-24 |
|
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: 100.83 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFGR-S 654
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQENI---AYGLTQKP----TMEEItaaavksgahsfisglpqgYDT--EVGE----AGSQLSGGQRQAVALARALIRKP 721
Cdd:COG0410 95 VEENLllgAYARRDRAevraDLERV-------------------YELfpRLKErrrqRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 722 CVLILDDATSALdanSQLQVEQlLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:COG0410 156 KLLLLDEPSLGL---APLIVEE-IFEIIRRLNRegvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
563-780 |
1.05e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 99.87 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPDVLVLqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 642
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLpQGYDTEVGEagsQLSGGQRQAVALARALIRKP 721
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV--GL-AGLEKRLPG---ELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
566-778 |
1.21e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTGGQLLLDGKPL-----PQY 632
Cdd:COG1117 15 RNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILLDGEDIydpdvDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 633 EHRylhRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKSgahsfiSGLpqgYDtEV----GEAGSQL 703
Cdd:COG1117 89 ELR---RRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIVEESLRK------AAL---WD-EVkdrlKKSALGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSlveQA----DHILFLEGG 778
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQ---QAarvsDYTAFFYLG 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
567-784 |
1.52e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQ 646
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQV-FGRSLQENIAYG----LTQKPTMEEITAAAVKSGAHSfiSGLPQGYDTEVgeagSQLSGGQRQAVALARALIRKP 721
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMER--TGVAQFADRPV----TSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
564-775 |
2.12e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhRQ 640
Cdd:COG4525 5 TVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGAD-----RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VaaVGQEPQVFG-RSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLpQGYDtevGEAGSQLSGGQRQAVALARAL 717
Cdd:COG4525 80 V--VFQKDALLPwLNVLDNVAFGLR----LRGVPKAERRARAEELLAlvGL-ADFA---RRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 718 IRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHlslVEQAdhiLFL 775
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEA---LFL 201
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
262-515 |
2.25e-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: 100.95 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDwILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYNNT-MG---HVHSHLQGEVFGAVLRQETEFFQ 337
Cdd:cd18541 16 LLIPRIIGRAID-ALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLiFGasrRIEYDLRNDLFAHLLTLSPSFYQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 338 QNQTGNIMSRVTEDTSTLSDSLSENlslfLWYLVRGLCL----LGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLE 413
Cdd:cd18541 93 KNRTGDLMARATNDLNAVRMALGPG----ILYLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 414 VQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISGMLLKVG---ILYIG 490
Cdd:cd18541 169 RKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR---VDALFFPLIGLLIGLSfliVLWYG 245
|
250 260
....*....|....*....|....*
gi 1168024055 491 GQLVTSGAVSSGNLVTFVLYQMQFT 515
Cdd:cd18541 246 GRLVIRGTITLGDLVAFNSYLGMLI 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
580-789 |
4.02e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVFGR-SLQEN 658
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 659 IAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSAL 733
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 734 DANSQLQVEQLLYESPERYS-RSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
545-802 |
4.36e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.02 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 545 TPRCPPSGLLTPLHLEGLVqFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLL 623
Cdd:PTZ00243 1292 EPASPTSAAPHPVQAGSLV-FEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 624 LDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtmEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 703
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 704 SGGQRQAVALARALIRKPCVLIL-DDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQADHILFLEGGAIRE 782
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250 260
....*....|....*....|.
gi 1168024055 783 GGTHQQL-MEKKGCYWAMVQA 802
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEA 1545
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
580-789 |
4.91e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-----LLDG-KPLPQYEH--RYLHRQVAAVGQEPQVF 651
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 652 -GRSLQENIAYG--LTQKPTMEEITAAAVKSGAHSFISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:PRK11264 98 pHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQL 789
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
585-734 |
5.15e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyEHRYL---HRQVAAVGQEPQVFGR-SLQENIA 660
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 661 YGL--------TQKPTMEEItaaAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSA 732
Cdd:PRK10771 94 LGLnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
..
gi 1168024055 733 LD 734
Cdd:PRK10771 160 LD 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
562-790 |
5.96e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH-RYLHRQ 640
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEP--QVFGRSLQENIAYG---LTQKPT--MEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 713
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPIeiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 714 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
575-785 |
7.77e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.42 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLV--LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP- 648
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 ------QVFGRSLQENIAYGltqkptmEEITAAAVKSGAHSFIS--GL-PQGYDtevgEAGSQLSGGQRQAVALARALIR 719
Cdd:PRK11308 103 gslnprKKVGQILEEPLLIN-------TSLSAAERREKALAMMAkvGLrPEHYD----RYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 785
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
580-792 |
1.00e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 97.79 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhRQVAAVGQEPQVFGR-SL 655
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDTevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLgIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 735 ANSQLQVEQLLYESPERYSRSVLLITQhlSLVEQ---ADHILFLEGGAIREGGTHQQLMEK 792
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTH--DFEEAwalADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
571-775 |
1.79e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 571 AYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVAAVGQ---E 647
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 648 PQVFGRSLQENIAYGLTQK-PTMEEITAAAVKSGAHSFisglpqgydTEVGEAG------SQLSGGQRQAVALARALIRK 720
Cdd:NF040873 67 PDSLPLTVRDLVAMGRWARrGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFL 775
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
562-793 |
2.15e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHR---YLH 638
Cdd:PRK13636 5 ILKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGahsfISGLPQgydtevgEAGSQLSGGQRQAV 711
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVE-QADHILFL-EGGAIREGGTHQQL 789
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMkEGRVILQGNPKEVF 230
|
....
gi 1168024055 790 MEKK 793
Cdd:PRK13636 231 AEKE 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
578-806 |
2.27e-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: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 578 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYL----HRQVAAVGQEpqvFG- 652
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQS---FAl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevgeagsQLSGGQRQAVALARALIRK 720
Cdd:cd03294 114 lphRTVLENVAFGLEvqgvpraerEERAAEALELVGLEGWEHKYPD---------------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQLmekkgcywam 799
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI---------- 248
|
....*..
gi 1168024055 800 VQAPADA 806
Cdd:cd03294 249 LTNPAND 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
563-791 |
2.44e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG-----GQLLLDGKPLpqYEHRY- 636
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 ---LHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQR 708
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGgthq 787
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGNENRIG---- 232
|
....
gi 1168024055 788 QLME 791
Cdd:PRK14258 233 QLVE 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
429-794 |
4.92e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.36 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 429 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSW---TTSISGMLLKVGI-LYIGGQLVTSGAVS 500
Cdd:PLN03232 484 EILASMDTVKCYAWE----KSFESRIQGIRneelSWFRKAQLLSAFNSFilnSIPVVVTLVSFGVfVLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 501 SGNLVTFVLYQMQ-----FTQAVEVLLSIyPRVQKAVGSSEKIfeyLDRTPRCPPSgllTPLhleglVQFQDVSFAYPNR 575
Cdd:PLN03232 560 SLSLFAVLRSPLNmlpnlLSQVVNANVSL-QRIEELLLSEERI---LAQNPPLQPG---APA-----ISIKNGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGRS 654
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQENIAYGLTQKPtmeEITAAAVKSGAHSFISGLPQGYD-TEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 733
Cdd:PLN03232 695 VRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 734 DANSQLQVeqllYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT----------HQQLMEKKG 794
Cdd:PLN03232 772 DAHVAHQV----FDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTfaelsksgslFKKLMENAG 841
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
557-789 |
8.28e-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: 100.14 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLvqfqDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQP---TGGQLLLDGKPL--- 629
Cdd:COG4172 7 LSVEDL----SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 630 PQYEHRYLH-RQVAAVGQEPQV-------FGRSLQENIA--YGLTQKPTMEEITAAavksgahsfisgLpqgydTEVG-- 697
Cdd:COG4172 82 SERELRRIRgNRIAMIFQEPMTslnplhtIGKQIAEVLRlhRGLSGAAARARALEL------------L-----ERVGip 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 698 EAGS-------QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-A 769
Cdd:COG4172 145 DPERrldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfA 224
|
250 260
....*....|....*....|
gi 1168024055 770 DHILFLEGGAIREGGTHQQL 789
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAEL 244
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
547-802 |
9.09e-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: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 547 RCPPSGLLTplhLEGLVQFQDVSFAYPN--RPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL 624
Cdd:cd03288 7 GSSNSGLVG---LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 625 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsFISGLPQGYDTEVGEAGSQ 702
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdpECKCTDDRLWEALEIAQLKN----MVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 703 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLEGGAIRE 782
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
250 260
....*....|....*....|.
gi 1168024055 783 GGTHQQLMEKK-GCYWAMVQA 802
Cdd:cd03288 235 CDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
262-538 |
9.43e-22 |
|
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: 96.38 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHV------------HSHLQGEVFGavl 329
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGD----LSGLLIIALLFLALNLVNWVASRLRIYLMAKVgqrilydlrqdlFSHLQKLSFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 330 rqeteFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKV 405
Cdd:cd18545 90 -----FFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVlpllVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 406 GKWYQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSW---TTSISGML 481
Cdd:cd18545 165 RKAWQ----RVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR---AVRLNALfwpLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 482 LKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
563-795 |
1.24e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRqva 642
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 aVGQEPQ---------------VFGRSlqeniaYGLTQKptmeeiTAAAVKSGAHSFiSGLPQGYDTEVGEagsqLSGGQ 707
Cdd:PRK13537 82 -VGVVPQfdnldpdftvrenllVFGRY------FGLSAA------AARALVPPLLEF-AKLENKADAKVGE----LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESperySRSVL------LITQHlsLVEQA----DHILFLEG 777
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWER----LRSLLargktiLLTTH--FMEEAerlcDRLCVIEE 213
|
250
....*....|....*....
gi 1168024055 778 G-AIREGGTHQQLMEKKGC 795
Cdd:PRK13537 214 GrKIAEGAPHALIESEIGC 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
580-789 |
1.29e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyEHRYL-HRQVAAVGQEPQVFGR-SLQE 657
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIqQRDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 658 NIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGY-DtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDA 735
Cdd:PRK11432 98 NVGYGLkMLGVPKEERKQRVKEALELVDLAGFEDRYvD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 736 NSQLQVEQLLYESPERYSRSVLLITQHLSlvEQ---ADHILFLEGGAIREGGTHQQL 789
Cdd:PRK11432 170 NLRRSMREKIRELQQQFNITSLYVTHDQS--EAfavSDTVIVMNKGKIMQIGSPQEL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
565-781 |
1.37e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 565 FQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGkplpqyehrylHRQVAAV 644
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 GQEPQVF-GRSLQENIAYGLTQ----KPTMEEITAAAVKS-----------------GAHSF-------ISGL---PQGY 692
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAElralEAELEELEAKLAEPdedlerlaelqeefealGGWEAearaeeiLSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 693 DTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT--QHLsLVEQAD 770
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVShdRYF-LDRVAT 217
|
250
....*....|.
gi 1168024055 771 HILFLEGGAIR 781
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
562-782 |
1.43e-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: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--EHRYLH 638
Cdd:COG4181 8 IIELRGLTKTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQvAAVGQepqVFgRSLQ--------ENIAYGLtqkptmEEITAAAVKSGAHSFIsglpqgydTEVGEAG------SQLS 704
Cdd:COG4181 88 RA-RHVGF---VF-QSFQllptltalENVMLPL------ELAGRRDARARARALL--------ERVGLGHrldhypAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 705 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 782
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
580-778 |
1.54e-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: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPLPQYEHRylhRQVAAVGQEPQVFGR-SLQ 656
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 ENIAYgltqkptmeeitAAAVKSgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDAN 736
Cdd:cd03213 101 ETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1168024055 737 SQLQVEQLLYESPERySRSVLLITQHLS--LVEQADHILFLEGG 778
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQG 188
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
549-795 |
2.02e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 549 PPSGLLTPLHLEglvqFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP 628
Cdd:PRK13536 32 SIPGSMSTVAID----LAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 629 LPQyEHRYLHRQVAAVGQ----EPQVfgrSLQEN-IAYGLTQKPTMEEItaAAVKSGAHSFiSGLPQGYDTEVgeagSQL 703
Cdd:PRK13536 105 VPA-RARLARARIGVVPQfdnlDLEF---TVRENlLVFGRYFGMSTREI--EAVIPSLLEF-ARLESKADARV----SDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQlqveQLLYESperySRSVL------LITQHlsLVEQA----DHIL 773
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR----HLIWER----LRSLLargktiLLTTH--FMEEAerlcDRLC 243
|
250 260
....*....|....*....|...
gi 1168024055 774 FLEGG-AIREGGTHQQLMEKKGC 795
Cdd:PRK13536 244 VLEAGrKIAEGRPHALIDEHIGC 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
563-785 |
2.28e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRYLH 638
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEpqvF----GRSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLPQGYDTevgeAGSQLSGGQRQAVA 712
Cdd:PRK11153 82 RQIGMIFQH---FnllsSRTVFDNVALPLE----LAGTPKAEIKARVTELLElvGLSDKADR----YPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 785
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
562-742 |
2.91e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.55 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQV 641
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaaavksgahsfisglpqgydTEVGEA-------------GSQLSGG 706
Cdd:PRK09452 89 NTVFQSYALFPHmTVFENVAFGLrMQKTPAAEIT--------------------PRVMEAlrmvqleefaqrkPHQLSGG 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDAN--SQLQVE 742
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKlrKQMQNE 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
562-783 |
3.11e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR---YLH 638
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQAL--QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEPQVF-GRSLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 712
Cdd:PRK10908 79 RQIGMIFQDHHLLmDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITQHLSLVEQADH-ILFLEGGAIREG 783
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLHGG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
563-784 |
3.97e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.26 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEhRYLHRQVA 642
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGR-SLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGeagsQLSGGQRQAVALARALIR 719
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY----IAWLKGIPSKEVKARVDEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
579-778 |
4.73e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.52 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 579 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LP-----------QYEHRYLHRQVAA- 643
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPghqiarmgvvrTFQHVRLFREMTVi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 ----VGQEpqvfgRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLpqgydTEVG--EAGSqLSGGQRQAVALARA 716
Cdd:PRK11300 99 enllVAQH-----QQLKTGLFSGLLKTPAFRRAESEALDRAATWLeRVGL-----LEHAnrQAGN-LAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGG 778
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQG 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
308-640 |
5.49e-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: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 308 IYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVS 386
Cdd:COG4615 70 LLLTRLGQhAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 387 L-TMVTLVTLPLLFLLPKKVGKWYQLLEvQVRE---SLAKSSQVAIE-----ALSAmPTVRSFANEEgeaqkFREKLQEI 457
Cdd:COG4615 149 LfLLTLVLLGLGVAGYRLLVRRARRHLR-RAREaedRLFKHFRALLEgfkelKLNR-RRRRAFFDED-----LQPTAERY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 458 KTLNQKEAVAYAVN-SWTTSIsgMLLKVG-ILYIGGQLvtsGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSS 535
Cdd:COG4615 222 RDLRIRADTIFALAnNWGNLL--FFALIGlILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 536 EKIfEYLDRTPRCPPSGLLTPLHLEGLVQFQ-----DVSFAYPNRPD--VLVLQGLTFTLRPGEVTALVGPNGSGKSTVA 608
Cdd:COG4615 297 RKI-EELELALAAAEPAAADAAAPPAPADFQtlelrGVTYRYPGEDGdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350
....*....|....*....|....*....|..
gi 1168024055 609 ALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ 640
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTA-DNREAYRQ 406
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
563-784 |
5.71e-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: 91.89 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlPQYEHRYLhRQVA 642
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEAL-RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFG-RSLQENI-----AYGLTQKPTMEEITaaavksgahsfISGLPQGYDTEVGeagsQLSGGQRQAVALARA 716
Cdd:cd03268 76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLD-----------VVGLKDSAKKKVK----GFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPErYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
559-791 |
5.89e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 559 LEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTG---GQLLLDGKPL--PQ 631
Cdd:PRK14243 7 TETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 632 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYG---LTQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQR 708
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLslvEQA----DHILFLEGGAIREGG 784
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM---QQAarvsDMTAFFNVELTEGGG 232
|
....*..
gi 1168024055 785 THQQLME 791
Cdd:PRK14243 233 RYGYLVE 239
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
262-538 |
6.92e-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: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEfVGDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLG-VVQTYLSARIGqGVMYDLRVQLYAHLQRMSLAFFTRTR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTED--------TSTLSDSLSENLSLFLwylvrglcLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 412
Cdd:cd18550 95 TGEIQSRLNNDvggaqsvvTGTLTSVVSNVVTLVA--------TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 EVQVRESLAKSSQVAIEALSA--MPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAyavNSWTTSISGMLLKVG---IL 487
Cdd:cd18550 167 TREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALA---GRWFFAALGLFTAIGpalVY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 488 YIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18550 244 WVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
555-780 |
1.02e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 555 TPLHLEGlvqfqdVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY-- 632
Cdd:PRK11247 11 TPLLLNA------VSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 633 EHRYLHrqvaavgQEPQVFG-RSLQENIAYGLTQ--KPTMEEITAAAvksgahsfisglpqGYDTEVGEAGSQLSGGQRQ 709
Cdd:PRK11247 82 DTRLMF-------QDARLLPwKKVIDNVGLGLKGqwRDAALQALAAV--------------GLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAI 780
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
560-785 |
1.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRPD---VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 636
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAA-VGQEP--QVFGRSLQENIAYG---LTQKPtmEEITA----AAVKSGAHSFISGLPQgydtevgeagsQLSGG 706
Cdd:PRK13633 82 DIRNKAGmVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGT 785
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
567-789 |
2.00e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTGGQLLLDGKPLPQYEHRYLHRQ 640
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGR-SLQENIAY-----GLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQRQAVALA 714
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYplkshGIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
584-760 |
2.40e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL---PQYEhrylhRQVAAVGQEPQVFGR-SLQENI 659
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQ-----RPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGLTQ-KPTMEEITA--AAVKSGAH--SFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:PRK11607 113 AFGLKQdKLPKAEIASrvNEMLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190
....*....|....*....|....*....|
gi 1168024055 735 AN----SQLQVEQLLyespERYSRSVLLIT 760
Cdd:PRK11607 182 KKlrdrMQLEVVDIL----ERVGVTCVMVT 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
562-792 |
2.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL----LLDGKPLPQYEHR 635
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKSgahsfisglpQGYDTEVGEAGS-QLSGGQR 708
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLEM----------VGLADEFWEKSPfELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 709 QAVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITqHL--SLVEQADHILFLEGGAIREGGTH 786
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVT-HLmdDVADYADYVYLLEKGHIISCGTP 228
|
....*.
gi 1168024055 787 QQLMEK 792
Cdd:PRK13643 229 SDVFQE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
563-781 |
2.58e-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: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRylHRqva 642
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR--NR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 aVGQEPQVFG----RSLQENIAY-----GLTQKPTMEEITAAAVKSGahsfISglpqGYDTEVGEagsQLSGGQRQAVAL 713
Cdd:cd03269 72 -IGYLPEERGlypkMKVIDQLVYlaqlkGLKKEEARRRIDEWLERLE----LS----EYANKRVE---ELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 714 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIR 781
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
562-784 |
3.02e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.12 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ 640
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGR-SLQENIAY-----GLtqKPTmeEITaAAVKSGAHSFisGLPQGYDTEVGEagsqLSGGQRQAVALA 714
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYfaglyGL--KGD--ELT-ARLEELADRL--GMEELLDRRVGG----FSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQlqveQLLYESPERYSR---SVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMAT----RALREFIRQLRAlgkCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
577-808 |
3.03e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHRylhrqvaavgqepqvfgrslq 656
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDR--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 ENIAY-----GLTQKPTMEE----------ITAAAVKSGAHSFIS--GLPQGYDTEVGEagsqLSGGQRQAVALARALIR 719
Cdd:COG4152 71 RRIGYlpeerGLYPKMKVGEqlvylarlkgLSKAEAKRRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 720 KPCVLILDDATSALDA-NSQLqVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKGCYW 797
Cdd:COG4152 147 DPELLILDEPFSGLDPvNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
250
....*....|.
gi 1168024055 798 AMVQAPADAPE 808
Cdd:COG4152 225 LRLEADGDAGW 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
563-778 |
3.97e-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: 87.50 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqva 642
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 avgqepqvfgrslqENIAYgltqkptmeeitaaavksgahsFisglpqgydtevgeagSQLSGGQRQAVALARALIRKPC 722
Cdd:cd03221 63 --------------VKIGY----------------------F----------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 723 VLILDDATSALDANSQLQVEQLLyespERYSRSVLLITQHLSLVEQ-ADHILFLEGG 778
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
562-780 |
4.26e-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: 90.53 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQnlyqptggqlLLDGkplpqyehrYLHrqv 641
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG---------DLP--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGR-----SLQE---NIAY---GLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTE-----------VGEA 699
Cdd:COG1119 55 PTYGNDVRLFGErrggeDVWElrkRIGLvspALQLRFPRDETVLDVVLSGFFDSI-GLYREPTDEqrerarellelLGLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 700 G------SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHI 772
Cdd:COG1119 134 HladrpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHV 213
|
....*...
gi 1168024055 773 LFLEGGAI 780
Cdd:COG1119 214 LLLKDGRV 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
577-784 |
4.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.36 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 650
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 FGRSLQENIAYGL-------TQKPTMEEITAAAVKSGahsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCV 723
Cdd:PRK14247 95 PNLSIFENVALGLklnrlvkSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
577-789 |
4.81e-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: 89.35 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQVAAVGQEPQVfGRSLQ 656
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 --ENIA-----YGLTQKPTMEEITAAAvksgahSFIsglpqgydtEVGEAGSQL----SGGQRQAVALARALIRKPCVLI 725
Cdd:cd03265 90 gwENLYiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 726 LDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
562-760 |
7.34e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhR 639
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAaVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKsgahsfisglpqgydtEVGEAGS------QLSGGQRQ 709
Cdd:PRK11248 73 GVV-FQNEGLLPWRNVQDNVAFGLqlagVEKMQRLEIAHQMLK----------------KVGLEGAekryiwQLSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLIT 760
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
567-794 |
8.44e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpQYEHR---YLHRQVAA 643
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSgAHSFISGlpQGYDTEVGEAgsqLSGGQRQAVALARALIRKP 721
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDA--QHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGG------THQQLMEKKG 794
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
563-780 |
8.69e-20 |
|
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: 88.87 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTGGQLLLDGKPLpqyeHRYL 637
Cdd:cd03234 4 LPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR----KPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQEPQVFGRSL--QENIAYGLTQKptMEEITAAAVKSgAHSFISGLPQGYDTEVGEAG-SQLSGGQRQAVALA 714
Cdd:cd03234 79 FQKCVAYVRQDDILLPGLtvRETLTYTAILR--LPRKSSDAIRK-KRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLL-ITQHLS-LVEQADHILFLEGGAI 780
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILtIHQPRSdLFRLFDRILLLSSGEI 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
572-769 |
1.30e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 572 YPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKP---LPQYEhRYlhRQVAAVGQE 647
Cdd:COG1101 12 NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK-RA--KYIGRVFQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 648 PQV---FGRSLQEN--IAYGLTQKPTMeeitAAAVKSGAHSFIS--------GLPQGYDTEVGeagsQLSGGQRQAVALA 714
Cdd:COG1101 89 PMMgtaPSMTIEENlaLAYRRGKRRGL----RRGLTKKRRELFRellatlglGLENRLDTKVG----LLSGGQRQALSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLslvEQA 769
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM---EQA 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
569-780 |
2.67e-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: 87.77 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 569 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKpLPqYEHR--YLHRQVAAVGQ 646
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VP-WKRRkkFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQVF-------GRSLQENIaYGLTQ---KPTMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARA 716
Cdd:cd03267 103 KTQLWwdlpvidSFYLLAAI-YDLPParfKKRLDELSELL----------DLEELLDTPV----RQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
559-784 |
3.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 559 LEGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLH 638
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 711
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSL-VEQADHILFL-EGGAIREGG 784
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLaAEWADQVIVLkEGRVLAEGD 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
562-782 |
3.85e-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: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQV 641
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVF--GRSLQENIAYGltqKPTMEEITAAAVK-----SGAHSFisglpqgydTEVGEagsqLSGGQRQAVALA 714
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELRDG---APGGTEQEVRGYLgrflfSGDDAF---------KPVGV----LSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLITqH----LSLVeqADHILFLEGGAIRE 782
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVS-HdryfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
555-784 |
4.63e-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: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 555 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEh 634
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 635 rylhrqvAAVGQEPQVFGRslqENI-----AYGLTQK---PTMEEItaaavksgaHSFiSGLPQGYDTEVGEagsqLSGG 706
Cdd:cd03220 91 -------LGGGFNPELTGR---ENIylngrLLGLSRKeidEKIDEI---------IEF-SELGDFIDLPVKT----YSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
562-780 |
7.23e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQYEHR-- 635
Cdd:PRK15439 11 LLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 -YLhrqvaaVGQEPQVF-GRSLQENIAYGLTQKP-TMEEITAAAVKSGAHsfisglpqgYDTEVgEAGSqLSGGQRQAVA 712
Cdd:PRK15439 88 iYL------VPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS-SAGS-LEVADRQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 713 LARALIRKPCVLILDDATSALdanSQLQVEQLLYESPERYSRSV--LLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
263-538 |
8.09e-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: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQD-GSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG---------HVHSHLQgevfgavlRQE 332
Cdd:cd18778 17 VPPWLIRELVDLVTIGsKSLGLLLGLALLLLGAYLLRALLNFL-RIYLNHVAEqkvvadlrsDLYDKLQ--------RLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 333 TEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 412
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKE----AVAYAVNSWTTSIsGMLLkvgILY 488
Cdd:cd18778 168 YRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAmklwAIFHPLMEFLTSL-GTVL---VLG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168024055 489 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18778 244 FGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
560-778 |
9.01e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ-----------NLYQPTGGQLLLdgkp 628
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaglwpygsgRIARPAGARVLF---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 629 LPQyeHRYLhrqvaavgqePQVfgrSLQENIAY-GLTQKPTMEEITAAAVKSGAHSFISGLpqgyDTEVgEAGSQLSGGQ 707
Cdd:COG4178 431 LPQ--RPYL----------PLG---TLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSLVEQADHILFLEGG 778
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
565-793 |
1.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 565 FQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP----QYEHRYLH 638
Cdd:PRK13634 5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYDTEvgeAGSQLSGGQRQAVALA 714
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG----PMNFGVSEEDAKQKAREMIElvGLPEELLAR---SPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 715 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKK 793
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
266-547 |
1.10e-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: 87.89 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 266 FFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHL----QGEVFGAVLRQETEFFQQ--N 339
Cdd:cd18578 30 ILFSKLIS-VFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLtrrlRKLAFRAILRQDIAWFDDpeN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDSLSENLSLFL-----------------WYLvrGLCLLGIM--LWGSVSLTMvtlvtlpllfl 400
Cdd:cd18578 109 STGALTSRLSTDASDVRGLVGDRLGLILqaivtlvagliiafvygWKL--ALVGLATVplLLLAGYLRM----------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 401 lpkkvgKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISg 479
Cdd:cd18578 176 ------RLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgFGLSQSLT- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 480 MLLKVGILYIGGQLVTSGAVSSGNLVTfVLYQMQFT-QAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPR 547
Cdd:cd18578 249 FFAYALAFWYGGRLVANGEYTFEQFFI-VFMALIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
586-790 |
1.13e-18 |
|
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: 88.62 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 586 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----------PqyeHRylhRQVAAVGQEPQVFG-RS 654
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflpP---HR---RRIGYVFQEARLFPhLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQENIAYGL------TQKPTMEEITAAAvksGahsfISGL----PQgydtevgeagsQLSGGQRQAVALARALIRKPCVL 724
Cdd:COG4148 94 VRGNLLYGRkrapraERRISFDEVVELL---G----IGHLldrrPA-----------TLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 725 ILDDATSALDANSQLQV----EQLlyesPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 790
Cdd:COG4148 156 LMDEPLAALDLARKAEIlpylERL----RDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
564-777 |
1.16e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 564 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQP--TGGQLLLDGK---PLPQYEhryl 637
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRrltALPAEQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 hRQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEE----ITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 712
Cdd:COG4136 76 -RRIGILFQDDLLFPHlSVGENLAFALPPTIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 713 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEG 777
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
563-793 |
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 1168024055 563 VQFQDVSFAYPN-RP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQYEHRY 636
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAVAL 713
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 714 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 792
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 1168024055 793 K 793
Cdd:PRK13646 237 K 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
562-789 |
1.99e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TGGQLLLDGKPLPQYEHR 635
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgea 699
Cdd:PRK15134 85 TLRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYPH--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 700 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGG 778
Cdd:PRK15134 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 1168024055 779 AIREGGTHQQL 789
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
576-779 |
2.17e-18 |
|
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: 84.69 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLL-------LDGKPLPQYEHRYlhrQVAAVGQEP 648
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRY---SVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 QVFGRSLQENIAYGltqKPTMEEITAAAVKSGA-HSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 727
Cdd:cd03290 89 WLLNATVEENITFG---SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 728 DATSALDAN-SQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGA 779
Cdd:cd03290 166 DPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
580-765 |
2.33e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.95 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR-SLQEN 658
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 659 I----AYGLTQKPTMEEITAAAvksgahsfisGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:TIGR01189 94 LhfwaAIHGGAQRTIEDALAAV----------GLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|.
gi 1168024055 735 ANSQLQVEQLLYESPERysRSVLLITQHLSL 765
Cdd:TIGR01189 160 KAGVALLAGLLRAHLAR--GGIVLLTTHQDL 188
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
580-789 |
3.34e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YLHRQVAAVGQepqvFGRSL 655
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 Q-----ENIAYGL---TQKPtmeeitaAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 727
Cdd:PRK11629 100 PdftalENVAMPLligKKKP-------AEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 728 DATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILfleggAIREGGTHQQL 789
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-----EMRDGRLTAEL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
575-738 |
5.68e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR----YL-HRQvaavGQEPQ 649
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 650 VfgrSLQENIA-----YGltQKPTMEEITAAAVKSGAhsfISGLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVL 724
Cdd:PRK13539 88 L---TVAENLEfwaafLG--GEELDIAAALEAVGLAP---LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....
gi 1168024055 725 ILDDATSALDANSQ 738
Cdd:PRK13539 150 ILDEPTAALDAAAV 163
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
575-772 |
9.39e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.54 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 653
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAY--GLTQKPTMEEITAAAVKSGAHSFISGlpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:cd03231 89 SVLENLRFwhADHSDEQVEEALARVGLNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1168024055 732 ALDANSQLQVEQLLYESPERYSRSVLliTQHLSLVEQADHI 772
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVL--TTHQDLGLSEAGA 193
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
261-530 |
1.13e-17 |
|
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: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGiYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQN 339
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTY-WGHVMGaRIETDMRRDLFEHLQKLSFSFFDNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 340 QTGNIMSRVTEDTSTLSDsLS----ENLslflwyLVRGLCLLG---IMLWGSVSLTMVTLV----TLPLLFLLPKKVGKW 408
Cdd:cd18549 97 KTGQLMSRITNDLFDISE-LAhhgpEDL------FISIITIIGsfiILLTINVPLTLIVFAllplMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 409 YQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGM---LLKV 484
Cdd:cd18549 170 FR----RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK---AYKAMAYFFSGMNFftnLLNL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168024055 485 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQK 530
Cdd:cd18549 242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
575-745 |
1.48e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 653
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAY--GLTQKPTMEEITAAAVKsgahsfisglpqgydteVGEAG------SQLSGGQRQAVALARALIRKPCVLI 725
Cdd:PRK13538 90 TALENLRFyqRLHGPGDDEALWEALAQ-----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|
gi 1168024055 726 LDDATSALDANSQLQVEQLL 745
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALL 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
563-735 |
1.66e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.89 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylHRQVA 642
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQE----PQVfgrSLQENIAYGL----TQKPTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 713
Cdd:PRK11650 80 MVFQNyalyPHM---SVRENMAYGLkirgMPKAEIEErVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAM 145
|
170 180
....*....|....*....|..
gi 1168024055 714 ARALIRKPCVLILDDATSALDA 735
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDA 167
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
572-787 |
1.94e-17 |
|
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: 82.21 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 572 YPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQV 650
Cdd:cd03218 10 YGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 FGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYdtevgeaGSQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:cd03218 87 FRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERySRSVlLITQH-----LSLVEQAdHILFlEGGAIREGGTHQ 787
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDR-GIGV-LITDHnvretLSITDRA-YIIY-EGKVLAEGTPEE 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
544-791 |
2.29e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 544 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNrpdvlvlqgltftlrpGEVTALVGPNGSGKSTvaaLLQNLyqptggqll 623
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSL--------- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 624 ldgkpLPQYE----HRYLHRQVAAVGQEPQVFGRSLQENIaygLTQKPTMEEITAAAVK-SGAHSFISGLPQGYDTEVGE 698
Cdd:PTZ00243 707 -----LSQFEisegRVWAERSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVRvSQLEADLAQLGGGLETEIGE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 699 AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN-SQLQVEQLLYESPERYSRsvLLITQHLSLVEQADHILFLEG 777
Cdd:PTZ00243 779 KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTR--VLATHQVHVVPRADYVVALGD 856
|
250
....*....|....
gi 1168024055 778 GAIREGGTHQQLME 791
Cdd:PTZ00243 857 GRVEFSGSSADFMR 870
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
325-509 |
3.46e-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: 82.98 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 325 FGAVLRQETEFFQQNQTGNIMSRVTEDT----STLSDSLSENL-----------SLFL----WYLVRGLCLLGIMLWGSV 385
Cdd:cd18574 82 FSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLrsvtqtvgcvvSLYLispkLTLLLLVIVPVVVLVGTL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 386 sltmvtlvtlpllfllpkkVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 465
Cdd:cd18574 162 -------------------YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLG 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1168024055 466 VAYAV-----NswtTSISGMLLkvGILYIGGQLVTSGAVSSGNLVTFVL 509
Cdd:cd18574 223 LGIGIfqglsN---LALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
563-778 |
4.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAY-PNRPdvLVLQGLT---FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYL 637
Cdd:PRK13641 3 IKFENVDYIYsPGTP--MEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 ---HRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAV 711
Cdd:PRK13641 81 kklRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpERYSRSVLLITQHLSLV-EQADHILFLEGG 778
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
580-780 |
4.43e-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: 79.78 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFG----RS 654
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKREGlvldLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQENIAygltqkptmeeitaaavksgahsfisglpqgydtevgeAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:cd03215 95 VAENIA--------------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1168024055 735 ANSQLQVEQLLYESPERySRSVLLITQHLS-LVEQADHILFLEGGAI 780
Cdd:cd03215 137 VGAKAEIYRLIRELADA-GKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
560-789 |
4.49e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQD--VSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQYEH 634
Cdd:PRK09473 10 DALLDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 635 RYLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAA--AVK-SGAHSFISGLPQgydtevge 698
Cdd:PRK09473 89 KELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEESVRMldAVKmPEARKRMKMYPH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 699 agsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEG 777
Cdd:PRK09473 161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYA 237
|
250
....*....|..
gi 1168024055 778 GAIREGGTHQQL 789
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
575-789 |
4.91e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyehRYLHRQV------------- 641
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRQVielseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 ------AAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPQgydtevgeags 701
Cdd:PRK10261 101 vrgadmAMIFQEPMtslnpVFtvGEQIAESIR--LHQGASREEAMVEAKRmldqvriPEAQTILSRYPH----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 702 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAI 780
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 1168024055 781 REGGTHQQL 789
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
563-785 |
6.19e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEHRYLH 638
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 RQVAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHsfISGLPqgYDTEVGEAGSQLSGGQRQAVALARA 716
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMN--IVGLD--YEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 785
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
580-790 |
6.73e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQEN 658
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 659 IAYG-LTQKPTM-------EEITAAAVKSGAHSFISGlpQGYDTevgeagsqLSGGQRQAVALARALIRKPCVLILDDAT 730
Cdd:PRK10253 102 VARGrYPHQPLFtrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 731 SALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
563-779 |
7.68e-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: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVA 642
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVFGRSLQENIAYgltqkPTMEEitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 722
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 723 VLILDDATSALDAnsqlQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGA 779
Cdd:cd03223 112 FVFLDEATSALDE----ESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
580-791 |
8.07e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGKPL--PQYEHRYLHRQVAAVGQEPQVFG 652
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 R-SLQENIAYGL------TQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLI 725
Cdd:PRK14267 99 HlTIYDNVAIGVklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 726 LDDATSALDANSQLQVEQLLYESPERYsrSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLME 791
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
576-744 |
8.78e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPlpqyeHRY------LHRQVAAVGQEPQ 649
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 650 -VFGRSLQENIAYGltQKPT-MEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 727
Cdd:PRK11288 90 lVPEMTVAENLYLG--QLPHkGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170
....*....|....*..
gi 1168024055 728 DATSALdanSQLQVEQL 744
Cdd:PRK11288 166 EPTSSL---SAREIEQL 179
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
585-790 |
9.91e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY---EHRYLHRQ-VAAVGQEPQVFGR-SLQENI 659
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGL-----TQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:PRK10070 128 AFGMelagiNAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 735 ANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
581-775 |
1.24e-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: 79.82 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQYEhrylhRQVaaVGQEPQVFG-RSLQE 657
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItePGPD-----RMV--VFQNYSLLPwLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 658 NIAYGLTQ-KPTMEEITAAAVKSgAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 736
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVE-EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1168024055 737 SQLQVEQLLYESPERYSRSVLLITQHLslveqaDHILFL 775
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDV------DEALLL 181
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
580-793 |
1.45e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGG-----QLLLDGKPLPQYEHRY-LHRQVAAVGQEPQVFGR 653
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 733
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 734 DANSQLQVEQLLYESPERYsrSVLLITQHLSlveQADHI-----LFLEGGAIREGGTHQQLMEKK 793
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRL--TVIIVTHNLA---QAARIsdraaLFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
562-780 |
2.11e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhrq 640
Cdd:PRK10535 4 LLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 vAAVGQEPqvFGRSLQEniaYGLTQKPTME---EITA-------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQA 710
Cdd:PRK10535 81 -AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAvyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
581-790 |
2.94e-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: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENI 659
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGLtQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVgeagSQLSGGQRQAVALARALIR-------KPCVLILDDATSA 732
Cdd:COG4138 91 ALHQ-PAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 733 LDANSQLQVEQLLYESPERySRSVLLITQHLSL-VEQADHILFLEGGAIREGGTHQQLM 790
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
576-784 |
7.34e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTGGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVF 651
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 652 GRSLQENIAYGL-----TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 726
Cdd:PRK10418 92 FNPLHTMHTHARetclaLGKPADDATLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 727 DDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG 784
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
563-793 |
7.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.63 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY----EHRY 636
Cdd:PRK13649 3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkP-----TMEEITAAAVKSGAHSFISglpqgyDTEVGEAGSQLSGGQRQ 709
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPERYSRSVLLITqHL--SLVEQADHILFLEGGAIREGGTHQ 787
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVT-HLmdDVANYADFVYVLEKGKLVLSGKPK 230
|
250
....*....|..
gi 1168024055 788 Q------LMEKK 793
Cdd:PRK13649 231 DifqdvdFLEEK 242
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
262-531 |
1.12e-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: 78.26 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSadtfTRNLTLMSI----LTIASAVLEFVgDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFF 336
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGD----INLLNIISIglilLYLFQSLLSYI-RSYLLLKLSqKLDIRLILGYFKHLLKLPLSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 337 QQNQTGNIMSRVTeDTSTLSDSLSEN-LSLFLWYLVrGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQl 411
Cdd:cd18570 94 ETRKTGEIISRFN-DANKIREAISSTtISLFLDLLM-VIISGIILFFYNWKLFLITLLIiplyILIILLFNKPFKKKNR- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 412 levQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGG 491
Cdd:cd18570 171 ---EVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGS 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1168024055 492 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 531
Cdd:cd18570 248 YLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
491-791 |
3.50e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 491 GQLVTSGAVSSgnlvTFVLYQMQFTQAvevLLSIYPRVQKAVGSS-EKIFEYL---DRTPRCPPSGLLTPLHLEGLVQFQ 566
Cdd:PRK10261 245 GEAVETGSVEQ----IFHAPQHPYTRA---LLAAVPQLGAMKGLDyPRRFPLIsleHPAKQEPPIEQDTVVDGEPILQVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEHR 635
Cdd:PRK10261 318 NLVTRFPLRSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQEP-------QVFGRSLQENI-AYGLTQKPTMEEITAAAVKSgahsfISGLPQgydtEVGEAGSQLSGGQ 707
Cdd:PRK10261 398 ALRRDIQFIFQDPyasldprQTVGDSIMEPLrVHGLLPGKAAAARVAWLLER-----VGLLPE----HAWRYPHEFSGGQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADH---ILFLegGAIREGG 784
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvaVMYL--GQIVEIG 546
|
....*..
gi 1168024055 785 THQQLME 791
Cdd:PRK10261 547 PRRAVFE 553
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
580-787 |
3.57e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-------KPLPQyEHRYLHRQVAAVGQepqvfg 652
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDK-AIRELRRNVGMVFQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 rslQENIAYGLTqkpTMEEITAAAVKsgahsfISGLPQgyDTEVGEAGS----------------QLSGGQRQAVALARA 716
Cdd:PRK11124 90 ---QYNLWPHLT---VQQNLIEAPCR------VLGLSK--DQALARAEKllerlrlkpyadrfplHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVlLITQHLSLVEQ-ADHILFLEGGAIREGGTHQ 787
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
573-785 |
3.82e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 573 PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTGGQLLLDGKplpqyehrylhrqVAA-----V 644
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILEPTSGRVEVNGR-------------VSAllelgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 GQEPQVFGRslqENI-----AYGLTQKPT---MEEITAaavksgahsFiSGLPQGYDTEVGeagsQLSGGQRQAVALARA 716
Cdd:COG1134 98 GFHPELTGR---ENIylngrLLGLSRKEIdekFDEIVE---------F-AELGDFIDQPVK----TYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGT 785
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
565-782 |
3.85e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 565 FQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQyEHRYLHRQ-VAA 643
Cdd:PRK10522 325 LRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKlFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 644 VGQEPQVFGRSLqeniaygltqKPTMEEITAAAVKsgahSFISGLPQGYDTEVGE---AGSQLSGGQRQAVALARALIRK 720
Cdd:PRK10522 402 VFTDFHLFDQLL----------GPEGKPANPALVE----KWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 721 PCVLILDDAtsALDANSQLQVE--QLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 782
Cdd:PRK10522 468 RDILLLDEW--AADQDPHFRREfyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
311-790 |
4.20e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 79.95 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 311 NTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSenLSLF----LWYLVRG-LCLLGIMLWGSV 385
Cdd:TIGR01271 951 HTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP--LTLFdfiqLTLIVLGaIFVVSVLQPYIF 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 386 SLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSsqvAIEALSAMPTVRSFANeegeaQKFREKLQEiKTLNQKEA 465
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH---LITSLKGLWTIRAFGR-----QSYFETLFH-KALNLHTA 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 466 VAYAvnsWTTSISGMLLKVGILY-----------IGGQLVTSGAVssGNLVTFVLYQMQFTQAVeVLLSIypRVQKAVGS 534
Cdd:TIGR01271 1100 NWFL---YLSTLRWFQMRIDIIFvfffiavtfiaIGTNQDGEGEV--GIILTLAMNILSTLQWA-VNSSI--DVDGLMRS 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 535 SEKIFEYLDRTPRCP-PSGLLTPLHL-----------------EGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTAL 596
Cdd:TIGR01271 1172 VSRVFKFIDLPQEEPrPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGL 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 597 VGPNGSGKST-VAALLQNLyqPTGGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSLQENI-AYgltQKPTMEE 671
Cdd:TIGR01271 1251 LGRTGSGKSTlLSALLRLL--STEGEIQIDGV---SWNSVTLQTWRKAFGVIPQkvfIFSGTFRKNLdPY---EQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 672 ITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESper 751
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS--- 1399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1168024055 752 YSRSVLLITQH-LSLVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:TIGR01271 1400 FSNCTVILSEHrVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
580-782 |
4.45e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQY--EHRYLHRqVAAVGQEPQVF----GR 653
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLR-AKHVGFVFQSFmlipTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:PRK10584 104 NALENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIRE 782
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
576-745 |
4.58e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL----PQyehrylhrqvAA-------V 644
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPR----------DAialgigmV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 GQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSgahsfISGLPQGY------DTEVGeagsQLSGGQRQAVALARAL 717
Cdd:COG3845 86 HQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARAR-----IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKAL 156
|
170 180
....*....|....*....|....*...
gi 1168024055 718 IRKPCVLILDDATSALdanSQLQVEQLL 745
Cdd:COG3845 157 YRGARILILDEPTAVL---TPQEADELF 181
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
566-790 |
7.63e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVG 645
Cdd:COG4604 5 KNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQV-----------FGR--------------SLQENIAY-GLtqkptmEEItaaavksgAHSFIsglpqgydtevgea 699
Cdd:COG4604 82 QENHInsrltvrelvaFGRfpyskgrltaedreIIDEAIAYlDL------EDL--------ADRYL-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 700 gSQLSGGQRQavalaRALI------RKPCVLiLDDATSALDANSQLQVEQLLYESPERYSRSVLLI-------TQHlslv 766
Cdd:COG4604 134 -DELSGGQRQ-----RAFIamvlaqDTDYVL-LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVlhdinfaSCY---- 202
|
250 260
....*....|....*....|....
gi 1168024055 767 eqADHILFLEGGAIREGGTHQQLM 790
Cdd:COG4604 203 --ADHIVAMKDGRVVAQGTPEEII 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
562-775 |
7.82e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:PRK09544 4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAvgqePQVFGRSLQeniaygLTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKP 721
Cdd:PRK09544 81 TL----PLTVNRFLR------LRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFL 775
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
576-744 |
1.01e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFGR- 653
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAYG--LTQK---------PTMEEITAAAVKsgahsfISGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPC 722
Cdd:PRK09700 96 TVLENLYIGrhLTKKvcgvniidwREMRVRAAMMLL------RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180
....*....|....*....|..
gi 1168024055 723 VLILDDATSALdanSQLQVEQL 744
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYL 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
580-794 |
1.15e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGKPL----PqyEHRylhrqvAAVG-----QEP 648
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelsP--DER------ARAGiflafQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 649 QVF-GRSLQE--NIAYGltqKPTMEEITAAAVKSGAHSFIS--GLPQGY-DTEVGEaGsqLSGGQRQAVALARALIRKPC 722
Cdd:COG0396 87 VEIpGVSVSNflRTALN---ARRGEELSAREFLKLLKEKMKelGLDEDFlDRYVNE-G--FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 723 VLILDDATSALDANSqLQ-----VEQLLyeSPErysRSVLLITQHLSLVE--QADHILFLEGGAI-REGGTH--QQLmEK 792
Cdd:COG0396 161 LAILDETDSGLDIDA-LRivaegVNKLR--SPD---RGILIITHYQRILDyiKPDFVHVLVDGRIvKSGGKElaLEL-EE 233
|
..
gi 1168024055 793 KG 794
Cdd:COG0396 234 EG 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
583-789 |
1.94e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 583 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPQVfgrSLQ--- 656
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLA---SLNprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 ---ENIAYGL-TQKPTM------EEITAAAVKSGahsFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 726
Cdd:PRK15079 116 tigEIIAEPLrTYHPKLsrqevkDRVKAMMLKVG---LLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 727 DDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQL 789
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
576-745 |
2.10e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKPLPQYEHRYLHRQ-VAAVGQE---- 647
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAgIAIIHQElalv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 648 PQVfgrSLQENIAYGltqkptmEEITA------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKP 721
Cdd:PRK13549 95 KEL---SVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180
....*....|....*....|....
gi 1168024055 722 CVLILDDATSALDANsqlQVEQLL 745
Cdd:PRK13549 163 RLLILDEPTASLTES---ETAVLL 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
575-789 |
2.14e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 575 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPTG----GQLLLDGKPLpqyEHRYLHRQVAAVgQEPQV 650
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPI---DAKEMRAISAYV-QQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 FGRSL--QENIAYGLTQKptMEEITAAAVKSGAHSFI---SGLPQGYDTEVGEAGSQ--LSGGQRQAVALARALIRKPCV 723
Cdd:TIGR00955 110 FIPTLtvREHLMFQAHLR--MPRRVTKKEKRERVDEVlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLS-LVEQADHILFLEGGAIREGGTHQQL 789
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
580-779 |
2.44e-14 |
|
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: 73.24 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL---YQPTGGQLLldgkplpqYEHRYlhRQVAAVGQEPQVFGRSLQ 656
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKST---LLKCIygnYLPDSGSIL--------VRHDG--GWVDLAQASPREILALRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 ENIAYgLTQ-------KPTMEEITAAAVKsgahsfisglpQGYDTEV--GEAGSQL-----------------SGGQRQA 710
Cdd:COG4778 93 RTIGY-VSQflrviprVSALDVVAEPLLE-----------RGVDREEarARARELLarlnlperlwdlppatfSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGA 779
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
580-790 |
4.37e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 646
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQVFGR-SLQENI------AYGLTQKPTMEEitaaAVKSGAHSFISGLPQGydtevgEAGSQLSGGQRQAVALARALIR 719
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
580-795 |
4.63e-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: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGK---PLPQYEhrylhrqvaavgqepqvfgRS 654
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEE-------------------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQeniayGLT---QKPtmEEITAAAVKsgahSFISGLPQGydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:cd03217 76 RL-----GIFlafQYP--PEIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 732 ALDANSQLQVEQLLYESPERySRSVLLITQHLSLVE--QADHILFLEGGAIREGGTHQ--QLMEKKGC 795
Cdd:cd03217 134 GLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
580-793 |
6.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQ---LLLDGKPLPQYEH---------------------R 635
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 636 YLHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYdteVGEAGSQLSGGQRQAV 711
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY---LQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFL-EGGAIREGGTHQQL 789
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLdNVLEWTKRTIFFkDGKIIKDGDTYDIL 253
|
....
gi 1168024055 790 MEKK 793
Cdd:PRK13651 254 SDNK 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
557-727 |
9.45e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.60 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVQfqdvsfAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYE 633
Cdd:COG1137 4 LEAENLVK------SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPMHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 634 hR------YLhrqvaavGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaAAVKSGAHSF-ISGLpqgYDTevgeAGSQLS 704
Cdd:COG1137 75 -RarlgigYL-------PQEASIFRKlTVEDNILAVLeLRKLSKKERE-ERLEELLEEFgITHL---RKS----KAYSLS 138
|
170 180
....*....|....*....|...
gi 1168024055 705 GGQRQAVALARALIRKPCVLILD 727
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLD 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
567-792 |
1.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQ-----YEHRYLHR 639
Cdd:PRK13645 11 NVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQEP--QVFGRSLQENIAYGltqkptmeEITAAAVKSGAHSFIS------GLPQGYdteVGEAGSQLSGGQRQAV 711
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFG--------PVNLGENKQEAYKKVPellklvQLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 712 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFL-EGGAIREGG----- 784
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMhEGKVISIGSpfeif 239
|
....*...
gi 1168024055 785 THQQLMEK 792
Cdd:PRK13645 240 SNQELLTK 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
580-793 |
1.78e-13 |
|
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: 74.56 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 659
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGLTqkptMEEITAAAVKSGAH--SFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 737
Cdd:TIGR01271 508 IFGLS----YDEYRYTSVIKACQleEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 738 qLQVEQLLYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKK 793
Cdd:TIGR01271 581 -VVTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
487-777 |
1.96e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 74.01 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 487 LYIGGQLVTSGAVSSGNLVTfVLYQMQ----FTQAVEVLLSIYPRVQK------AVGSSEKIFEYLDRTPRCPPSGLLtp 556
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLML-AGRDMTrlagFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVQFQDVSFAYPNRpDVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgKPLPQyehry 636
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT---KPAKG----- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 lhrQVAAVGQEPQVFGRSLQENIAY----------GLTQKpTMEEITAAaVKSGahsFISGLPQGYDTeVGEAGSQLSGG 706
Cdd:TIGR00954 516 ---KLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDK-DLEQILDN-VQLT---HILEREGGWSA-VQDWMDVLSGG 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALdansQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEG 777
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
580-807 |
2.08e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTV----AALLQNLYQPTG----GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 650
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 FGRSLQENIAYGltQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARAL---------IRKP 721
Cdd:PRK13547 96 FAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK---KGCYW 797
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPahiARCYG 253
|
250
....*....|...
gi 1168024055 798 ---AMVQAPADAP 807
Cdd:PRK13547 254 favRLVDAGDGVP 266
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
290-538 |
2.68e-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: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 290 LMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWY 369
Cdd:cd18565 59 LTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 370 LVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQ 448
Cdd:cd18565 139 VVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNARLE-NNLSGIAVIKAFTAEDFERE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 449 KFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAV------SSGNLVTFVLYQMQFTQAVE 519
Cdd:cd18565 218 RVADASEEYRDANWR---AIRLRAAFFPVIRLVAGAGfvaTFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLT 294
|
250
....*....|....*....
gi 1168024055 520 VLLSIYPRVQKAVGSSEKI 538
Cdd:cd18565 295 RLGDLIDQYQRAMASAKRV 313
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
262-538 |
3.27e-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: 71.30 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQD--GSADTFTRNLTLMS-----ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETE 334
Cdd:cd18554 16 LLLPLILKYIVDDVIQGssLTLDEKVYKLFTIIgimffIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV 414
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 415 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQ--EIKTLNQKEAVAYAVNSWTTSIS-GMLLKVGilyIGG 491
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKTFSAVNTITDlAPLLVIG---FAA 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168024055 492 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
569-741 |
3.63e-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: 69.21 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 569 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGKPLPQYEHRYlHRQVAAVG 645
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEpqvfgrslQENIAYgLTQKPTMEeitaAAVKSGAHSFISGlpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLI 725
Cdd:cd03233 90 EE--------DVHFPT-LTVRETLD----FALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLC 141
|
170
....*....|....*.
gi 1168024055 726 LDDATSALDANSQLQV 741
Cdd:cd03233 142 WDNSTRGLDSSTALEI 157
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
563-784 |
5.36e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK---PLPQYEhrylhR 639
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 QVAAVGQE----PQVfgrSLQENIAYGLT-QKPTMEEI-----TAAAVKSGAHsFISGLPQGydtevgeagsqLSGGQRQ 709
Cdd:PRK11000 76 GVGMVFQSyalyPHL---SVAENMSFGLKlAGAKKEEInqrvnQVAEVLQLAH-LLDRKPKA-----------LSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQhlSLVEQ---ADHILFLEGGAIREGG 784
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
580-789 |
5.52e-13 |
|
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: 70.27 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 659
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AYGLT--QKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 737
Cdd:cd03291 119 IFGVSydEYRYKSVVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 738 qLQVEQLLYES---PERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:cd03291 192 -VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
578-792 |
6.12e-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: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 578 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK-PLPQyEHRYLhRQVAAvgqepqVFGrslq 656
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKR-RKEFA-RRIGV------VFG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 657 eniaygltQK-------PTME---------EITAAAVKSGAHSFISGLPQG--YDTEVgeagSQLSGGQRQAVALARALI 718
Cdd:COG4586 103 --------QRsqlwwdlPAIDsfrllkaiyRIPDAEYKKRLDELVELLDLGelLDTPV----RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 719 RKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 792
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
262-538 |
1.07e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 69.44 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDgIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 340
Cdd:cd18546 16 LAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQT-RLTGRTGErLLYDLRLRVFAHLQRLSLDFHERET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 341 TGNIMSRVTEDTSTLSDSLSENLSLFLwylVRGLCLLGI---MLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQLLEV--- 414
Cdd:cd18546 95 SGRIMTRMTSDIDALSELLQTGLVQLV---VSLLTLVGIavvLLVLDPRLALVALAALPPLAL----ATRWFRRRSSray 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 415 -QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 493
Cdd:cd18546 168 rRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1168024055 494 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
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 ... |
261-538 |
1.24e-12 |
|
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: 69.05 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 261 EMAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMG----HVHSHLQGEVFGAVLRQETEFF 336
Cdd:cd18543 15 GLAIPLLTRRAIDGPIAHGD----RSALWPLVLLLLALGVAEAVLSFLRRYLAGrlslGVEHDLRTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 337 QQNQTGNIMSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 416
Cdd:cd18543 91 DRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 417 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 496
Cdd:cd18543 170 QDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVAN 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1168024055 497 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18543 250 GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
577-785 |
1.43e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------------LLDGKPLPQYEHRY--LHRQ 640
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhELITNPYSKKIKNFkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEP--QVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLPQGYD-TEVGEAGsqLSGGQRQAVALARAL 717
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 718 IRKPCVLILDDATSALDANSQLQVEQLLYESpERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGT 785
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
293-538 |
1.75e-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: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 293 ILTIASAVLEFVGDgIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLV 371
Cdd:cd18564 62 GIALLRGLASYAGT-YLTALVGqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 372 RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFR 451
Cdd:cd18564 141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 452 EklQEIKTLnQKEAVAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRV 528
Cdd:cd18564 221 R--ENRKSL-RAGLRAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRI 297
|
250
....*....|
gi 1168024055 529 QKAVGSSEKI 538
Cdd:cd18564 298 AKASASAERV 307
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
580-793 |
1.80e-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: 68.73 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTGGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSL 655
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGV---SWNSVPLQKWRKAFGVIPQkvfIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:cd03289 94 RKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 735 ANSQLQVEQLLYESperYSRSVLLITQH-LSLVEQADHILFLEGGAIREGGTHQQLMEKK 793
Cdd:cd03289 171 PITYQVIRKTLKQA---FADCTVILSEHrIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
566-760 |
2.09e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQllldGKPLPQYEHRYLHrqvaavg 645
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----ARPQPGIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQ------VFG----------RSLQE----NIAYG---------LTQKPTMEEITAAAvksGAHSFISGL-------- 688
Cdd:TIGR03719 75 QEPQldptktVREnveegvaeikDALDRfneiSAKYAepdadfdklAAEQAELQEIIDAA---DAWDLDSQLeiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 689 -PQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT 760
Cdd:TIGR03719 152 cPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVT 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
590-762 |
2.11e-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: 65.47 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 590 PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgkplpqyehrylhrqvaavgqepqvfgrslqeniaygltqkptm 669
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 670 eeitaaaVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ-----LQVEQL 744
Cdd:smart00382 35 -------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRL 107
|
170
....*....|....*...
gi 1168024055 745 LYESPERYSRSVLLITQH 762
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
567-730 |
2.43e-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: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRPD-----VLVLQGLT---------FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqy 632
Cdd:COG1129 240 ELEDLFPKRAAapgevVLEVEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 633 ehryLHRQVAAVGQ-----------EPQVFGRSLQENIA---------YGLTQKPTMEEITAAAVKSgahsfisgL---P 689
Cdd:COG1129 318 ----IRSPRDAIRAgiayvpedrkgEGLVLDLSIRENITlasldrlsrGGLLDRRRERALAEEYIKR--------LrikT 385
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1168024055 690 QGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDAT 730
Cdd:COG1129 386 PSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
577-792 |
2.96e-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: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGKPLPQYEhrYLHRQvAAVGQEPQVFGRS 654
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCG--YVERP-SKVGEPCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 LQENIA--YGLTQKptmeeITAAAVKSGAHSF----------------ISGLPQ-GYDTE--VGEA-------------- 699
Cdd:TIGR03269 89 LEPEEVdfWNLSDK-----LRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEGKeaVGRAvdliemvqlshrit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 700 --GSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSvLLITQHLSLV--EQADHILFL 775
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS-MVLTSHWPEVieDLSDKAIWL 242
|
250
....*....|....*..
gi 1168024055 776 EGGAIREGGTHQQLMEK 792
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
560-791 |
3.34e-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: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAY--PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-LLDG-------KPL 629
Cdd:TIGR03269 277 EPIIKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewvdmtKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 630 PQYEHRyLHRQVAAVGQEPQVFG-RSLQENiaygLTQKPTMEEITAAAVKSGAHSFISGlpqGYDTEVGEA-----GSQL 703
Cdd:TIGR03269 357 PDGRGR-AKRYIGILHQEYDLYPhRTVLDN----LTEAIGLELPDELARMKAVITLKMV---GFDEEKAEEildkyPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIRE 782
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVK 508
|
....*....
gi 1168024055 783 GGTHQQLME 791
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
578-792 |
5.17e-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: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 578 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP----TGGQLLLDGKPL----PQYEHRYLHRQVAAVGQEPQ 649
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklsPRERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 650 V-------FGRSLQENI-AYGLT----QKPTMEEITAAA------VKSgaHSFI-SGLPQgydtevgeagsQLSGGQRQA 710
Cdd:COG4170 100 ScldpsakIGDQLIEAIpSWTFKgkwwQRFKWRKKRAIEllhrvgIKD--HKDImNSYPH-----------ELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHL-SLVEQADHILFLEGGAIREGGTHQQL 789
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 1168024055 790 MEK 792
Cdd:COG4170 247 LKS 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
577-735 |
1.05e-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: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKPLPQYEHRYLHRQ-VAAVGQE-PQVF 651
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQElTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 652 GRSLQENIAYGltqkptmEEITA-------AAVKSGAHSFISGLpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 724
Cdd:TIGR02633 92 ELSVAENIFLG-------NEITLpggrmayNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170
....*....|.
gi 1168024055 725 ILDDATSALDA 735
Cdd:TIGR02633 164 ILDEPSSSLTE 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
584-790 |
1.38e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENIAYG 662
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 663 LTQKPTMEEItAAAVKSGAHSFisglpqGYDTEVGEAGSQLSGGQRQAVALARALIR-----KP--CVLILDDATSALDA 735
Cdd:PRK03695 94 QPDKTRTEAV-ASALNEVAEAL------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 736 NSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK03695 167 AQQAALDRLLSELCQQ-GIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
580-789 |
1.51e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGKPLPQyehryLHRQVAAVGQEPQVFGR-SL 655
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENIAY-GLTQKPtmEEITAAAVKSGAHSFIS--GLPQGYDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:PLN03211 158 RETLVFcSLLRLP--KSLTKQEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 732 ALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQA-DHILFL-EGGAIREGGTHQQL 789
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLsEGRCLFFGKGSDAM 295
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
562-733 |
1.53e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQ 640
Cdd:PRK11614 5 MLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGR-SLQENIAYG--LTQKPTMEEITAAAVKSgahsfisgLPQGYDTEVGEAGSqLSGGQRQAVALARAL 717
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGgfFAERDQFQERIKWVYEL--------FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170
....*....|....*.
gi 1168024055 718 IRKPCVLILDDATSAL 733
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL 168
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
263-538 |
1.66e-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: 66.04 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 342
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 343 NIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 421
Cdd:cd18568 100 DIITRFQE-NQKIRRFLTRSaLTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEegeaQKFREKLQE--IKTLNQK-EAVAYAVN-SWTTSISGMLLKVGILYIGGQLVTSG 497
Cdd:cd18568 178 EQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNTRfRGQKLSIVlQLISSLINHLGTIAVLWYGAYLVISG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1168024055 498 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18568 254 QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
584-785 |
2.35e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.92 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG----GQLLLDGKPL---PQYEHRYL-HRQVAAVGQEPQVfgrSL 655
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLqriSEKERRNLvGAEVAMIFQDPMT---SL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENIAYGLTqkpTMEEI------TAAAVKSGAHSFIS--GLPQGyDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 727
Cdd:PRK11022 103 NPCYTVGFQ---IMEAIkvhqggNKKTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 728 DATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLV-EQADHILFLEGGAIREGGT 785
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
566-762 |
6.79e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK-----PLpqyeHRYLHRQ 640
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 641 VAAVGQEPQVFGR-SLQENIAYGLTQKptmEEITAAAVKSGAHSFISGLPQGYDTEvgEAGSQLSGGQRQAVALARALIR 719
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1168024055 720 KPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVlLITQH 762
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGV-LITDH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
584-785 |
7.62e-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: 66.19 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--------------PQYEHRYLHRQVAavgqEPQ 649
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmcPQHNILFHHLTVA----EHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 650 VFGRSLQeniayGLTQKPTMEEITAAAVKSGAHSfisglpqgydtEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDA 729
Cdd:TIGR01257 1025 LFYAQLK-----GRSWEEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 730 TSALDANSQLQVEQLLYESpeRYSRSVLLITQHLSLVE-QADHILFLEGGAIREGGT 785
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
560-728 |
9.99e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.25 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 560 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHR 639
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 640 ---------QVAAVGQEPQVFgrslqENIAYGL---TQKP-------TMEEITAAAVKSGAHSfisgLPqgydtevgeag 700
Cdd:PRK11831 82 vrkrmsmlfQSGALFTDMNVF-----DNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKL----MP----------- 141
|
170 180
....*....|....*....|....*...
gi 1168024055 701 SQLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
585-807 |
1.13e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPqyehryLHRQVAAV-----------GQEPQVFGR 653
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIA---------YGLTQKPTMEEITAAavksgahSFISGL----PQGyDTEVGeagsQLSGGQRQAVALARALIRK 720
Cdd:PRK11288 347 SVADNINisarrhhlrAGCLINNRWEAENAD-------RFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEKKGCYWAM 799
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQALSLAL 493
|
....*...
gi 1168024055 800 VQAPADAP 807
Cdd:PRK11288 494 PRTSAAVA 501
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
263-538 |
1.19e-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: 63.29 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 342
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 343 NIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQ-LLEVQVRESl 420
Cdd:cd18588 100 DTVARVRE-LESIRQFLTGSaLTLVL-DLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRrRLEEKFQRG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 421 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLK---VGILYIGGQLVTSG 497
Cdd:cd18588 177 AENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK---TANLSNLASQIVQLIQKlttLAILWFGAYLVMDG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1168024055 498 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18588 254 ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
567-771 |
2.38e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 567 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYlHRQVAAVGQ 646
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFISgLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVLI 725
Cdd:PRK13540 82 RSGINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1168024055 726 LDDATSALDANSQLQVEQLLYEspERYSRSVLLITQHLSL-VEQADH 771
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQE--HRAKGGAVLLTSHQDLpLNKADY 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
566-760 |
3.06e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGqlllDGKPLPQYEHRYLHrqvaavg 645
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQV-FGRSLQENIAYGLTQKP----------------------------TMEEITAAAvksGAHSFIS---------G 687
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGVAEVKaaldrfneiyaayaepdadfdalaaeqgELQEIIDAA---DAWDLDSqleiamdalR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 688 LPQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLIT 760
Cdd:PRK11819 154 CPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVT 217
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
285-538 |
3.22e-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: 62.29 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 285 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLS 364
Cdd:cd18558 59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 365 LFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPkkvGKWYQLLEVQV---RESLAKSSQVAIEALSAMPTVRSFA 441
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSA---VVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 442 NEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL 521
Cdd:cd18558 216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQ 295
|
250
....*....|....*..
gi 1168024055 522 LSIYPRVQKAVGSSEKI 538
Cdd:cd18558 296 VPSIEAFANARGAAYHI 312
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
263-538 |
3.62e-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: 61.73 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFV---GDGIYNNTMGH-----VHSHLQgevfgavlRQETE 334
Cdd:cd18540 20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLfirLAGKIEMGVSYdlrkkAFEHLQ--------TLSFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 FFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQ--LL 412
Cdd:cd18540 92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV----VSIYFQkkIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 413 EVQvRESLAKSSQV--AI-EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYI 489
Cdd:cd18540 168 KAY-RKVRKINSRItgAFnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1168024055 490 GGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18540 247 GGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
563-777 |
4.10e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQVA 642
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQEPQVF--GRSLQENIAYGLtqkptmEEITAAAVKSGAHSFISGLP-QGYDTE--VGeagsQLSGGQRQAVALARAL 717
Cdd:TIGR03719 389 YVDQSRDALdpNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 718 IRKPCVLILDDATSALDansqlqVEQL--LYESPERYSRSVLLITqH----LSLVeqADHILFLEG 777
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD------VETLraLEEALLNFAGCAVVIS-HdrwfLDRI--ATHILAFEG 515
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
260-529 |
4.11e-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: 61.65 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 260 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLefvgdGIYNNTMGhvhSHL-QGevFGAVLRQET----- 333
Cdd:cd18548 14 LELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIA-----GILAGYFA---AKAsQG--FGRDLRKDLfekiq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 334 ----EFFQQNQTGNIMSRVTEDTSTLSDSLSenlsLFLWYLVRG--LCLLGI--MLWGSVSLTMVTLVT----LPLLFLL 401
Cdd:cd18548 84 sfsfAEIDKFGTSSLITRLTNDVTQVQNFVM----MLLRMLVRApiMLIGAIimAFRINPKLALILLVAipilALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 402 PKKVGKWYQllevQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNS-WTTSISGM 480
Cdd:cd18548 160 MKKAIPLFK----KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNpLMMLIMNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 481 LLkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL---LSIYPRVQ 529
Cdd:cd18548 236 AI-VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLsmvFVMLPRAS 286
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
557-733 |
4.14e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLvqfqDVSFaypnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRy 636
Cdd:PRK10762 5 LQLKGI----DKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 lHRQVAAVG---QE----PQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGEagsqLSGGQ 707
Cdd:PRK10762 75 -SSQEAGIGiihQElnliPQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGE 146
|
170 180
....*....|....*....|....*.
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSAL 733
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
557-780 |
4.46e-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: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVqfqdvsfaYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRY 636
Cdd:COG3845 258 LEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQ-VAAVGQEPQVFG----RSLQENIA-----------YGLTQKPTMEEITAAAVKsgahSF-ISglPQGYDTEVGea 699
Cdd:COG3845 330 RRRLgVAYIPEDRLGRGlvpdMSVAENLIlgryrrppfsrGGFLDRKAIRAFAEELIE----EFdVR--TPGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 700 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLS-LVEQADHILFLEGG 778
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeILALSDRIAVMYEG 478
|
..
gi 1168024055 779 AI 780
Cdd:COG3845 479 RI 480
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
584-780 |
4.73e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR-YLHRQVAAVGQEPQVFGRSLQENIAY- 661
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPEDRQSSGLYLDAPLAWn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 662 ---------GLTQKPTMEeitaAAVKSGAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSA 732
Cdd:PRK15439 362 vcalthnrrGFWIKPARE----NAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1168024055 733 LDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAI 780
Cdd:PRK15439 434 VDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
563-778 |
5.09e-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: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----GGQLLLDGKPLPQyehrY 636
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 637 LHRQVAAVGQEPQVFGrslqeniayGLTQKPTMEeitaaavksgahsfISGLPQGydtevgeagsqLSGGQRQAVALARA 716
Cdd:cd03232 77 FQRSTGYVEQQDVHSP---------NLTVREALR--------------FSALLRG-----------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLL-ITQ-HLSLVEQADHILFLEGG 778
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCtIHQpSASIFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
576-779 |
8.04e-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: 60.07 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------LLD---GKPLPQYEHRYLHRQVAAV 644
Cdd:cd03236 12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 gQEPQ---VFGRSLQENIAYGLTQKP---TMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARALI 718
Cdd:cd03236 91 -VKPQyvdLIPKAVKGKVGELLKKKDergKLDELVDQL----------ELRHVLDRNI----DQLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 719 RKPCVLILDDATSALDANSQLQVEQLLYE--SPERYsrsVLLITQHLSLVEQ-AD--HILFLEGGA 779
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRElaEDDNY---VLVVEHDLAVLDYlSDyiHCLYGEPGA 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
587-741 |
1.05e-09 |
|
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: 59.73 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 587 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL---PQY-EHRY-------LHRQVAAVGQEPQvfgrsL 655
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYiKADYegtvrdlLSSITKDFYTHPY-----F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 QENIAygltqKPTMEEitaaavksgahsfisglpQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDA 735
Cdd:cd03237 96 KTEIA-----KPLQIE------------------QILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
....*.
gi 1168024055 736 NSQLQV 741
Cdd:cd03237 149 EQRLMA 154
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
577-797 |
1.13e-09 |
|
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: 59.58 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPLPQYE--HRylhrqvAAVG-----QE 647
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpdER------ARAGlflafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 648 P-QVFGRSLQENIAYGLT---QKPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQ--LSGGQRQAVALARALIRKP 721
Cdd:TIGR01978 86 PeEIPGVSNLEFLRSALNarrSARGEEPLDLLDFEKLLKEKLALL--DMDEEFLNRSVNegFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 722 CVLILDDATSALDANS-QLQVEQL-LYESPErysRSVLLITQHLSLVE--QADHILFLEGGAI-REGGTHqqLM---EKK 793
Cdd:TIGR01978 164 KLAILDEIDSGLDIDAlKIVAEGInRLREPD---RSFLIITHYQRLLNyiKPDYVHVLLDGRIvKSGDVE--LAkelEAK 238
|
....
gi 1168024055 794 GCYW 797
Cdd:TIGR01978 239 GYDW 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
576-738 |
1.18e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGKP-----LPQYEHR---YLHRQVAAV 644
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkdIRDSEALgivIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 645 gqePQVfgrSLQENI-------AYGL-----TQKPTMEEItaAAVksgahsfisGLPQGYDTEVGEAGSqlsgGQRQAVA 712
Cdd:NF040905 91 ---PYL---SIAENIflgneraKRGVidwneTNRRARELL--AKV---------GLDESPDTLVTDIGV----GKQQLVE 149
|
170 180
....*....|....*....|....*..
gi 1168024055 713 LARALIRKPCVLILDDATSAL-DANSQ 738
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSA 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
562-745 |
1.45e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLpqyehrylhrqv 641
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------------ 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVFGRSLQEN-IAYGLTQKPTMEEitaaaVKSGAH--SF-ISG---LPQGYdtevgeagsQLSGGQRQAVALA 714
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSNpLLYMMRCFPGVPE-----QKLRAHlgSFgVTGnlaLQPMY---------TLSGGQKSRVAFA 639
|
170 180 190
....*....|....*....|....*....|.
gi 1168024055 715 RALIRKPCVLILDDATSALDANSqlqVEQLL 745
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDA---VEALI 667
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
579-796 |
1.68e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 579 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG---------------KPLPQY------EHRYL 637
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYvidgdrEYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQVAAVGQepqvfgRSLQENIAyglTQKPTMEEITAAAVKSGAHSFISGLpqGYDTE-VGEAGSQLSGGQRQAVALARA 716
Cdd:PRK10636 95 EAQLHDANE------RNDGHAIA---TIHGKLDAIDAWTIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 717 LIRKPCVLILDDATSALDANSQLQVEQLLyespERYSRSVLLITQHLSLVEQ-ADHILFLEggaireggtHQQLMEKKGC 795
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPiVDKIIHIE---------QQSLFEYTGN 230
|
.
gi 1168024055 796 Y 796
Cdd:PRK10636 231 Y 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
580-734 |
1.85e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY--QPTGGQLLLDGKPLPQyehrylhrqvaavgqepqvfGRSLQE 657
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLID 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 658 NIAYGLTQKPTMEEITAAavksgahsfisGL--PQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALD 734
Cdd:COG2401 105 AIGRKGDFKDAVELLNAV-----------GLsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
581-785 |
2.56e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLhrqVAAVGQEPQVFGR--SLQEN 658
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 659 IAY-------GLTQKPTMEE---ITAAAVKSGAHSFisglpqgYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDD 728
Cdd:PRK15056 100 VVMmgryghmGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 729 ATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFLEGGAIREGGT 785
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLgSVTEFCDYTVMVKGTVLASGPT 225
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
580-797 |
3.54e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 580 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGKPL----P------------QY--------E 633
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPedragegifmafQYpveipgvsN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 634 HRYLHRQVAAV----GQEPQ---VFGRSLQENIAygLTQKPtmEEITAAAVKSGahsfisglpqgydtevgeagsqLSGG 706
Cdd:PRK09580 96 QFFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIA--LLKMP--EDLLTRSVNVG----------------------FSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 707 QRQAVALARALIRKPCVLILDDATSALDANSqLQVEQLLYESPERYSRSVLLITQHLSLVE--QADHILFLEGGAIREGG 784
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSG 228
|
250
....*....|....*
gi 1168024055 785 THQ--QLMEKKGCYW 797
Cdd:PRK09580 229 DFTlvKQLEEQGYGW 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
576-744 |
5.07e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 576 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLP-QYEHRYLHRQVAAVGQE-PQVFGR 653
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 654 SLQENIAYGltQKPT---------MEEITAAAVKSgahsfisglpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 724
Cdd:PRK10982 89 SVMDNMWLG--RYPTkgmfvdqdkMYRDTKAIFDE----------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180
....*....|....*....|
gi 1168024055 725 ILDDATSALdanSQLQVEQL 744
Cdd:PRK10982 157 IMDEPTSSL---TEKEVNHL 173
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
262-518 |
1.28e-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: 57.09 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADtftrNLTLMSI----LTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 337
Cdd:cd18567 19 LASPLYLQLVIDEVIVSGDRD----LLTVLAIgfglLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 338 QNQTGNIMSR---VTEDTSTLSDSLSENL--SLFlwylvrGLCLLGIMLWGSVSLTMVTLVTLPLLFllpkkVGKW--YQ 410
Cdd:cd18567 95 KRHLGDIVSRfgsLDEIQQTLTTGFVEALldGLM------AILTLVMMFLYSPKLALIVLAAVALYA-----LLRLalYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 411 LLEVQVRESL---AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLqeIKTLNQKEAVAYaVNSWTTSISGMLL---KV 484
Cdd:cd18567 164 PLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLL--VDAINADIRLQR-LQILFSAANGLLFgleNI 240
|
250 260 270
....*....|....*....|....*....|....
gi 1168024055 485 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAV 518
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 ... |
262-538 |
1.66e-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: 56.83 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 341
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 342 GNIMSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 420
Cdd:cd18782 99 GELSTRISE-LDTIRGFLTGTaLTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 421 AKSSQVAIEALSAMPTVRSFANEEgeaqKFREKLQEikTLNQ------KEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 494
Cdd:cd18782 177 AKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN--RYARslgegfKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1168024055 495 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18782 251 LRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
581-789 |
2.25e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGK--------PLPQYEHRYLHR-------QVAAVG 645
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRRLLRtewgfvhQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEPQVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAH-----SFISGLPqgydtevgeagSQLSGGQRQA 710
Cdd:PRK11701 102 LRMQV---SAGGNIGerlmavgarhYG--------DIRATAGDWLERveidaARIDDLP-----------TTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 711 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGG-THQQ 788
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGlTDQV 239
|
.
gi 1168024055 789 L 789
Cdd:PRK11701 240 L 240
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
263-538 |
2.31e-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: 56.36 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGsadtftrNLTLMSILTIASAVLeFVGDGIYNNTMG--------HVHSHLQGEVFGAVLRQETE 334
Cdd:cd18555 20 LIPILTQYVIDNVIVPG-------NLNLLNVLGIGILIL-FLLYGLFSFLRGyiiiklqtKLDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 335 FFQQNQTGNIMSRVtEDTSTLSDSLSENLSL----FLWYLVrglcLLGIMLWGSVSLTMVTLVTLPLLFL----LPKKVg 406
Cdd:cd18555 92 FFENRSSGDLLFRA-NSNVYIRQILSNQVISliidLLLLVI----YLIYMLYYSPLLTLIVLLLGLLIVLllllTRKKI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 407 kwYQLLEVQVREsLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA-VNSWTTSISgMLLKVG 485
Cdd:cd18555 166 --KKLNQEEIVA-QTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNiLNSISSSIQ-FIAPLL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 486 ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18555 242 ILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
587-743 |
2.44e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 587 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQY-EHRYLHRQVAAVGQEPQVFGRS-LQENIAYG 662
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykPQYiKPDYDGTVEDLLRSITDDLGSSyYKSEIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 663 LtqkptmeeitaaavksgahsfisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansqlqVE 742
Cdd:PRK13409 441 L-----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VE 487
|
.
gi 1168024055 743 Q 743
Cdd:PRK13409 488 Q 488
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
584-790 |
2.53e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 584 LTFTLRPGEVTALVGPNGSGKSTVA----ALLQNLYQPTGGQLLLDGKPL----PQYEHRYLHRQVAAVGQEPQV----- 650
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGHNVSMIFQEPQScldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 --FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFIsglpqgydteVGEAGSQLSGGQRQAVALARAL 717
Cdd:PRK15093 106 erVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDA----------MRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 718 IRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
585-790 |
2.63e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL-PQYEHRYLHRQVAAVGQEPQ----VFGRSLQENI 659
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKrdglVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 660 AygLTQKP----TMEEITAAAVKSGAHSFISGL----PqGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATS 731
Cdd:PRK10762 352 S--LTALRyfsrAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 732 ALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAI-----REGGTHQQLM 790
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
581-785 |
4.13e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVaaLLQNLYqpTGGQLLLDgKPLPQYEHrylhrqvaavgqEPQVFGRSLQENIA 660
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI-SFLPKFSR------------NKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 661 YGLtqkptmeeitaaavksgahsfisglpqGYDTeVGEAGSQLSGGQRQAVALARALIR--KPCVLILDDATSALDansQ 738
Cdd:cd03238 74 VGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLH---Q 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1168024055 739 LQVEQLLyESPERY---SRSVLLITQHLSLVEQADHILFLEGGAIREGGT 785
Cdd:cd03238 123 QDINQLL-EVIKGLidlGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
581-737 |
7.17e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLyqpTGgqlLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRS------ 654
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHL---SG---LITGDKSAGSHIELLGRTVQREGRLARDIRKSrantgy 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 655 --LQENIAYGLTqkpTMEEITAAAVKSGAH-----SFISGLPQGYD----TEVGEAG------SQLSGGQRQAVALARAL 717
Cdd:PRK09984 91 ifQQFNLVNRLS---VLENVLIGALGSTPFwrtcfSWFTREQKQRAlqalTRVGMVHfahqrvSTLSGGQQQRVAIARAL 167
|
170 180
....*....|....*....|
gi 1168024055 718 IRKPCVLILDDATSALDANS 737
Cdd:PRK09984 168 MQQAKVILADEPIASLDPES 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
587-741 |
7.55e-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: 55.95 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 587 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPL--PQY-EHRYlHRQVAAV--GQEPQVFGRS-LQENIA 660
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISykPQYiSPDY-DGTVEEFlrSANTDDFGSSyYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 661 YGLtqkptmeeitaaavksgahsfisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQ 740
Cdd:COG1245 441 KPL-----------------------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
.
gi 1168024055 741 V 741
Cdd:COG1245 494 V 494
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
593-781 |
1.32e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 593 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHR-YL---HRQVAAVGQEPQVFGR-SLQENIAYGLtqKP 667
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGM--AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 668 TMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLy 746
Cdd:PRK11144 104 SMVAQFDKIVALlGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1168024055 747 espERYSRSV----LLITQHL-SLVEQADHILFLEGGAIR 781
Cdd:PRK11144 172 ---ERLAREInipiLYVSHSLdEILRLADRVVVLEQGKVK 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
566-759 |
2.41e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRpdVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKplpqYEHRYLHRQVAAVG 645
Cdd:PRK11147 323 ENVNYQIDGK--QLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 646 QEpqvfgRSLQENIAYGltqkptMEEITAAAVKSGAHSFISGL---PQGYDTEVgeagSQLSGGQRQAVALARALIRKPC 722
Cdd:PRK11147 396 PE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSN 460
|
170 180 190
....*....|....*....|....*....|....*....
gi 1168024055 723 VLILDDATSALDansqlqVE--QLLYESPERYSRSVLLI 759
Cdd:PRK11147 461 LLILDEPTNDLD------VEtlELLEELLDSYQGTVLLV 493
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
577-797 |
2.95e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTGGQLLLDGKPLPQY--EHRYlHRQVAAVGQEP-QVF 651
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 652 GRSLQE--NIAYGLTQK----PTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAgsqLSGGQRQAVALARALIRKPCVLI 725
Cdd:CHL00131 98 GVSNADflRLAYNSKRKfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168024055 726 LDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVE--QADHILFLEGGAIREGGTHQ--QLMEKKGCYW 797
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGI-NKLMTSENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGDAElaKELEKKGYDW 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
588-748 |
3.00e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 588 LRPGEVTALVGPNGSGKST-VAALLQNLYQ---PTGGQLLLDGKPLPQYEHRY-----------LHRQVAAVGqEPQVFG 652
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTVG-ETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 RSLQ--ENIAYGLTQKPTMEEITAAAVKsgahsfISGLPQGYDTEVG-EAGSQLSGGQRQAVALARALIRKPCVLILDDA 729
Cdd:TIGR00956 163 ARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170
....*....|....*....
gi 1168024055 730 TSALDANSQLQVEQLLYES 748
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTS 255
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
562-734 |
4.34e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAypnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhRQV 641
Cdd:PRK13543 11 LLAAHALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPqvfgrSLQENIAygltqkpTMEEITAAAVKSGAHSfiSGLPQGYDTEVGEAG------SQLSGGQRQAVALAR 715
Cdd:PRK13543 85 AYLGHLP-----GLKADLS-------TLENLHFLCGLHGRRA--KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALAR 150
|
170
....*....|....*....
gi 1168024055 716 ALIRKPCVLILDDATSALD 734
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLD 169
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
566-778 |
4.83e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 566 QDVSFAYPNRPDVLV-LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQP------TGGQLLLDGKPLPQyehrylh 638
Cdd:TIGR00956 763 RNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPLDS------- 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 rqvaavgqepqvfgrSLQENIAYGLTQKPTMEEIT-------AAAVKSGAHSFIS-------------GLPQGYDTEVGE 698
Cdd:TIGR00956 833 ---------------SFQRSIGYVQQQDLHLPTSTvreslrfSAYLRQPKSVSKSekmeyveevikllEMESYADAVVGV 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 699 AGSQLSGGQRQAVALARALIRKPCVLI-LDDATSALDANSQLQVEQLLYESPErYSRSVLLITQHLS--LVEQADHILFL 775
Cdd:TIGR00956 898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLL 976
|
...
gi 1168024055 776 EGG 778
Cdd:TIGR00956 977 QKG 979
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
262-541 |
1.25e-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: 50.97 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQ-------DGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMG-----HVHSHLqgevFGAVL 329
Cdd:cd18580 8 LLLLAFLSQFSNIWLDwwssdwsSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGlrasrRLHDKL----LRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 330 RQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGS--VSLTMVTLVTLPLlfllpkKVGK 407
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSpyFLIVLPPLLVVYY------LLQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 408 WYQLLEVQVR--ESLAKS---SQVAiEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKeavAY----AVNSWTTSIS 478
Cdd:cd18580 158 YYLRTSRQLRrlESESRSplySHFS-ETLSGLSTIRAFGWQERFIEENLRLLDA----SQR---AFylllAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 479 GMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQ-MQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 541
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
697-808 |
1.28e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 697 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQADHIL-FL 775
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVI 217
|
90 100 110
....*....|....*....|....*....|...
gi 1168024055 776 EGGAIREGGTHQQLMEKKGCYWAMVQaPADAPE 808
Cdd:NF000106 218 DRGRVIADGKVDELKTKVGGRTLQIR-PAHAAE 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
562-791 |
1.67e-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: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTGGQLLLDGKPL----PQY---- 632
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnPAQaira 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 633 ------EHRYLHRQVAAVGQEPQVFGRSLQE-----NIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeags 701
Cdd:TIGR02633 337 giamvpEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKT-ASPF---LPIG---------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 702 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILF-----L 775
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVlGLSDRVLVigegkL 481
|
250
....*....|....*.
gi 1168024055 776 EGGAIREGGTHQQLME 791
Cdd:TIGR02633 482 KGDFVNHALTQEQVLA 497
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
263-538 |
2.03e-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: 50.21 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 263 AIPFFTGRLTDWILQDGSADTFTRnLTLMSILTIA-SAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 341
Cdd:cd18783 20 APPIFFQIVIDKVLVHQSYSTLYV-LTIGVVIALLfEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 342 GNIMSRVTEdTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 421
Cdd:cd18783 99 GVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISG---MLLKVGILYIGGQLVTSGA 498
Cdd:cd18783 178 ERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNWPQTLTGpleKLMTVGVIWVGAYLVFAGS 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1168024055 499 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18783 255 LTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
585-750 |
2.04e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ------PTGGQLL---------------------LDGKPLPQYEHRYL 637
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTT---FLRYMAMhaidgiPKNCQILhveqevvgddttalqcvlntdIERTQLLEEEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 638 HRQvaAVGQEPQVFGRSLQENIAyGLTQKPT----------MEEITAAAVKSGAHSFISGLPQGYDTEVgEAGSQLSGGQ 707
Cdd:PLN03073 274 AQQ--RELEFETETGKGKGANKD-GVDKDAVsqrleeiykrLELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGW 349
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1168024055 708 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 750
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
581-778 |
2.55e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFG------- 652
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEERRSTGiyayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 --RSLQENI-----AYGLTQKPTMEE-----ITAAAVKSGAHSfisglpqgydTEVGeagsQLSGGQRQAVALARALIRK 720
Cdd:PRK10982 344 gfNSLISNIrnyknKVGLLDNSRMKSdtqwvIDSMRVKTPGHR----------TQIG----SLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168024055 721 PCVLILDDATSALDANSQLQVEQLLYESPERySRSVLLITQHL-SLVEQADHILFLEGG 778
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
562-748 |
3.03e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqpTGGQllldgkplPQYEHRYLHrqv 641
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDH--------PQGYSNDLT--- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 aavgqepqVFGR---------SLQENIAYgLTQKPTMEEITAAAVK----SGAHSFIsGLPQ-----------------G 691
Cdd:PRK10938 320 --------LFGRrrgsgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFDSI-GIYQavsdrqqklaqqwldilG 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 692 YDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQ---VEQLLYES 748
Cdd:PRK10938 390 IDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlNRQLVrrfVDVLISEG 451
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
577-745 |
3.32e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 577 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLyqpTGGQLLLDGKPlpQYEHRYLhrqVAAVGQEP------QV 650
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKST---LMKIL---NGEVLLDDGRI--IYEQDLI---VARLQQDPprnvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 651 F----------GRSLQE--NIAYGLTQKPT------MEEITAAAVKSGAHSFIS---------GLPQgyDTEVgeagSQL 703
Cdd:PRK11147 84 YdfvaegieeqAEYLKRyhDISHLVETDPSeknlneLAKLQEQLDHHNLWQLENrinevlaqlGLDP--DAAL----SSL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1168024055 704 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLL 745
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
521-791 |
3.93e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 521 LLSIYPRVQKAVGssEKIFEyldrtprcppsglltplhleglvqFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPN 600
Cdd:PRK13549 244 LTALYPREPHTIG--EVILE------------------------VRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 601 GSGKSTVAALLQNLYQptG---GQLLLDGKPL----PQY----------EHRYLHRQVA--AVGQE------PQVFGRSL 655
Cdd:PRK13549 298 GAGRTELVQCLFGAYP--GrweGEIFIDGKPVkirnPQQaiaqgiamvpEDRKRDGIVPvmGVGKNitlaalDRFTGGSR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 656 qenIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDA 735
Cdd:PRK13549 376 ---IDDAAELKTILESIQRLKVKT-ASPE---LAIA----------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 736 NSQLQVEQLLYESPERySRSVLLITQHLSLV-EQADHILFLEGGAIR-----EGGTHQQLME 791
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVlGLSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
563-777 |
4.80e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGKPLpqyehrylhrQVA 642
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQ-----EPQvfgRSLQENIAYGLtqkptmEEITAA--AVKS----GAHSFisglpQGYDTE--VGeagsQLSGGQRQ 709
Cdd:PRK11819 391 YVDQsrdalDPN---KTVWEEISGGL------DIIKVGnrEIPSrayvGRFNF-----KGGDQQkkVG----VLSGGERN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 710 AVALARALIRKPCVLILDDATSALDansqlqVEQL--LYESPERYSRSVLLITqH----LSLVeqADHILFLEG 777
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLD------VETLraLEEALLEFPGCAVVIS-HdrwfLDRI--ATHILAFEG 517
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
585-776 |
9.85e-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: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 585 TFTLRPGeVTALVGPNGSGKSTV-AALLQNLY---QPTGGQLLLDGKPLPQYEHR---YLHRQVAA-----VGQEPQVFg 652
Cdd:cd03240 17 EIEFFSP-LTLIVGQNGAGKTTIiEALKYALTgelPPNSKGGAHDPKLIREGEVRaqvKLAFENANgkkytITRSLAIL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 653 rslqENIAY---GLTQKPTMEEITaaavksgahsfisglpqgydtevgeagsQLSGGQRQAV------ALARALIRKPCV 723
Cdd:cd03240 95 ----ENVIFchqGESNWPLLDMRG----------------------------RCSGGEKVLAsliirlALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 724 LILDDATSALDA-NSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLE 776
Cdd:cd03240 143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
563-795 |
1.52e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 563 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRylhrqvA 642
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 643 AVGQE----PQVFGR------SLQENIA-----YGLTQ---KPTMEEITAAavkSGAHSFISgLPQGydtevgeagsQLS 704
Cdd:NF033858 73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPFAD-RPAG----------KLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 705 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQ----VEQLLYESPerySRSVLLITQHLSLVEQADHILFLEGGAI 780
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRIRAERP---GMSVLVATAYMEEAERFDWLVAMDAGRV 215
|
250
....*....|....*
gi 1168024055 781 REGGTHQQLMEKKGC 795
Cdd:NF033858 216 LATGTPAELLARTGA 230
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
262-538 |
1.54e-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: 47.47 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 262 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVgDGIY----NNTMGHVHShlqGEVFGAVLRQETEFFQ 337
Cdd:cd18569 19 LVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWL-QQYYllrlETKLALSSS---SRFFWHVLRLPVEFFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 338 QNQTGNIMSRV-TEDT--STLSDSLSE---NLSLFLWYLVrglcllgIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQL 411
Cdd:cd18569 95 QRYAGDIASRVqSNDRvaNLLSGQLATtvlNLVMAVFYAL-------LMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 412 L-EVQVRESlAKSSQVAIEALSAMPTVRSFANEEGeaqkFREK---LQEiKTLNQKEAVAyAVNSWTTSISGMLLKVG-- 485
Cdd:cd18569 168 LnRRLLQDS-GKLTGTTMSGLQMIETLKASGAESD----FFSRwagYQA-KVLNAQQELG-RTNQLLGALPTLLSALTna 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 486 -ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 538
Cdd:cd18569 241 aILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
581-792 |
1.90e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 581 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgkplpqyeHRYLHRQVAAV--GQEPQVFGrslQEN 658
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAIsaGLSGQLTG---IEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 659 IAY-----GLTQKpTMEEITAAAVKSgahsfisglpqgydTEVGEAGSQ----LSGGQRQAVALARALIRKPCVLILDDA 729
Cdd:PRK13546 106 IEFkmlcmGFKRK-EIKAMTPKIIEF--------------SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 730 TSALDANSQLQVEQLLYESPERySRSVLLITQHLSLVEQ-ADHILFLEGGAIREGGTHQQLMEK 792
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
328-541 |
2.02e-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: 47.08 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 328 VLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVR-----GLCL---------LGIMLWGSVSLTMVtlv 393
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSiigtfILIIiylpwfaiaLPPLLVLYYFIANY--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 394 tlpllfllpkkvgkwYQ--LLEVQVRESLAKSSQVA--IEALSAMPTVRSFaneeGEAQKFREKLQE-IKTLNQKEAVAY 468
Cdd:cd18606 155 ---------------YRasSRELKRLESILRSFVYAnfSESLSGLSTIRAY----GAQDRFIKKNEKlIDNMNRAYFLTI 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 469 AVNSW----TTSISGML-LKVGILYIGGQLVTSGAvSSGNLVTFVLyqmQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 541
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; ... |
293-542 |
2.61e-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: 47.08 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 293 ILTIASAVLEFVGDGIYnnTMG------HVHSHLQGEVFGAVLRqeteFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLF 366
Cdd:cd18604 51 LISLLSVLLGTLRYLLF--FFGslrasrKLHERLLHSVLRAPLR----WLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 367 LWYLVRGLCLLG-------IMLWGSVSLTMVTLVtlpllfllpkkVGKWYqlLEVQ--VR--ESLAKS---SQVAiEALS 432
Cdd:cd18604 125 LESTLSLLVILIaivvvspAFLLPAVVLAALYVY-----------IGRLY--LRASreLKrlESVARSpilSHFG-ETLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 433 AMPTVRSFANEEgeaqKFREKLQE-IKTLNQKEAVAYAVNSW----TTSISGML-LKVGILyiggqLVTSGAVSSGnLVT 506
Cdd:cd18604 191 GLVTIRAFGAEE----RFIEEMLRrIDRYSRAFRYLWNLNRWlsvrIDLLGALFsFATAAL-----LVYGPGIDAG-LAG 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 1168024055 507 FVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 542
Cdd:cd18604 261 FSLsFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
697-785 |
3.58e-05 |
|
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: 46.07 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 697 GEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESperySRSVLLITQHLSLVEQAD 770
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK----GNTVVVIEHNLDVIKCAD 239
|
90
....*....|....*..
gi 1168024055 771 HILFL--EGGAirEGGT 785
Cdd:cd03271 240 WIIDLgpEGGD--GGGQ 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
586-790 |
3.79e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 586 FTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqptggqLLLDGkplpQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLT 664
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALArALAGEL-------PLLSG----ERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 665 QKP-----TMEEITAAAVKSGAhsfisgLPQGYDTEVGEAG------SQLSGGQRQAVALARALIRKPCVLILDDATSAL 733
Cdd:PRK10938 93 PGEddtgrTTAEIIQDEVKDPA------RCEQLAQQFGITAlldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 734 DANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLM 790
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
591-777 |
4.01e-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: 44.87 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 591 GEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGkPLPQYEHRYLhrqvaavgqepqvfgrslqeniaygltqkptme 670
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 671 eitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 750
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*...
gi 1168024055 751 RYSRSVLLITQHLSLVEQ-ADHILFLEG 777
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
587-779 |
4.45e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 587 TLRPGEVTALVGPNGSGKSTVAALLQ-----NLYQPTGG-------------------QLLLDG--KPL--PQYehrylh 638
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEpswdevlkrfrgtelqnyfKKLYNGeiKVVhkPQY------ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 639 rqvaaVGQEPQVFgrslqeniaygltqKPTMEEITAAAVKSGAHSFIS---GLPQGYDTEVgeagSQLSGGQRQAVALAR 715
Cdd:PRK13409 169 -----VDLIPKVF--------------KGKVRELLKKVDERGKLDEVVerlGLENILDRDI----SELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168024055 716 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQ-AD--HILFLEGGA 779
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYlADnvHIAYGEPGA 290
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
697-785 |
5.18e-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: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 697 GEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESperySRSVLLITQHLSLVEQAD 770
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKTAD 899
|
90
....*....|....*..
gi 1168024055 771 HILFL--EGGAirEGGT 785
Cdd:TIGR00630 900 YIIDLgpEGGD--GGGT 914
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
323-525 |
1.14e-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: 44.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 323 EVFGAVLRQETEFFQQNQTG---NIMSRVTEDTSTLSDSLSENL----------SLFLWYLVrGLCLLGIMLwGSVSL-- 387
Cdd:cd18582 76 RVFRHLHSLSLRFHLSRKTGalsRAIERGTRGIEFLLRFLLFNIlptilelllvCGILWYLY-GWSYALITL-VTVALyv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 388 --TMvtlvtlpllfllpkKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 465
Cdd:cd18582 154 afTI--------------KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168024055 466 VAYAVNSWTTSI---SGMllkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIY 525
Cdd:cd18582 220 TSLALLNIGQALiisLGL---TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
550-748 |
1.71e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 550 PSGLLTPLhleglVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQL-LLDGKP 628
Cdd:PRK10636 305 PESLPNPL-----LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 629 L---PQYEHRYLHRQVAAVGQ----EPQVFGRSLQENIaygltqkptmeeitaaavksGAHSFisglpQGydTEVGEAGS 701
Cdd:PRK10636 377 LgyfAQHQLEFLRADESPLQHlarlAPQELEQKLRDYL--------------------GGFGF-----QG--DKVTEETR 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1168024055 702 QLSGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES 748
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEA 472
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
647-784 |
2.96e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQVFGRSLQENIAYGLTQKPTMEEITAAAvksgaHSFI-SGLpqGYdTEVGEAGSQLSGGQRQAVALARALI---RKPC 722
Cdd:PRK00635 1651 EGKHFGQLLQTPIEEVAETFPFLKKIQKPL-----QALIdNGL--GY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPT 1722
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168024055 723 VLILDDATSALDANSQLQVEQLLyESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGG 784
Cdd:PRK00635 1723 LFLLDEIATSLDNQQKSALLVQL-RTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
587-779 |
3.34e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 587 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQllLDGKP-----LPQYE----HRYLhRQVAA-----------VGQ 646
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPswdevLKRFRgtelQDYF-KKLANgeikvahkpqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 647 EPQVF---GRSLQENIayglTQKPTMEEITAAAvksgahsfisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCV 723
Cdd:COG1245 172 IPKVFkgtVRELLEKV----DERGKLDELAEKL----------GLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 724 LILDDATSALDANSQLQVEQLLYE-SPErySRSVLLITQHLSLVEQ-AD--HILFLEGGA 779
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRElAEE--GKYVLVVEHDLAILDYlADyvHILYGEPGV 291
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
563-620 |
8.16e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 8.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168024055 563 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGG 620
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
265-532 |
1.32e-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: 41.44 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 265 PFFTGRLTDWILQDGSADTFT--RNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 342
Cdd:cd18560 16 PLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 343 N---IMSRVTEDTSTLsdslsenLSLFLWYLVRGL--CLLGIMLW---GSVSLTMVTLVTLPLLFLLPKKVGKWyqllEV 414
Cdd:cd18560 96 EvvrIMDRGTESANTL-------LSYLVFYLVPTLleLIVVSVVFafhFGAWLALIVFLSVLLYGVFTIKVTEW----RT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 415 QVRESLAK----SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIG 490
Cdd:cd18560 165 KFRRAANKkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1168024055 491 GQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAV 532
Cdd:cd18560 245 GYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
701-778 |
1.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 701 SQLSGGQRQAVALARALI---RKPCVLILDDATSALDANSqlqVEQLLY--ESPERYSRSVLLITQHLSLVEQADHILFL 775
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD---IKALIYvlQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
....*
gi 1168024055 776 --EGG 778
Cdd:PRK00635 885 gpEGG 889
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
271-542 |
1.96e-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: 40.98 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 271 LTDWILQDGSADTFTRN------------LTLM-SILTIASAVLEFVGdgiYNNTMGHVHSHLqgevFGAVLRQETEFFQ 337
Cdd:cd18605 22 LSYWVSHSNNSFFNFINdsfnffltvygfLAGLnSLFTLLRAFLFAYG---GLRAARRLHNKL----LSSILFAKMSFFD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 338 QNQTGNIMSRVTEDTSTLSDSLS-------ENLSLFLWYLVrGLCLlgIMLWGSVSLTMVTLVTLpllfllpkKVGKWYQ 410
Cdd:cd18605 95 KTPVGRILNRFSSDVYTIDDSLPfilnillAQLFGLLGYLV-VICY--QLPWLLLLLLPLAFIYY--------RIQRYYR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 411 LLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFANEEGEAQKFREKLqeikTLNQKEAVA-YAVNSWttsISGMLLKVG 485
Cdd:cd18605 164 ATSRELKrlNSVNLSPLYTHfsETLKGLVTIRAFRKQERFLKEYLEKL----ENNQRAQLAsQAASQW---LSIRLQLLG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168024055 486 ILYIGGQLVTS------GAVSSGNLVTFVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 542
Cdd:cd18605 237 VLIVTFVALTAvvqhffGLSIDAGLIGLALsYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
582-611 |
2.12e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|....
gi 1168024055 582 QGLTFTLRPGEVTALVGPNGSGKST----VAALL 611
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
586-607 |
4.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 4.30e-03
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
422-537 |
5.91e-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: 39.43 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 422 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEiktlnqKEAVAYAVNSWTTSISG---MLLKVGIL---YIGGQLVT 495
Cdd:cd18583 174 EERSILTESLLNWETVKYFNREPYEKERYREAVKN------YQKAERKYLFSLNLLNAvqsLILTLGLLagcFLAAYQVS 247
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1168024055 496 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEK 537
Cdd:cd18583 248 QGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
557-615 |
6.57e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 6.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 557 LHLEGLVQFQDVsfaypnrpdvlvlqglTFTLRPGeVTALVGPNGSGKST-VAALLQNLY 615
Cdd:pfam13476 1 LTIENFRSFRDQ----------------TIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
271-370 |
6.88e-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: 39.38 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 271 LTDW---ILQDGSADTFTRN--LTLMSILTIASAVLEFVGDGIYnnTMGHVHS--HLQGEVFGAVLRQETEFFQQNQTGN 343
Cdd:cd18603 22 LSEWsddPALNGTQDTEQRDyrLGVYGALGLGQAIFVFLGSLAL--ALGCVRAsrNLHNKLLHNILRAPMSFFDTTPLGR 99
|
90 100
....*....|....*....|....*..
gi 1168024055 344 IMSRVTEDTSTLSDSLSENLSLFLWYL 370
Cdd:cd18603 100 ILNRFSKDIDTVDNTLPQNIRSFLNCL 126
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
285-381 |
7.58e-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: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 285 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENls 364
Cdd:cd18601 59 DFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT-- 136
|
90
....*....|....*..
gi 1168024055 365 lFLWYLVRGLCLLGIML 381
Cdd:cd18601 137 -FLDFLQLLLQVVGVVL 152
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
562-776 |
9.49e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 562 LVQFQDVSFAYPNRpdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQV 641
Cdd:PRK13541 1 MLSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168024055 642 AAVGQEPQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISglpqgydtevgEAGSQLSGGQRQAVALARALIRKP 721
Cdd:PRK13541 77 HNLGLKLEM---TVFENLKFWSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1168024055 722 CVLILDDATSALDANSQLQVEQLLYESPErySRSVLLITQHLSLVEQADHILFLE 776
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVMKAN--SGGIVLLSSHLESSIKSAQILQLD 195
|
|
| |
