|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-711 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 721.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 32 TGPISFDV--FGSLLRLWVVAGIRLVIL----FGVSLLTLGSIKPVLKRWLAVHCFLAPVYETGQLMLHGSSPESTHGSL 105
Cdd:TIGR00958 25 QGIFGLLLpfEKGLYVLWLEGTLRLGVLwlgaLGILLNKAGGLLAAVKPLVAALCLATPSLSSLRALAFWEALDPAVRVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 106 GGPSLWLLCTAAAAA-AALFWEKTFPDSSEESNGKEKTQKARVLFMRVLYFYRPDTLLLVGAFIFLSLAVLCEMFIPFYT 184
Cdd:TIGR00958 105 LGLWSWFVWSYGAALpAAALWAVLSSAGASEKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 185 GKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRL 264
Cdd:TIGR00958 185 GRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 265 STDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAG 344
Cdd:TIGR00958 265 SSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 345 ETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFI 424
Cdd:TIGR00958 345 EALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 425 LYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDREPQVSTKGTLQPETLTGHVHFHNLSFSYPTRQERKVLQGFSLEL 504
Cdd:TIGR00958 425 LYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 505 RPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSL 584
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 585 ERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEaLTSCP 664
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRA 663
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 59275972 665 SQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:TIGR00958 664 SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
142-711 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 555.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 142 TQKARVLFMRVLYFYRPDTLLLVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCR 221
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 222 GGLFMCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSW 301
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 302 KLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRD 381
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 382 TVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDRE 461
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 462 PQV-STKGTLQPETLTGHVHFHNLSFSYPTrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL 540
Cdd:COG1132 322 PEIpDPPGAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 541 DGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSG 620
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQ 699
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|..
gi 59275972 700 ELMDRKGGYYKL 711
Cdd:COG1132 560 ELLARGGLYARL 571
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
166-454 |
2.82e-150 |
|
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: 438.70 E-value: 2.82e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALV 245
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 246 KQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYY 325
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 326 LRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYY 405
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 59275972 406 GRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
155-715 |
3.39e-144 |
|
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: 433.74 E-value: 3.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 155 FYRPDTLLLVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTS 234
Cdd:TIGR02204 12 FVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVT 314
Cdd:TIGR02204 92 DIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVyvllrrLT 394
Cdd:TIGR02204 172 LLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL------LT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 395 ALVMQ------VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDREPQVstKG 468
Cdd:TIGR02204 246 AIVIVlvfgaiVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDI--KA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 469 TLQPETL----TGHVHFHNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQP 544
Cdd:TIGR02204 324 PAHPKTLpvplRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 545 LHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQ 624
Cdd:TIGR02204 404 LRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPS-QTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMd 703
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKgRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI- 562
|
570
....*....|..
gi 59275972 704 RKGGYYKLRERL 715
Cdd:TIGR02204 563 AKGGLYARLARL 574
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
130-714 |
2.54e-139 |
|
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: 425.79 E-value: 2.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 130 PDSSEESNGKEKTQKARvlFMRVLYFYRPDTLLLVGAFIFLSLAVLcemFIPFYTGKVID-ILASQYKwnDFLTAI-ILM 207
Cdd:COG2274 130 PTPEFDKRGEKPFGLRW--FLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDrVLPNQDL--STLWVLaIGL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 208 GLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRLStDTTKMARAVAlnvNVLLRTLI 287
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLT---GSLLTALL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 288 KI---VGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEAS 364
Cdd:COG2274 279 DLlfvLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 365 HYDHRLmdTHTLKTRRDTvRAVYVLLRRLTALVMQ---VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIF 441
Cdd:COG2274 359 RWENLL--AKYLNARFKL-RRLSNLLSTLSGLLQQlatVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 442 GDMLNSVGAAGKVFEYLDREP-QVSTKGTLQPETLTGHVHFHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGK 520
Cdd:COG2274 436 QRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 521 STCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFI 600
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 601 SQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIE 679
Cdd:COG2274 595 EALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTVIIIAHRLSTIR 674
|
570 580 590
....*....|....*....|....*....|....*
gi 59275972 680 RADQIILIDQGTVLEQGTHQELMDRKGGYYKLRER 714
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
148-718 |
3.58e-131 |
|
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: 400.25 E-value: 3.58e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 148 LFMRVLYFYRPDTLLLVGAFIFLSLAVLCEMFIPFYTGKVIDILAS----QYKWNDFLTAIILMGLYSLGSSFSAGCRGg 223
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGgrdrSVLWWVPLVVIGLAVLRGICSFVSTYLLS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 224 lfmCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKL 303
Cdd:TIGR02203 80 ---WVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 304 TLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHTLKTRRDTV 383
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD-AVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 384 -RAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDREP 462
Cdd:TIGR02203 236 aGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 463 QVSTkGTLQPETLTGHVHFHNLSFSYPTRqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG 542
Cdd:TIGR02203 316 EKDT-GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 543 QPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYG-LADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGG 621
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 622 EKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSC-PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQE 700
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|....*...
gi 59275972 701 LMDRKGGYYKLRERLFTE 718
Cdd:TIGR02203 554 LLARNGLYAQLHNMQFRE 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
468-692 |
1.79e-130 |
|
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: 385.29 E-value: 1.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 468 GTLQPETLTGHVHFHNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS 547
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 548 YQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIA 627
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSCPS-QTLLVIAHRLKTIERADQIILIDQGTV 692
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
479-711 |
2.38e-121 |
|
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: 362.24 E-value: 2.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 639 LILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALdRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
352-711 |
3.47e-105 |
|
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: 333.71 E-value: 3.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 352 TVRSFNTERSEASHYDHRLMD--THTLKTRR-----DTVRAVyvllrrLTALVMqVAMLYYGRLFIQRGQMSTGNLVsFI 424
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARyeRAAVKSQTslallNFGQAL------IIALGL-TAMMLMAAQGVVAGTMTVGDFV-LV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 425 ------LYQ--SNLGTNIRTLIYIFGDMlnsvgaaGKVFEYLDREPQVSTKGTLQPETLT-GHVHFHNLSFSYptRQERK 495
Cdd:COG5265 302 nayliqLYIplNFLGFVYREIRQALADM-------ERMFDLLDQPPEVADAPDAPPLVVGgGEVRFENVSFGY--DPERP 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNI 575
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHM 655
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 656 VQEALTSCPS-QTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:COG5265 533 IQAALREVARgRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
479-712 |
9.73e-102 |
|
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: 311.47 E-value: 9.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 639 LILDEVTSALDTESEHMVQEALTSC-PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKLR 712
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLmKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
166-454 |
8.76e-100 |
|
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: 308.47 E-value: 8.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALV 245
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 246 KQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYY 325
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 326 LRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYY 405
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 59275972 406 GRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
434-706 |
2.75e-98 |
|
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: 314.39 E-value: 2.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 434 IRTLIYIFGDMLNSVGAAGKVFEYLDREPQVSTKGTLQPETLTG-HVHFHNLSFSYPtrQERKVLQGFSLELRPGQLTAL 512
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYP--GGRPALDGLSLTIPPGERVAL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 513 VGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAAR 592
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 593 RANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVI 671
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTVILI 528
|
250 260 270
....*....|....*....|....*....|....*
gi 59275972 672 AHRLKTIERADQIILIDQGTVLEQGTHQELMDRKG 706
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
236-718 |
6.39e-98 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 313.88 E-value: 6.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 236 MKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTG 315
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 316 LLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDH--RLMDTHTLKTRrdTVRAVYVLLRRL 393
Cdd:PRK11176 180 IAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsNRMRQQGMKMV--SASSISDPIIQL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 394 TALVMQVAMLYygrlfiqrgqmstgnLVSFILYQSNLGTNirTLIYIFGDML------------NS-----VGAAGKVFE 456
Cdd:PRK11176 258 IASLALAFVLY---------------AASFPSVMDTLTAG--TITVVFSSMIalmrplksltnvNAqfqrgMAACQTLFA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 457 YLDREPQVSTkGTLQPETLTGHVHFHNLSFSYPTRqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQG 536
Cdd:PRK11176 321 ILDLEQEKDE-GKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 537 EILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLAD-CSLERVQEAARRANAHSFISQLEKGYDTDVGERG 615
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 616 GQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSC-PSQTLLVIAHRLKTIERADQIILIDQGTVLE 694
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
490 500
....*....|....*....|....
gi 59275972 695 QGTHQELMDRKGGYYKLRERLFTE 718
Cdd:PRK11176 559 RGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
477-706 |
1.64e-96 |
|
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: 297.98 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSYptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK 556
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKG 706
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGrTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
479-714 |
3.15e-95 |
|
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: 294.91 E-value: 3.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 639 LILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKLRER 714
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDvSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
233-714 |
3.04e-91 |
|
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: 295.91 E-value: 3.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 233 TSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMaravalnVNVLLRT-------LIKIVGMLSLMMSLSWKLTL 305
Cdd:COG4987 87 LADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-------DNLYLRVllpllvaLLVILAAVAFLAFFSPALAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 306 LMLMETPVTGLLqGVYDNYYL--RLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTV 383
Cdd:COG4987 160 VLALGLLLAGLL-LPLLAARLgrRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 384 RAvyvLLRRLTALVMQ---VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDR 460
Cdd:COG4987 239 SA---LAQALLQLAAGlavVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 461 EPQVSTKGTLQPETLTGHVHFHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL 540
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 541 DGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSG 620
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQ 699
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLlEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
|
490
....*....|....*
gi 59275972 700 ELMDRKGGYYKLRER 714
Cdd:COG4987 555 ELLAQNGRYRQLYQR 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
148-721 |
1.27e-86 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 284.16 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 148 LFMRVLYFYRPD---TLLLVGAFIFLSLAVLCEmfiPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSS--------- 215
Cdd:PRK13657 6 LYARVLQYLGAEkrlGILLAVANVLLAAATFAE---PILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGvlvarhadr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 216 FSAGCRGGLFmcainsftsrmkVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARavaLNVNVL---LRTLIKIVGM 292
Cdd:PRK13657 83 LAHRRRLAVL------------TEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFG---LWLEFMrehLATLVALVVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 293 LSLMMSLSWKLTLLMLmetpVTGLLQGVYDNYYLRLTKEVQDSMARAN----EAAGETVAGIRTVRSFNTERSEAS---H 365
Cdd:PRK13657 148 LPLALFMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVEEHYhdlfAHVSDAIGNVSVVQSYNRIEAETQalrD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 366 YDHRLMDTHTlktrrdTVR---AVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLgtnIRTLIYIFG 442
Cdd:PRK13657 224 IADNLLAAQM------PVLswwALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLL---IGRLDQVVA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 443 DMLNSVGAAGKV---FEYLDREPQVSTK-GTLQPETLTGHVHFHNLSFSYPTRqeRKVLQGFSLELRPGQLTALVGPSGG 518
Cdd:PRK13657 295 FINQVFMAAPKLeefFEVEDAVPDVRDPpGAIDLGRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 519 GKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHS 598
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 599 FISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKT 677
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdELMKGRTTFIIAHRLST 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 59275972 678 IERADQIILIDQGTVLEQGTHQELMDRKGGYYKL-RERLFTEDDT 721
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALlRAQGMLQEDE 577
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
166-454 |
1.05e-84 |
|
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: 269.41 E-value: 1.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALV 245
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 246 KQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYY 325
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 326 LRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYY 405
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 59275972 406 GRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
165-711 |
4.24e-84 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 280.68 E-value: 4.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 165 GAFIFLSLAVLCEM----FIPFYTGKVID--ILASQYKWndfLTAIIL-MGLYSLGSSFSAGCRGGLFMCAINSFTSRMK 237
Cdd:TIGR03796 154 GALLYLLLAGLLLVlpglVIPAFSQIFVDeiLVQGRQDW---LRPLLLgMGLTALLQGVLTWLQLYYLRRLEIKLAVGMS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 238 VELFGALVKQEISFFETIKTGDITSRLSTDTtKMARAVAlnvNVLLRTLIKIVGM---LSLMMSLSWKLTLLMLmetpVT 314
Cdd:TIGR03796 231 ARFLWHILRLPVRFFAQRHAGDIASRVQLND-QVAEFLS---GQLATTALDAVMLvfyALLMLLYDPVLTLIGI----AF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMAR-ANEAAGETVAGIRTVRSFNTERSEA------SHYDHRLMDTH-TLKTRRDTVRAV 386
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQdAGKLTGVAISGLQSIETLKASGLESdffsrwAGYQAKLLNAQqELGVLTQILGVL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 387 YVLLRRLTAlvmqVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFG---DMLNSVGAAGKVFEY----LD 459
Cdd:TIGR03796 383 PTLLTSLNS----ALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGtlqELEGDLNRLDDVLRNpvdpLL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 460 REPQVSTKGTLQPETLTGHVHFHNLSFSYpTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIL 539
Cdd:TIGR03796 459 EEPEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEIL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 540 LDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAygLADCSL--ERVQEAARRANAHSFISQLEKGYDTDVGERGGQ 617
Cdd:TIGR03796 538 FDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLT--LWDPTIpdADLVRACKDAAIHDVITSRPGGYDAELAEGGAN 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 618 MSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALT--SCpsqTLLVIAHRLKTIERADQIILIDQGTVLEQ 695
Cdd:TIGR03796 616 LSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRrrGC---TCIIVAHRLSTIRDCDEIIVLERGKVVQR 692
|
570
....*....|....*.
gi 59275972 696 GTHQELMDRKGGYYKL 711
Cdd:TIGR03796 693 GTHEELWAVGGAYARL 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
235-711 |
1.11e-83 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 276.60 E-value: 1.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVT 314
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNT-----ER-SEAS--HYdhrlmdthtlKTRRDTVRAV 386
Cdd:PRK10790 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQqarfgERmGEASrsHY----------MARMQTLRLD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 387 YVLLRRL----TALVMQVAMLYYGrlFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLDREP 462
Cdd:PRK10790 249 GFLLRPLlslfSALILCGLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 463 QvsTKGTLQPETLTGHVHFHNLSFSYptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG 542
Cdd:PRK10790 327 Q--QYGNDDRPLQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 543 QPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGlADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGE 622
Cdd:PRK10790 403 RPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 623 KQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHtTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
490
....*....|
gi 59275972 702 MDRKGGYYKL 711
Cdd:PRK10790 562 LAAQGRYWQM 571
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
479-711 |
2.43e-83 |
|
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: 263.96 E-value: 2.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 639 LILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDiCAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
479-690 |
5.62e-77 |
|
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: 244.60 E-value: 5.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSGSIKDNIaygladcslervqeaarranahsfisqlekgydtdvgerggqMSGGEKQRIAIARALIREPQV 638
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 59275972 639 LILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILIDQG 690
Cdd:cd03228 118 LILDEATSALDPETEALILEALRAlAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
249-711 |
3.09e-76 |
|
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: 259.67 E-value: 3.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 249 ISFFETIKTGDITSRLsTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRL 328
Cdd:TIGR01193 244 MSFFSTRRTGEIVSRF-TDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 329 TKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYYGRL 408
Cdd:TIGR01193 323 NHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 409 FIQRGQMSTGNLVSF---ILYQSNLGTNIRTL------IYIFGDMLNSVgaagkvfeYLDREPQVSTKGTLQPETLTGHV 479
Cdd:TIGR01193 403 LVMRGKLTLGQLITFnalLSYFLTPLENIINLqpklqaARVANNRLNEV--------YLVDSEFINKKKRTELNNLNGDI 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPTrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAM 559
Cdd:TIGR01193 475 VINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINY 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVLFSGSIKDNIAYGL-ADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:TIGR01193 553 LPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 639 LILDEVTSALDTESEHMVQEALTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
237-708 |
1.14e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 249.24 E-value: 1.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 237 KVELFGA---------------LVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLsLMMS--L 299
Cdd:PRK10789 57 RVLLFGAsyqlavelredfyrqLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVL-IVMStqI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 300 SWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHtlktr 379
Cdd:PRK10789 136 SWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTG----- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 380 RDTVRAVYVLLRRLTALVMQVAM-----LYYGRLFIQRGQMSTGNLVSFILYqsnLGTNIRTLIYIfGDMLNSV---GAA 451
Cdd:PRK10789 211 KKNMRVARIDARFDPTIYIAIGManllaIGGGSWMVVNGSLTLGQLTSFVMY---LGLMIWPMLAL-AWMFNIVergSAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 452 GKVFEYLDREPQVSTKGTL----QPETLTGHVHfhnlSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL 527
Cdd:PRK10789 287 YSRIRAMLAEAPVVKDGSEpvpeGRGELDVNIR----QFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 528 ERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGY 607
Cdd:PRK10789 362 QRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 608 DTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIERADQIIL 686
Cdd:PRK10789 442 DTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILV 521
|
490 500
....*....|....*....|..
gi 59275972 687 IDQGTVLEQGTHQELMDRKGGY 708
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQSGWY 543
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
145-720 |
7.23e-73 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 247.49 E-value: 7.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 145 ARVLfmRVLYFYRPDTLLLVGAFIFLSLAVLCEmfiPFYTGKVIDILASQYK-------WNDF-LTAIILMGLYSLGSS- 215
Cdd:TIGR01192 8 VRAL--SYLNVHKNRVLLIVIANITLAAITIAE---PILFGRIIDAISSKSDvlptlalWAGFgVFNTIAYVLVAREADr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 216 FSAGCRGGLFmcainsftsrmkVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSL 295
Cdd:TIGR01192 83 LAHGRRATLL------------TEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 296 MMSLSWKLTLLMLMETPVTGLL-----------QGVYDNYYLRLTKEVQDSmaraneaagetVAGIRTVRSFN---TERS 361
Cdd:TIGR01192 151 AFAMDWRLSIVLMVLGILYILIaklvmqrtkngQAAVEHHYHNVFKHVSDS-----------ISNVSVVHSYNrieAETS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 362 EASHYDHRLMDTHTlktrrdTVRAVYVL---LRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLgtnIRTLI 438
Cdd:TIGR01192 220 ALKQFTNNLLSAQY------PVLDWWALasgLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLL---IGRLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 439 YIFGDMLNSVGAAGKVFEYLDREPqvSTKGTLQPETL------TGHVHFHNLSFSYPTRQERkvLQGFSLELRPGQLTAL 512
Cdd:TIGR01192 291 QMSGFITQIFEARAKLEDFFDLED--SVFQREEPADApelpnvKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 513 VGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAAR 592
Cdd:TIGR01192 367 VGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 593 RANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALtSCPSQ--TLLV 670
Cdd:TIGR01192 447 AAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAI-DALRKnrTTFI 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 671 IAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKLRER--LFTEDD 720
Cdd:TIGR01192 526 IAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRsgLLTNQP 577
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
166-454 |
4.94e-71 |
|
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: 233.22 E-value: 4.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALV 245
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 246 KQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYY 325
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 326 LRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYY 405
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 59275972 406 GRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
450-715 |
2.71e-66 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 229.33 E-value: 2.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 450 AAGKVFEYLDREPQVSTKGTLQPETLTGHVHFHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLER 529
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 530 FYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQlEKGYDT 609
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 610 DVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESE-HMVQEALTSCPSQTLLVIAHRLKTIERADQIILID 688
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*..
gi 59275972 689 QGTVLEQGTHQELMDRKGGYYKLRERL 715
Cdd:PRK11160 548 NGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
327-687 |
4.66e-66 |
|
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: 227.55 E-value: 4.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 327 RLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEA-------SHYDHRLMDT--------------HTLKTrrdTVRA 385
Cdd:TIGR02857 170 AAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAaairrssEEYRERTMRVlriaflssavlelfATLSV---ALVA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 386 VYVLLRrltalvmqvamLYYGRLFIQRGqmstgnLVSFIL----YQSnlgtnIRTLIYIFGDMLNSVGAAGKVFEYLDRE 461
Cdd:TIGR02857 247 VYIGFR-----------LLAGDLDLATG------LFVLLLapefYLP-----LRQLGAQYHARADGVAAAEALFAVLDAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 462 PQVSTKGTLQPETLTGHVHFHNLSFSYPTRqeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLD 541
Cdd:TIGR02857 305 PRPLAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 542 GQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGG 621
Cdd:TIGR02857 383 GVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGG 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 622 EKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILI 687
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAlAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
477-696 |
5.26e-64 |
|
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: 212.06 E-value: 5.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK 556
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 637 QVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQG 696
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLrQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
169-454 |
1.44e-59 |
|
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: 202.70 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 169 FLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALVKQE 248
Cdd:cd18589 4 LVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 249 ISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRL 328
Cdd:cd18589 84 IAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 329 TKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYYGRL 408
Cdd:cd18589 164 AVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 59275972 409 FIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18589 244 LVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
477-697 |
7.16e-59 |
|
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: 198.49 E-value: 7.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSYptRQERK-VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHR 555
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIRE 635
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 636 PQVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGT 697
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIrEAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
448-711 |
1.13e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 208.93 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 448 VGAAGKVFEYLDREPQVSTKGTLQPETLTG-HVHFHNLS-FSYptrqERKVLQG-FSLELRPGQLTALVGPSGGGKSTCV 524
Cdd:PRK11174 318 VGAAESLVTFLETPLAHPQQGEKELASNDPvTIEAEDLEiLSP----DGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 525 SLLERFYqPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLE 604
Cdd:PRK11174 394 NALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 605 KGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCP-SQTLLVIAHRLKTIERADQ 683
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASrRQTTLMVTHQLEDLAQWDQ 552
|
250 260
....*....|....*....|....*...
gi 59275972 684 IILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
166-454 |
8.87e-56 |
|
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: 192.73 E-value: 8.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFL------TAIILMGLYSLGSSFSAGcRGGLFMCAINSFTSRMKVE 239
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslktFALALLGVFVVGAAANFG-RVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 240 LFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQG 319
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 320 VYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQ 399
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 400 VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
392-704 |
1.02e-55 |
|
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: 199.97 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 392 RLTALVMQVAMLYYGR-LFIQrGQMSTGNLV--SFILyqsnlGtniRTLIYIfgDML--------NSVGAAGKVFEYLDR 460
Cdd:COG4618 246 KFLRLLLQSAVLGLGAyLVIQ-GEITPGAMIaaSILM-----G---RALAPI--EQAiggwkqfvSARQAYRRLNELLAA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 461 EPQvSTKGTLQPEtLTGHVHFHNLSFSYPTRQeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL 540
Cdd:COG4618 315 VPA-EPERMPLPR-PKGRLSVENLTVVPPGSK-RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 541 DGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSG 620
Cdd:COG4618 392 DGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILIDQGTVLEQGTH 698
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPR 550
|
....*.
gi 59275972 699 QELMDR 704
Cdd:COG4618 551 DEVLAR 556
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
166-454 |
3.36e-54 |
|
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: 188.23 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFL-------TAIILMGLYSLGSSFSAgCRGGLFMCAINSFTSRMKV 238
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEalralnqAVLILLGVVLIGSIATF-LRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 239 ELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQ 318
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 319 GVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVM 398
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 399 QVAMLYYG-RLFIQrGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18780 240 IVLVLWYGgRLVID-GELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
396-702 |
1.06e-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: 188.33 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 396 LVMQVAMLYYGRLFIQRGQMSTGNLV-SFILYQSNLGTnIRTLIYIFGDMLNSVGAAGKVFEYLDREPQVSTKGTL-QPE 473
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIaGSILVGRALAP-IDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLpEPE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 474 tltGHVHFHNLSFSyPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYL 553
Cdd:TIGR01842 315 ---GHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALI 633
Cdd:TIGR01842 391 GKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEEGEQALANAIKALKARgiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-710 |
1.28e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 188.70 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 126 EKTFPDSSEESNGKEKTQKARVLF---------MRVLY----FYRPDTlllvgAFIFLSLAVLCEMFIPF------YTGK 186
Cdd:PTZ00265 780 CKMSDENASENNAGGKLPFLRNLFkrkpkapnnLRIVYreifSYKKDV-----TIIALSILVAGGLYPVFallyakYVST 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 187 VIDILASQYKWNDFLTAIILMGLyslgSSFSAGCRGGLFMCAINSFTSR-MKVELFGALVKQEISFFETIKT--GDITSR 263
Cdd:PTZ00265 855 LFDFANLEANSNKYSLYILVIAI----AMFISETLKNYYNNVIGEKVEKtMKRRLFENILYQEISFFDQDKHapGLLSAH 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 264 LSTDTTKMAraVALNVNVLLRTLIKIVGMLSLMMSLSWkltllmlmeTP-VTGLLQGVYDNYY------LRLTKEVQDSM 336
Cdd:PTZ00265 931 INRDVHLLK--TGLVNNIVIFTHFIVLFLVSMVMSFYF---------CPiVAAVLTGTYFIFMrvfairARLTANKDVEK 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 337 ARANEAAG-------------------ETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALV 397
Cdd:PTZ00265 1000 KEINQPGTvfaynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLF 1079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 398 MQVAMLYYGRLFIQRGQMSTGN----LVSFILYQSNLGTnirtLIYIFGDMLNSVGAAGKVFEYLDREPQVSTK--GTLQ 471
Cdd:PTZ00265 1080 INSFAYWFGSFLIRRGTILVDDfmksLFTFLFTGSYAGK----LMSLKGDSENAKLSFEKYYPLIIRKSNIDVRdnGGIR 1155
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 472 PET---LTGHVHFHNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFY----------------- 531
Cdd:PTZ00265 1156 IKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtnd 1235
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 532 ----QPQQ---------------------------------GEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDN 574
Cdd:PTZ00265 1236 mtneQDYQgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 575 IAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEH 654
Cdd:PTZ00265 1316 IKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 655 MVQEALTSC---PSQTLLVIAHRLKTIERADQIILIDQ----GTVLE-QGTHQELMDRKGGYYK 710
Cdd:PTZ00265 1396 LIEKTIVDIkdkADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
481-692 |
4.27e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMV 560
Cdd:COG4619 3 LEGLSFRV---GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEPVLFSGSIKDNIAYGLADCSLERVQEAARRAnahsfisqLEK-GYDTDVGERG-GQMSGGEKQRIAIARALIREPQV 638
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRERALEL--------LERlGLPPDILDKPvERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 639 LILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEegrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
234-675 |
1.39e-48 |
|
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: 179.48 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 234 SRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMAravalnvNVLLRTLIKIVGMLSLMMS-------LSWKLTLL 306
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQ-------DLYVRVIVPAGVALVVGAAavaaiavLSVPAALI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 307 M--------LMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSfnteRSEASHYDHRLmdtHTLKT 378
Cdd:TIGR02868 159 LaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAA----LAQVEEADREL---TRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 379 RRDTVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYL 458
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 459 D-----REPQVSTKGTLQPETLTghVHFHNLSFSYPTRQErkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQP 533
Cdd:TIGR02868 312 DaagpvAEGSAPAAGAVGLGKPT--LELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 534 QQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGE 613
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 614 RGGQMSGGEKQRIAIARALIREPQVLILDEVTSALD--TESEhMVQEALTSCPSQTLLVIAHRL 675
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDaeTADE-LLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
481-696 |
1.22e-47 |
|
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: 166.33 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHyLHRKVAMV 560
Cdd:cd03247 3 INNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEPVLFSGSIKDNIaygladcslervqeaarranahsfisqlekgydtdvgerGGQMSGGEKQRIAIARALIREPQVLI 640
Cdd:cd03247 81 NQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 641 LDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIERADQIILIDQGTVLEQG 696
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEvLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
205-711 |
2.38e-47 |
|
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: 181.68 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 205 ILMGLYSLGSSFSAGCrGGLFMcainsfTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLR 284
Cdd:TIGR00957 1016 ILQGFAVFGYSMAVSI-GGIQA------SRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 285 TLIKIVGMLSLMMSLSWKLTLLMlmetPVTGLLQGVYDNYYLRLTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTER 360
Cdd:TIGR00957 1089 SLFNVIGALIVILLATPIAAVII----PPLGLLYFFVQRFYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQE 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 361 seashydhRLMDTHTLKTRRDTvRAVY--VLLRRLTALVMQVA---MLYYGRLF--IQRGQMSTGNLVSFILYQSNLGTN 433
Cdd:TIGR00957 1165 --------RFIHQSDLKVDENQ-KAYYpsIVANRWLAVRLECVgncIVLFAALFavISRHSLSAGLVGLSVSYSLQVTFY 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 434 IRTLIYIFGDMLNSVGAAGKVFEYLDREPQV--STKGTLQPETL--TGHVHFHNLSFSYptRQERK-VLQGFSLELRPGQ 508
Cdd:TIGR00957 1236 LNWLVRMSSEMETNIVAVERLKEYSETEKEApwQIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGE 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 509 LTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQ 588
Cdd:TIGR00957 1314 KVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVW 1392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 589 EAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEAL-TSCPSQT 667
Cdd:TIGR00957 1393 WALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIrTQFEDCT 1472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 59275972 668 LLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKL 711
Cdd:TIGR00957 1473 VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
479-705 |
4.29e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.74 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPV--LFSGSIKDNIAYGLADCSL------ERVQEAARRAN----AHSFISQLekgydtdvgerggqmSGGEKQRI 626
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLpreeirERVEEALELVGlehlADRPPHEL---------------SGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 627 AIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgkTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
..
gi 59275972 704 RK 705
Cdd:COG1122 224 DY 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
235-709 |
9.40e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 176.71 E-value: 9.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSwKLTLLMLMetPVT 314
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLL 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYdNYYLRLTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTeRSEASHYDHRLMDTHTLKTRRDTVRAVYVLL 390
Cdd:PLN03232 1061 ILFYAAY-LYYQSTSREVRrlDSVTRSPIYAqfGEALNGLSSIRAYKA-YDRMAKINGKSMDNNIRFTLANTSSNRWLTI 1138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 391 RRLTA------LVMQVAMLYYGRLFIQRGQMSTGNLVsfILYQSNLGTNIRTLIYIFGDMLNSVGAAGKVFEYLD--REP 462
Cdd:PLN03232 1139 RLETLggvmiwLTATFAVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlpSEA 1216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 463 QVSTKGTLQPET--LTGHVHFHNLSFSYptRQE-RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIL 539
Cdd:PLN03232 1217 TAIIENNRPVSGwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 540 LDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMS 619
Cdd:PLN03232 1295 IDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFS 1373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQ----EALTSCpsqTLLVIAHRLKTIERADQIILIDQGTVLEQ 695
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQrtirEEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEY 1450
|
490
....*....|....
gi 59275972 696 GTHQELMDRKGGYY 709
Cdd:PLN03232 1451 DSPQELLSRDTSAF 1464
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
483-692 |
6.04e-45 |
|
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: 158.53 E-value: 6.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:cd03246 5 NVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EPVLFSGSIKDNIaygladcslervqeaarranahsfisqlekgydtdvgerggqMSGGEKQRIAIARALIREPQVLILD 642
Cdd:cd03246 84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 643 EVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILIDQGTV 692
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-711 |
7.20e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 174.06 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 198 NDFLTAIILMGLYSLGSSF-SAGCrgglfMCAINS-FTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAV 275
Cdd:PTZ00265 97 NDIIFSLVLIGIFQFILSFiSSFC-----MDVVTTkILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 276 ALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTgLLQGVYDNYYLRLTKEV-----QDSMARANEAagetVAGI 350
Cdd:PTZ00265 172 GTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI-YICGVICNKKVKINKKTsllynNNTMSIIEEA----LVGI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 351 RTVRSFNTERSEASHYD--HRLMDTHTLKTrrDTVRAVYVLLRRLTALVMQVAMLYYG-RLFIQ-------RGQMSTGNL 420
Cdd:PTZ00265 247 RTVVSYCGEKTILKKFNlsEKLYSKYILKA--NFMESLHIGMINGFILASYAFGFWYGtRIIISdlsnqqpNNDFHGGSV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 421 VSFILyqsnlgtniRTLIYIF---------GDMLNSVGAAGKVFEYLDREPQVSTKGTLQPETLTGHVHFHNLSFSYPTR 491
Cdd:PTZ00265 325 ISILL---------GVLISMFmltiilpniTEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 492 QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL-DGQPLHSYQHHYLHRKVAMVGQEPVLFSGS 570
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 571 IKDNIAYGL-------------------------------ADCSLE--------------------------RVQEAARR 593
Cdd:PTZ00265 476 IKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrAKCAGDlndmsnttdsneliemrknyqtikdsEVVDVSKK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 594 ANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCP---SQTLLV 670
Cdd:PTZ00265 556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITII 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 671 IAHRLKTIERADQIILI----------------------------------------------DQGT-VLEQGTHQELMD 703
Cdd:PTZ00265 636 IAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMK 715
|
....*...
gi 59275972 704 RKGGYYKL 711
Cdd:PTZ00265 716 NKNGIYYT 723
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
481-691 |
3.93e-44 |
|
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: 157.63 E-value: 3.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMV 560
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEP--VLFSGSIKDNIAYGLADCSLERVQEAARRANAhsfisqLEKGYDTDVGERG-GQMSGGEKQRIAIARALIREPQ 637
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEA------LELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 638 VLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGT 691
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
235-707 |
6.92e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 171.07 E-value: 6.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNV-------LLRT--LIKIVGMLSLmmslsWKLTL 305
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMflgqifqLLSTfvLIGIVSTISL-----WAIMP 1061
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 306 LMLmetpvtgLLQGVYdNYYLRLTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTERSEAShYDHRLMDTH---TLKT 378
Cdd:PLN03130 1062 LLV-------LFYGAY-LYYQSTAREVKrlDSITRSPVYAqfGEALNGLSTIRAYKAYDRMAE-INGRSMDNNirfTLVN 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 379 ----RRDTVRAVYV--LLRRLTAlvmQVAMLYYGRLFIQRGQMST-GNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAA 451
Cdd:PLN03130 1133 mssnRWLAIRLETLggLMIWLTA---SFAVMQNGRAENQAAFASTmGLLLSYALNITSLLTAVLRLASLAENSLNAVERV 1209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 452 GKVFEYLDREPQVSTKGTLQPE-TLTGHVHFHNLSFSYptRQE-RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLER 529
Cdd:PLN03130 1210 GTYIDLPSEAPLVIENNRPPPGwPSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFR 1287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 530 FYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNI----AYGLADcslerVQEAARRANAHSFISQLEK 605
Cdd:PLN03130 1288 IVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdpfnEHNDAD-----LWESLERAHLKDVIRRNSL 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 606 GYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQ----EALTSCpsqTLLVIAHRLKTIERA 681
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQktirEEFKSC---TMLIIAHRLNTIIDC 1439
|
490 500
....*....|....*....|....*.
gi 59275972 682 DQIILIDQGTVLEQGTHQELMDRKGG 707
Cdd:PLN03130 1440 DRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
163-454 |
8.07e-44 |
|
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: 159.64 E-value: 8.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYD 322
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 323 NYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAM 402
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 403 LYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
449-704 |
1.01e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 165.08 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 449 GAAGKVFEY---LDREPQVSTKGTLQPETLTGH---VHFHNLSFSYPTR--QERKVLQGFSLELRPGQLTALVGPSGGGK 520
Cdd:COG1123 225 GPPEEILAApqaLAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRgkGGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 521 STCVSLLERFYQPQQGEILLDGQPLHSYQH---HYLHRKVAMVGQEPV--LFSG-SIKDNIAYGLADCSLERVQEAARRA 594
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLRLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 595 NAhsfisQLEK-GYDTDVGER-GGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLL 669
Cdd:COG1123 385 AE-----LLERvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElglTYL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 59275972 670 VIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG1123 460 FISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-646 |
1.36e-43 |
|
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: 153.96 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 576 AYGLADCSLERVQEAARRANAHSFISQLEKgYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTS 646
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDL-ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
481-699 |
2.02e-43 |
|
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: 156.19 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFY-----QPQQGEILLDGQPLHSYQHH--YL 553
Cdd:cd03260 3 LRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSGSIKDNIAYGL-------ADCSLERVQEAARRAnahsfisqlekGYDTDVGER--GGQMSGGEKQ 624
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklKEELDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQG-THQ 699
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAElKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGpTEQ 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
163-428 |
2.58e-43 |
|
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: 157.80 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGC--RGGLFMCAINSFTSRMKVEL 240
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSflQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGV 320
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 321 YDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQV 400
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*...
gi 59275972 401 AMLYYGRLFIQRGQMSTGNLVSFILYQS 428
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
166-454 |
2.81e-43 |
|
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: 158.03 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVID-ILASQYKWNDFLTAIILMGLYSLGSSFSAGcRGGLFMCAINSFTSRMKVELFGAL 244
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaALGGGDTASLNQIALLLLGLFLLQAVFSFF-RIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 245 VKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNY 324
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 325 YLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLY 404
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 59275972 405 YGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
479-695 |
2.09e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPT-RQERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHS------- 547
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSlserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 548 ----------YQHHYLHrkvamvgqePVLfsgSIKDNIAYGLAdcsLERVQEAARRANAHSFISQLekgydtDVGERG-- 615
Cdd:COG1136 82 rlrrrhigfvFQFFNLL---------PEL---TALENVALPLL---LAGVSRKERRERARELLERV------GLGDRLdh 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 616 --GQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSC---PSQTLLVIAHRLKTIERADQIILIDQG 690
Cdd:COG1136 141 rpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnreLGTTIVMVTHDPELAARADRVIRLRDG 220
|
....*
gi 59275972 691 TVLEQ 695
Cdd:COG1136 221 RIVSD 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
482-703 |
1.14e-40 |
|
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: 149.42 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVG 561
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVL-FSGSIKDNIAYG----------LADCSLERVQEAARRANAHSFIsqlEKGYDTdvgerggqMSGGEKQRIAIAR 630
Cdd:COG1120 82 QEPPApFGLTVRELVALGryphlglfgrPSAEDREAVEEALERTGLEHLA---DRPVDE--------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQE---ALTSCPSQTLLVIAH------RLktierADQIILIDQGTVLEQGTHQEL 701
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLEllrRLARERGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEV 225
|
..
gi 59275972 702 MD 703
Cdd:COG1120 226 LT 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
479-704 |
2.71e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.90 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyQHHYLHRKVA 558
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNI-----AYGL-ADCSLERVQEAARRANahsfisqLEKGYDTdvgeRGGQMSGGEKQRIAIARA 631
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLpRKEARERIDELLELFG-------LTDAADR----KVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEgkTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
479-704 |
3.45e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.83 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSYQHH--YL 553
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDLTDSKKDinKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSG-SIKDNIAYGLadcslERVQ-----EAARRANAhsfisQLEKgydtdVG--ERG----GQMSGG 621
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTLAP-----IKVKkmskaEAEERAME-----LLER-----VGlaDKAdaypAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 622 EKQRIAIARALIREPQVLILDEVTSALDTEsehMVQEALTSCPS-----QTLLVIAH-----RlktiERADQIILIDQGT 691
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVMRDlakegMTMVVVTHemgfaR----EVADRVVFMDGGR 213
|
250
....*....|...
gi 59275972 692 VLEQGTHQELMDR 704
Cdd:COG1126 214 IVEEGPPEEFFEN 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
479-660 |
5.01e-40 |
|
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: 146.46 E-value: 5.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQER-KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyqhhyLHRKV 557
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPVLFS-GSIKDNIAYGLadcSLERVQEAARRANAHSFISQlekgydtdVGERG------GQMSGGEKQRIAIAR 630
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL---ELQGVPKAEARERAEELLEL--------VGLSGfenaypHQLSGGMRQRVALAR 144
|
170 180 190
....*....|....*....|....*....|
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEAL 660
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
483-704 |
1.05e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.05 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERkvlqgFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQ---PLHSYQhhylhRKVAM 559
Cdd:COG3840 6 DLTYRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltALPPAE-----RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVLFSG-SIKDNIAYGL-ADCSL-----ERVQEAARRANAHSFISQLEkgydtdvgergGQMSGGEKQRIAIARAL 632
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGLrPGLKLtaeqrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 633 IREPQVLILDEVTSALD----TESEHMVQEAltsCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDEL---CRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
481-696 |
1.35e-39 |
|
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: 145.73 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRQ-ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---QHHYLHRK 556
Cdd:cd03257 4 VKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQE------PVLfsgSIKDNIAYGLADCSLERVQEAARRAnahsfISQLEKG---YDTDVGERGGQMSGGEKQRIA 627
Cdd:cd03257 84 IQMVFQDpmsslnPRM---TIGEQIAEPLRIHGKLSKKEARKEA-----VLLLLVGvglPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-704 |
2.91e-39 |
|
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: 145.33 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQERK-VLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSYQHHYLHRKV 557
Cdd:COG1124 5 RNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPvlfSGS------IKDNIAYGLADCSLERVQEAARRAnahsfisqLEK-GYDTDVGER-GGQMSGGEKQRIAIA 629
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAEPLRIHGLPDREERIAEL--------LEQvGLPPSFLDRyPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 630 RALIREPQVLILDEVTSALDTesehMVQ-------EALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:COG1124 151 RALILEPELLLLDEPTSALDV----SVQaeilnllKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
...
gi 59275972 702 MDR 704
Cdd:COG1124 227 LAG 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
480-691 |
5.56e-39 |
|
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: 141.23 E-value: 5.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAM 559
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQepvlfsgsikdniaygladcslervqeaarranahsfisqlekgydtdvgerggqMSGGEKQRIAIARALIREPQVL 639
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 640 ILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERA-DQIILIDQGT 691
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEgrTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
479-696 |
6.35e-39 |
|
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: 143.04 E-value: 6.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVA 558
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYGLAdcsLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQ 637
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLK---LRGVPKAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 638 VLILDEVTSALDTES----EHMVQEALTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQG 696
Cdd:cd03259 151 LLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
478-649 |
6.68e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.85 E-value: 6.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 478 HVHFHNLSFSYPTRQ-ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyqhhyLHRK 556
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFs-gSIKDNIAYGLadcSLERVQEAARRANAHSFISQlekgydtdVGERG------GQMSGGEKQRIAIA 629
Cdd:COG1116 82 RGVVFQEPALLpwlTVLDNVALGL---ELRGVPKAERRERARELLEL--------VGLAGfedaypHQLSGGMRQRVAIA 150
|
170 180
....*....|....*....|
gi 59275972 630 RALIREPQVLILDEVTSALD 649
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
476-697 |
3.88e-38 |
|
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: 141.01 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 476 TGHVHFHNLSFSYPTRQErKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHR 555
Cdd:cd03369 4 HGEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSGSIKDNI-AYGlaDCSLERVQEAARranahsfisqlekgydtdVGERGGQMSGGEKQRIAIARALIR 634
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD--EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGT 697
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIrEEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
483-692 |
8.14e-38 |
|
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: 140.32 E-value: 8.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQER-KVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSY----QHHYLH 554
Cdd:cd03255 5 NLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekeLAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQEPVLFSG-SIKDNIAYGLadcSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALI 633
Cdd:cd03255 82 RHIGFVFQSFNLLPDlTALENVELPL---LLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTV 692
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEagtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
479-704 |
1.85e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 143.31 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS---YQhhylhR 555
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEK-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSG-SIKDNIAYGLadcSLERVQEAARRANAHSFIS--QLEkgydtDVGERG-GQMSGGEKQRIAIARA 631
Cdd:COG3842 78 NVGMVFQDYALFPHlTVAENVAFGL---RMRGVPKAEIRARVAELLElvGLE-----GLADRYpHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 632 LIREPQVLILDEVTSALDTES-EHMVQEaltscpsqtllviahrLKTIER-------------------ADQIILIDQGT 691
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLrEEMREE----------------LRRLQRelgitfiyvthdqeealalADRIAVMNDGR 213
|
250
....*....|...
gi 59275972 692 VLEQGTHQELMDR 704
Cdd:COG3842 214 IEQVGTPEEIYER 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
479-691 |
3.10e-37 |
|
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: 137.99 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQER--KVLQGFSLELRPGQLTALVGPSGGGKST-CVSLLerfyqpqqGEI-LLDGqplhsyqHHYLH 554
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSlLSALL--------GELeKLSG-------SVSVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQEPVLFSGSIKDNIAYG-----------LADCSLERVqeaarranahsfISQLEKGYDTDVGERGGQMSGGEK 623
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGkpfdeeryekvIKACALEPD------------LEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 624 QRIAIARALIREPQVLILDEVTSALDTE-SEHMVQEALtsCP----SQTLLVIAHRLKTIERADQIILIDQGT 691
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCI--LGlllnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
479-701 |
7.16e-37 |
|
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: 138.10 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYP-TRQERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSYQHHYL- 553
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 --HRKVAMVGQEPVLFSG-SIKDNIAYGLADCSLERvQEAARRAN-----------AHSFISQLekgydtdvgerggqmS 619
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPK-AEIEERVLellelvgledkADAYPAQL---------------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQ 695
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElglTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*.
gi 59275972 696 GTHQEL 701
Cdd:cd03258 223 GTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-704 |
8.96e-37 |
|
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: 145.05 E-value: 8.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERFYQPQQGEILLDGQPLHSYQHHYLHR 555
Cdd:COG1123 5 LEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTlalALMGLLPHGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEP--VLFSGSIKDNIAYGLADCSLERvQEAARRAnahsfISQLEK-GYDTDVGERGGQMSGGEKQRIAIARAL 632
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSR-AEARARV-----LELLEAvGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 633 IREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
479-692 |
1.48e-36 |
|
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: 136.51 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPL--HSYQHHYL 553
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSG-SIKDNIAYGLADCSLERVQEAARRANAHsfisqLEK-GYDTDVGERGGQMSGGEKQRIAIARA 631
Cdd:cd03262 75 RQKVGMVFQQFNLFPHlTVLENITLAPIKVKGMSKAEAEERALEL-----LEKvGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 632 LIREPQVLILDEVTSALDTEsehMVQEALTSCPS-----QTLLVIAHRLKTI-ERADQIILIDQGTV 692
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeegMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
166-451 |
1.03e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 136.46 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRgglfmcaiNSFTSRM--KV----- 238
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR--------FYLVSWLgeRVvadlr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 239 -ELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLL 317
Cdd:cd18575 73 kAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 318 QGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVyvllrrLTALV 397
Cdd:cd18575 153 IILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARAL------LTALV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 398 MQ------VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAA 451
Cdd:cd18575 227 IFlvfgaiVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
483-703 |
1.91e-35 |
|
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: 134.17 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLH---RKVAM 559
Cdd:cd03261 5 GLTKSF---GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVLFSG-SIKDNIAYGL---ADCSLERVQEAARranahsfiSQLEKgydtdVGERG------GQMSGGEKQRIAIA 629
Cdd:cd03261 82 LFQSGALFDSlTVFENVAFPLrehTRLSEEEIREIVL--------EKLEA-----VGLRGaedlypAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
482-696 |
2.62e-35 |
|
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: 131.79 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVG 561
Cdd:cd03214 3 ENLSVGYG---GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QepvlfsgsikdniaygladcSLERVQeaarranahsfISQL-EKGYDTdvgerggqMSGGEKQRIAIARALIREPQVLI 640
Cdd:cd03214 80 Q--------------------ALELLG-----------LAHLaDRPFNE--------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 641 LDEVTSALDTESEHMVQEAL-TSCPSQTLLVIA--HRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLrRLARERGKTVVMvlHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
479-701 |
3.18e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEP-VLFSGS-IKDNIAYGLADCS------LERVQEAARRANAHSFISQlekgydtdvgeRGGQMSGGEKQRIAIAR 630
Cdd:PRK13635 85 MVFQNPdNQFVGAtVQDDVAFGLENIGvpreemVERVDQALRQVGMEDFLNR-----------EPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
483-702 |
1.24e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 132.94 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPtRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG-QPLHSYQHHYLHRKVAMVG 561
Cdd:TIGR04520 5 NVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEP--VLFSGSIKDNIAYGLADCSL------ERVQEAARRANAHSFI----SQLekgydtdvgerggqmSGGEKQRIAIA 629
Cdd:TIGR04520 84 QNPdnQFVGATVEDDVAFGLENLGVpreemrKRVDEALKLVGMEDFRdrepHLL---------------SGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
479-691 |
1.79e-34 |
|
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: 129.61 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPL--HSYQHHYLHRK 556
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSG-SIKDNIAYGLadcslervqeaarranahsfisqlekgydtdvgerggqmSGGEKQRIAIARALIRE 635
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 636 PQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGT 691
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
479-703 |
1.99e-34 |
|
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: 131.26 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---QHHYLHR 555
Cdd:COG1127 6 IEVRNLTKSF---GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSG-SIKDNIAYGL---ADCSLERVQEAARRAnahsfisqLEKgydtdVGERG------GQMSGGEKQR 625
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLrehTDLSEAEIRELVLEK--------LEL-----VGLPGaadkmpSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 626 IAIARALIREPQVLILDEVTSALDTESEHMV-------QEALTScpsqTLLVIAHRLKTIER-ADQIILIDQGTVLEQGT 697
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDELGL----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
....*.
gi 59275972 698 HQELMD 703
Cdd:COG1127 226 PEELLA 231
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
163-451 |
2.64e-34 |
|
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: 132.55 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWND-FLTAIILMGLYSLGSSFSAGcrGGLFMCAI-NSFTSRMKVEL 240
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEAlLLVPLAIIGLFLLRGLASYL--QTYLMAYVgQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGV 320
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 321 YDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYV-LLRRLTALVMq 399
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSpLMELLGAIAI- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 400 VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAA 451
Cdd:cd18552 238 ALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAA 289
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
163-454 |
1.01e-33 |
|
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: 131.01 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYD 322
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 323 NYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYD---HRLMDThTLKTRRdtVRAVYVLLRRLTALVMQ 399
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDkenEEYRDL-NIKLAK--LLAKYWPLMDFLSGLQI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 400 VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18542 238 VLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
479-703 |
2.00e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH------SY--QH 550
Cdd:COG1121 7 IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrriGYvpQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 551 HYLHRK--------VAM--VGQEPVLFSGSIKDniaYGLADCSLERV--QEAARRAnahsfISQLekgydtdvgerggqm 618
Cdd:COG1121 84 AEVDWDfpitvrdvVLMgrYGRRGLFRRPSRAD---REAVDEALERVglEDLADRP-----IGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 619 SGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDqGTVLEQ 695
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgkTILVVTHDLGAVREyFDRVLLLN-RGLVAH 219
|
....*...
gi 59275972 696 GTHQELMD 703
Cdd:COG1121 220 GPPEEVLT 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
482-704 |
2.54e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSyQHHYLHRKVA 558
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYGLadcsleRVQ---EAARRANAHSFIS--QLEkgydtDVGER-GGQMSGGEKQRIAIARA 631
Cdd:COG1118 79 FVFQHYALFPHmTVAENIAFGL------RVRppsKAEIRARVEELLElvQLE-----GLADRyPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 632 LIREPQVLILDEVTSALDT----ESEHMVQEALTSCPSQTLLVI-----AHRLktierADQIILIDQGTVLEQGTHQELM 702
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEVY 222
|
..
gi 59275972 703 DR 704
Cdd:COG1118 223 DR 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
482-702 |
1.05e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.20 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSyptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVG 561
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVL-FSGSIKDNIAYGLADCSLE--RVQEAARRAnahsfisqLEKgydTDVGERGG----QMSGGEKQRIAIARALIR 634
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAPHGLSraEDDALVAAA--------LAQ---VDLAHLAGrdypQLSGGEQQRVQLARVLAQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 635 ------EPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErglAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
483-692 |
1.11e-32 |
|
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: 124.05 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLhRKVAMVGQ 562
Cdd:cd03230 5 NLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EPVLFSG-SIKDNIAYgladcslervqeaarranahsfisqlekgydtdvgerggqmSGGEKQRIAIARALIREPQVLIL 641
Cdd:cd03230 81 EPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 59275972 642 DEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEgkTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
478-697 |
1.12e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.43 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 478 HVHFHNLSFSYPTR-QERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSYQHHYL 553
Cdd:COG1135 1 MIELENLSKTFPTKgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 H---RKVAMVGQEPVLFSG-SIKDNIAYGLadcSLERV--QEAARRAN-----------AHSFISQLekgydtdvgergg 616
Cdd:COG1135 78 RaarRKIGMIFQHFNLLSSrTVAENVALPL---EIAGVpkAEIRKRVAellelvglsdkADAYPSQL------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 617 qmSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:COG1135 142 --SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 59275972 693 LEQGT 697
Cdd:COG1135 220 VEQGP 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
483-649 |
5.23e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.15 E-value: 5.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFY--QPQQ---GEILLDGQPLhsYQHHY----L 553
Cdd:COG1117 16 NLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDI--YDPDVdvveL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSGSIKDNIAYGL----------ADcslERVQEAARRANahsfisqLekgYDtDVGER----GGQMS 619
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikskseLD---EIVEESLRKAA-------L---WD-EVKDRlkksALGLS 156
|
170 180 190
....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
481-705 |
6.59e-32 |
|
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: 124.22 E-value: 6.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLH---RKV 557
Cdd:cd03256 3 VENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPVLFSG-SIKDNIAYG-LADCSLERV------QEAARRAnahsfISQLEK-GYDTDVGERGGQMSGGEKQRIAI 628
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGrLGRRSTWRSlfglfpKEEKQRA-----LAALERvGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIA--HRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVslHQVDLAREyADRIVGLKDGRIVFDGPPAELTDE 235
|
.
gi 59275972 705 K 705
Cdd:cd03256 236 V 236
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
475-709 |
6.61e-32 |
|
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: 124.64 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 475 LTGHVHFHNLSFSYPTRQeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLH 554
Cdd:cd03288 16 LGGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIR 634
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQE-ALTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYY 709
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKvVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
479-702 |
8.82e-32 |
|
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: 123.95 E-value: 8.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRqeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYGLadcSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQ 637
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVP---KLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 638 VLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRL-KTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
479-704 |
1.63e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQP---LHSYQhhy 552
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLED---PTSGEILIGGRDvtdLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 lhRKVAMVGQEPVLF-SGSIKDNIAYGL---------ADcslERVQEAARRANahsfISQLEKgydtdvgERGGQMSGGE 622
Cdd:COG3839 75 --RNIAMVFQSYALYpHMTVYENIAFPLklrkvpkaeID---RRVREAAELLG----LEDLLD-------RKPKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 623 KQRIAIARALIREPQVLILDEVTSALDTES-EHMVQEaltscpsqtllvIA---HRLKT---------IER---ADQIIL 686
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE------------IKrlhRRLGTttiyvthdqVEAmtlADRIAV 206
|
250
....*....|....*...
gi 59275972 687 IDQGTVLEQGTHQELMDR 704
Cdd:COG3839 207 MNDGRIQQVGTPEELYDR 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
480-690 |
1.80e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 122.26 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsyqhhYLHRKVAM 559
Cdd:cd03235 1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVL---FSGSIKDNIAYGL-ADCSLERVQEAARRANAHSfisQLEKGYDTDVGERG-GQMSGGEKQRIAIARALIR 634
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAKVDE---ALERVGLSELADRQiGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQG 690
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREgmTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
500-696 |
3.44e-31 |
|
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: 121.06 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 500 FSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVAMVGQEPVLFSG-SIKDNIAYG 578
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 579 LADcSL---ERVQEAARRANAHSFISQLEKgydtdvgERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEH- 654
Cdd:cd03298 95 LSP-GLkltAEDRQAIEVALARVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAe 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 59275972 655 MVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03298 167 MLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
153-464 |
3.63e-31 |
|
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: 124.49 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 153 LYFYRPDTLLLVGAFIFlslAVLCEMFIPFY---TGKVIDILASQ---------YKWndfltAIILMGLySLGSSFSAGC 220
Cdd:cd18578 1 LKLNKPEWPLLLLGLIG---AIIAGAVFPVFailFSKLISVFSLPdddelrseaNFW-----ALMFLVL-AIVAGIAYFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 221 RGGLFMCAINSFTSRMKVELFGALVKQEISFF--ETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMS 298
Cdd:cd18578 72 QGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 299 LSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKT 378
Cdd:cd18578 152 YGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 379 RRDTVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNL--VSFILYQSnlGTNIRTLIYIFGDMLNSVGAAGKVFE 456
Cdd:cd18578 232 RRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFfiVFMALIFG--AQSAGQAFSFAPDIAKAKAAAARIFR 309
|
....*...
gi 59275972 457 YLDREPQV 464
Cdd:cd18578 310 LLDRKPEI 317
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
479-652 |
4.17e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHH---YLHR 555
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQE-PVLFSGSIKDNIAYGLadcsleRVQ-----EAARRAN-----------AHSFISQLekgydtdvgerggqm 618
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPL------RVTgksrkEIRRRVRevldlvglsdkAKALPHEL--------------- 138
|
170 180 190
....*....|....*....|....*....|....
gi 59275972 619 SGGEKQRIAIARALIREPQVLILDEVTSALDTES 652
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
500-703 |
9.44e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.46 E-value: 9.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 500 FSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPlhsyqHHYL---HRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTppsRRPVSMLFQENNLFSHlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGLaDCSL-------ERVQEAARRANAHSFISQLEkgydtdvgergGQMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:PRK10771 93 GLGL-NPGLklnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 649 DTESEH-MVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK10771 161 DPALRQeMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
495-702 |
1.02e-30 |
|
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: 120.62 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYL-HRKVAMVGQEPVLFSG-SIK 572
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYGL-------ADCSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVT 645
Cdd:cd03219 94 ENVMVAAqartgsgLLLARARREEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 646 SAL-DTESEHMVqEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:cd03219 172 AGLnPEETEELA-ELIRELRERgiTVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
494-704 |
1.07e-30 |
|
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: 124.06 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSL----ELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPL-HSYQHHYL---HRKVAMVGQ 562
Cdd:COG4148 8 RLRRGGFTLdvdfTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEVLqDSARGIFLpphRRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EPVLFSG-SIKDNIAYGLAdcsleRVQEAARRANAHSFISQLEKGydtDVGERG-GQMSGGEKQRIAIARALIREPQVLI 640
Cdd:COG4148 85 EARLFPHlSVRGNLLYGRK-----RAPRAERRISFDEVVELLGIG---HLLDRRpATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 641 LDEVTSALDTES--------EHMVQEAltSCPsqtLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG4148 157 MDEPLAALDLARkaeilpylERLRDEL--DIP---ILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
481-705 |
2.10e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.87 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMV 560
Cdd:PRK13632 10 VENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEP-VLFSGS-IKDNIAYGLADCSLER------VQEAARRANAHSFISQlEKGYdtdvgerggqMSGGEKQRIAIARAL 632
Cdd:PRK13632 89 FQNPdNQFIGAtVEDDIAFGLENKKVPPkkmkdiIDDLAKKVGMEDYLDK-EPQN----------LSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 633 IREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
496-704 |
5.61e-30 |
|
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: 118.49 E-value: 5.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVAMVGQEPVLFSG-SIKDN 574
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 575 IAYGLadcSLERVQEAARRANAHSFISQLE-KGYDtdvGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTE-S 652
Cdd:cd03300 93 IAFGL---RLKKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 653 EHMvQEALTSCPSQ---TLLVIAH-RLKTIERADQIILIDQGTVLEQGTHQELMDR 704
Cdd:cd03300 167 KDM-QLELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
185-422 |
1.09e-29 |
|
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: 119.50 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 185 GKVIDILASQYKWN----DFL-----TAIILMGLySLGSSFSAGCRGGLFMCAINSFTSRMKVELFGALVKQEISFFETI 255
Cdd:cd18577 23 GDLFDAFTDFGSGEsspdEFLddvnkYALYFVYL-GIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 256 KTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDS 335
Cdd:cd18577 102 GAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 336 MARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQM 415
Cdd:cd18577 182 YAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEI 261
|
....*..
gi 59275972 416 STGNLVS 422
Cdd:cd18577 262 SPGDVLT 268
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
494-696 |
2.60e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.86 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELR---PGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPL-HSYQHHYL---HRKVAMVGQE 563
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLfDSRKKINLppqQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 PVLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDtdvgergGQMSGGEKQRIAIARALIREPQVLILD 642
Cdd:cd03297 84 YALFPHlNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 643 EVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlniPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
478-670 |
3.28e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 478 HVHFHNLSFSYP-TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS--------Y 548
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadrgvvF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 549 QHHYLHrkvamvgqePVLfsgSIKDNIAYGLadcSLERVQEAARRANAHSFISQLekGYDtDVGERG-GQMSGGEKQRIA 627
Cdd:COG4525 83 QKDALL---------PWL---NVLDNVAFGL---RLRGVPKAERRARAEELLALV--GLA-DFARRRiWQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 59275972 628 IARALIREPQVLILDEVTSALDtesehmvqeALTSCPSQTLLV 670
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD---------ALTREQMQELLL 178
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
495-697 |
4.76e-29 |
|
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: 116.29 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylhrKVAMVG-----QEPVLFSG 569
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 -SIKDNIA------------YGLADCSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:COG0411 94 lTVLENVLvaaharlgrgllAALLRLPRARREEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 637 QVLILDEVTSAL-DTESEHMVQ--EALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGT 697
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELAEliRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
163-454 |
7.79e-29 |
|
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: 116.76 E-value: 7.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQykwNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLL----- 317
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIilplg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 318 QGVYdnyylRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALV 397
Cdd:cd18551 158 RRIR-----KASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 398 MQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
497-703 |
7.97e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 115.51 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQplHSYQHHYLHRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGL-ADCSLERVQEAARRANAHSFIS--QLEKGYDtdvgERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTEs 652
Cdd:cd03296 96 AFGLrVKPRSERPPEAEIRAKVHELLKlvQLDWLAD----RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 653 ehmVQEALTSCPSQ--------TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMD 703
Cdd:cd03296 171 ---VRKELRRWLRRlhdelhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
494-705 |
8.13e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 118.29 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELR---PGQ-LTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHYL---HRKVAMVGQEPV 565
Cdd:TIGR02142 6 SKRLGDFSLDADftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLppeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 LFSG-SIKDNIAYGLADCsleRVQEaaRRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEV 644
Cdd:TIGR02142 86 LFPHlSVRGNLRYGMKRA---RPSE--RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 645 TSALDTESEHMVQEALTSCPSQT---LLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
479-702 |
5.04e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:PRK11231 3 LRTENLTVGY---GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYG----------LADCSLERVQEAARRANahsfISQLEKGYDTDvgerggqMSGGEKQRIA 627
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 628 IARALIREPQVLILDEVTSALD----TESEHMVQEALTScpSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRELNTQ--GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
479-704 |
5.94e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLErfyQPQQGEILLDGQPLH--SYQHHYL 553
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDGLKVNdpKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSG-SIKDNIAYGLAdcsleRVQeAARRANAHSFISQLEkgydTDVG--ERGG----QMSGGEKQRI 626
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPL-----RVR-GASKEEAEKQARELL----AKVGlaERAHhypsELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 627 AIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
.
gi 59275972 704 R 704
Cdd:PRK09493 226 N 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
482-692 |
6.99e-28 |
|
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: 111.58 E-value: 6.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQhhyLHRKVAMVG 561
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEP--VLFSGSIKDNIAYGL--ADCSLERVQEAARRANahsfISQLEKGYDTDvgerggqMSGGEKQRIAIARALIREPQ 637
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLD----LYALKERHPLS-------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 638 VLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQgkAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
479-686 |
8.60e-28 |
|
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: 111.42 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSyptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTcvsLLeR----FYQPQQGEILLDGQPLHSYQHHYlH 554
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTT---LL-RilagLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQEPVLFSG-SIKDNIA-----YGLAdCSLERVQEAARRANahsfisqLEKGYDTDVGerggQMSGGEKQRIAI 628
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVG-------LAGLADLPVR----QLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTS-CPSQTLLVIA-HRLKTIERADQIIL 686
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
493-685 |
1.46e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.34 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIK 572
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYGLaDCSLERVQEAARRANAHSF---ISQLEKGYDtdvgerggQMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:PRK10247 99 DNLIFPW-QIRNQQPDPAIFLDDLERFalpDTILTKNIA--------ELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 59275972 650 TESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQII 685
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREqniAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
163-426 |
1.55e-27 |
|
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: 113.28 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQykwNDFLTAIILMGLYSLGSSF-SAGCRGGLFMCAINsfTSR-----M 236
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAG---TLTASQLLRYALLILLLALlIGIFRFLWRYLIFG--ASRrieydL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 237 KVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGL 316
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 317 LQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRlmdthTLKTRRDTVRAVYV--LLRRLT 394
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKL-----NEEYVEKNLRLARVdaLFFPLI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 59275972 395 ALVMQVAM---LYYGRLFIQRGQMSTGNLVSFILY 426
Cdd:cd18541 231 GLLIGLSFlivLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-697 |
1.81e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.09 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPT------RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---QH 550
Cdd:PRK10419 5 NVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 551 HYLHRKVAMVGQEP---VLFSGSIKDNIAYGLAdcSLERVQEAARRANAHSFISQLEKGyDTDVGERGGQMSGGEKQRIA 627
Cdd:PRK10419 85 KAFRRDIQMVFQDSisaVNPRKTVREIIREPLR--HLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQT---LLVIAHRLKTIER-ADQIILIDQGTVLEQGT 697
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVETQP 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
482-704 |
2.09e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVG 561
Cdd:PRK13650 8 KNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEP-VLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQlekgydTDVGERG-GQMSGGEKQRIAIARALIREPQV 638
Cdd:PRK13650 88 QNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALELVGM------QDFKEREpARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 639 LILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDR 704
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
163-426 |
3.34e-27 |
|
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: 112.10 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVID--ILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVEL 240
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGV 320
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 321 YDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHtLKTRRDTVRaVYVLLRRLTALVMQV 400
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFD-EINQEY-RKANLKSIK-LFALFRPLVELLSSL 237
|
250 260
....*....|....*....|....*....
gi 59275972 401 AM---LYYGRLFIQRGQMSTGNLVSFILY 426
Cdd:cd18544 238 ALalvLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
483-704 |
3.79e-27 |
|
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: 116.32 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQ--------ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFyQPQQGEILLDGQPLHSYQHHYLH 554
Cdd:COG4172 280 DLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 ---RKVAMVGQEPvlFSG-----SIKDNIAYGLadcsleRVQE-----AARRANAhsfISQLEK-GYDTDVGER-GGQMS 619
Cdd:COG4172 359 plrRRMQVVFQDP--FGSlsprmTVGQIIAEGL------RVHGpglsaAERRARV---AEALEEvGLDPAARHRyPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALDtesehM-VQealtscpSQ--------------TLLVIAHRLKTIER-ADQ 683
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALD-----VsVQ-------AQildllrdlqrehglAYLFISHDLAVVRAlAHR 495
|
250 260
....*....|....*....|.
gi 59275972 684 IILIDQGTVLEQGTHQELMDR 704
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
483-705 |
3.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:PRK13647 9 DLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EP--VLFSGSIKDNIAYGLADCSL------ERVQEAARRANAHSFISQLEKgydtdvgerggQMSGGEKQRIAIARALIR 634
Cdd:PRK13647 87 DPddQVFSSTVWDDVAFGPVNMGLdkdeveRRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLK-TIERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgkTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
477-691 |
3.99e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.45 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSypTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplhsyqhhylHRK 556
Cdd:COG4178 361 GALALEDLTLR--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSGSIKDNIAYGLADC--SLERVQEAARRANAHSFISQLekgydtDVGERGGQ-MSGGEKQRIAIARALI 633
Cdd:COG4178 428 VLFLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERL------DEEADWDQvLSLGEQQRLAFARLLL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEAL-TSCPSQTLLVIAHRLKTIERADQIILIDQGT 691
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-701 |
4.59e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.96 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQ--------ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYqPQQGEILLDGQPLHSY---QHH 551
Cdd:PRK15134 280 QLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLnrrQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 552 YLHRKVAMVGQEPvlFSG-----SIKDNIAYGLadcsleRVQE----AARRANAhsFISQLEK-GYDTDVGER-GGQMSG 620
Cdd:PRK15134 359 PVRHRIQVVFQDP--NSSlnprlNVLQIIEEGL------RVHQptlsAAQREQQ--VIAVMEEvGLDPETRHRyPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIeRA--DQIILIDQGTVLEQ 695
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlAYLFISHDLHVV-RAlcHQVIVLRQGEVVEQ 507
|
....*.
gi 59275972 696 GTHQEL 701
Cdd:PRK15134 508 GDCERV 513
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-680 |
5.34e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.90 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQpQQGEILLDGQPLHSYQHHY------ 552
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 --LHRKVAMVGQEPVLFSGSIKDNIAYGLA------DCSLERVQEAARRAnahsfiSQLEKGYDTDVGERGGQMSGGEKQ 624
Cdd:PRK14258 84 nrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTES----EHMVQeALTSCPSQTLLVIAHRLKTIER 680
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQ-SLRLRSELTMVIVSHNLHQVSR 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
495-698 |
7.19e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH--SYqHHYLHRKVAMVGQEPVLFSG-SI 571
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrSP-RDAQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 KDNIAYGLADCSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSAL-DT 650
Cdd:COG1129 97 AENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLtER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 59275972 651 ESEHM--VQEALTscpSQ--TLLVIAHRLKTIER-ADQIilidqgTVLEQGTH 698
Cdd:COG1129 175 EVERLfrIIRRLK---AQgvAIIYISHRLDEVFEiADRV------TVLRDGRL 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
479-703 |
9.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVA 558
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPV-LFSGSI-KDNIAYGLADcslervqEAARRANAHSFISQLEKgyDTDVGERGG----QMSGGEKQRIAIARAL 632
Cdd:PRK13648 87 IVFQNPDnQFVGSIvKYDVAFGLEN-------HAVPYDEMHRRVSEALK--QVDMLERADyepnALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 633 IREPQVLILDEVTSALDTESE----HMVQEaLTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARqnllDLVRK-VKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
496-701 |
1.28e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.45 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKST---CVSLLErfyQP-----QQGEILLDG-QPLHSYQH--HYLHRKVAMVGQEP 564
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLE---QPeagtiRVGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 565 VLFSG-SIKDNIAYGLADCSLERVQEAARRAN---AHSFISQLEKGYDTdvgerggQMSGGEKQRIAIARALIREPQVLI 640
Cdd:PRK11264 95 NLFPHrTVLENIIEGPVIVKGEPKEEATARARellAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 641 LDEVTSALDTEsehMVQEALTSCPS-----QTLLVIAHRLK-TIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK11264 168 FDEPTSALDPE---LVGEVLNTIRQlaqekRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-426 |
1.44e-26 |
|
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: 110.32 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLT--AIILMGLYSLGSSFSAGcRGGLFMCAINSFTSRMKVEL 240
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLglALLLLGAYLLRALLNFL-RIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGV 320
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 321 YDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHydhrlMDTHTLKTRRDTVRAVYV------LLRRLT 394
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKR-----FEALSRRYRKAQLRAMKLwaifhpLMEFLT 234
|
250 260 270
....*....|....*....|....*....|..
gi 59275972 395 ALVMqVAMLYYGRLFIQRGQMSTGNLVSFILY 426
Cdd:cd18778 235 SLGT-VLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
476-715 |
1.77e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 476 TGHVHFHnlsfsYPTRQErkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLhSYQHH---Y 552
Cdd:PRK13636 8 VEELNYN-----YSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQEP--VLFSGSIKDNIAYGLADCSL--ERVQEAARRANAHSFISQLeKGYDTDVgerggqMSGGEKQRIAI 628
Cdd:PRK13636 80 LRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHL-KDKPTHC------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIE-RADQIILIDQGTVLEQGTHQELMDR 704
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
250
....*....|.
gi 59275972 705 KGGYYKLRERL 715
Cdd:PRK13636 233 KEMLRKVNLRL 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
501-702 |
2.07e-26 |
|
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: 109.27 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 501 SLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYL----HRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGLadcSLERVQEAARRANAhsfISQLEKgydtdVGERG------GQMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:cd03294 124 AFGL---EVQGVPRAEREERA---AEALEL-----VGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 650 TESEHMVQEALTSCPSQ---TLLVIAHRL-KTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:cd03294 193 PLIRREMQDELLRLQAElqkTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
481-697 |
2.72e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 110.66 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRQERKV-LQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLHSYQHHYL--- 553
Cdd:PRK11153 4 LKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSG-SIKDNIAYGL--ADCS-----------LERVQEAARranAHSFISQLekgydtdvgerggqmS 619
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSrTVFDNVALPLelAGTPkaeikarvtelLELVGLSDK---ADRYPAQL---------------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQ 695
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
..
gi 59275972 696 GT 697
Cdd:PRK11153 223 GT 224
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
180-454 |
4.04e-26 |
|
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: 109.17 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 180 IPFYTGKVIDILASQYKWN--DFLTAII-----LMGLYSLGSSFSAGCRGGLFMCAINsFTSRMKVELFGALVKQEISFF 252
Cdd:cd18574 15 IPLLLGDLVNVISRSLKETngDFIEDLKkpalkLLGLYLLQSLLTFAYISLLSVVGER-VAARLRNDLFSSLLRQDIAFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 253 ETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVG-MLSLMMsLSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKE 331
Cdd:cd18574 94 DTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGcVVSLYL-ISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 332 VQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhrlmdthtLKTRRDTVRAVYV-----LLRRLTALV---MQVAML 403
Cdd:cd18574 173 AQAQVAKATGVADEALGNIRTVRAFAMEDRELELYE--------EEVEKAAKLNEKLglgigIFQGLSNLAlngIVLGVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 404 YYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18574 245 YYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
496-703 |
4.09e-26 |
|
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: 107.13 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG-SIKD 573
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 574 NI---AYGLADC----SLERVQE-----AARRANahsfisqlekgydtdvgeRGGQMSGGEKQRIAIARALIREPQVLIL 641
Cdd:cd03224 95 NLllgAYARRRAkrkaRLERVYElfprlKERRKQ------------------LAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 642 DEVTSALdteSEHMVQE---ALTSCPSQ--TLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELMD 703
Cdd:cd03224 157 DEPSEGL---APKIVEEifeAIRELRDEgvTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-717 |
4.12e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQ--PQ---QGEILLDGQPLHSYQHHYLHRKVAMVGQEP-VLFS 568
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIAYGLADCSL--------ERVQEAARRAnahsfisQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLI 640
Cdd:PRK14247 97 LSIFENVALGLKLNRLvkskkelqERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 641 LDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRKggYYKLRERLFT 717
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDmTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTNP--RHELTEKYVT 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
479-696 |
4.45e-26 |
|
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: 106.10 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSF---SYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL--ERFYQPQQGEILLDGQPLHSYQhhyL 553
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSgsikdniaygladcSLErVQEAARranahsFISQLekgydtdvgeRGgqMSGGEKQRIAIARALI 633
Cdd:cd03213 81 RKIIGYVPQDDILHP--------------TLT-VRETLM------FAAKL----------RG--LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKT--IERADQIILIDQGTVLEQG 696
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgrTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
163-454 |
4.60e-26 |
|
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: 109.03 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYK------WNDFLTAIILM-GLYSLGSSFSAGCrgGLFM-CAINSFTS 234
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLlGLYLLSALFSYLQ--NRLMaRVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVT 314
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFN-TERSEAShydhrlMDTHTLKTRRDTVRAVYV----- 388
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNrEEEAIEE------FDEINEELYKASFKAQFYsgllm 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 389 -LLRRLTALvMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18547 233 pIMNFINNL-GYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
479-649 |
6.23e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVA 558
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYGL------ADCSLERVQEAARranahsfISQLEkgydtDVGERG-GQMSGGEKQRIAIAR 630
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLrmqktpAAEITPRVMEALR-------MVQLE-----EFAQRKpHQLSGGQQQRVAIAR 157
|
170
....*....|....*....
gi 59275972 631 ALIREPQVLILDEVTSALD 649
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
483-649 |
1.11e-25 |
|
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: 108.22 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQER-KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ---QGEILLDGQPLHSYQH----HYLH 554
Cdd:COG0444 6 NLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEkelrKIRG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQE------PVLfsgSIKDNIAYGLAdcSLERVQEAARRANAhsfISQLEKgydtdVG-----ERGG----QMS 619
Cdd:COG0444 86 REIQMIFQDpmtslnPVM---TVGDQIAEPLR--IHGGLSKAEARERA---IELLER-----VGlpdpeRRLDryphELS 152
|
170 180 190
....*....|....*....|....*....|
gi 59275972 620 GGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-707 |
1.15e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.97 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRkVA 558
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQ----EPVLfsgSIKDNIA-----YGLAdcslerVQEAARRANAHSFISQLEKGYDTDVGErggqMSGGEKQRIAIA 629
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLS------AAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPS--QTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRKG 706
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESEI 230
|
.
gi 59275972 707 G 707
Cdd:PRK13537 231 G 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
483-713 |
1.27e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.68 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLerfyqpqQGEIlldgqPLHSYQHHYLHRKVAMVGQ 562
Cdd:PLN03130 619 NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-------LGEL-----PPRSDASVVIRGTVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EPVLFSGSIKDNIAYGlADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILD 642
Cdd:PLN03130 687 VSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 643 EVTSALDTeseHMVQEALTSC-----PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKLRE 713
Cdd:PLN03130 766 DPLSALDA---HVGRQVFDKCikdelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
479-695 |
1.75e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 106.43 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPT------RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---Q 549
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 550 HHYLHRKVAMVGQE---PVLFSGSIKDNIAYGLADcsLERVQEAARRANAHSFISQLekGYDTDVGER-GGQMSGGEKQR 625
Cdd:TIGR02769 83 RRAFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRH--LTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 626 IAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQ 695
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
479-698 |
2.60e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.09 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG------QPLHSYQHHY 552
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQE----PVLfsgSIKDNIAYglADCSLERVQEAARRANAHSFISQLEKgydTDVGER-GGQMSGGEKQRIA 627
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENLIE--APCKVLGLSKEQAREKAMKLLARLRL---TDKADRfPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTH 698
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
163-454 |
3.23e-25 |
|
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: 106.41 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALnVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYD 322
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 323 NYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAM 402
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 403 LYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
163-426 |
3.49e-25 |
|
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: 106.33 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGglFMCAI--NSFTSRMKVEL 240
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAG--YFAAKasQGFGRDLRKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALvkQEISF--FETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQ 318
Cdd:cd18548 79 FEKI--QSFSFaeIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 319 GVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDH---RLMDThTLKTRRdtvraVYVLLRRLTA 395
Cdd:cd18548 157 FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKandDLTDT-SLKAGR-----LMALLNPLMM 230
|
250 260 270
....*....|....*....|....*....|....
gi 59275972 396 LVMQVAM---LYYGRLFIQRGQMSTGNLVSFILY 426
Cdd:cd18548 231 LIMNLAIvaiLWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-451 |
4.73e-25 |
|
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: 106.05 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVID------ILASQYKWndFLTAIILMGLYSLGSSFSAGCRGglFMCAI--NSFTS 234
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvliqlGPGGNTSL--LLLLVLGLAGAYVLSALLGILRG--RLLARlgERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVT 314
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDthtLKTRRDTVRAVYVLLRRLT 394
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE---LLDANIRAEKLWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 395 ALVMQ---VAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAA 451
Cdd:cd18563 234 TFLTSlgtLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSA 293
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
496-715 |
5.86e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.41 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNI 575
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGLaDCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLIL-DEVTSALDTESEH 654
Cdd:PTZ00243 1405 DPFL-EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDR 1483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 655 MVQEALTSCPSQ-TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL-MDRKGGYYKLRERL 715
Cdd:PTZ00243 1484 QIQATVMSAFSAyTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEAL 1546
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
482-694 |
6.20e-25 |
|
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: 104.05 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQER-KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyqhhyLH------ 554
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-----LDedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 ---RKVAMVGQ-EPVLFSGSIKDNIAYGLadcSLERVQEAARRANAhsfisQLEK-GydtdVGERG----GQMSGGEKQR 625
Cdd:COG4181 87 lraRHVGFVFQsFQLLPTLTALENVMLPL---ELAGRRDARARARA-----LLERvG----LGHRLdhypAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 626 IAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLE 694
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
479-696 |
6.98e-25 |
|
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: 103.04 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGqLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLhSYQHHYLHRKVA 558
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAY--GLADCSLERVQEAARRAnahsfisqLEKGYDTDVG-ERGGQMSGGEKQRIAIARALIR 634
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiaWLKGIPSKEVKARVDEV--------LELVNLGDRAkKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQEALTSCPSQTLLVIA-HRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILStHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
167-438 |
7.91e-25 |
|
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: 105.22 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 167 FIFLSLAVL---CEMFIPFYTGKVIDILASQYKWNDFLT-AIILMGLYSL--GSSFSAGCRGGLFMCAInsfTSRMKVEL 240
Cdd:cd18549 5 FLDLFCAVLiaaLDLVFPLIVRYIIDDLLPSKNLRLILIiGAILLALYILrtLLNYFVTYWGHVMGARI---ETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 FGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLqGV 320
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIF-TI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 321 YDNYYLRLT-KEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHtLKTRRDTVRAVYVLLRRLTAL--V 397
Cdd:cd18549 161 YFNKKMKKAfRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFD-EGNDRF-LESKKKAYKAMAYFFSGMNFFtnL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 59275972 398 MQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLI 438
Cdd:cd18549 239 LNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLV 279
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
479-651 |
8.89e-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: 102.87 E-value: 8.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQP---LHSYQHHYLHR 555
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSG-SIKDNIAYGLaDCSLERVQEAARRANAHSFISQLEKGYDTdvgeRGGQMSGGEKQRIAIARALIR 634
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRA----LPAELSGGEQQRVAIARAIVN 153
|
170
....*....|....*..
gi 59275972 635 EPQVLILDEVTSALDTE 651
Cdd:cd03292 154 SPTILIADEPTGNLDPD 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
496-704 |
9.10e-25 |
|
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: 103.57 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVAMVGQEPVLFSG-SIKDN 574
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 575 IAYGLADCSLERVQEAARRANAHSFIsqlekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEH 654
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 59275972 655 MVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:cd03299 167 KLREELKKIRKEfgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
490-651 |
1.37e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 490 TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ---QGEILLDGQPLHSYQHHylHRKVAMVGQEPVL 566
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 567 FSG-SIKDNIAYGLAdcslERVQEAARRANAHSFISQLEKGydtDVGERG-GQMSGGEKQRIAIARALIREPQVLILDEV 644
Cdd:COG4136 88 FPHlSVGENLAFALP----PTIGRAQRRARVEQALEEAGLA---GFADRDpATLSGGQRARVALLRALLAEPRALLLDEP 160
|
....*..
gi 59275972 645 TSALDTE 651
Cdd:COG4136 161 FSKLDAA 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
483-705 |
1.59e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.32 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERF--YQPQ---QGEILLDGQPLHSYQHHY--LHR 555
Cdd:PRK14239 10 DLSVYY---NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTvdLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSGSIKDNIAYGL-----ADCSL--ERVQEAARRANAHSFISqlEKGYDTDVGerggqMSGGEKQRIAI 628
Cdd:PRK14239 87 EIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVldEAVEKSLKGASIWDEVK--DRLHDSALG-----LSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER-ADQIILIDQGTVLEQG-THQELMDRK 705
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMNPK 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
197-713 |
1.90e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.07 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 197 WNDFLTAIILMglysLGSSFSAGCRGGLFMcAINSFTSRMKVELFGALVKQEISFF----ETIKTGDITSRLSTDTTKMa 272
Cdd:PLN03232 338 WVGYVYAFLIF----FGVTFGVLCESQYFQ-NVGRVGFRLRSTLVAAIFHKSLRLThearKNFASGKVTNMITTDANAL- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 273 RAVALNVNVLLRTLIKIVGMLSLM------MSLSWKLTLLMLMETpvtgllQGVYDNYYLRLTKEvqdSMARANEAAG-- 344
Cdd:PLN03232 412 QQIAEQLHGLWSAPFRIIVSMVLLyqqlgvASLFGSLILFLLIPL------QTLIVRKMRKLTKE---GLQWTDKRVGii 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 345 -ETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVmqVAMLYYGRLFIQRGQMSTGN-LVS 422
Cdd:PLN03232 483 nEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVV--VTLVSFGVFVLLGGDLTPARaFTS 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 423 FILYQSnLGTNIRTLIYIFGDMLNSVGAAGKVFE-YLDREPQVSTKGTLQPETLTghVHFHNLSFSYPTRQERKVLQGFS 501
Cdd:PLN03232 561 LSLFAV-LRSPLNMLPNLLSQVVNANVSLQRIEElLLSEERILAQNPPLQPGAPA--ISIKNGYFSWDSKTSKPTLSDIN 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 502 LELRPGQLTALVGPSGGGKSTCVS-LLERFYQPQQGEILLDGQplhsyqhhylhrkVAMVGQEPVLFSGSIKDNIAYGlA 580
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQVSWIFNATVRENILFG-S 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 581 DCSLERVQEAARrANAHSFISQLEKGYD-TDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTeseHMVQEA 659
Cdd:PLN03232 704 DFESERYWRAID-VTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA---HVAHQV 779
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 660 LTSC-----PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRKGGYYKLRE 713
Cdd:PLN03232 780 FDSCmkdelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
479-701 |
2.26e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ---QGEILLDGQPLHSYQHHYLHR 555
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEP-VLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKgydtdVGERGGQMSGGEKQRIAIARALI 633
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDY-----IDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
483-701 |
2.50e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EP--VLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEkgYDTdvgERGGQMSGGEKQRIAIARALIREPQVLI 640
Cdd:PRK13642 89 NPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD--FKT---REPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 641 LDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
495-692 |
3.74e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.43 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYqhhylhrkvamvgqepvlfsgSIKDN 574
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA---------------------SPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 575 IAYGLAdcslervqeaarranahsFISQLekgydtdvgerggqmSGGEKQRIAIARALIREPQVLILDEVTSAL-DTESE 653
Cdd:cd03216 73 RRAGIA------------------MVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 59275972 654 HM--VQEALTscpSQ--TLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:cd03216 120 RLfkVIRRLR---AQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
483-704 |
4.11e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.04 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQ---ERKV-----LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYL- 553
Cdd:COG4608 12 DLKKHFPVRGglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 --HRKVAMVGQEPvlfSGS------IKDNIAYGLADCSLERVQEAARRANAhsfisQLEK-GYDTDVGER-GGQMSGGEK 623
Cdd:COG4608 92 plRRRMQMVFQDP---YASlnprmtVGDIIAEPLRIHGLASKAERRERVAE-----LLELvGLRPEHADRyPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 624 QRIAIARALIREPQVLILDEVTSALDTeSehmVQealtscpSQ--------------TLLVIAHRLKTIER-ADQIILID 688
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDV-S---IQ-------AQvlnlledlqdelglTYLFISHDLSVVRHiSDRVAVMY 232
|
250
....*....|....*.
gi 59275972 689 QGTVLEQGTHQELMDR 704
Cdd:COG4608 233 LGKIVEIAPRDELYAR 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
493-692 |
4.70e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHhylhrKVAMVGQEPVLFS-GSI 571
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE-----DTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 KDNIAYGLADcsleRVQEAARRAnahsfisqLEK-GYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDT 650
Cdd:PRK11247 99 IDNVGLGLKG----QWRDAALQA--------LAAvGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 59275972 651 ESEHMVQEALTSCPSQ---TLLVIAHRL-KTIERADQIILIDQGTV 692
Cdd:PRK11247 167 LTRIEMQDLIESLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
483-701 |
5.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQErkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLhSYQHHYL---HRKVAM 559
Cdd:PRK13639 6 DLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEP--VLFSGSIKDNIAYGLADCSL------ERVQEAARRANAhsfisqleKGYDTDVGErggQMSGGEKQRIAIARA 631
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLskeeveKRVKEALKAVGM--------EGFENKPPH---HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
479-649 |
5.97e-24 |
|
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: 100.41 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHylHRKVA 558
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYGL------ADCSLERVQEAARranahsfISQLEKGYDtdvgERGGQMSGGEKQRIAIARA 631
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLklrkvpKDEIDERVREVAE-------LLQIEHLLD----RKPKQLSGGQRQRVALGRA 144
|
170
....*....|....*...
gi 59275972 632 LIREPQVLILDEVTSALD 649
Cdd:cd03301 145 IVREPKVFLMDEPLSNLD 162
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
483-701 |
6.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLS--FSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL-------DGQPLHSYQHHY- 552
Cdd:PRK13631 26 NLYcvFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELITNPYs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 --------LHRKVAMVGQEP--VLFSGSIKDNIAYGLADCSLERvQEAARRANAHsfisqLEK-GYDTDVGERGG-QMSG 620
Cdd:PRK13631 106 kkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFY-----LNKmGLDDSYLERSPfGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEH-MVQEALTSCPS-QTLLVIAHRL-KTIERADQIILIDQGTVLEQGT 697
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANnKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
....
gi 59275972 698 HQEL 701
Cdd:PRK13631 260 PYEI 263
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
479-705 |
1.15e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYP--TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQH----HY 552
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQ--EPVLFSGSIKDNIAYGLAD--CSLERVQEaarraNAHSFISQLekGYDTDVGERGG-QMSGGEKQRIA 627
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKN-----YAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSC---PSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 59275972 704 RK 705
Cdd:PRK13646 236 DK 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
483-704 |
1.83e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.96 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQ-----ER--KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY--- 552
Cdd:PRK11308 10 DLKKHYPVKRglfkpERlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQEPVlfsGSI--KDNIAYGLAD-----CSLERvqeAARRANAHSFISQLekGYDTDVGERGGQM-SGGEKQ 624
Cdd:PRK11308 90 LRQKIQIVFQNPY---GSLnpRKKVGQILEEpllinTSLSA---AERREKALAMMAKV--GLRPEHYDRYPHMfSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTESEHMV--------QEALTScpsqtLLVIAHRLKTIER-ADQIILIDQGTVLEQ 695
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlqQELGLS-----YVFISHDLSVVEHiADEVMVMYLGRCVEK 236
|
....*....
gi 59275972 696 GTHQELMDR 704
Cdd:PRK11308 237 GTKEQIFNN 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
462-701 |
1.94e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 462 PQVSTKGTLQPetltgHVHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLD 541
Cdd:PRK11607 8 PQAKTRKALTP-----LLEIRNLTKSF---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 542 GQPLHS---YQhhylhRKVAMVGQEPVLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGydtdvGERGGQ 617
Cdd:PRK11607 80 GVDLSHvppYQ-----RPINMMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-----KRKPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 618 MSGGEKQRIAIARALIREPQVLILDEVTSALDTE----SEHMVQEALTSCPSQTLLVIAHRLKTIERADQIILIDQGTVL 693
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
....*...
gi 59275972 694 EQGTHQEL 701
Cdd:PRK11607 230 QIGEPEEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
494-701 |
2.25e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.08 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsyQHHYLHRKVAMVGQEPVLFSG-SIK 572
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRHmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYGLadcsleRVQEAARRANAHSfISQ-----LEKGYDTDVGER-GGQMSGGEKQRIAIARALIREPQVLILDEVTS 646
Cdd:PRK10851 93 DNIAFGL------TVLPRRERPNAAA-IKAkvtqlLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 647 ALDTEsehmVQEALTSCPSQ-------TLLVIAH-RLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK10851 166 ALDAQ----VRKELRRWLRQlheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
482-703 |
2.41e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 99.29 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQ-HHYLHRKVAMV 560
Cdd:COG0410 7 ENLHAGYGGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEPVLFSG-SIKDNI---AYGLADCS-----LERVQE-----AARRANahsfisqlekgydtdvgeRGGQMSGGEKQRI 626
Cdd:COG0410 84 PEGRRIFPSlTVEENLllgAYARRDRAevradLERVYElfprlKERRRQ------------------RAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 627 AIARALIREPQVLILDEVTSALdteSEHMVQEaltscpsqtllvIAHRLKTI------------------ERADQIILID 688
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEE------------IFEIIRRLnregvtillveqnarfalEIADRAYVLE 210
|
250
....*....|....*
gi 59275972 689 QGTVLEQGTHQELMD 703
Cdd:COG0410 211 RGRIVLEGTAAELLA 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
496-701 |
3.31e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.72 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPL--HSYQHhylhRKVAMVGQEPVLFSG-SIK 572
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQ----RDICMVFQSYALFPHmSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYGL------ADCSLERVQEAARRANAHSFisqlEKGYdTDvgerggQMSGGEKQRIAIARALIREPQVLILDEVTS 646
Cdd:PRK11432 97 ENVGYGLkmlgvpKEERKQRVKEALELVDLAGF----EDRY-VD------QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 647 ALDTESEHMVQEALTSCPSQ---TLLVIAH-RLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-430 |
3.56e-23 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 100.25 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQykwNDFLTAIILMGLyslgsSFSAGCRGGLFMCAINSFTSR------- 235
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQ---GDLGLLVLLALG-----MVAVAVASALLGVVQTYLSARigqgvmy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 236 -MKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVT 314
Cdd:cd18550 73 dLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 315 GLLQGVYDNYYLRLTKEVQDSMARANEAAGET--VAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTV-RAVYVLLR 391
Cdd:cd18550 153 VLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAgRWFFAALG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 59275972 392 RLTALVmqVAMLY-YGRLFIQRGQMSTGNLVSFILYQSNL 430
Cdd:cd18550 233 LFTAIG--PALVYwVGGLLVIGGGLTIGTLVAFTALLGRL 270
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
483-681 |
4.32e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.00 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS--------YQHHYLh 554
Cdd:PRK11248 6 HLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvFQNEGL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 rkvamvgqepvLFSGSIKDNIAYGLadcSLERVQEAARRANAHSFISQLE-KGYDTdvgERGGQMSGGEKQRIAIARALI 633
Cdd:PRK11248 82 -----------LPWRNVQDNVAFGL---QLAGVEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSQT---LLVIAHrlkTIERA 681
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkqVLLITH---DIEEA 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
483-702 |
6.78e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.71 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:PRK10575 16 NVSFRVP---GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 E-PVLFSGSIKDNIA------------YGLADcsLERVQEAARRANAHSFISQLekgYDTdvgerggqMSGGEKQRIAIA 629
Cdd:PRK10575 93 QlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 630 RALIREPQVLILDEVTSALDTesEHMVQE-ALTSCPSQT--LLVIA--HRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDI--AHQVDVlALVHRLSQErgLTVIAvlHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-701 |
7.09e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY------LHRK 556
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaikLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIRE 635
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 636 PQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
483-696 |
1.19e-22 |
|
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: 96.52 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQplhSYQHhyLHRKVAMVG- 561
Cdd:cd03268 5 DLTKTY---GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQK--NIEALRRIGa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 --QEPVLFSG-SIKDNIAYG--LADCSLERVQEAARRAnahsfisqlekGYDTDVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:cd03268 77 liEAPGFYPNlTARENLRLLarLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQgiTVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
479-701 |
1.29e-22 |
|
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: 96.81 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsYQHHYLHRKVA 558
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFSG-SIKDNIAYglaDCSLERVQEAARRANAHSFISQLEkgyDTDVGER-GGQMSGGEKQRIAIARALIREP 636
Cdd:cd03263 79 YCPQFDALFDElTVREHLRF---YARLKGLPKSEIKEEVELLLRVLG---LTDKANKrARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCPSQTLLVIA-HRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTtHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
482-712 |
1.85e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.26 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsyqhhylHRKVAMVG 561
Cdd:COG4152 5 KGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 ---QEPVLFSG-SIKDNIAY-----GLADcslervQEAARRANAHsfisqLEKgydTDVGERGG----QMSGGEKQRIAI 628
Cdd:COG4152 75 ylpEERGLYPKmKVGEQLVYlarlkGLSK------AEAKRRADEW-----LER---LGLGDRANkkveELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRk 705
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgtTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ- 219
|
....*..
gi 59275972 706 GGYYKLR 712
Cdd:COG4152 220 FGRNTLR 226
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
162-438 |
2.15e-22 |
|
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: 97.90 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 162 LLVGAFIFLSLAVLCEMFIPFYTGKVID-ILASQYKWNDFLTAIILMGLYSLGSSFSAgCRGGLfmcaINSFTSRMKVEL 240
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILIDdIIPSGDINLLNIISIGLILLYLFQSLLSY-IRSYL----LLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 241 ----FGALVKQEISFFETIKTGDITSRLStDTTKMARAVA-LNVNVLLRTLIKIVGmLSLMMSLSWKLTLLMLMETPVTG 315
Cdd:cd18570 78 ilgyFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISsTTISLFLDLLMVIIS-GIILFFYNWKLFLITLLIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 316 LLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTA 395
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 59275972 396 LVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLI 438
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLI 278
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
479-696 |
2.53e-22 |
|
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: 95.81 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHY----- 552
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIgylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 ---LHRKVamvgqepvlfsgSIKDNIAYgLAdcSLERVQEAARRANAHSFISQLEKGYDTDvgERGGQMSGGEKQRIAIA 629
Cdd:cd03269 78 ergLYPKM------------KVIDQLVY-LA--QLKGLKKEEARRRIDEWLERLELSEYAN--KRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgkTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
482-702 |
3.35e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.83 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTR------QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHR 555
Cdd:COG4167 8 RNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPvlfSGSIKDNIAYGladcsleRVQEAARRANAH-SFISQLEKGYDT--DVGERGGQ-------MSGGEKQR 625
Cdd:COG4167 88 HIRMIFQDP---NTSLNPRLNIG-------QILEEPLRLNTDlTAEEREERIFATlrLVGLLPEHanfyphmLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 626 IAIARALIREPQVLILDEVTSALDtesehmvqealTSCPSQTL--------------LVIAHRLKTIER-ADQIILIDQG 690
Cdd:COG4167 158 VALARALILQPKIIIADEALAALD-----------MSVRSQIInlmlelqeklgisyIYVSQHLGIVKHiSDKVLVMHQG 226
|
250
....*....|..
gi 59275972 691 TVLEQGTHQELM 702
Cdd:COG4167 227 EVVEYGKTAEVF 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
483-702 |
4.62e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 95.69 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAMVG 561
Cdd:cd03218 5 NLSKRY---GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVLFSG-SIKDNIayglaDCSLE--RVQEAARRANAHSFIS--QLEKGYDTdvgeRGGQMSGGEKQRIAIARALIREP 636
Cdd:cd03218 82 QEASIFRKlTVEENI-----LAVLEirGLSKKEREEKLEELLEefHITHLRKS----KASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 637 QVLILDEVTSALDTESEHMVQEaltscpsqtllvIAHRLK---------------TIERADQIILIDQGTVLEQGTHQEL 701
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQK------------IIKILKdrgigvlitdhnvreTLSITDRAYIIYEGKVLAEGTPEEI 220
|
.
gi 59275972 702 M 702
Cdd:cd03218 221 A 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
483-706 |
5.92e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY--LHRKVAMV 560
Cdd:PRK13638 6 DLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlaLRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEP--VLFSGSIKDNIAYGLADCSL------ERVQEAARRANAHSFISQLEKGydtdvgerggqMSGGEKQRIAIARAL 632
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVpeaeitRRVDEALTLVDAQHFRHQPIQC-----------LSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 633 IREPQVLILDEVTSALDTESEHMVQEALTSCPSQTLLVI--AHRLKTI-ERADQIILIDQGTVLEQG------THQELMD 703
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIisSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAME 231
|
...
gi 59275972 704 RKG 706
Cdd:PRK13638 232 QAG 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
483-704 |
5.93e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:PRK13652 8 DLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EP--VLFSGSIKDNIAYGLADCSLE------RVQEAARRANAHSFISQLEKgydtdvgerggQMSGGEKQRIAIARALIR 634
Cdd:PRK13652 86 NPddQIFSPTVEQDIAFGPINLGLDeetvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 635 EPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELMDR 704
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
479-696 |
6.88e-22 |
|
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: 94.74 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSY-PTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKV 557
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPVLFSGSIKDNIAY-----GLA-DCSLERVQEAARRANAHSFisqLEKgydtdvgeRGGQMSGGEKQRIAIARA 631
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYfaglyGLKgDELTARLEELADRLGMEEL---LDR--------RVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
501-696 |
1.03e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 501 SLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQ-HHYLHRKVAMVGQEPVLFSG-SIKDNIAYG 578
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 579 LADCSLERV--QEAARRanahsfISQLEKGY--DTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSAL-DTESE 653
Cdd:COG3845 105 LEPTKGGRLdrKAARAR------IRELSERYglDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 654 H-------MVQEALtscpsqTLLVIAHRLKTIER-ADQIilidqgTVLEQG 696
Cdd:COG3845 179 ElfeilrrLAAEGK------SIIFITHKLREVMAiADRV------TVLRRG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
461-720 |
1.32e-21 |
|
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: 100.79 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 461 EPQVSTKGTLQPETLTGhVHFHNLSFSYpTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL 540
Cdd:TIGR00957 620 EPDSIERRTIKPGEGNS-ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 541 DGQplhsyqhhylhrkVAMVGQEPVLFSGSIKDNIAYGladCSLE--RVQEAARRANAHSFISQLEKGYDTDVGERGGQM 618
Cdd:TIGR00957 698 KGS-------------VAYVPQQAWIQNDSLRENILFG---KALNekYYQQVLEACALLPDLEILPSGDRTEIGEKGVNL 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 619 SGGEKQRIAIARALIREPQVLILDEVTSALDTE-SEHMVQEALTS---CPSQTLLVIAHRLKTIERADQIILIDQGTVLE 694
Cdd:TIGR00957 762 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
250 260
....*....|....*....|....*..
gi 59275972 695 QGTHQELMDRKGGYYK-LRERLFTEDD 720
Cdd:TIGR00957 842 MGSYQELLQRDGAFAEfLRTYAPDEQQ 868
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
497-691 |
1.42e-21 |
|
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: 93.93 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIL----LDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIK 572
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYGlADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTE- 651
Cdd:cd03290 97 ENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 59275972 652 SEHMVQEALTSC---PSQTLLVIAHRLKTIERADQIILIDQGT 691
Cdd:cd03290 176 SDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
483-700 |
1.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSY--PTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPL--HSYQHHYLHRKVA 558
Cdd:PRK13637 7 NLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEP--VLFSGSIKDNIAYGLADCSLERvQEAARRANAHSFISQLEkgYDTDVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:PRK13637 87 LVFQYPeyQLFEETIEKDIAFGPINLGLSE-EEIENRVKRAMNIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQE 700
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-690 |
2.48e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 93.30 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLhsyqhhylhrkvamvgQEP-----VLFSG-- 569
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----------------TEPgpdrmVVFQNys 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 -----SIKDNIAYGLaDCSLERVQEAARRANAHSFISQLEKGYDTDvgERGGQMSGGEKQRIAIARALIREPQVLILDEV 644
Cdd:TIGR01184 65 llpwlTVRENIALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 59275972 645 TSALDTESEHMVQEALTSCPSQ---TLLVIAHRL-KTIERADQIILIDQG 690
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEhrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-451 |
3.36e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 94.89 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 203 AIILMGLYSLGSSFSAGcrgGLFMCAI--NSFTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVN 280
Cdd:cd18564 57 AAALVGIALLRGLASYA---GTYLTALvgQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 281 VLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVtgLLQGVYdnyylRLTKEVQDSM--ARANE-----AAGETVAGIRTV 353
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFWLDWQLALIALAVAPL--LLLAAR-----RFSRRIKEASreQRRREgalasVAQESLSAIRVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 354 RSFNTERSEASHYdhrlmDTHTLKTRRDTVRAVYV--LLRRLTALVMQVA---MLYYGRLFIQRGQMSTGNLVSFILYQS 428
Cdd:cd18564 207 QAFGREEHEERRF-----ARENRKSLRAGLRAARLqaLLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLK 281
|
250 260
....*....|....*....|...
gi 59275972 429 NLGTNIRTLiyifGDMLNSVGAA 451
Cdd:cd18564 282 NLYKPVRDL----AKLTGRIAKA 300
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
501-709 |
6.79e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.49 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 501 SLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYL----HRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYG--LADCSLERVQEAARRANAHSFISQLEKGYDTdvgerggQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESE 653
Cdd:PRK10070 128 AFGmeLAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 654 HMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRKGGYY 709
Cdd:PRK10070 201 TEMQDELVKLQAKhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
485-696 |
8.43e-21 |
|
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: 92.01 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 485 SFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQE- 563
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 ------PVLFSGSIKDNIaYGLADcslervQEAARRANAHSFISQLEKGYDTDVgeRggQMSGGEKQRIAIARALIREPQ 637
Cdd:cd03267 105 qlwwdlPVIDSFYLLAAI-YDLPP------ARFKKRLDELSELLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 638 VLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
497-703 |
9.17e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTcvsLLERF--YQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQE-PVLFSGSIKD 573
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 574 NIAYGLADCSLERVQEAARRANAHSFisQLEKGYDTDVgergGQMSGGEKQRIAIARALIR-------EPQVLILDEVTS 646
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 647 ALDtesehMVQEA-----LTSCPSQTLLVI--AHRLK-TIERADQIILIDQGTVLEQGTHQELMD 703
Cdd:COG4138 163 SLD-----VAQQAaldrlLRELCQQGITVVmsSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
481-692 |
1.38e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplhsyqhhylHRKVAMV 560
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEPVLFSG-SIKDNIAYGLADCS----------------------LERVQEAARRANAHSFISQLEK-----GYDTDVG 612
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeleeleaklaepdedlerLAELQEEFEALGGWEAEARAEEilsglGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 613 ERG-GQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH-R--LKTIerADQIILID 688
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG-TVLVVSHdRyfLDRV--ATRILELD 223
|
....
gi 59275972 689 QGTV 692
Cdd:COG0488 224 RGKL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
482-704 |
1.74e-20 |
|
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: 95.52 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPT-RQERKVLQGFSLELRPGQLTALVGPSGGGKS-TCVS---LLERFYQPQQGEILLDGQPLhsyqhhyLH-- 554
Cdd:COG4172 10 EDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSilrLLPDPAAHPSGSILFDGQDL-------LGls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 ---------RKVAMVGQEPV-----LFSgsIKDNIAYGLA---------------DCsLERVQ--EAARRANA--Hsfis 601
Cdd:COG4172 83 erelrrirgNRIAMIFQEPMtslnpLHT--IGKQIAEVLRlhrglsgaaararalEL-LERVGipDPERRLDAypH---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 602 qlekgydtdvgerggQMSGGEKQRIAIARALIREPQVLILDEVTSALD--------------TESEHMvqealtscpsqT 667
Cdd:COG4172 156 ---------------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqildllkdlQRELGM-----------A 209
|
250 260 270
....*....|....*....|....*....|....*...
gi 59275972 668 LLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDR 704
Cdd:COG4172 210 LLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
491-696 |
1.91e-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: 90.79 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTcvsLLERFYQPQQ------GEILLDGQPLHSYQhhyLHRKVAMVGQEP 564
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTT---LLDAISGRVEgggttsGQILFNGQPRKPDQ---FQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 565 VLFSG-SIKDNIAYgLADCSLERVQEAARRANAHSFISQLEKGyDTDVG-ERGGQMSGGEKQRIAIARALIREPQVLILD 642
Cdd:cd03234 91 ILLPGlTVRETLTY-TAILRLPRKSSDAIRKKRVEDVLLRDLA-LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 643 EVTSALDTESEHMVqealtscpSQTLLVIAHRLKTI------------ERADQIILIDQGTVLEQG 696
Cdd:cd03234 169 EPTSGLDSFTALNL--------VSTLSQLARRNRIViltihqprsdlfRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
479-702 |
2.08e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-V 557
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEP-VLFSG-SIKDNIAYGLADCSLERVQEAARRANAHSfisqlEKGYDTDVGERGGQMSGGEKQRIAIARALIRE 635
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALA-----EIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 636 PQVLILDEVTSALDTESEHMVQEALTSC--PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-701 |
2.16e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSY-PTRQERKVLQGFSLELRPGQLTALVGPSGGGKS-TCVSLLERFYQPQ----QGEILLDGQPLHSYQHHYLHR- 555
Cdd:PRK15134 10 NLSVAFrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 ---KVAMVGQEPVLfSGSIKDNIAYGLADC-SLER--VQEAARRanahSFISQLEKgydtdVGERGG---------QMSG 620
Cdd:PRK15134 90 rgnKIAMIFQEPMV-SLNPLHTLEKQLYEVlSLHRgmRREAARG----EILNCLDR-----VGIRQAakrltdyphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGRCVEQN 239
|
....*
gi 59275972 697 THQEL 701
Cdd:PRK15134 240 RAATL 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
233-703 |
2.35e-20 |
|
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: 96.52 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 233 TSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSwklTLLMLMETP 312
Cdd:TIGR01271 957 SKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQ---PYIFIAAIP 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 313 VTGLLQgVYDNYYLRLTKEVQDSMARANEAAGE----TVAGIRTVRSFNTErseaSHYD---HRLMDTHT------LKTR 379
Cdd:TIGR01271 1034 VAVIFI-MLRAYFLRTSQQLKQLESEARSPIFShlitSLKGLWTIRAFGRQ----SYFEtlfHKALNLHTanwflyLSTL 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 380 RdtvravYVLLR-RLTALVMQVAMLYYGRLFIQRGQMSTGNLVSF-ILYQSNLGTNIRTLIYIFGdMLNSVGaagKVFEY 457
Cdd:TIGR01271 1109 R------WFQMRiDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLaMNILSTLQWAVNSSIDVDG-LMRSVS---RVFKF 1178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 458 LDREPQVS-TKGTLQPETLT-----------------GHVHFHNLSFSYpTRQERKVLQGFSLELRPGQLTALVGPSGGG 519
Cdd:TIGR01271 1179 IDLPQEEPrPSGGGGKYQLStvlvienphaqkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSG 1257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 520 KSTCVSLLERFYQpQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSGSIKDNIAyGLADCSLERVQEAARRANAHSF 599
Cdd:TIGR01271 1258 KSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSV 1335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 600 ISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTI 678
Cdd:TIGR01271 1336 IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNcTVILSEHRVEAL 1415
|
490 500
....*....|....*....|....*
gi 59275972 679 ERADQIILIDQGTVLEQGTHQELMD 703
Cdd:TIGR01271 1416 LECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
168-438 |
2.47e-20 |
|
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: 92.14 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 168 IFLSLAV-LCEMFIPFYTGKVID-ILASQYKwnDFLTAIIL-MGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFGAL 244
Cdd:cd18567 8 LLLSLALeLFALASPLYLQLVIDeVIVSGDR--DLLTVLAIgFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 245 VKQEISFFETIKTGDITSRL-STD------TTKMARAValnVNVLLrtlikIVGMLSLMMSLSWKLTLLMLMETPVTGLL 317
Cdd:cd18567 86 LRLPLSYFEKRHLGDIVSRFgSLDeiqqtlTTGFVEAL---LDGLM-----AILTLVMMFLYSPKLALIVLAAVALYALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 318 QGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDT--HTLKTRRdtVRAVYVLLRRLTA 395
Cdd:cd18567 158 RLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAinADIRLQR--LQILFSAANGLLF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 59275972 396 LVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLI 438
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLI 278
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
479-694 |
2.70e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLdGQPLH-SY--QHH-YLH 554
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYfdQHQeELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 rkvamvGQEPVLfsgsikDNIAygladcsleRVQEAARRANAHSFISQ-LEKGydTDVGERGGQMSGGEKQRIAIARALI 633
Cdd:COG0488 392 ------PDKTVL------DELR---------DGAPGGTEQEVRGYLGRfLFSG--DDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 634 REPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH-R--LKTIerADQIILIDQGTVLE 694
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
493-702 |
2.90e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKST---CVSLLERfyqPQQGEILLDGQPLH-------------SYQHHYLHRK 556
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSG-SIKDNIAYGLADCSLERVQEAARRAnahsfISQLEK-GYDTDV-GERGGQMSGGEKQRIAIARALI 633
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERA-----VKYLAKvGIDERAqGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 634 REPQVLILDEVTSALDTEsehMVQEALT-----SCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPE---LVGEVLRimqqlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-707 |
3.00e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyQHHYLHRKVA 558
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVL-FSGSIKDNIA-----YGLADCSLERV----QEAARranahsfisqLEKGYDTDVGErggqMSGGEKQRIAI 628
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvfgryFGMSTREIEAVipslLEFAR----------LESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgkTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
..
gi 59275972 706 GG 707
Cdd:PRK13536 264 IG 265
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
482-699 |
3.14e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG------QPLHSYQHHYLHR 555
Cdd:PRK11124 6 NGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQE----PVLfsgSIKDNIAYglADCSLERVQEAARRANAHSFISQLEKgydTDVGERGG-QMSGGEKQRIAIAR 630
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNLIE--APCRVLGLSKDQALARAEKLLERLRL---KPYADRFPlHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCpSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQ 699
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AEtgiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
497-680 |
3.82e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKST---CVS----LLERFYQpqQGEILLDGQPLhsYQHHY----LHRKVAMVGQEPV 565
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNrlndLIPGFRV--EGKVTFHGKNL--YAPDVdpveVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 LFSGSIKDNIAYGL------ADCSlERVQEAARRAnahsfisQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVL 639
Cdd:PRK14243 102 PFPKSIYDNIAYGAringykGDMD-ELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 59275972 640 ILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER 680
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQyTIIIVTHNMQQAAR 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
200-545 |
4.51e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 94.48 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 200 FLTAIILMGLYSLGSSFsagcrggLFMCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNV 279
Cdd:COG4615 54 FAGLLVLLLLSRLASQL-------LLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 280 NvLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLqgvydnyYLRLTKEVQDSMARANEAAGETVAGIRTVRS---- 355
Cdd:COG4615 127 E-LLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAG-------YRLLVRRARRHLRRAREAEDRLFKHFRALLEgfke 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 356 --FNTERSEASHYDHrlMDTHTLKTRRDTVRA--VYVLLRRLTALVMQVAM---LYYGRLFiqrGQMSTGNLVSFILyqs 428
Cdd:COG4615 199 lkLNRRRRRAFFDED--LQPTAERYRDLRIRAdtIFALANNWGNLLFFALIgliLFLLPAL---GWADPAVLSGFVL--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 429 nlgtnirTLIYIFGDMLNSVG----------AAGKV---FEYLDREPQVSTKGTLQPE-TLTGHVHFHNLSFSYPTRQER 494
Cdd:COG4615 271 -------VLLFLRGPLSQLVGalptlsranvALRKIeelELALAAAEPAAADAAAPPApADFQTLELRGVTYRYPGEDGD 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 495 KvlqGF-----SLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPL 545
Cdd:COG4615 344 E---GFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
494-690 |
4.66e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQP---LHSYQHHYLHRKVAMVGQEP-VLFSG 569
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIKDNIAYGL--ADCSLERVQEaaRRANAHSFISQLEKGYDTDVgerggQMSGGEKQRIAIARALIREPQVLILDEVTSA 647
Cdd:PRK10908 95 TVYDNVAIPLiiAGASGDDIRR--RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 59275972 648 LDTE-SEHMVQ--EALTSCpSQTLLVIAHRLKTIERAD-QIILIDQG 690
Cdd:PRK10908 168 LDDAlSEGILRlfEEFNRV-GVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
479-702 |
5.14e-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: 90.14 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSyptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQG-EILLDGQPLHSYQHHYLHRKV 557
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVG---QEPVLFSGSIKDNIAYGLADcSLERVQE--AARRANAHSFISQLEKGYDTDvgERGGQMSGGEKQRIAIARAL 632
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFD-SIGLYREptDEQRERARELLELLGLAHLAD--RPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 633 IREPQVLILDEVTSALDTES-EHMVQ--EALTSCPSQTLLVIAHRL----KTIERAdqiILIDQGTVLEQGTHQELM 702
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGArELLLAllDKLAAEGAPTLVLVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
499-701 |
5.25e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 499 GFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG-------- 569
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREmtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 -----SIKDNIAYGLADCSLERVQEAARRANAHSFisqLEKGYDTDVGER-GGQMSGGEKQRIAIARALIREPQVLILDE 643
Cdd:PRK11300 103 vaqhqQLKTGLFSGLLKTPAFRRAESEALDRAATW---LERVGLLEHANRqAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 644 VTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEhnvTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
481-701 |
5.55e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.85 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRQ--ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY----LH 554
Cdd:PRK13634 5 FQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkpLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 RKVAMVGQ--EPVLFSGSIKDNIAYGLADCSLERvQEAARRAnahsfiSQLEK--GYDTDVGERGG-QMSGGEKQRIAIA 629
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKA------REMIElvGLPEELLARSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQE---ALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
490-696 |
5.96e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 490 TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVL-FS 568
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIAYG---------LADCSLER-VQEAARRANAHSFIsqlekgyDTDVGErggqMSGGEKQRIAIARALIREPQV 638
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdTWTETDRAaVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 639 LILDEVTSALDTesEHMVQealTSCPSQTLL-----VIA--HRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:PRK09536 161 LLLDEPTASLDI--NHQVR---TLELVRRLVddgktAVAaiHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
496-691 |
7.69e-20 |
|
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: 89.03 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILldgqplhsYQHHYlhRKVAMVGQEPVLFSGSIKDNI 575
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG--GWVDLAQASPREILALRRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYgladCS-----------LERVQEAArranahsfisqLEKGYDTDVG-ERGGQM------------------SGGEKQR 625
Cdd:COG4778 96 GY----VSqflrviprvsaLDVVAEPL-----------LERGVDREEArARARELlarlnlperlwdlppatfSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 626 IAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGT 691
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgtAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
491-712 |
1.00e-19 |
|
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: 87.93 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsYQHHYLHRKVAMVGQEPVLFSG- 569
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIKDNIAYGLADCSLERVQEAARRANAHSFisqlekgYDTDVgergGQMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 650 TESEHMVQEALTscpsqtllviAHrlktIERADQIILidqgtvleqGTHQELMDRKGGYYKLR 712
Cdd:cd03231 158 KAGVARFAEAMA----------GH----CARGGMVVL---------TTHQDLGLSEAGARELD 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
482-701 |
1.38e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCvsllerFY------QPQQGEILLDGQPLHSYQhhyLHR 555
Cdd:COG1137 7 ENLVKSY---GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLP---MHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAM-VG---QEPVLFSG-SIKDNIaygLADCSLERVQEAARRANAHSFIS--QLEKGYDTdvgeRGGQMSGGEKQRIAI 628
Cdd:COG1137 75 RARLgIGylpQEASIFRKlTVEDNI---LAVLELRKLSKKEREERLEELLEefGITHLRKS----KAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALD--------------TE-------SEHMVQEALTSCpsqtllviahrlktiERAdqiILI 687
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavadiqkiirhlKErgigvliTDHNVRETLGIC---------------DRA---YII 209
|
250
....*....|....
gi 59275972 688 DQGTVLEQGTHQEL 701
Cdd:COG1137 210 SEGKVLAEGTPEEI 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
482-703 |
2.22e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVG 561
Cdd:COG4604 5 KNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVLFSG-SIKDNIAYG--------LADCSLERVQEAARRAN----AHSFISQLekgydtdvgerggqmSGGEKQRIAI 628
Cdd:COG4604 82 QENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDledlADRYLDEL---------------SGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTesEHMVQealtscpsqtLLVIAHRL-----KTI-----------ERADQIILIDQGTV 692
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDM--KHSVQ----------MMKLLRRLadelgKTVvivlhdinfasCYADHIVAMKDGRV 214
|
250
....*....|.
gi 59275972 693 LEQGTHQELMD 703
Cdd:COG4604 215 VAQGTPEEIIT 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-701 |
4.24e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQP-----QQGEILLDGQPLHSYQHHY-LHRKVAMVGQEPVLF 567
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 568 SGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSA 647
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 648 LDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
494-702 |
5.91e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.15 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDgqplhsyqhhylhRKVAMVGQEPVLFSGSIKD 573
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 574 NIAYgLADCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTE-S 652
Cdd:PTZ00243 740 NILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 653 EHMVQEA-LTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:PTZ00243 819 ERVVEECfLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
473-702 |
6.04e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 473 ETLtghVHFHNLS--FSYPT----RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH 546
Cdd:PRK15112 2 ETL---LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 547 SYQHHYLHRKVAMVGQEPvlfSGSIKDNIAYG-LADCSLERVQEAARRANAHSFISQLEK-GYDTDVGERGGQM-SGGEK 623
Cdd:PRK15112 79 FGDYSYRSQRIRMIFQDP---STSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLRQvGLLPDHASYYPHMlAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 624 QRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQT----LLVIAHRLKTIERADQIILIDQGTVLEQGTHQ 699
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgisyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
...
gi 59275972 700 ELM 702
Cdd:PRK15112 236 DVL 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
483-693 |
6.23e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQER-KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS-------------- 547
Cdd:PRK10535 9 DIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalaqlrrehf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 548 ---YQHHYL--HRKVAMVGQEPVLFSGSIKdniaygladcslervqeAARRANAHSFISQLekGYDTDVGERGGQMSGGE 622
Cdd:PRK10535 89 gfiFQRYHLlsHLTAAQNVEVPAVYAGLER-----------------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 623 KQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILIDQGTVL 693
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
163-451 |
6.27e-19 |
|
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: 87.91 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYD 322
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 323 NYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHtlktRRDTVRAVYV------LLRRLTAL 396
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFD-ELNREN----RKANMRAVRLnalfwpLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 397 VMqVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAA 451
Cdd:cd18545 237 GT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASA 290
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
481-698 |
6.54e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHsYQH--HYLHRKVA 558
Cdd:PRK11288 7 FDGIGKTFPGV---KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASttAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQE----PVLfsgSIKDNIAYGLADCSLERVQEAARRANAHsfiSQLEK-GYDTDVGERGGQMSGGEKQRIAIARALI 633
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAR---EQLEHlGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 634 REPQVLILDEVTSALDT-ESEHM--VQEALTScPSQTLLVIAHRLKTIERadqiiLIDQGTVLEQGTH 698
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLfrVIRELRA-EGRVILYVSHRMEEIFA-----LCDAITVFKDGRY 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
481-688 |
8.25e-19 |
|
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: 84.13 E-value: 8.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSypTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIlldgqplhsyqHHYLHRKVAMV 560
Cdd:cd03223 3 LENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQEPVLFSGSIKDNIAYGLADcslervqeaarranahsfisqlekgydtdvgerggQMSGGEKQRIAIARALIREPQVLI 640
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDD-----------------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 59275972 641 LDEVTSALDTESEH----MVQEALTscpsqTLLVIAHRlKTIER-ADQIILID 688
Cdd:cd03223 115 LDEATSALDEESEDrlyqLLKELGI-----TVISVGHR-PSLWKfHDRVLDLD 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
496-699 |
8.62e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---QHHYLhrKVAMVGQEPVLFSG-SI 571
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAHQL--GIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 KDNIAYGLAdcsleRVQEAARRANAhsFISQLEKGYDTDVgeRGGQMSGGEKQRIAIARALIREPQVLILDEVTSALD-T 650
Cdd:PRK15439 104 KENILFGLP-----KRQASMQKMKQ--LLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 59275972 651 ESEHMVQEaLTSCPSQT--LLVIAHRLKTI-ERADQI-ILIDQGTVLEQGTHQ 699
Cdd:PRK15439 175 ETERLFSR-IRELLAQGvgIVFISHKLPEIrQLADRIsVMRDGTIALSGKTAD 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
487-649 |
8.80e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 88.75 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 487 SYPTRQErkVLQGFSLELRPGQLTALVGPSGGGKSTC---VSLLERFyqpQQGEILLDGQ------PLHsyqhhylhRKV 557
Cdd:PRK11650 12 SYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRvvnelePAD--------RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPVLFSG-SIKDNIAYGL-------ADCSlERVQEAARranahsfISQLEKGYDtdvgERGGQMSGGEKQRIAIA 629
Cdd:PRK11650 79 AMVFQNYALYPHmSVRENMAYGLkirgmpkAEIE-ERVAEAAR-------ILELEPLLD----RKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 59275972 630 RALIREPQVLILDEVTSALD 649
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
479-680 |
1.12e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERK----VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS------- 547
Cdd:PRK11629 6 LQCDNLCKRY---QEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 548 ----------YQHHYLH------RKVAMvgqePVLFSGSikdniaygladcsleRVQEAARRAnaHSFISQLekGYDTDV 611
Cdd:PRK11629 83 elrnqklgfiYQFHHLLpdftalENVAM----PLLIGKK---------------KPAEINSRA--LEMLAAV--GLEHRA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 612 GERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER 680
Cdd:PRK11629 140 NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqgtAFLVVTHDLQLAKR 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
497-701 |
2.79e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 84.34 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyQHHYLHRKVAMVGQEPVLFSG-SIKDNI 575
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 A-----YGLADCSL-ERVQEAARRANAHSFISQLEKGYdtdvgerggqmSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:cd03265 95 YiharlYGVPGAERrERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 650 TES-EHM--VQEALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:cd03265 164 PQTrAHVweYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
493-715 |
2.84e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL---ERfYQPQQGEILLDGQPLhsyqhhyLHRKV----------AM 559
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI-------LELSPderaragiflAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 vgQEPVLFSG-SIKD--NIAYGladcslERVQEAARRANAHSFISQLEK--GYDTDVGERG---GqMSGGEKQRIAIARA 631
Cdd:COG0396 84 --QYPVEIPGvSVSNflRTALN------ARRGEELSAREFLKLLKEKMKelGLDEDFLDRYvneG-FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSC--PSQTLLVIAH--RLKTIERADQIILIDQGTVLEQGTHqELMDR--K 705
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALEleE 233
|
250
....*....|
gi 59275972 706 GGYYKLRERL 715
Cdd:COG0396 234 EGYDWLKEEA 243
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
163-451 |
3.37e-18 |
|
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: 85.62 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVID--ILASQykwndfLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRM---- 236
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGD------LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLlydl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 237 KVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGL 316
Cdd:cd18546 75 RLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 317 LQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHtLKTRRDTVR--AVYVLLRRLT 394
Cdd:cd18546 155 ATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFA-ELSDDY-RDARLRAQRlvAIYFPGVELL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 395 ALVMQVAMLYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFgDMLNSVGAA 451
Cdd:cd18546 233 GNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVF-DSYQQARAA 288
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
479-701 |
4.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPTRQ--ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY---- 552
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQEP--VLFSGSIKDNIAYGLADCSLERvQEAARRAnahsfISQLEK-GYDTDVGERGG-QMSGGEKQRIAI 628
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIA-----AEKLEMvGLADEFWEKSPfELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTSC--PSQTLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhqSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
483-705 |
6.74e-18 |
|
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: 84.52 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplhsyqhhylhrKVAMVGQ 562
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EPVLFSGSIKDNIAYGLAdCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILD 642
Cdd:cd03291 106 FSWIMPGTIKENIIFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 643 EVTSALDTESEhmvQEALTSC-----PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:cd03291 185 SPFGYLDVFTE---KEIFESCvcklmANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
479-649 |
7.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.41 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYP--TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHH----Y 552
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQ--EPVLFSGSIKDNIAYGLADCSLERvQEAARRAnahsfisqLEK----GYDTDVGERGG-QMSGGEKQR 625
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALA--------REKlalvGISESLFEKNPfELSGGQMRR 153
|
170 180
....*....|....*....|....
gi 59275972 626 IAIARALIREPQVLILDEVTSALD 649
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-430 |
9.95e-18 |
|
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: 84.54 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDF----------------LTAIILMGLYSLGSSFSagcrgGLFM 226
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPlvpaslgpadprgqlwLLGGLTVAAFLLESLFQ-----YLSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 227 CAINSFTSRM----KVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWK 302
Cdd:cd18565 76 VLWRRFAQRVqhdlRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 303 LTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDT 382
Cdd:cd18565 156 LALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 59275972 383 VRAVYVLLRRLTALVMQVAMLYYGRLFIQ------RGQMSTGNLVSFILYQSNL 430
Cdd:cd18565 236 LRAAFFPVIRLVAGAGFVATFVVGGYWVLdgpplfTGTLTVGTLVTFLFYTQRL 289
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
479-705 |
1.07e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYP--TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY---- 552
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQ--EPVLFSGSIKDNIAYGLADCSLERvQEAARRAnahsfISQLEK-GYDTDVGERGG-QMSGGEKQRIAI 628
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKA-----LKWLKKvGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 629 ARALIREPQVLILDEVTSALDTESEHMVQEALTS--CPSQTLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyqKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
491-709 |
1.12e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLErFYQPQ----QGEILLDGQPLHSYQhhyLHRKVAMVgQEPVL 566
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKE---MRAISAYV-QQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 567 FSGSI--------------KDNIAyglADCSLERVQEAARRANahsfisqLEKGYDTDVGERGGQ--MSGGEKQRIAIAR 630
Cdd:TIGR00955 110 FIPTLtvrehlmfqahlrmPRRVT---KKEKRERVDEVLQALG-------LRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVqealtscpSQTLLVIAHRLKTI------------ERADQIILIDQGTVLEQGTH 698
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSV--------VQVLKGLAQKGKTIictihqpsselfELFDKIILMAEGRVAYLGSP 251
|
250
....*....|...
gi 59275972 699 QELMD--RKGGYY 709
Cdd:TIGR00955 252 DQAVPffSDLGHP 264
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
479-691 |
1.33e-17 |
|
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: 79.80 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplhsyqhhylhrkva 558
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 mvgqepvlfsgsiKDNIAYgladcslervqeaarranahsfisqLEkgydtdvgerggQMSGGEKQRIAIARALIREPQV 638
Cdd:cd03221 62 -------------TVKIGY-------------------------FE------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 639 LILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH-R--LKTIerADQIILIDQGT 691
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
494-687 |
1.93e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIlldgqplhsyqHHYLHRKVAMVGQ---EPVLFSGS 570
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseVPDSLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 571 IKDNIAYGL-ADCSLERVQEAARRAnahSFISQLEK-GYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:NF040873 74 VRDLVAMGRwARRGLWRRLTRDDRA---AVDDALERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 59275972 649 DTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILI 687
Cdd:NF040873 151 DAESRERIIALLAEEHARgaTVVVVTHDLELVRRADPCVLL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
496-705 |
2.27e-17 |
|
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: 86.89 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplhsyqhhylhrKVAMVGQEPVLFSGSIKDNI 575
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 576 AYGLADCSLeRVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEhm 655
Cdd:TIGR01271 508 IFGLSYDEY-RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE-- 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 656 vQEALTSC-----PSQTLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:TIGR01271 585 -KEIFESClcklmSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
493-708 |
2.82e-17 |
|
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: 80.65 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERF--YQPQQGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG 569
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 -SIKDniaygladcslervqeaarranahsFISQLEKGYdtdvgerggqmSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:cd03217 92 vKNAD-------------------------FLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 649 DTESEHMVQEALTSC--PSQTLLVIAHRLKTIE--RADQIILIDQGTVLEQGThQELMDR--KGGY 708
Cdd:cd03217 136 DIDALRLVAEVINKLreEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGD-KELALEieKKGY 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
479-701 |
2.83e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFsypTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQ--PLHSYQHHYLHRK 556
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 -VAMVGQEPVLFSG-SIKDNIAYGLADCSleRVQEAARRAnahSFISQLEKgydtdVGERGG------QMSGGEKQRIAI 628
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDNVAYPLREHT--QLPAPLLHS---TVMMKLEA-----VGLRGAaklmpsELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 629 ARALIREPQVLILDEVTSALDTESE----HMVQEaLTSCPSQTLLVIAHRL-KTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMgvlvKLISE-LNSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
482-704 |
4.25e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYPtrqeRKVLQGFSLELRPGQLTALVGPSGGGKS-TCVSLLERF---YQPQQGEILLDGQPLHSYQHHylHRKV 557
Cdd:PRK10418 8 RNIALQAA----QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEP-VLFsgsikdNIAYGLADCSLERVQEAARRANAHSFISQLEkgydtDVG----ER-----GGQMSGGEKQRIA 627
Cdd:PRK10418 82 ATIMQNPrSAF------NPLHTMHTHARETCLALGKPADDATLTAALE-----AVGlenaARvlklyPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 628 IARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQT---LLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRalgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
.
gi 59275972 704 R 704
Cdd:PRK10418 231 A 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
493-708 |
5.31e-17 |
|
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: 81.15 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL--ERFYQPQQGEILLDGQPLHSYQHHYLHRK---VAMvgQEPVLF 567
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPDERARAglfLAF--QYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 568 SG-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEK--GYDTDVGERG---GqMSGGEKQRIAIARALIREPQVLIL 641
Cdd:TIGR01978 90 PGvSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRSvneG-FSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 642 DEVTSALDTESEHMVQEALTSCPSQT--LLVIAHRLKTIE--RADQIILIDQGTVLEQGThQELMDR--KGGY 708
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREPDrsFLIITHYQRLLNyiKPDYVHVLLDGRIVKSGD-VELAKEleAKGY 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
506-696 |
6.63e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 506 PGQ-LTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHYL---HRKVAMVGQEPVLFSG-SIKDNIAYGL 579
Cdd:PRK11144 22 PAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLppeKRRIGYVFQDARLFPHyKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 580 AdcslervqeAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEA 659
Cdd:PRK11144 102 A---------KSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 59275972 660 LtSCPSQTL----LVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:PRK11144 171 L-ERLAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
483-701 |
7.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERK---VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHY-LHRKVA 558
Cdd:PRK13633 9 NVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEP--VLFSGSIKDNIAYGLADCSL------ERVQEAARRANAHSFisqleKGYDTDVgerggqMSGGEKQRIAIAR 630
Cdd:PRK13633 89 MVFQNPdnQIVATIVEEDVAFGPENLGIppeeirERVDESLKKVGMYEY-----RRHAPHL------LSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
491-702 |
7.36e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.41 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLE-RFYQPQ-------QGEILLDGQPLHSYQHHYLHRKVAMVGQ 562
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 --EPVlFSGSIKDNIAYGLadcslervQEAARRANAHS-----FISQ-LEK-GYDTDVGERGGQMSGGEKQRIAIARAL- 632
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR--------YPHARRAGALThrdgeIAWQaLALaGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 633 --------IREPQVLILDEVTSALDTESEHMVQE---ALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQE 700
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDtvrRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
..
gi 59275972 701 LM 702
Cdd:PRK13547 242 VL 243
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-703 |
7.61e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQ-----GEILLDGQPLHSYQHHYLH--RKVAMVGQEPVLFS 568
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 G-SIKDNIAYGLADCSL--------ERVQEAARRANAHSFISQLEKGYdtdvgerGGQMSGGEKQRIAIARALIREPQVL 639
Cdd:PRK14267 99 HlTIYDNVAIGVKLNGLvkskkeldERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 640 ILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEyTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
496-701 |
1.64e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 79.49 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG-SIKD 573
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 574 NIAYGLadcslervqEAARRANAH--SFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTE 651
Cdd:TIGR03410 95 NLLTGL---------AALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 59275972 652 SEHMVQEALTSCPSQT----LLVIAHRLKTIERADQIILIDQGTVLEQGTHQEL 701
Cdd:TIGR03410 166 IIKDIGRVIRRLRAEGgmaiLLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
474-704 |
1.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 474 TLTGHVHFHNLSFSYPTRQ--ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHS---- 547
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 548 -YQHHYLHRKVAMVGQEP--VLFSGSIKDNIAYGLADCSLERvQEAARRANAHSFISQLEKGYdtdVGERGGQMSGGEKQ 624
Cdd:PRK13645 82 iKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTESEH---MVQEALTSCPSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQG---- 696
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGspfe 237
|
250
....*....|
gi 59275972 697 --THQELMDR 704
Cdd:PRK13645 238 ifSNQELLTK 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
492-695 |
2.77e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 492 QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY---QHHYLH-RKVAMVGQE---- 563
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSfmli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 PVLfsgsikdniaygladCSLERVQ---------EAARRANAHSFISQLekgydtDVGER----GGQMSGGEKQRIAIAR 630
Cdd:PRK10584 101 PTL---------------NALENVElpallrgesSRQSRNGAKALLEQL------GLGKRldhlPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCP---SQTLLVIAHRLKTIERADQIILIDQGTVLEQ 695
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
495-698 |
3.06e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYqPQ---QGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG- 569
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIKDNIAYGLADCSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALd 649
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 650 TESEHMV--------QEALTSCpsqtlLVIAHRLKTIER-ADQIilidqgTVLEQGTH 698
Cdd:PRK13549 175 TESETAVlldiirdlKAHGIAC-----IYISHKLNEVKAiSDTI------CVIRDGRH 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
496-702 |
3.18e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 496 VLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPVLFSG-SIKDN 574
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 575 IAYG------LADCSLERVQEAARRANAHSFISQL-EKGYDTdvgerggqMSGGEKQRIAIARALIREPQVLILDEVTSA 647
Cdd:PRK10253 102 VARGryphqpLFTRWRKEDEEAVTKAMQATGITHLaDQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 648 LDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK10253 174 LDISHQIDLLELLSELNREkgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-702 |
3.42e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 500 FSLELRPGQLTALVGPSGGGKSTcvsLLERF--YQPQQGEILLDGQPLHSYQHHYL-HRKVAMVGQEPVLFSGSIKDNIA 576
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 577 YGLADCSLERVQEAARRANAHSFisQLekgydTDVGERG-GQMSGGEKQRIAIARALIR-------EPQVLILDEVTSAL 648
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEAL--GL-----DDKLGRSvNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 649 DTESEHMVQEALTSCPSQTLLVI--AHRL-KTIERADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVmsSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
477-705 |
3.49e-16 |
|
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: 79.51 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSYpTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQpQQGEILLDGQPLHSYQHHYLHRK 556
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQEPVLFSGSIKDNI-AYGlaDCSLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIRE 635
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 636 PQVLILDEVTSALDTESEHMVQEALTSCPSQ-TLLVIAHRLKTIERADQIILIDQGTVLEQGTHQELMDRK 705
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-702 |
3.56e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQ-----PLHSYQHhylhRKV 557
Cdd:PRK10895 8 NLAKAY---KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARAR----RGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 558 AMVGQEPVLFSG-SIKDNIAYGLA---DCSLERVQEAARRANAHSFISQLEKGYdtdvgerGGQMSGGEKQRIAIARALI 633
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQirdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 634 REPQVLILDEVTSALDTES--------EHMVQEALtscpsqTLLVIAHRLK-TIERADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISvidikriiEHLRDSGL------GVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
207-425 |
8.79e-16 |
|
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: 78.86 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 207 MGLYSL-------GSSFSAGCRGGLFMCAINSFTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNV 279
Cdd:cd18558 58 MTLYAYyyliigaIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 280 NVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTE 359
Cdd:cd18558 138 GVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQ 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 360 RSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSFIL 425
Cdd:cd18558 218 QKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFF 283
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
490-658 |
1.18e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 490 TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQ----PLHSYQHHYLHRKVAMvgqEPV 565
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRNAM---KPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 LfsgSIKDNIA-----YGLADCSLErvqEAARRANAHsfisqlekgydtDVGER-GGQMSGGEKQRIAIARALIREPQVL 639
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEELDIA---AALEAVGLA------------PLAHLpFGYLSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....*....
gi 59275972 640 ILDEVTSALDTESEHMVQE 658
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAE 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
479-690 |
1.67e-15 |
|
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: 75.36 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPT-RQERKVLQGFSLELRPGQLTALVGPSGGGKSTcvsLLERFYQPQ-----QGEILLDGQPLHSyqhhY 552
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQEPVLFSGSikdniaygladcsleRVQEAARranahsFISQLekgydtdvgeRGgqMSGGEKQRIAIARAL 632
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNL---------------TVREALR------FSALL----------RG--LSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 633 IREPQVLILDEVTSALDTESEHMVQEAL--TSCPSQTLLVIAHR--LKTIERADQIILIDQG 690
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLkkLADSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
482-662 |
2.93e-15 |
|
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: 74.70 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSyptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYlHRKVAMVG 561
Cdd:TIGR01189 4 RNLACS---RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVLFSG-SIKDNIAYGLADCSLER--VQEAArranahsfisqlekgydTDVGERG------GQMSGGEKQRIAIARAL 632
Cdd:TIGR01189 80 HLPGLKPElSALENLHFWAAIHGGAQrtIEDAL-----------------AAVGLTGfedlpaAQLSAGQQRRLALARLW 142
|
170 180 190
....*....|....*....|....*....|
gi 59275972 633 IREPQVLILDEVTSALDTESEHMVQEALTS 662
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
502-649 |
3.01e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 502 LELRPGQLTALVGPSGGGKST---CVSLLERFyqpQQGEILLDGQPLHSYQHHylHRKVAMVGQEPVLFSG-SIKDNIAY 577
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTllrMIAGLEDI---TSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHlSVAENMSF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 578 GLADCSLERvQEAARRANAHSFISQLEKGYDtdvgERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:PRK11000 99 GLKLAGAKK-EEINQRVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
493-649 |
3.96e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAM---VGQEPVLFSG 569
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLpltVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIKDNIAygladCSLERVQEaarranAHSFISQLEKgydtdvgerggqMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:PRK09544 96 TKKEDIL-----PALKRVQA------GHLIDAPMQK------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
163-457 |
5.03e-15 |
|
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: 76.39 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAVLCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFM-CAINSfTSRMKVELF 241
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVlAGLRA-SRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 242 GALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQgvy 321
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQ--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 322 dNYYLRLTKEVQ--DSMARA--NEAAGETVAGIRTVRSFNTERSEASHYDHRLmDTHTlktrrdtvRAVYVLL--RR--- 392
Cdd:cd18580 157 -RYYLRTSRQLRrlESESRSplYSHFSETLSGLSTIRAFGWQERFIEENLRLL-DASQ--------RAFYLLLavQRwlg 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 393 -----LTALVMQVAMLyygrLFIQRGQMSTGNLVSFILYQS-NLGTNIRTLIYIFGDMLNSVGAAGKVFEY 457
Cdd:cd18580 227 lrldlLGALLALVVAL----LAVLLRSSISAGLVGLALTYAlSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
481-696 |
5.43e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAM 559
Cdd:PRK11614 8 FDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVLFSG-SIKDNIAYGLADCSLERVQEAARRANAhSFISQLEKGYdtdvgERGGQMSGGEKQRIAIARALIREPQV 638
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYE-LFPRLHERRI-----QRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 639 LILDEVTSAL---------DTeSEHMVQEALTscpsqTLLViahrlktIERADQII-LIDQGTVLEQG 696
Cdd:PRK11614 159 LLLDEPSLGLapiiiqqifDT-IEQLREQGMT-----IFLV-------EQNANQALkLADRGYVLENG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
486-692 |
5.76e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 486 FSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRKVAMVGQEPV 565
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 L---FSGSIKDNIAygLADC-----SLERVQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQ 637
Cdd:COG1101 91 MgtaPSMTIEENLA--LAYRrgkrrGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 638 VLILDEVTSALDTESEHMVQEaLTscpSQ-------TLLVIAHRLK-TIERADQIILIDQGTV 692
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLE-LT---EKiveennlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
495-702 |
1.37e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEI-------LLDGQPLHSYQHHYLHRKVAMVGQEPVLF 567
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 568 S-GSIKDNIAYGLadcSLERVQEAARRANAHSFISQlekGYDTDVGER-----GGQMSGGEKQRIAIARALIREPQVLIL 641
Cdd:TIGR03269 378 PhRTVLDNLTEAI---GLELPDELARMKAVITLKMV---GFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 642 DEVTSALD-------TESEHMVQEALtscpSQTLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELM 702
Cdd:TIGR03269 452 DEPTGTMDpitkvdvTHSILKAREEM----EQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
162-454 |
2.44e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 74.05 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 162 LLVGAFIFLSLAVLCEMFIPFYTGKVIDILASQykwNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAI---NSFTSRMKV 238
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITP---GTLDGLTGFILLYLGLILIQALSVFLFIRLAGkieMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 239 ELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQ 318
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 319 GVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYdhrlmDTHTLKTRRDTVRAVyvllrRLTALVM 398
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREF-----KELTEEMRRASVRAA-----RLSALFL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 399 QVAM----------LYYGRLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18540 230 PIVLflgsiatalvLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
491-678 |
3.37e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYlHRKVAMVGQEPvlfsgS 570
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQP-----G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 571 IKD------NIAYGladCSLERVQEAARRANAhsfisqLEKgydtdVGERG------GQMSGGEKQRIAIARALIREPQV 638
Cdd:PRK13538 85 IKTeltaleNLRFY---QRLHGPGDDEALWEA------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 59275972 639 LILDEVTSALDTES-----EHMVQEA-------LTScpSQTLLVIAHRLKTI 678
Cdd:PRK13538 151 WILDEPFTAIDKQGvarleALLAQHAeqggmviLTT--HQDLPVASDKVRKL 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
491-694 |
4.43e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYqhhylhRKVAMVgqEPVLFSGS 570
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG------REASLI--DAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 571 IKDNIAYgLADCSLERVQEAARRanahsfisqlekgYDtdvgerggQMSGGEKQRIAIARALIREPQVLILDEVTSALDT 650
Cdd:COG2401 112 FKDAVEL-LNAVGLSDAVLWLRR-------------FK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 651 ES----EHMVQEALTSCpSQTLLVIAHRlKTIERA---DQIILIDQGTVLE 694
Cdd:COG2401 170 QTakrvARNLQKLARRA-GITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
163-460 |
4.67e-14 |
|
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: 73.31 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 163 LVGAFIFLSLAV-LCEMFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKVELF 241
Cdd:cd18555 3 LLISILLLSLLLqLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 242 GALVKQEISFFETIKTGDITSRL-STDTTK---MARAVALNVNVLLrtlikIVGMLSLMMSLSWKLTLLMLmetpVTGLL 317
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRAnSNVYIRqilSNQVISLIIDLLL-----LVIYLIYMLYYSPLLTLIVL----LLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 318 QGVYDNYYLRLTKEVQD----SMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRL 393
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQeeivAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 394 TALVMQVAMLYYGRLFIQRGQMSTGNLVSFilyqSNLGTNIRTLIYIFGDMLNSVgaaGKVFEYLDR 460
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGELIAF----SSLAGSFLTPIVSLINSYNQF---ILLKSYLER 293
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
460-696 |
6.96e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 460 REPQVSTKGTLQPETLtghVHFHNLSFSYPTR--------QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFY 531
Cdd:PRK10261 298 QEPPIEQDTVVDGEPI---LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 532 QPQQGEILLDGQ---PLHSYQHHYLHRKVAMVGQEPVLF---SGSIKDNIAYGLADCSLERVQEAARRanahsfISQLEk 605
Cdd:PRK10261 375 ESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASldpRQTVGDSIMEPLRVHGLLPGKAAAAR------VAWLL- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 606 gydtdvgERGG-----------QMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVI 671
Cdd:PRK10261 448 -------ERVGllpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfgiAYLFI 520
|
250 260
....*....|....*....|....*.
gi 59275972 672 AHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:PRK10261 521 SHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
495-704 |
7.08e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERF--YQPQQGEIL----------------LDGQP-------LHSYQ 549
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPcpvcggtLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 550 HHY------------------LHRKVAMVGQEPVLfsgsikDNIAYGLADCSLErVQEAARRAnaHSFISQLEKGYDTDV 611
Cdd:TIGR03269 94 VDFwnlsdklrrrirkriaimLQRTFALYGDDTVL------DNVLEALEEIGYE-GKEAVGRA--VDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 612 GERggQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILI 687
Cdd:TIGR03269 165 IAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgiSMVLTSHWPEVIEDlSDKAIWL 242
|
250
....*....|....*..
gi 59275972 688 DQGTVLEQGTHQELMDR 704
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
497-697 |
7.48e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGqplHSYQH--HYLHRK--VAMVGQE-PVLFSGSI 571
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKldHKLAAQlgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 KDNIAYGLAD----CSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSA 647
Cdd:PRK09700 98 LENLYIGRHLtkkvCGVNIIDWREMRVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 59275972 648 L-DTESEH--MVQEALTScPSQTLLVIAHRLKTIERadqiiLIDQGTVLEQGT 697
Cdd:PRK09700 176 LtNKEVDYlfLIMNQLRK-EGTAIVYISHKLAEIRR-----ICDRYTVMKDGS 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
480-658 |
8.97e-14 |
|
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: 74.59 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPTRqeRKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLdgQPlhsyqhhylHRKVAM 559
Cdd:TIGR03719 6 TMNRVSKVVPPK--KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP---------GIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 560 VGQEPVL-FSGSIKDNIAYGLADC--------------------------SLERVQEAARRANAHSFISQLEKG------ 606
Cdd:TIGR03719 73 LPQEPQLdPTKTVRENVEEGVAEIkdaldrfneisakyaepdadfdklaaEQAELQEIIDAADAWDLDSQLEIAmdalrc 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 607 --YDTDVGErggqMSGGEKQRIAIARALIREPQVLILDEVTSALDTES----EHMVQE 658
Cdd:TIGR03719 153 ppWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
495-653 |
1.09e-13 |
|
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: 74.09 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYqPQ---QGEILLDGQPLHSYQHHYLHRK-VAMVGQEPVLFSG- 569
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIKDNIAYGlADCSLE--RVQEAARRANAHSFISQLeKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSA 647
Cdd:TIGR02633 94 SVAENIFLG-NEITLPggRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
....*.
gi 59275972 648 LdTESE 653
Cdd:TIGR02633 172 L-TEKE 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
492-678 |
1.41e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 492 QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ--QGEILLDGQPLHSYqhhyLHRKVAMVGQEPVLFSG 569
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ----ILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 -SIKDNIAYgladCSLERVQEAARRAN----AHSFISQL--EKGYDTDVGE---RGgqMSGGEKQRIAIARALIREPQVL 639
Cdd:PLN03211 155 lTVRETLVF----CSLLRLPKSLTKQEkilvAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*....
gi 59275972 640 ILDEVTSALDTESEHMVqealtscpSQTLLVIAHRLKTI 678
Cdd:PLN03211 229 ILDEPTSGLDATAAYRL--------VLTLGSLAQKGKTI 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
483-705 |
2.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSY----PTrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEI---LLDGQPLHSYQHHY--- 552
Cdd:PRK13651 7 NIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEkvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 ------------------LHRKVAMVGQ--EPVLFSGSIKDNIAYGLADCSLERvQEAARRANahSFISQLekGYDTDVG 612
Cdd:PRK13651 85 eklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAA--KYIELV--GLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 613 ERGG-QMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTI-ERADQIILID 688
Cdd:PRK13651 160 QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgkTIILVTHDLDNVlEWTKRTIFFK 239
|
250
....*....|....*...
gi 59275972 689 QGTVLEQG-THQELMDRK 705
Cdd:PRK13651 240 DGKIIKDGdTYDILSDNK 257
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
481-694 |
3.14e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYPTrqerkvlQGFS-----LELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSY-QHHYLH 554
Cdd:PRK10522 325 LRNVTFAYQD-------NGFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 555 rkvamvgqepvLFSGSIKDniaYGLADCSLERVQEAARRANAHSFISQLEKGYDTDVgeRGG-----QMSGGEKQRIAIA 629
Cdd:PRK10522 398 -----------LFSAVFTD---FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLEL--EDGrisnlKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 630 RALIREPQVLILDEVTSALD--------TESEHMVQEAltscpSQTLLVIAHRLKTIERADQIILIDQGTVLE 694
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEM-----GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
488-688 |
3.23e-13 |
|
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: 70.13 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 488 YPTRQERKVLQGFSLELRPGQLT-----ALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLhSYQHHYLHRKVAMVGQ 562
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EpVLFSgsiKDNIAYGLADCSLERVQEAarranahsfisQLEKGYDTDVGErggqMSGGEKQRIAIARALIREPQVLILD 642
Cdd:cd03237 80 D-LLSS---ITKDFYTHPYFKTEIAKPL-----------QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 59275972 643 EVTSALDTESEHMVQEALTSC---PSQTLLVIAHRLKTIER-ADQIILID 688
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFaenNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
495-707 |
3.33e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYqPQ---QGEILLDGQP-----LHSYQHH---YLHRKVAMVgqe 563
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcrfkdIRDSEALgivIIHQELALI--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 PVLfsgSIKDNI-------AYGLADCslervQEAARRAnahsfISQLEK-GYDTDVGERGGQMSGGEKQRIAIARALIRE 635
Cdd:NF040905 91 PYL---SIAENIflgneraKRGVIDW-----NETNRRA-----RELLAKvGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 636 PQVLILDEVTSAL-DTESEHMV-------QEALTScpsqtlLVIAHRLKTIER-ADQIilidqgTVLEQGTHQELMDRKG 706
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLdlllelkAQGITS------IIISHKLNEIRRvADSI------TVLRDGRTIETLDCRA 225
|
.
gi 59275972 707 G 707
Cdd:NF040905 226 D 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
490-701 |
3.36e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 490 TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTC-----------------VSLLERFYQpQQGEILLDGQPLHSyQHHY 552
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagshIELLGRTVQ-REGRLARDIRKSRA-NTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 553 LHRKVAMVGQEPVLfsgsikDNIAYG-LADCSLER--VQEAARRANAHSFISQLEKGYDTDVGERGGQMSGGEKQRIAIA 629
Cdd:PRK09984 91 IFQQFNLVNRLSVL------ENVLIGaLGSTPFWRtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQEL 701
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
495-696 |
5.75e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH------------SYQHHYL----HRKVA 558
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeagiGIIHQELnlipQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 ---MVGQEPVLFSGSIKDNIAYGLADCSLER--VQEAARRanahsfisqlekgydtdvgeRGGQMSGGEKQRIAIARALI 633
Cdd:PRK10762 98 eniFLGREFVNRFGRIDWKKMYAEADKLLARlnLRFSSDK--------------------LVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 634 REPQVLILDEVTSAL-DTESEHM--VQEALTS--CpsqTLLVIAHRLKTI-ERADQIilidqgTVLEQG 696
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLfrVIRELKSqgR---GIVYISHRLKEIfEICDDV------TVFRDG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
480-696 |
6.28e-13 |
|
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: 68.71 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQP---------LHSyqh 550
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllglgggFNP--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 551 hylhrkvAMVGQEPVLFSGSIkdniaYGladcsLERVQEAARRANAHSFiSQLEKGYDTDVGErggqMSGGEKQRIAIAR 630
Cdd:cd03220 98 -------ELTGRENIYLNGRL-----LG-----LSRKEIDEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQGTVLEQG 696
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
489-712 |
6.35e-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: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 489 PTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLhRKVAMV-GQE---- 563
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFA-RRIGVVfGQRsqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 ---PVLFSGSIKDNIaYgladcsleRVQEAARRANAHSFISQLEKG--YDTDVgeRggQMSGGEKQRIAIARALIREPQV 638
Cdd:COG4586 109 wdlPAIDSFRLLKAI-Y--------RIPDAEYKKRLDELVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 639 LILDEVTSALDTESEHMVQEAL--------TscpsqTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRKGGYY 709
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLkeynrergT-----TILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 59275972 710 KLR 712
Cdd:COG4586 251 TIV 253
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
179-451 |
9.95e-13 |
|
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: 69.51 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 179 FIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLfmcaINSFTSRMKVELFGALVKQ----EISFFET 254
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYL----LDYFANRIDLSLLSDFYKHllslPLSFFAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 255 IKTGDITSRLSTD------TTKMARAVALNvnvllrtLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVYDNYYLRL 328
Cdd:cd18568 96 RKVGDIITRFQENqkirrfLTRSALTTILD-------LLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 329 TKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLmdTHTLKTRRDTVRAVYVL--LRRLTALVMQVAMLYYG 406
Cdd:cd18568 169 SREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF--AKALNTRFRGQKLSIVLqlISSLINHLGTIAVLWYG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 59275972 407 RLFIQRGQMSTGNLVSFILYQSNLGTNIRTLIYIfGDMLNSVGAA 451
Cdd:cd18568 247 AYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL-WDELQETRIS 290
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
495-703 |
1.16e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK---VAMVGQEPvLFS--- 568
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LASlnp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 -GSIKDNIAYGLadcslervqeaarranaHSFISQLEKGydtDVGERGGQM------------------SGGEKQRIAIA 629
Cdd:PRK15079 114 rMTIGEIIAEPL-----------------RTYHPKLSRQ---EVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 630 RALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMD 703
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYH 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
499-649 |
1.64e-12 |
|
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: 70.58 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 499 GFSL----ELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIllDGQP-----LHSYQ----HHYLHR------KVA- 558
Cdd:COG1245 87 GFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYFKKlangeiKVAh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 ---MVGQEPVLFSGSIKDniaygladcSLERVQEaarRANAHSFISQL--EKGYDTDVGErggqMSGGEKQRIAIARALI 633
Cdd:COG1245 165 kpqYVDLIPKVFKGTVRE---------LLEKVDE---RGKLDELAEKLglENILDRDISE----LSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 59275972 634 REPQVLILDEVTSALD 649
Cdd:COG1245 229 RDADFYFFDEPSSYLD 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
494-645 |
5.58e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLerF--YQPQQGEILLDGQPLH--SYqHHYLHRKVAMV----GQEPV 565
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVRirSP-RDAIRAGIAYVpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 LFSGSIKDNIAygLAdcSLER------VQEAARRANAHSFISQLE---KGYDTDVGerggQMSGGEKQRIAIARALIREP 636
Cdd:COG1129 342 VLDLSIRENIT--LA--SLDRlsrgglLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
....*....
gi 59275972 637 QVLILDEVT 645
Cdd:COG1129 414 KVLILDEPT 422
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
477-696 |
6.76e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 477 GHVHFHNLSFSYPTrqerkvlqgfslelrpGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLhrk 556
Cdd:PRK15056 19 GHTALRDASFTVPG----------------GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQE-------PVLfsgsIKDNIAYGladcsleRVQEAA--RRANAHSFISQLEKGYDTDVGE----RGGQMSGGEK 623
Cdd:PRK15056 80 VAYVPQSeevdwsfPVL----VEDVVMMG-------RYGHMGwlRRAKKRDRQIVTAALARVDMVEfrhrQIGELSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 624 QRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTI-ERADQIILIdQGTVLEQG 696
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgkTMLVSTHNLGSVtEFCDYTVMV-KGTVLASG 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
494-649 |
7.26e-12 |
|
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: 64.76 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYLHRK-VAMV----GQEPVLFS 568
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIAygladcslervqeaarranahsfISQLekgydtdvgerggqMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:cd03215 93 LSVAENIA-----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
.
gi 59275972 649 D 649
Cdd:cd03215 136 D 136
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
492-698 |
1.32e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.20 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 492 QERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL--ERFYQPQQGEILLDGQPLHSYQ-HHYLHRKVAMVGQEPVLFS 568
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 G-SIKDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYD--TDVGERGGQM--SGGEKQRIAIARALIREPQVLILDE 643
Cdd:PRK09580 92 GvSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKmpEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 644 VTSALDTESEHMVQEALTSC--PSQTLLVIAHRLKTIE--RADQIILIDQGTVLEQGTH 698
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLrdGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGDF 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
479-649 |
1.59e-11 |
|
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: 64.21 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSF-SYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKST----CVSLLERFYQPqQGEILLDGQPLHSYQHHYl 553
Cdd:cd03233 4 LSWRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFsgsikdniayglADCSLERVQEAARRANAHSFIsqlekgydtdvgeRGgqMSGGEKQRIAIARALI 633
Cdd:cd03233 82 PGEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170
....*....|....*.
gi 59275972 634 REPQVLILDEVTSALD 649
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
505-649 |
1.60e-11 |
|
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: 65.08 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 505 RPGQLTALVGPSGGGKSTCVSLLERFYQPQQG---------EIL--LDGQPLHSYQHHYLH------RKVAMVGQEPVLF 567
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQNYFTKLLEgdvkviVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 568 SGSIKDNiaygladcsLERVQEaarRANAHSFISQLEKgydTDVGERG-GQMSGGEKQRIAIARALIREPQVLILDEVTS 646
Cdd:cd03236 104 KGKVGEL---------LKKKDE---RGKLDELVDQLEL---RHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
...
gi 59275972 647 ALD 649
Cdd:cd03236 169 YLD 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
494-651 |
2.16e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQL-----TALVGPSGGGKSTCVSLLERFYQPQQGEIllDGQPLHSYQHHYLHRKVAMVGQEpvlFS 568
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVED---LL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIayglaDCSLERVqEAARRAnahsfisQLEKGYDTDVGErggqMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:PRK13409 422 RSITDDL-----GSSYYKS-EIIKPL-------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
...
gi 59275972 649 DTE 651
Cdd:PRK13409 485 DVE 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
494-651 |
3.73e-11 |
|
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: 66.35 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQL-----TALVGPSGGGKSTCVSLLERFYQPQQGEIllDGQPLHSYQHHYLHRKVAMvgqepvlfs 568
Cdd:COG1245 348 TKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDG--------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 gsikdniaygladcsleRVQEAARRANAHSFIS-----------QLEKGYDTDVGErggqMSGGEKQRIAIARALIREPQ 637
Cdd:COG1245 417 -----------------TVEEFLRSANTDDFGSsyykteiikplGLEKLLDKNVKD----LSGGELQRVAIAACLSRDAD 475
|
170
....*....|....
gi 59275972 638 VLILDEVTSALDTE 651
Cdd:COG1245 476 LYLLDEPSAHLDVE 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
483-655 |
3.81e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRqerKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHYLHRKVAMVG 561
Cdd:PRK10982 3 NISKSFPGV---KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QE-PVLFSGSIKDNIAYGLADCSLERVQEAARRANAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLI 640
Cdd:PRK10982 80 QElNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170
....*....|....*.
gi 59275972 641 LDEVTSAL-DTESEHM 655
Cdd:PRK10982 158 MDEPTSSLtEKEVNHL 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
480-652 |
6.83e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 480 HFHNLSFSYPtrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGE-ILLDGQplhsyqhhylhrKVA 558
Cdd:PRK11819 8 TMNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI------------KVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPVLFS------------GSIKD--------NIAYGLADCSLE-------RVQEAARRANAHSFISQLEKG----- 606
Cdd:PRK11819 74 YLPQEPQLDPektvrenveegvAEVKAaldrfneiYAAYAEPDADFDalaaeqgELQEIIDAADAWDLDSQLEIAmdalr 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 59275972 607 ---YDTDVGerggQMSGGEKQRIAIARALIREPQVLILDEVTSALDTES 652
Cdd:PRK11819 154 cppWDAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
483-692 |
9.49e-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: 64.85 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ-QGEILLDGQPLHSYQ-HHYLHRKVAMV 560
Cdd:TIGR02633 262 NLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 GQE-------PVLFSGSikdNIAYGLAD--CSLERVQEAARRANAHSFISQLE-KGYDTDVGErgGQMSGGEKQRIAIAR 630
Cdd:TIGR02633 342 PEDrkrhgivPILGVGK---NITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKvKTASPFLPI--GRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 631 ALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRL-KTIERADQIILIDQGTV 692
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgvAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
482-701 |
1.63e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSY-PTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH---------SYQHH 551
Cdd:PRK10261 16 ENLNIAFmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqvielSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 552 YLHRKV-----AMVGQEPVL-----------FSGSIKDNIAYGLADCSLE--RVQEAARRANAHSFISQLEKgydtdvge 613
Cdd:PRK10261 96 AQMRHVrgadmAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEakRMLDQVRIPEAQTILSRYPH-------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 614 rggQMSGGEKQRIAIARALIREPQVLILDEVTSALD-TESEHMVQ--EALTSCPSQTLLVIAHRLKTI-ERADQIILIDQ 689
Cdd:PRK10261 168 ---QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQ 244
|
250
....*....|..
gi 59275972 690 GTVLEQGTHQEL 701
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
499-649 |
2.21e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 499 GFSL----ELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEilLDGQP-----LHSYQ----HHYLHR---------- 555
Cdd:PRK13409 87 GFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevLKRFRgtelQNYFKKlyngeikvvh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 556 KVAMVGQEPVLFSGSIKDniaygladcSLERVQEaarRANAHSFISQL--EKGYDTDVGErggqMSGGEKQRIAIARALI 633
Cdd:PRK13409 165 KPQYVDLIPKVFKGKVRE---------LLKKVDE---RGKLDEVVERLglENILDRDISE----LSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 59275972 634 REPQVLILDEVTSALD 649
Cdd:PRK13409 229 RDADFYFFDEPTSYLD 244
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
157-423 |
2.86e-10 |
|
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: 61.84 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 157 RPDTLLLVGAFIFLSLAVLcemFIPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRM 236
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 237 KVELFGALVKQEISFFETIKTGDITSRLS-TDTTK---MARAVALNVNVLLrtlikIVGMLSLMMSLSWKLTLLMLMETP 312
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISeLDTIRgflTGTALTTLLDVLF-----SVIYIAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 313 VTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDT--HTLKTRR--DTVRAVYV 388
Cdd:cd18782 153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSlgEGFKLTVlgTTSGSLSQ 232
|
250 260 270
....*....|....*....|....*....|....*
gi 59275972 389 LLRRLTalvmQVAMLYYGRLFIQRGQMSTGNLVSF 423
Cdd:cd18782 233 FLNKLS----SLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
482-711 |
3.49e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILL---DGQPLHSY-----QHHYL 553
Cdd:PRK11701 10 RGLTKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYalseaERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HR-KVAMVGQEP---VLFSGSIKDNIAygladcslERVQEA-AR-----RANAHSFISQLEkgYDTD-VGERGGQMSGGE 622
Cdd:PRK11701 87 LRtEWGFVHQHPrdgLRMQVSAGGNIG--------ERLMAVgARhygdiRATAGDWLERVE--IDAArIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 623 KQRIAIARALIREPQVLILDEVTSALDTEsehmVQ-------EALTSCPSQTLLVIAHRLkTIER--ADQIILIDQGTVL 693
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQarlldllRGLVRELGLAVVIVTHDL-AVARllAHRLLVMKQGRVV 231
|
250
....*....|....*....
gi 59275972 694 EQG-THQELMDRKGGYYKL 711
Cdd:PRK11701 232 ESGlTDQVLDDPQHPYTQL 250
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
493-673 |
7.23e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEI-LLDGQPLHSYQHHYLHrkvamvgqepvlfsgsi 571
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE----------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 kdniaYGLADCS-LERVQEAARRANAHSFISQLEK-GYDTD-VGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:PRK10636 387 -----FLRADESpLQHLARLAPQELEQKLRDYLGGfGFQGDkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180
....*....|....*....|....*
gi 59275972 649 DTESEHMVQEALTSCPSqTLLVIAH 673
Cdd:PRK10636 462 DLDMRQALTEALIDFEG-ALVVVSH 485
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
479-673 |
7.27e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLdGQPLhsyqhhylhrKVA 558
Cdd:TIGR03719 323 IEAENLTKAF---GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQepvlFSGSIKDN------IAYGLadcslERVQEAARRANAHSFISQLE-KGydTDVGERGGQMSGGEKQRIAIARA 631
Cdd:TIGR03719 389 YVDQ----SRDALDPNktvweeISGGL-----DIIKLGKREIPSRAYVGRFNfKG--SDQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH 673
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG-CAVVISH 498
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
240-454 |
7.92e-10 |
|
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: 60.51 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 240 LFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQG 319
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 320 VYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRA-VYVLLRRLTALVM 398
Cdd:cd18554 165 YFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAkTFSAVNTITDLAP 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 399 QVAMLYYGRLFIQrGQMSTGNLVSFILYQSNLGTNIRTLIYIFGDMLNSVGAAGKV 454
Cdd:cd18554 245 LLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
483-649 |
8.62e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ-QGEILLDGQPLH-SYQHHYLHRKVAMV 560
Cdd:PRK13549 264 NLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 561 -------GQEPVLfsgSIKDNIAYGLAD--CSLERVQEAARRANAHSFISQLeKGYDTDVGERGGQMSGGEKQRIAIARA 631
Cdd:PRK13549 344 pedrkrdGIVPVM---GVGKNITLAALDrfTGGSRIDDAAELKTILESIQRL-KVKTASPELAIARLSGGNQQKAVLAKC 419
|
170
....*....|....*...
gi 59275972 632 LIREPQVLILDEVTSALD 649
Cdd:PRK13549 420 LLLNPKILILDEPTRGID 437
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
483-682 |
1.10e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHYlHRKVAMVGQ 562
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 E----PVLfsgSIKDNIAYGLADCSLE-RVQEAARranahsfISQLEKGYDTDVgergGQMSGGEKQRIAIARALIREPQ 637
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPGAvGITELCR-------LFSLEHLIDYPC----GLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 59275972 638 VLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERAD 682
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKggAVLLTSHQDLPLNKAD 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
494-697 |
1.13e-09 |
|
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: 62.34 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSyQHHYLHRKVAMVGQEPVLFSG-SIK 572
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 DNIAYgLADCSLERVQEAARRANAhsfisQLE-KGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTE 651
Cdd:TIGR01257 1022 EHILF-YAQLKGRSWEEAQLEMEA-----MLEdTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 59275972 652 SEHMVQEALTSCPS-QTLLVIAHRLKTIE-RADQIILIDQGTVLEQGT 697
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSgRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
504-700 |
1.25e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 504 LRPGQLTALVGPSGGGKSTCV----SLLERFYQPQQGEILLDGQPLHSYQHHYlHRKVAMVGQEPVLF-SGSIKDNIAY- 577
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGITPEEIKKHY-RGDVVYNAETDVHFpHLTVGETLDFa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 578 ------GLADCSLERVQEAARRANAHSFISQLEKGYDTDVGE---RGgqMSGGEKQRIAIARALIREPQVLILDEVTSAL 648
Cdd:TIGR00956 163 arcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 649 DTESEHMVQEALTSCPS---QTLLVIAHRL--KTIERADQIILIDQGTVLEQGTHQE 700
Cdd:TIGR00956 241 DSATALEFIRALKTSANildTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
497-696 |
4.36e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 497 LQGFSLELRPGQLTALVGPSGGGKSTCVslLERFYQPQQgEILLDGQPLHSYQhhylhrkvamvgqePVLFSGSIKDNIA 576
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGK-ARLISFLPKFSRN--------------KLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 577 YGLadcslervqeaarranahsfisqlekGYDTdVGERGGQMSGGEKQRIAIARALIREPQ--VLILDEVTSALDTESEH 654
Cdd:cd03238 74 VGL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 59275972 655 MVQEALTSCPSQ--TLLVIAHRLKTIERADQIILI------DQGTVLEQG 696
Cdd:cd03238 127 QLLEVIKGLIDLgnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
484-652 |
4.86e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 484 LSFSY-PtrqerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLerfyqpqQGEILLDGQPLHSYQHhylhRKVAMVGQ 562
Cdd:PRK11147 11 LSFSDaP------LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIYEQD----LIVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 EP---VlfSGSIKDNIAYGLA------------------DCS------LERVQEAARRANAHSF-------ISQLEKGYD 608
Cdd:PRK11147 74 DPprnV--EGTVYDFVAEGIEeqaeylkryhdishlvetDPSeknlneLAKLQEQLDHHNLWQLenrinevLAQLGLDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 59275972 609 TDVGErggqMSGGEKQRIAIARALIREPQVLILDEVTSALDTES 652
Cdd:PRK11147 152 AALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
473-652 |
6.84e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 473 ETLTGHVHFH--NLSFSYPTRQE-RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLL-ERFYQP--QQGEILLDGQPLH 546
Cdd:TIGR00956 752 EKESGEDIFHwrNLTYEVKIKKEkRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGRPLD 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 547 S-------Y-QHHYLHRKVAMVgQEPVLFSG--------SIKDNIAYgladcslerVQEAARranahsfISQLEKGYDTD 610
Cdd:TIGR00956 832 SsfqrsigYvQQQDLHLPTSTV-RESLRFSAylrqpksvSKSEKMEY---------VEEVIK-------LLEMESYADAV 894
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 59275972 611 VGERGGQMSGGEKQRIAIARALIREPQVLI-LDEVTSALDTES 652
Cdd:TIGR00956 895 VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-697 |
9.36e-09 |
|
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: 54.69 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 506 PGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLdgqplhsyqhhylhrkvamvgqepvlfsgsikdniayglADCSLE 585
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 586 RVQEAARRANahsfisqlekgydTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEA------ 659
Cdd:smart00382 42 LEEVLDQLLL-------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 59275972 660 --LTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQGT 697
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
495-674 |
1.47e-08 |
|
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: 58.22 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLE--------RFYQPQQGEILLdgqplhsyqhhylhrkvamVGQEPVL 566
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY-------------------VPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 567 FSGSIKDNIAY----------GLADCSLERVQEAARRANahsfISQLEKGYDTdVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:TIGR00954 527 TLGTLRDQIIYpdssedmkrrGLSDKDLEQILDNVQLTH----ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190
....*....|....*....|....*....|....*...
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCpSQTLLVIAHR 674
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLCREF-GITLFSVSHR 638
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
483-673 |
2.76e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPTRQerkVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQG-------------------------- 536
Cdd:PRK11147 324 NVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklevayfdqhraeldpektv 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 537 ---------EILLDGQPLH--SYQHHYL-HRKVAMVgqePVlfsgsikdniaygladcslervqeaarRAnahsfisqle 604
Cdd:PRK11147 401 mdnlaegkqEVMVNGRPRHvlGYLQDFLfHPKRAMT---PV---------------------------KA---------- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 605 kgydtdvgerggqMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH 673
Cdd:PRK11147 441 -------------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG-TVLLVSH 495
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
495-702 |
3.07e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 495 KVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLErfyqpqqGE-ILLDGQPLHSYQH---------------HYLHRKVA 558
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALA-------GElPLLSGERQSQFSHitrlsfeqlqklvsdEWQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQEPvlfsgsikDNIAYGLADCSLERVQEAARRAN-AHSF-ISQLekgydtdVGERGGQMSGGEKQRIAIARALIREP 636
Cdd:PRK10938 90 MLSPGE--------DDTGRTTAEIIQDEVKDPARCEQlAQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 637 QVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTI-ERADQIILIDQGTVLEQGTHQELM 702
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSgiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEIL 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
617-701 |
6.44e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 617 QMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTI-ERADQIILIDQGTV 692
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenmALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*....
gi 59275972 693 LEQGTHQEL 701
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
493-703 |
6.68e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERF--YQPQQGEILLDGQPLHSYQ-HHYLHRKVAMVGQEPVLFSG 569
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SikDNIAYGLADCSLERVQEAARRANAHSFISQLEKGYDT----------DVGErggQMSGGEKQRIAIARALIREPQVL 639
Cdd:CHL00131 99 V--SNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLvgmdpsflsrNVNE---GFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 640 ILDEVTSALDTESehmvqealtscpsqtLLVIAHRLKTIERADQ-IILIdqgtvleqgTH-QELMD 703
Cdd:CHL00131 174 ILDETDSGLDIDA---------------LKIIAEGINKLMTSENsIILI---------THyQRLLD 215
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
234-423 |
7.31e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 54.44 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 234 SRMKVELFGALVKQEISFFETIKTGDITSRLStDTTKMARAValnVNVLLRTLIKIVGMLSL---MMSLSWKLTLLMLME 310
Cdd:cd18783 75 ARLALRTFDRLLSLPIDFFERTPAGVLTKHMQ-QIERIRQFL---TGQLFGTLLDATSLLVFlpvLFFYSPTLALVVLAF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 311 TPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTV----RAV 386
Cdd:cd18783 151 SALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLsnwpQTL 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 59275972 387 YVLLRRLtalvMQVAMLYYGRLFIQRGQMSTGNLVSF 423
Cdd:cd18783 231 TGPLEKL----MTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
501-685 |
1.09e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 501 SLELRPGQLTALVGPSGGGKST---CVSLLErfyqpqqgeilldgqplhSYQHHYLHRKvamvgqepvlfsgsikdniay 577
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTildAIGLAL------------------GGAQSATRRR--------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 578 glaDCSLERVQEAARRANAHSFISQLekgydtdvgerggqmSGGEKQRIAIARAL----IREPQVLILDEVTSALDTESE 653
Cdd:cd03227 56 ---SGVKAGCIVAAVSAELIFTRLQL---------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....
gi 59275972 654 HMVQEAL--TSCPSQTLLVIAHRLKTIERADQII 685
Cdd:cd03227 118 QALAEAIleHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
483-706 |
1.63e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 483 NLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEIlldgqplhsyqhhylhrkvamvgq 562
Cdd:PRK15064 324 NLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 563 epvlfSGSIKDNIAYgladCSLERVQEAARRANAHSFISQLEKGYDTDVGERG--GQM--------------SGGEKQRI 626
Cdd:PRK15064 377 -----KWSENANIGY----YAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVRGtlGRLlfsqddikksvkvlSGGEKGRM 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 627 AIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAHrlktiER------ADQIILI-DQGTVLEQGTHQ 699
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG-TLIFVSH-----DRefvsslATRIIEItPDGVVDFSGTYE 521
|
....*..
gi 59275972 700 ELMDRKG 706
Cdd:PRK15064 522 EYLRSQG 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
491-694 |
2.08e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 491 RQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLerfyqpqQGEILLDGQPLhSYQHHYlhrKVAMVGQE-PVLFSG 569
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSY-TFPGNW---QLAWVNQEtPALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 570 SIK-----------------------DNIAYGLADCSLERVQEAARRANAHSFISQLekGYDTDVGERG-GQMSGGEKQR 625
Cdd:PRK10636 80 ALEyvidgdreyrqleaqlhdanernDGHAIATIHGKLDAIDAWTIRSRAASLLHGL--GFSNEQLERPvSDFSGGWRMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 626 IAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAHR---LKTIerADQIILIDQGTVLE 694
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG-TLILISHDrdfLDPI--VDKIIHIEQQSLFE 226
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
233-423 |
3.02e-07 |
|
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: 52.89 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 233 TSRMKVEL----FGALVKQEISFFETIKTGDITSRLStdttKMARAVALNVNVLLRTLIKIVGM---LSLMMSLSWKLTL 305
Cdd:cd18588 70 TNRIDAELgarlFRHLLRLPLSYFESRQVGDTVARVR----ELESIRQFLTGSALTLVLDLVFSvvfLAVMFYYSPTLTL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 306 LMLMETPVTGLLQGVYDNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLmdTHTLKTRRDTVR- 384
Cdd:cd18588 146 IVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELL--ARYVKASFKTANl 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 59275972 385 -AVYVLLRRLTALVMQVAMLYYGRLFIQRGQMSTGNLVSF 423
Cdd:cd18588 224 sNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
479-706 |
3.08e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYptrQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQH--HYLHRk 556
Cdd:NF033858 2 ARLEGVSHRY---GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrrAVCPR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVGQ------EPVLfsgSIKDNIA-----YGLAdcslerVQEAARRanahsfISQLEKgyDTDVG---ER-GGQMSGG 621
Cdd:NF033858 78 IAYMPQglgknlYPTL---SVFENLDffgrlFGQD------AAERRRR------IDELLR--ATGLApfaDRpAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 622 EKQRIAIARALIREPQVLILDEVTSALDTES--------EHMVQEAltscPSQTLLVIAHRLKTIERADQIILIDQGTVL 693
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfweliDRIRAER----PGMSVLVATAYMEEAERFDWLVAMDAGRVL 216
|
250
....*....|...
gi 59275972 694 EQGTHQELMDRKG 706
Cdd:NF033858 217 ATGTPAELLARTG 229
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
166-446 |
3.22e-07 |
|
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: 52.61 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILASQyKWNDFLTAIILMGLYSL---GSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLA-KVKDLESAVTLILLYALlrfSSKLLKELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIK-IVGMLSLMMSLSWKLTLLMLMETPVTGLLQGVY 321
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLElIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 322 DNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHtlKTRRdTVRAVYVLLRRLTALVMQVA 401
Cdd:cd18560 160 TEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQ--KSSV-KVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 402 M---LYYGRLFIQRGQMSTGNLVS-----FILYQ--SNLGTNIRTLIYIFGDMLN 446
Cdd:cd18560 237 LtlgLLLAGYRVVDGGLSVGDFVAvntyiFQLFQplNFLGTIYRMIIQSLTDMEN 291
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
166-421 |
5.91e-07 |
|
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: 51.73 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 166 AFIFLSLAVLCEMFIPFYTGKVIDILaSQYKWNDFLTAIILMGLYSL---GSSFSAGCRGGLFMCAINSFTSRMKVELFG 242
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL-SAPASALLAVPLLLLLAYGLariLSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 243 ALVKQEISFFETIKTGDITS---RLSTDTTKMARAVALNVnvlLRTLIKIVGMLSLMMSL-SWKLTLLMLmetpVTGLLQ 318
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALSRaieRGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITL----VTVALY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 319 GVY----DNYYLRLTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRDTVRAVYVLLRRLT 394
Cdd:cd18582 153 VAFtikvTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALI 232
|
250 260
....*....|....*....|....*..
gi 59275972 395 ALVMQVAMLYYGRLFIQRGQMSTGNLV 421
Cdd:cd18582 233 ISLGLTAIMLLAAQGVVAGTLTVGDFV 259
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
481-656 |
6.43e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 481 FHNLSFSYptrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDG-------QPLHSYQHHYL 553
Cdd:PRK13541 4 LHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 554 HRKVAMVGQEPVLFSGSIKDniaygladcSLERVQEAARRANAHSFISqlEKGYdtdvgerggQMSGGEKQRIAIARALI 633
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYN---------SAETLYAAIHYFKLHDLLD--EKCY---------SLSSGMQKIVAIARLIA 139
|
170 180
....*....|....*....|...
gi 59275972 634 REPQVLILDEVTSALDTESEHMV 656
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENRDLL 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
501-649 |
1.05e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 501 SLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHH--------YLH--RKvamvGQEPVLfSGS 570
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivYISedRK----RDGLVL-GMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 571 IKDNIAYgladCSLE-------RVQEAARRANAHSFIsQLEKGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDE 643
Cdd:PRK10762 347 VKENMSL----TALRyfsraggSLKHADEQQAVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
....*.
gi 59275972 644 VTSALD 649
Cdd:PRK10762 422 PTRGVD 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
612-707 |
1.05e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 612 GERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSC--PSQTLLVIAHRLKTIER-ADQIILID 688
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*....
gi 59275972 689 QGTVLEQGTHQELMDRKGG 707
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
482-662 |
1.18e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 482 HNLSFSyptRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHhylHRKVAMVG 561
Cdd:PRK13543 15 HALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 562 QEPVLFSG-SIKDNIAY--GLADCSLERVQEAARRanahsfISQLEKGYDTDVgergGQMSGGEKQRIAIARALIREPQV 638
Cdd:PRK13543 89 HLPGLKADlSTLENLHFlcGLHGRRAKQMPGSALA------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPL 158
|
170 180
....*....|....*....|....
gi 59275972 639 LILDEVTSALDTESEHMVQEALTS 662
Cdd:PRK13543 159 WLLDEPYANLDLEGITLVNRMISA 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
498-690 |
1.34e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 498 QGF---SLELRPGQLTALVGPSGGGKStcvSLLERFY---QPQQGEILLDGQPLHSYqhhylhrkvamvgqepvlfsgSI 571
Cdd:PRK15439 277 EGFrniSLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINAL---------------------ST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 572 KDNIAYGLADCSLERVQ-----EAARRANAHSFISQ-----LEKGYDTDVGER---------------GGQMSGGEKQRI 626
Cdd:PRK15439 333 AQRLARGLVYLPEDRQSsglylDAPLAWNVCALTHNrrgfwIKPARENAVLERyrralnikfnhaeqaARTLSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59275972 627 AIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIER-ADQIILIDQG 690
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQnvAVLFISSDLEEIEQmADRVLVMHQG 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
569-708 |
1.61e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIAYGLADC--SLERVQEAARRANAHSFISQLEKGYDTDVgERGGQMSGGEKQRIAIARALIREPQVLILDEVTS 646
Cdd:PLN03073 295 GVDKDAVSQRLEEIykRLELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTN 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 647 ALDTESEHMVQEALTSCPsQTLLVIAHRLKTIERADQIILIDQGtvleqgthQELMDRKGGY 708
Cdd:PLN03073 374 HLDLHAVLWLETYLLKWP-KTFIVVSHAREFLNTVVTDILHLHG--------QKLVTYKGDY 426
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
479-673 |
2.69e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 479 VHFHNLSFSYPtrqERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLdGQPLhsyqhhylhrKVA 558
Cdd:PRK11819 325 IEAENLSKSFG---DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 559 MVGQepvlFSGSIKDN------IAYGLadcslERVQEAARRANAHSFISQLE-KGydTDVGERGGQMSGGEKQRIAIARA 631
Cdd:PRK11819 391 YVDQ----SRDALDPNktvweeISGGL-----DIIKVGNREIPSRAYVGRFNfKG--GDQQKKVGVLSGGERNRLHLAKT 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 59275972 632 LIREPQVLILDEVTSALDTESEHMVQEALTSCPSqTLLVIAH 673
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLDVETLRALEEALLEFPG-CAVVISH 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
617-702 |
9.57e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 617 QMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSC---PSQTLLVIAHRLKTIER-ADQIILIDQGTV 692
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqnNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 59275972 693 LEQGTHQELM 702
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
494-649 |
1.22e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 494 RKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHYLHRKVAMV----GQEPVLFS 568
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCpedrKAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 569 GSIKDNIA------YGLADCSLERVQEAArraNAHSFISQLE---KGYDTDVGerggQMSGGEKQRIAIARALIREPQVL 639
Cdd:PRK11288 346 HSVADNINisarrhHLRAGCLINNRWEAE---NADRFIRSLNiktPSREQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170
....*....|
gi 59275972 640 ILDEVTSALD 649
Cdd:PRK11288 419 LLDEPTRGID 428
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
610-701 |
1.71e-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: 48.47 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 610 DVG---ERGGQ----MSGGEKQRIAIARALIRE---PQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKT 677
Cdd:TIGR00630 815 DVGlgyIRLGQpattLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgnTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 59275972 678 IERADQIILIDQ------GTVLEQGTHQEL 701
Cdd:TIGR00630 895 IKTADYIIDLGPeggdggGTVVASGTPEEV 924
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
493-685 |
2.18e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 45.92 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 493 ERKVLQGF-------SLELRPGqLTALVGPSGGGKSTCVSLLeRFyqpqqgeiLLDGQPLHSyqhhylhrkvaMVGQ--E 563
Cdd:cd03278 2 KKLELKGFksfadktTIPFPPG-LTAIVGPNGSGKSNIIDAI-RW--------VLGEQSAKS-----------LRGEkmS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 564 PVLFSGSiKDNIAYGLADCSLErvqeAARRANAHSFISQlekGydtDVGE----------RGGQMSGGEKQRIAIAR--A 631
Cdd:cd03278 61 DVIFAGS-ETRKPANFAEVTLT----FDNSDGRYSIISQ---G---DVSEiieapgkkvqRLSLLSGGEKALTALALlfA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 59275972 632 LIRE---PQVlILDEVTSALDtesEH-------MVQEAltSCPSQtLLVIAHRLKTIERADQII 685
Cdd:cd03278 130 IFRVrpsPFC-VLDEVDAALD---DAnverfarLLKEF--SKETQ-FIVITHRKGTMEAADRLY 186
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
503-701 |
2.58e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 503 ELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ---QGEILLDGQPLHSYQHHYLHR----KVAMVGQEP----------- 564
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDPmtslnpymrvg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 565 -----VL-----------FSGSIKdniaygladcSLERVQ--EAARRAN--AHSFisqlekgydtdvgerggqmSGGEKQ 624
Cdd:PRK09473 118 eqlmeVLmlhkgmskaeaFEESVR----------MLDAVKmpEARKRMKmyPHEF-------------------SGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 625 RIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQ---TLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQE 700
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfntAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248
|
.
gi 59275972 701 L 701
Cdd:PRK09473 249 V 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
621-706 |
3.17e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 621 GEKQRIAIARALIREPQVLILDEVTSALDTES-----EHMVQeaLTSCPSQTLLVIAHRLKTIERADQIILIDQGTVLEQ 695
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfwRLLIE--LSREDGVTIFISTHFMNEAERCDRISLMHAGRVLAS 478
|
90
....*....|.
gi 59275972 696 GTHQELMDRKG 706
Cdd:NF033858 479 DTPAALVAARG 489
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
201-396 |
3.43e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 46.44 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 201 LTAIILMGLYSLGSSFsAGCRGglfmcainsfTSRMKVELFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVN 280
Cdd:cd18602 61 LGAVILSLVTNLAGEL-AGLRA----------ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 281 VLLRTLIKIVGMLSLMMSLSWKLTLLMLmetPVTGL---LQgvydNYYLRLTKEVQ--DSMARANEAAG--ETVAGIRTV 353
Cdd:cd18602 130 RLLRFLLLCLSAIIVNAIVTPYFLIALI---PIIIVyyfLQ----KFYRASSRELQrlDNITKSPVFSHfsETLGGLTTI 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 354 RSFNTERsEASHYDHRLMDTHT------------LKTRRDTVRAVYVLLRRLTAL 396
Cdd:cd18602 203 RAFRQQA-RFTQQMLELIDRNNtaflflntanrwLGIRLDYLGAVIVFLAALSSL 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
618-697 |
8.58e-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: 44.91 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 618 MSGGEKQRIAIARALIRE---PQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQIILIDQ--- 689
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgnTVVVIEHNLDVIKCADWIIDLGPegg 249
|
90
....*....|.
gi 59275972 690 ---GTVLEQGT 697
Cdd:cd03271 250 dggGQVVASGT 260
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
167-370 |
8.90e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 45.21 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 167 FIFLSLAVLCEMFIPF----YTGKVIDILASQYKW--NDFLTA-IILMGLYSLGSSFsagcRGGLFMCAINSFTSRMKVE 239
Cdd:cd18605 5 LLSLILMQASRNLIDFwlsyWVSHSNNSFFNFINDsfNFFLTVyGFLAGLNSLFTLL----RAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 240 LFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLQg 319
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 59275972 320 vydNYYLRLTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTERSEASHYDHRL 370
Cdd:cd18605 160 ---RYYRATSRELKrlNSVNLSPLYThfSETLKGLVTIRAFRKQERFLKEYLEKL 211
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
240-375 |
1.77e-04 |
|
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: 44.23 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 240 LFGALVKQEISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLS-WkltllMLMETPVTGLLQ 318
Cdd:cd18601 98 MFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNpW-----VLIPVIPLVILF 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 319 GVYDNYYLRLTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTERSEASHYDhRLMDTHT 375
Cdd:cd18601 173 LFLRRYYLKTSREVKriEGTTRSPVFShlSSTLQGLWTIRAYSAQERFQEEFD-AHQDLHS 232
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
618-690 |
1.93e-04 |
|
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: 42.94 E-value: 1.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59275972 618 MSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEA---LTSCPSQTLLVIAHRLKTIERADQIILIDQG 690
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAirrLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
509-691 |
2.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 509 LTALVGPSGGGKSTCvsLLERFYQpqQGE-------------ILLDGQPLHSYQHH----------YLHRKVAMVGQEPV 565
Cdd:PRK00635 1518 LVAISGVSGSGKTSL--LLEGFYK--QACaliekgpsvfseiIFLDSHPQISSQRSdistyfdiapSLRNFYASLTQAKA 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 L------FSGSIKDN-------IAYGLAD-------------CSLERVQEAARR-------------------ANAHSFI 600
Cdd:PRK00635 1594 LnisasmFSTNTKQGqcsdcwgLGYQWIDrafyalekrpcptCSGFRIQPLAQEvvyegkhfgqllqtpieevAETFPFL 1673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 601 SQLEK----------GYdTDVGERGGQMSGGEKQRIAIARALI---REPQVLILDEVTSALDTESEHMVQEALTSCPSQ- 666
Cdd:PRK00635 1674 KKIQKplqalidnglGY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLg 1752
|
250 260
....*....|....*....|....*.
gi 59275972 667 -TLLVIAHRLKTIERADQIILIDQGT 691
Cdd:PRK00635 1753 hSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
618-685 |
2.54e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59275972 618 MSGGEKQRIAIARALI---REPQVLILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQII 685
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQghTVVIIEHNMHVVKVADYVL 882
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
504-720 |
3.29e-04 |
|
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: 44.23 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 504 LRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLHSYQHHyLHRKVA-----------MVGQEPVLFSGSIK 572
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-VHQNMGycpqfdaiddlLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 573 dniayGLADCSLERVqeaarranAHSFISQLekGYDTDVGERGGQMSGGEKQRIAIARALIREPQVLILDEVTSALDTES 652
Cdd:TIGR01257 2041 -----GVPAEEIEKV--------ANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 59275972 653 EHMVQEALTSC--PSQTLLVIAHRLKTIER-ADQIILIDQGTVLEQGTHQELMDRKGGYYKLRERLFTEDD 720
Cdd:TIGR01257 2106 RRMLWNTIVSIirEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKD 2176
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
160-423 |
3.85e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 42.96 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 160 TLLLVGAFI-FLSLAVlcemfiPFYTGKVIDILASQYKWNDFLTAIILMGLYSLGSSFSAGCRGGLFMCAINSFTSRMKV 238
Cdd:cd18566 6 QVLLASLFInILALAT------PLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 239 ELFGALVKQEISFFETIKTGDITSRLsTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLMETPVTGLLq 318
Cdd:cd18566 80 AAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 319 GVYDNYYLR-LTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDhRLMDTHTLKTRRDTVRAVyvLLRRLTALV 397
Cdd:cd18566 158 AILLGPILRrALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYE-RLQANAAYAGFKVAKINA--VAQTLGQLF 234
|
250 260
....*....|....*....|....*....
gi 59275972 398 MQVAM---LYYGRLFIQRGQMSTGNLVSF 423
Cdd:cd18566 235 SQVSMvavVAFGALLVINGDLTVGALIAC 263
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
490-649 |
5.23e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 490 TRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQQGEILLDGQPLH-SYQHHYLHRKVAMVGQ---EPV 565
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 566 LFSG-SIKDNIA-------------YGLADCSLERVQEAARRANAHSFISQLEKgydtDVGErggqMSGGEKQRIAIARA 631
Cdd:PRK09700 352 FFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLALKCHSVNQ----NITE----LSGGNQQKVLISKW 423
|
170
....*....|....*...
gi 59275972 632 LIREPQVLILDEVTSALD 649
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGID 441
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
249-458 |
5.80e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 42.45 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 249 ISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMMSLSWKLTLLMLmetpVTGLLQGVYDNYYLRL 328
Cdd:cd18604 91 LRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 329 TKEVQ--DSMARAN--EAAGETVAGIRTVRSFNTERSEASHYdHRLMDTHTlktrrdtvRAVYVL--LRR--------LT 394
Cdd:cd18604 167 SRELKrlESVARSPilSHFGETLAGLVTIRAFGAEERFIEEM-LRRIDRYS--------RAFRYLwnLNRwlsvridlLG 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59275972 395 ALVMQVAMLYygrlFIQRGQMSTGnLVSFIL-YQSNLGTNIRTLIYIFGDM---LNSVgaaGKVFEYL 458
Cdd:cd18604 238 ALFSFATAAL----LVYGPGIDAG-LAGFSLsFALGFSSAILWLVRSYNELeldMNSV---ERIQEYL 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
489-649 |
5.93e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 489 PTRQERKVLQGFSLELRPGQLTALVGPSGGGKS-TCVSLLERFY-QPQQGEILLDGQPLHsyqhhylhrkVAMVGQepvl 566
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYgRNISGTVFKDGKEVD----------VSTVSD---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 567 fsgSIKDNIAY--------GL-------ADCSLERVQEAARRA--NAHSFISQLEkGYDT-------DVGERGGQMSGGE 622
Cdd:NF040905 334 ---AIDAGLAYvtedrkgyGLnliddikRNITLANLGKVSRRGviDENEEIKVAE-EYRKkmniktpSVFQKVGNLSGGN 409
|
170 180
....*....|....*....|....*..
gi 59275972 623 KQRIAIARALIREPQVLILDEVTSALD 649
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
484-696 |
6.25e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 484 LSFSYPTRQERKVLQGFSLELRPGQLTALVGPSGGGKSTCVSLLERFYQPQ---QGEILLDGQPLHSY----QHHYLHRK 556
Cdd:PLN03140 168 LGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFvprkTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 557 VAMVG----QEPVLFSGSI-----------------KDNIAYGLADCSLERVQEAARRANAHSF------ISQLEKGYDT 609
Cdd:PLN03140 248 DVHVGvmtvKETLDFSARCqgvgtrydllselarreKDAGIFPEAEVDLFMKATAMEGVKSSLItdytlkILGLDICKDT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 610 DVGE---RGgqMSGGEKQRIAIARALIREPQVLILDEVTSALDTESEHMVQEALTSCPSQTLLVIAHRL-----KTIERA 681
Cdd:PLN03140 328 IVGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLlqpapETFDLF 405
|
250
....*....|....*
gi 59275972 682 DQIILIDQGTVLEQG 696
Cdd:PLN03140 406 DDIILLSEGQIVYQG 420
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
617-685 |
6.57e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 6.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 617 QMSGGEKQRIAIarALI-----REPQVL-ILDEVTSALDTES----EHMVQEAltSCPSQtLLVIAHRLKTIERADQII 685
Cdd:pfam02463 1077 LLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNvsrvANLLKEL--SKNAQ-FIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
249-374 |
6.65e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.46 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 249 ISFFETIKTGDITSRLSTDTTKMARAVALNVNVLLRTLIKIVGMLSLMM-SLSWkltlLMLMETPVTGLLQGVYdNYYLR 327
Cdd:cd18606 83 MSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIiYLPW----FAIALPPLLVLYYFIA-NYYRA 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 59275972 328 LTKEVQ--DSMARANEAA--GETVAGIRTVRSFNTErSEASHYDHRLMDTH 374
Cdd:cd18606 158 SSRELKrlESILRSFVYAnfSESLSGLSTIRAYGAQ-DRFIKKNEKLIDNM 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
617-685 |
1.29e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59275972 617 QMSGGEKQRIAIAR--ALIRE---PQVlILDEVTSALDtESE-----HMVQEAltSCPSQtLLVIAHRLKTIERADQII 685
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKVkpaPFC-ILDEVDAPLD-DANverfaNLLKEF--SKNTQ-FIVITHNKGTMEVADQLY 1162
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
618-685 |
1.79e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59275972 618 MSGGEKQRIAIARALIRE-PQVL-ILDEVTSALDTESEHMVQEALTSCPSQ--TLLVIAHRLKTIERADQII 685
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
616-649 |
2.21e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.21e-03
10 20 30
....*....|....*....|....*....|....
gi 59275972 616 GQMSGGEKQRIAIARALIREPQVLILDEVTSALD 649
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
616-687 |
5.39e-03 |
|
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: 38.74 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 616 GQMSGGEKQ------RIAIARALIREPQVLILDEVTSALDTES-EHMVQEALTSCPSQT---LLVIAHRLKTIERADQII 685
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKnfqLIVITHDEELVDAADHIY 193
|
..
gi 59275972 686 LI 687
Cdd:cd03240 194 RV 195
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
161-424 |
9.18e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 38.68 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 161 LLLVGAFIFLSLAVLCemfIPFYTGKVID--ILASQYkwnDFLT----AIILMGLYSLGSSFsagCRGGLFMCAINSFTS 234
Cdd:cd18779 5 GQILLASLLLQLLGLA---LPLLTGVLVDrvIPRGDR---DLLGvlglGLAALVLTQLLAGL---LRSHLLLRLRTRLDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 235 RMKVELFGALVKQEISFFETIKTGDITSRLSTDTtkMARAVALN--VNVLLRTLIkIVGMLSLMMSLSWKLTLLMLmetp 312
Cdd:cd18779 76 QLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNA--TIRELLTSqtLSALLDGTL-VLGYLALLFAQSPLLGLVVL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59275972 313 VTGLLQ-GVYDNYYLR---LTKEVQDSMARANEAAGETVAGIRTVRSFNTERSEASHYDHRLMDTHTLKTRRD----TVR 384
Cdd:cd18779 149 GLAALQvALLLATRRRvreLMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGrldaLVD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 59275972 385 AVYVLLRRLTALVmqvaMLYYGRLFIQRGQMSTGNLVSFI 424
Cdd:cd18779 229 ALLATLRLAAPLV----LLWVGAWQVLDGQLSLGTMLALN 264
|
|
| |
