|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
99-701 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 725.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 99 TVWLV-GTVAAALACLFWEITLPDTNEESNGKERKQKARVLFIRVIRLYRPDYILLFGAFVFLALAVLCEMFIPLYTGEV 177
Cdd:TIGR00958 108 WSWFVwSYGAALPAAALWAVLSSAGASEKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 178 IDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTD 257
Cdd:TIGR00958 188 IDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 258 TTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAV 337
Cdd:TIGR00958 268 TQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEAL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 338 SGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQ 417
Cdd:TIGR00958 348 SGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 418 QDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPDHNVLKDFSLELKPG 497
Cdd:TIGR00958 428 EQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 498 QITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERV 577
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEI 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 578 KEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQaLSCCPTQT 657
Cdd:TIGR00958 588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRASRT 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 29561855 658 LLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:TIGR00958 667 VLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
132-701 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 545.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 132 KQKARVLFIRVIRLYRPDYILLFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCR 211
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 212 GGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSW 291
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 292 KLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRD 371
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 372 TVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRK 451
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 452 SEV-SIDGNLMPKDLKGHVKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILL 530
Cdd:COG1132 322 PEIpDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 531 DGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSG 610
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 611 GEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSC-CPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHE 689
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|..
gi 29561855 690 ELMEKKGSYYKL 701
Cdd:COG1132 560 ELLARGGLYARL 571
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
156-444 |
3.43e-161 |
|
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: 466.43 E-value: 3.43e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLI 235
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 236 RQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHY 315
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 316 QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYY 395
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29561855 396 GRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
143-701 |
6.71e-149 |
|
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: 446.07 E-value: 6.71e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 143 IRLYRPDYIllfGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSF 222
Cdd:TIGR02204 13 VRPYRGRVL---AALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 223 TCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETP 302
Cdd:TIGR02204 90 VADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 303 LTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRR 382
Cdd:TIGR02204 170 LVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 383 MTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRKSEVSIDGN--L 460
Cdd:TIGR02204 250 VLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHpkT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 461 MPKDLKGHVKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQH 540
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 541 KYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIAR 620
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIAR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQALSCCPT-QTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYY 699
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAESEQLVQQALETLMKgRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
..
gi 29561855 700 KL 701
Cdd:TIGR02204 570 RL 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
458-682 |
1.44e-147 |
|
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: 429.20 E-value: 1.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 458 GNLMPKDLKGHVKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQD 537
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 538 YQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIA 617
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 618 IARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPT-QTLLVIAHRLKTIERADQIVVIDSGEL 682
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
129-704 |
2.82e-135 |
|
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: 415.39 E-value: 2.82e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 129 KERKQKARVL--FIRVIRLYRPDYILLFGAFVFLALAVLcemFIPLYTGEVID-ILGSHYQwDNFRSAIIFMGLFSLGSS 205
Cdd:COG2274 135 DKRGEKPFGLrwFLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDrVLPNQDL-STLWVLAIGLLLALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 206 FSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRL-STDT---TLMGRAVALNVNVLLrtlvkTLG 281
Cdd:COG2274 211 LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrDVESireFLTGSLLTALLDLLF-----VLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 282 MLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLM 361
Cdd:COG2274 286 FLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 362 ETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAA 441
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 442 GKVFEYQDRKSEVSIDGNLMPKD-LKGHVKFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERF 520
Cdd:COG2274 446 ERLDDILDLPPEREEGRSKLSLPrLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 521 YQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTD 600
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 601 VGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDS 679
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLrRLLKGRTVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|....*
gi 29561855 680 GELVEKGTHEELMEKKGSYYKLRER 704
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
138-708 |
2.35e-123 |
|
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: 379.83 E-value: 2.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 138 LFIRVIRLYRPDYILLFGAFVFLALAVLCEMFIPlytGEVIDILGSHYQWDNfRSAIIFMGLFSLGSSFSAG-CRGGLFM 216
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLA---ALLKPLLDDGFGGRD-RSVLWWVPLVVIGLAVLRGiCSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 217 C---AINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKL 293
Cdd:TIGR02203 77 LlswVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 294 TLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTV 373
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 374 RAIYlliRRMTEL--GMKVAMLYYGRLFI-QYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDR 450
Cdd:TIGR02203 237 GSIS---SPITQLiaSLALAVVLFIALFQaQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 451 KSEVSiDGNLMPKDLKGHVKFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILL 530
Cdd:TIGR02203 314 PPEKD-TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 531 DGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYG-LQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLS 609
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 610 GGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALS-CCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTH 688
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALErLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
570 580
....*....|....*....|
gi 29561855 689 EELMEKKGSYYKLRERLFSD 708
Cdd:TIGR02203 552 NELLARNGLYAQLHNMQFRE 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
469-701 |
1.07e-115 |
|
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: 347.99 E-value: 1.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQV 628
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 629 LILDEVTSSLDTESEQMVQQALS-CCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDrAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
469-702 |
4.50e-104 |
|
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: 317.64 E-value: 4.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQV 628
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 629 LILDEVTSSLDTESEQMVQQALS-CCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLR 702
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 ... |
156-444 |
1.74e-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: 310.40 E-value: 1.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLI 235
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 236 RQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHY 315
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 316 QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYY 395
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29561855 396 GRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
230-708 |
7.70e-100 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 318.89 E-value: 7.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 230 LFGSLIRQDIGFFETIKTGDITSRLSTDTTLmgraVALNVNVLLRTLVK----TLGMLYLMVSLSWKLTLLMLMETPLTG 305
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQ----VASSSSGALITVVRegasIIGLFIMMFYYSWQLSLILIVIAPIVS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 306 LLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDgrlmETHNlktrrdtvraiyllirRMTE 385
Cdd:PRK11176 180 IAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFD----KVSN----------------RMRQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 386 LGMKvaMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTL-----IYIFGDML------------NS-----VGAAGK 443
Cdd:PRK11176 240 QGMK--MVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLtagtiTVVFSSMIalmrplksltnvNAqfqrgMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 444 VFEYQDRKSEVSiDGNLMPKDLKGHVKFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQP 523
Cdd:PRK11176 318 LFAILDLEQEKD-EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 524 QQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQG-CSMERVKEAASKANAHSFISKLEKGYDTDVG 602
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 603 ERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGE 681
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
490 500
....*....|....*....|....*..
gi 29561855 682 LVEKGTHEELMEKKGSYYKLRERLFSD 708
Cdd:PRK11176 556 IVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
342-701 |
1.34e-98 |
|
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: 316.38 E-value: 1.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 342 TVKSFKTELGEAHRYDGRLM--ETHNLKTRR-----DTVRAIyllirrMTELGMkVAMLYYGRLFIQYGQMSTGN--LVS 412
Cdd:COG5265 230 TVKYFGNEAREARRYDEALAryERAAVKSQTslallNFGQAL------IIALGL-TAMMLMAAQGVVAGTMTVGDfvLVN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 413 FILYQqdlgdnirtlIYIFGDMLNSV------GAA--GKVFEYQDRKSEVSIDGNlmPKDLK---GHVKFQKLTFSY-PR 480
Cdd:COG5265 303 AYLIQ----------LYIPLNFLGFVyreirqALAdmERMFDLLDQPPEVADAPD--APPLVvggGEVRFENVSFGYdPE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 481 RPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGT 560
Cdd:COG5265 371 RP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDT 640
Cdd:COG5265 448 IAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 641 ESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:COG5265 528 RTERAIQAALrEVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
467-696 |
7.21e-98 |
|
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: 301.45 E-value: 7.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSK 546
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREP 626
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKG 696
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALeKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
424-696 |
3.08e-94 |
|
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: 303.60 E-value: 3.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 424 IRTLIYIFGDMLNSVGAAGKVFEYQDRKSEVSIDGNL-MPKDLKGHVKFQKLTFSYPrrPDHNVLKDFSLELKPGQITAL 502
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVAL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 503 VGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAAS 582
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 583 KANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVI 661
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALrRLAKGRTVILI 528
|
250 260 270
....*....|....*....|....*....|....*
gi 29561855 662 AHRLKTIERADQIVVIDSGELVEKGTHEELMEKKG 696
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
469-704 |
3.46e-92 |
|
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: 286.82 E-value: 3.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSY-PRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKV 547
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQ 627
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 628 VLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLRER 704
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALrDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
156-444 |
1.36e-91 |
|
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: 287.52 E-value: 1.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLI 235
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 236 RQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHY 315
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 316 QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYY 395
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29561855 396 GRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
225-704 |
6.58e-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: 295.14 E-value: 6.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 225 RVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGravalnvNVLLRTL-------VKTLGMLYLMVSLSWKLTLLM 297
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALD-------NLYLRVLlpllvalLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 298 LMETPLTGLLQNIYDTHYQK-LSKEVQDSMAQANDAAGEAVSGIRTVKSFktelGEAHRYDGRLMETHNLKTRRDTVRAI 376
Cdd:COG4987 162 ALGLLLAGLLLPLLAARLGRrAGRRLAAARAALRARLTDLLQGAAELAAY----GALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 377 YLLIRR-MTELGMK---VAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRKS 452
Cdd:COG4987 238 LSALAQaLLQLAAGlavVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 453 EVSIDGNLMPKDLKGHVKFQKLTFSYPRRPdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG 532
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 533 KPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGE 612
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 613 KQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLlEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|...
gi 29561855 692 MEKKGSYYKLRER 704
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
235-701 |
5.83e-84 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 277.37 E-value: 5.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 235 IRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTH 314
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRY 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 315 YQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELgeahRYDGRLMETH--NLKTRRDTVRAIYLLIRRMteLGMKVAM 392
Cdd:PRK10790 189 STPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQA----RFGERMGEASrsHYMARMQTLRLDGFLLRPL--LSLFSAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 393 LYYGrLFIQYGQMSTGN-----LVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDR-KSEVSIDGNLMPKdlk 466
Cdd:PRK10790 263 ILCG-LLMLFGFSASGTievgvLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGpRQQYGNDDRPLQS--- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSK 546
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSGTVRDNIAYGlQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREP 626
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHtTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
469-701 |
2.56e-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: 2.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYprRPDH-NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKV 547
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQ 627
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 628 VLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMhDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
265-701 |
1.56e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 270.68 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 265 VALNVNVLLRTLVKTLGMLYLMVSlswklTLLMLMetplTGLLQNIYDTHYQKLSKEVQDsmaqandaageAVSGIRTVK 344
Cdd:PRK13657 150 LALFMNWRLSLVLVVLGIVYTLIT-----TLVMRK----TKDGQAAVEEHYHDLFAHVSD-----------AIGNVSVVQ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 345 SF---KTELGEAHRYDGRLMETHNlktrrdTVR---AIYLLIRRM-TELGMkVAMLYYGRLFIQYGQMSTGNLVSFILYQ 417
Cdd:PRK13657 210 SYnriEAETQALRDIADNLLAAQM------PVLswwALASVLNRAaSTITM-LAILVLGAALVQKGQLRVGEVVAFVGFA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 418 QDLG---DNIRTLIYI----------FGDMLNSVGAAgkvfeyQDRksevsiDGNLMPKDLKGHVKFQKLTFSYP-RRPd 483
Cdd:PRK13657 283 TLLIgrlDQVVAFINQvfmaapkleeFFEVEDAVPDV------RDP------PGAIDLGRVKGAVEFDDVSFSYDnSRQ- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 hnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRD 563
Cdd:PRK13657 350 --GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIED 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESE 643
Cdd:PRK13657 428 NIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 644 QMVQQALSCCPT-QTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:PRK13657 508 AKVKAALDELMKgRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
155-701 |
1.18e-77 |
|
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: 263.34 E-value: 1.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 155 GAFVFLALAVLCEM----FIPLYTGEVID--ILGSHYQWdnFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKV 228
Cdd:TIGR03796 154 GALLYLLLAGLLLVlpglVIPAFSQIFVDeiLVQGRQDW--LRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTTLmgrAVALNVNvLLRTLVKTLGMLY---LMVSLSWKLTLLMLMETPLTG 305
Cdd:TIGR03796 232 RFLWHILRLPVRFFAQRHAGDIASRVQLNDQV---AEFLSGQ-LATTALDAVMLVFyalLMLLYDPVLTLIGIAFAAINV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 306 LLqniydthYQKLSKEVQDS----MAQANDAAGEAVSGIRTVKSFKTELGEAH---RYDGRLMETHNLKTRRDTVRAIYL 378
Cdd:TIGR03796 308 LA-------LQLVSRRRVDAnrrlQQDAGKLTGVAISGLQSIETLKASGLESDffsRWAGYQAKLLNAQQELGVLTQILG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 379 LI-RRMTELGmKVAMLYYGRLFIQYGQMSTG-----------------NLVSFILYQQDL-GDNIRtliyiFGDMLNSvg 439
Cdd:TIGR03796 381 VLpTLLTSLN-SALILVVGGLRVMEGQLTIGmlvafqslmssflepvnNLVGFGGTLQELeGDLNR-----LDDVLRN-- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 440 aagKVFEYQDRKSEVSIDGNLMPKdLKGHVKFQKLTFSYPR--RPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLL 517
Cdd:TIGR03796 453 ---PVDPLLEEPEGSAATSEPPRR-LSGYVELRNITFGYSPlePP---LIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 518 ERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGY 597
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGY 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 598 DTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL---SCcptqTLLVIAHRLKTIERADQI 674
Cdd:TIGR03796 606 DAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLrrrGC----TCIIVAHRLSTIRDCDEI 681
|
570 580
....*....|....*....|....*..
gi 29561855 675 VVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
469-681 |
2.16e-75 |
|
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: 240.36 E-value: 2.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSGTVRDNIayglqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIREPQV 628
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 629 LILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGE 681
Cdd:cd03228 118 LILDEATSALDPETEALILEALrALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
156-444 |
4.87e-74 |
|
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: 241.31 E-value: 4.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLI 235
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 236 RQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHY 315
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 316 QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYY 395
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29561855 396 GRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
234-715 |
8.40e-74 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 249.63 E-value: 8.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 234 LIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLM-VSLSWKLTLLMLMETPLTGLLQNIYD 312
Cdd:PRK10789 79 LSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 313 THYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMET--HNLKTRRDTVR---AIYLLIrrmtelG 387
Cdd:PRK10789 159 DQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkKNMRVARIDARfdpTIYIAI------G 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 388 M-KVAMLYYGRLFIQYGQMSTGNLVSFILYqqdLGDNIRTLIYIfGDMLNSV---GAAGKVFEYQDRKSEVSIDGNLMPK 463
Cdd:PRK10789 233 MaNLLAIGGGSWMVVNGSLTLGQLTSFVMY---LGLMIWPMLAL-AWMFNIVergSAAYSRIRAMLAEAPVVKDGSEPVP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 464 DLKGHVKFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYL 543
Cdd:PRK10789 309 EGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALI 623
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSY---- 698
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmy 547
|
490
....*....|....*...
gi 29561855 699 -YKLRERLFSDDKTTKQE 715
Cdd:PRK10789 548 rYQQLEAALDDAPEIREE 565
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
241-701 |
8.23e-73 |
|
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: 250.43 E-value: 8.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 241 FFETIKTGDITSRLsTDTTLMGRAVAlnvNVLLrTLVKTLGMLyLMVSL-----SWKLTLLMLMETPLTGLLQNIYDTHY 315
Cdd:TIGR01193 246 FFSTRRTGEIVSRF-TDASSIIDALA---STIL-SLFLDMWIL-VIVGLflvrqNMLLFLLSLLSIPVYAVIIILFKRTF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 316 QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYY 395
Cdd:TIGR01193 320 NKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWT 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 396 GRLFIQYGQMSTGNLVSF---ILYQQDLGDNIRTL------IYIFGDMLNSVGAAGKVFEYQDRKSEVSidgnlmpkDLK 466
Cdd:TIGR01193 400 GAYLVMRGKLTLGQLITFnalLSYFLTPLENIINLqpklqaARVANNRLNEVYLVDSEFINKKKRTELN--------NLN 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYPRrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSK 546
Cdd:TIGR01193 472 GDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSGTVRDNIAYGLQ-GCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIRE 625
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
265-713 |
1.40e-70 |
|
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: 241.33 E-value: 1.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 265 VALNVNVLLRTLVKTLGMLYLMVSLswkltllMLMETPLTGllQNIYDTHYQKLSKEVQDSMAQandaageaVSGIRTVK 344
Cdd:TIGR01192 150 TAFAMDWRLSIVLMVLGILYILIAK-------LVMQRTKNG--QAAVEHHYHNVFKHVSDSISN--------VSVVHSYN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 345 SFKTELGEAHRYdgrlmeTHNLKTRRDTVRAIYLL---IRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLg 421
Cdd:TIGR01192 213 RIEAETSALKQF------TNNLLSAQYPVLDWWALasgLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLL- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 422 dnIRTLIYIFGDMLNSVGAAGKV---FEYQDRKSEVSIDGNLMP-KDLKGHVKFQKLTFSYPRRPDHnvLKDFSLELKPG 497
Cdd:TIGR01192 286 --IGRLDQMSGFITQIFEARAKLedfFDLEDSVFQREEPADAPElPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 498 QITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERV 577
Cdd:TIGR01192 362 QTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEV 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 578 KEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCC-PTQ 656
Cdd:TIGR01192 442 YEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALrKNR 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 657 TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLRER--LFSDDKTTK 713
Cdd:TIGR01192 522 TTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRsgLLTNQPATK 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
440-705 |
3.23e-65 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 226.63 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 440 AAGKVFEYQDRKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLER 519
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 520 FYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANahsfISKL---EKG 596
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG----LEKLledDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 597 YDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSC-CPTQTLLVIAHRLKTIERADQIV 675
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260 270
....*....|....*....|....*....|
gi 29561855 676 VIDSGELVEKGTHEELMEKKGSYYKLRERL 705
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
290-677 |
3.51e-63 |
|
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: 219.85 E-value: 3.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 290 SWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFktelGEAHRYDGRLMET-HNLKT 368
Cdd:TIGR02857 143 DWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLF----GRAKAQAAAIRRSsEEYRE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 369 RRDTVRAIYLLIRRMTEL--GMKVAM--------LYYGRLFIQYGqmstgnLVSFIL----YQQdlgdnIRTLIYIFGDM 434
Cdd:TIGR02857 219 RTMRVLRIAFLSSAVLELfaTLSVALvavyigfrLLAGDLDLATG------LFVLLLapefYLP-----LRQLGAQYHAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 435 LNSVGAAGKVFEYQDRKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPdhNVLKDFSLELKPGQITALVGMSGGGKSTCV 514
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 515 SLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLE 594
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 595 KGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSC-CPTQTLLVIAHRLKTIERADQ 673
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAlAQGRTVLLVTHRLALAALADR 525
|
....
gi 29561855 674 IVVI 677
Cdd:TIGR02857 526 IVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
467-687 |
1.67e-62 |
|
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: 208.12 E-value: 1.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYprRPD-HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS 545
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSGTVRDNIAyGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIRE 625
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGT 687
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIrEAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
467-686 |
2.17e-62 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 207.83 E-value: 2.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYPRRPdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSK 546
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREP 626
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQALS-CCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKG 686
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRqLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
158-444 |
3.08e-60 |
|
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: 204.63 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 158 VFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQ 237
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 238 DIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQK 317
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 318 LSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGR 397
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 29561855 398 LFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
491-701 |
1.10e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 203.15 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 491 SLELKPGQITALVGMSGGGKSTCVSLLERFYqPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQ 570
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 571 GCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:PRK11174 449 DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29561855 651 -SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKL 701
Cdd:PRK11174 529 nAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
466-694 |
1.05e-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: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 466 KGHVKFQKLTFSYP--RRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYL 543
Cdd:COG4618 328 KGRLSVENLTVVPPgsKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSGTVRDNIAyGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALI 623
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALSccptQ------TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIR----AlkargaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
156-444 |
3.93e-55 |
|
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: 190.92 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNF-------RSAIIFMGLFSLGSSFSAgCRGGLFMCAINSFTCRVKV 228
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEealralnQAVLILLGVVLIGSIATF-LRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQ 308
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 309 NIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGM 388
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 389 KVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
156-444 |
1.30e-53 |
|
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: 186.57 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRS------AIIFMGLFSLGSSFSAGcRGGLFMCAINSFTCRVKVQ 229
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGlslktfALALLGVFVVGAAANFG-RVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 230 LFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQN 309
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 310 IYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLlirRMTELGMK 389
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFF---GSTGFSGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 390 VAM---LYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18573 237 LSLlsvLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
394-700 |
1.00e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 194.86 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 394 YYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRKSEVSI--DGNLMPK---DLKGH 468
Cdd:PTZ00265 1086 WFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKnknDIKGK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFY---------------------QPQQ-- 525
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneQDYQgd 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 526 -------------------------------GTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSM 574
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 575 ERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCC- 653
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 654 --PTQTLLVIAHRLKTIERADQIVVID----SGELVE-KGTHEELMEKKGSYYK 700
Cdd:PTZ00265 1406 dkADKTIITIAHRIASIKRSDKIVVFNnpdrTGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
225-699 |
1.51e-50 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 191.34 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 225 RVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSwKLTLLMLMetPLT 304
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLL 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 305 GLLQNIYdTHYQKLSKEVQ--DSMAQANDAA--GEAVSGIRTVKSFKTeLGEAHRYDGRLMETHNLKTRRDTVRAIYLLI 380
Cdd:PLN03232 1061 ILFYAAY-LYYQSTSREVRrlDSVTRSPIYAqfGEALNGLSSIRAYKA-YDRMAKINGKSMDNNIRFTLANTSSNRWLTI 1138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 381 RRMTELGMKV------AMLYYGRLFIQYGQMST-GNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGaagKVFEYQDRKSE 453
Cdd:PLN03232 1139 RLETLGGVMIwltatfAVLRNGNAENQAGFASTmGLLLSYTLNITTLLSGVLRQASKAENSLNSVE---RVGNYIDLPSE 1215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 454 VS-IDGNLMPKD---LKGHVKFQKLTFSY-PRRPDhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI 528
Cdd:PLN03232 1216 ATaIIENNRPVSgwpSRGSIKFEDVHLRYrPGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 529 LLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMErVKEAASKANAHSFISKLEKGYDTDVGERGNLL 608
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-----SCcptqTLLVIAHRLKTIERADQIVVIDSGELV 683
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIreefkSC----TMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
490
....*....|....*.
gi 29561855 684 EKGTHEELMEKKGSYY 699
Cdd:PLN03232 1449 EYDSPQELLSRDTSAF 1464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
470-682 |
3.77e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.54 E-value: 3.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYlHSKVA 548
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEW-RRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSGTVRDNIAYGLQ----GCSMERVKEAASKANahsfiskLEKGY-DTDVGErgnlLSGGEKQRIAIARALI 623
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQlrerKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGEL 682
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEegrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
469-695 |
4.12e-49 |
|
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: 172.13 E-value: 4.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPV--LFSGTVRDNIAYGL--QGCS----MERVKEAASKANahsfISKLEkgyDTDVgergNLLSGGEKQRIAIAR 620
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPenLGLPreeiRERVEEALELVG----LEHLA---DRPP----HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgkTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
471-686 |
3.40e-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: 165.18 E-value: 3.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYPRRPDHnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQhKYLHSKVAMV 550
Cdd:cd03247 3 INNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 GQEPVLFSGTVRDNIayglqgcsmervkeaaskanahsfisklekgydtdvGERgnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:cd03247 81 NQRPYLFDTTLRNNL------------------------------------GRR---FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 631 LDEVTSSLDTESE-QMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKG 686
Cdd:cd03247 122 LDEPTVGLDPITErQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
156-444 |
3.94e-47 |
|
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: 168.82 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVID-ILGSHYQWDNFRSAIIFMGLFSLGSSFSAGcRGGLFMCAINSFTCRVKVQLFGSL 234
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaALGGGDTASLNQIALLLLGLFLLQAVFSFF-RIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 235 IRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTH 314
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 315 YQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLY 394
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 29561855 395 YGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
225-665 |
5.92e-47 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 174.86 E-value: 5.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 225 RVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGravalnvNVLLRTLVKTLGMLYLMVS-------LSWKLTLLM 297
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQ-------DLYVRVIVPAGVALVVGAAavaaiavLSVPAALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 298 --------LMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRtVKSFKTELGEAHRydgRLMETHNLKTR 369
Cdd:TIGR02868 160 aaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGA-LPAALAQVEEADR---ELTRAERRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 370 RDTVR-AIYLLIRRMTELGMKVAmlyyGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQ 448
Cdd:TIGR02868 236 ATALGaALTLLAAGLAVLGALWA----GGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 449 DRKSEVSI-----DGNLMPKDLKghVKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQP 523
Cdd:TIGR02868 312 DAAGPVAEgsapaAGAVGLGKPT--LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 524 QQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGE 603
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 604 RGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTE-SEQMVQQALSCCPTQTLLVIAHRL 665
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
388-694 |
6.59e-47 |
|
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: 174.84 E-value: 6.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 388 MKVAMLYYGRLFIQYGQMSTGNLV-SFILYQQDLGDnIRTLIYIFGDMLNSVGAAGKVFEYQDrksEVSIDGNLMP-KDL 465
Cdd:TIGR01842 238 LQSLVLGLGAYLAIDGEITPGMMIaGSILVGRALAP-IDGAIGGWKQFSGARQAYKRLNELLA---NYPSRDPAMPlPEP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 466 KGHVKFQKLTFSYPRrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS 545
Cdd:TIGR01842 314 EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIRE 625
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARgiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
149-701 |
1.67e-44 |
|
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: 172.82 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 149 DYILLFGAFVFLALavlcemfIPLYTGEVIDILGSHY---QWDN------------FRSAI-----IFMGLFSLGSSFSA 208
Cdd:TIGR00957 957 DYMKAIGLFITFLS-------IFLFVCNHVSALASNYwlsLWTDdpmvngtqnntsLRLSVygalgILQGFAVFGYSMAV 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 209 GCrGGLFMCAinsftcRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVS 288
Cdd:TIGR00957 1030 SI-GGIQASR------VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILL 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 289 LSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMEthNLKT 368
Cdd:TIGR00957 1103 ATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDE--NQKA 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 369 RRDTVRAIYLLIRRMTELGMKVAMlyYGRLFIQYGQMS-TGNLVSF-ILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFE 446
Cdd:TIGR00957 1181 YYPSIVANRWLAVRLECVGNCIVL--FAALFAVISRHSlSAGLVGLsVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 447 YQDRKSEV--SIDGNLMPKDL--KGHVKFQKLTFSYprRPDHN-VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFY 521
Cdd:TIGR00957 1259 YSETEKEApwQIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 522 QPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAyGLQGCSMERVKEAASKANAHSFISKLEKGYDTDV 601
Cdd:TIGR00957 1337 ESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC 1415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 602 GERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSccpTQ----TLLVIAHRLKTIERADQIVVI 677
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR---TQfedcTVLTIAHRLNTIMDYTRVIVL 1492
|
570 580
....*....|....*....|....
gi 29561855 678 DSGELVEKGTHEELMEKKGSYYKL 701
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
433-725 |
1.86e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 172.91 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 433 DMLNSVGAAGKVFEYQDRKS--EVSIDGNLMPkDLKgHVKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGK 510
Cdd:PTZ00265 347 EYMKSLEATNSLYEIINRKPlvENNDDGKKLK-DIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 511 STCVSLLERFYQPQQGTILL-DGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGL-------------------- 569
Cdd:PTZ00265 425 STILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgnds 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 570 -------QGCSME------------------------------RVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGE 612
Cdd:PTZ00265 505 qenknkrNSCRAKcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 613 KQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQA---LSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHE 689
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVD 664
|
330 340 350
....*....|....*....|....*....|....*.
gi 29561855 690 ELMEKkgsyyKLRERLFSDDKTTKQEKEKSDTVKTQ 725
Cdd:PTZ00265 665 IIGED-----PTKDNKENNNKNNKDDNNNNNNNNNN 695
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
230-697 |
7.34e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 171.07 E-value: 7.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 230 LFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSwKLTLLMLMetPLTGLLQN 309
Cdd:PLN03130 992 MLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS-TISLWAIM--PLLVLFYG 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 310 IYdTHYQKLSKEVQ--DSMAQANDAA--GEAVSGIRTVKSFKTELGEAhRYDGRLMETH------NLKTRRdtvraiYLL 379
Cdd:PLN03130 1069 AY-LYYQSTAREVKrlDSITRSPVYAqfGEALNGLSTIRAYKAYDRMA-EINGRSMDNNirftlvNMSSNR------WLA 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 380 IRRMTELGMKV------AMLYYGRLFIQYGQMST-GNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKvfeYQDRKS 452
Cdd:PLN03130 1141 IRLETLGGLMIwltasfAVMQNGRAENQAAFASTmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGT---YIDLPS 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 453 EVS--IDGNLMPKD--LKGHVKFQKLTFSYprRPD-HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGT 527
Cdd:PLN03130 1218 EAPlvIENNRPPPGwpSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGR 1295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 528 ILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAyGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNL 607
Cdd:PLN03130 1296 ILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGEN 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 LSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-----SCcptqTLLVIAHRLKTIERADQIVVIDSGEL 682
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIreefkSC----TMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
490
....*....|....*
gi 29561855 683 VEKGTHEELMEKKGS 697
Cdd:PLN03130 1451 VEFDTPENLLSNEGS 1465
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
153-417 |
1.00e-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: 158.96 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGC--RGGLFMCAINSFTCRVKVQL 230
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSflQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNI 310
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 311 YDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKV 390
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*..
gi 29561855 391 AMLYYGRLFIQYGQMSTGNLVSFILYQ 417
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
487-636 |
3.36e-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: 152.80 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSG-TVRDNI 565
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 566 AYGLqgcSMERVKEAASKANAHSFISKLEKGYDTD--VGERGNLLSGGEKQRIAIARALIREPQVLILDEVTS 636
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
470-681 |
5.32e-43 |
|
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: 154.55 E-value: 5.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAM 549
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEP--VLFSGTVRDNIAYGL--QGCSMERVKEAASKANAHSFISKLEkgyDTDVGErgnlLSGGEKQRIAIARALIRE 625
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenLGLPEEEIEERVEEALELVGLEGLR---DRSPFT----LSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALS--CCPTQTLLVIAHRLKTIER-ADQIVVIDSGE 681
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKklKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
469-691 |
1.14e-42 |
|
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: 154.26 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFY-----QPQQGTILLDGKPL--QDYQHK 541
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 542 YLHSKVAMVGQEPVLFSGTVRDNIAYG--LQGCS-----MERVKEAASKAnahsfisklekGYDTDVGER--GNLLSGGE 612
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrLHGIKlkeelDERVEEALRKA-----------ALWDEVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 613 KQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEE 690
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIaELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 29561855 691 L 691
Cdd:cd03260 227 I 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
469-693 |
1.56e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.61 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHNV--LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQH---KYL 543
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPV--LFSG-TVRDNIAYGLQGCSMERVKEAASKANAHsfiskLEK-GYDTDVGER-GNLLSGGEKQRIAI 618
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPLRLHGLLSRAERRERVAEL-----LERvGLPPDLADRyPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 619 ARALIREPQVLILDEVTSSLDTeSEQM--------VQQALSCcptqTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDV-SVQAqilnllrdLQRELGL----TYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
....
gi 29561855 690 ELME 693
Cdd:COG1123 491 EVFA 494
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
472-682 |
3.05e-41 |
|
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: 148.13 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:cd03246 4 ENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVLFSGTVRDNIayglqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIREPQVLIL 631
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29561855 632 DEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIVVIDSGEL 682
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
153-444 |
3.51e-41 |
|
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: 152.32 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFG 232
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 233 SLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYD 312
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 313 THYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDG--RLMETHNLKTRRdTVRAIYLLIRRMTELGMkV 390
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREanRDLRDANLRAAR-LSALFSPLIGLLTALGT-A 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 391 AMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd07346 239 LVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
469-691 |
5.80e-41 |
|
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: 149.65 E-value: 5.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYL- 543
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 --HSKVAMVGQEPVLFSG-TVRDNIAYGLQGCSMERvKEAASKAN-----------AHSFISKLekgydtdvgergnllS 609
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPK-AEIEERVLellelvgledkADAYPAQL---------------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 610 GGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEK 685
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElglTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*.
gi 29561855 686 GTHEEL 691
Cdd:cd03258 223 GTVEEV 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
462-687 |
2.33e-40 |
|
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: 147.17 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 462 PKDlkGHVKFQKLTFSYprRPD-HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGK-----PL 535
Cdd:cd03369 2 PEH--GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 536 QDyqhkyLHSKVAMVGQEPVLFSGTVRDNI-AYGLQgcSMERVKEAASkanahsfisklekgydtdVGERGNLLSGGEKQ 614
Cdd:cd03369 78 ED-----LRSSLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 615 RIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGT 687
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
474-686 |
1.43e-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: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRPDHN-VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGK---PLQDYQHKYLHSKVAM 549
Cdd:cd03257 7 LSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQE------PVLfsgTVRDNIAYGLQGCSMERVKEAASKAnahsfISKLEKGYDTDvGERGNL----LSGGEKQRIAIA 619
Cdd:cd03257 87 VFQDpmsslnPRM---TIGEQIAEPLRIHGKLSKKEARKEA-----VLLLLVGVGLP-EEVLNRypheLSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
469-692 |
8.97e-39 |
|
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: 144.03 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVL-FSGTVRDNIAYG-------LQGCS---MERVKEAASKANAHSFIsklEKGYDTdvgergnlLSGGEKQRIA 617
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglFGRPSaedREAVEEALERTGLEHLA---DRPVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 618 IARALIREPQVLILDEVTSSLDteseqmvqqalsccptqtllvIAHRLKTIER-------------------------AD 672
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLD---------------------LAHQLEVLELlrrlarergrtvvmvlhdlnlaaryAD 206
|
250 260
....*....|....*....|
gi 29561855 673 QIVVIDSGELVEKGTHEELM 692
Cdd:COG1120 207 RLVLLKDGRIVAQGPPEEVL 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
474-693 |
1.47e-38 |
|
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: 143.41 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRPDHN-VLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYLHSKVAM 549
Cdd:COG1124 7 LSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEPvlFS-----GTVRDNIAYGLQGCSMERVKEAASKAnahsfiskLEK-GYDTDVGER-GNLLSGGEKQRIAIARAL 622
Cdd:COG1124 84 VFQDP--YAslhprHTVDRILAEPLRIHGLPDREERIAEL--------LEQvGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 623 IREPQVLILDEVTSSLD--TESE-----QMVQQALsccpTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:COG1124 154 ILEPELLLLDEPTSALDvsVQAEilnllKDLREER----GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
469-694 |
6.14e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 141.35 E-value: 6.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLhSKVA 548
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAY--GLQGCSMERVKEAASKAnAHSFisKLEKGYDTDVGErgnlLSGGEKQRIAIARALIRE 625
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfaRLYGLPRKEARERIDEL-LELF--GLTDAADRKVGT----LSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEK 694
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEgkTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
156-441 |
6.74e-38 |
|
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: 143.01 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRgglFMCaINSFTCRV----KVQLF 231
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR---FYL-VSWLGERVvadlRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 232 GSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIY 311
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 312 DTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVA 391
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 29561855 392 MLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAA 441
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
469-691 |
1.01e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 140.51 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHK--YL 543
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDLTDSKKDinKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSG-TVRDNIAYGLQgcsmeRVK-----EAASKANAHsfiskLEKgydtdVG--ERGNL----LSGG 611
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTLAPI-----KVKkmskaEAEERAMEL-----LER-----VGlaDKADAypaqLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 612 EKQRIAIARALIREPQVLILDEVTSSLDTEseqMVQQALSccpT--------QTLLVIAH-----RlktiERADQIVVID 678
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD---VmrdlakegMTMVVVTHemgfaR----EVADRVVFMD 210
|
250
....*....|...
gi 29561855 679 SGELVEKGTHEEL 691
Cdd:COG1126 211 GGRIVEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
469-693 |
8.09e-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: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHnVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS 545
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTlalALMGLLPHGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEP--VLFSGTVRDNIAYGLQGCSMERvKEAASKANAHSFISKLEKGYDTDVGErgnlLSGGEKQRIAIARALI 623
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSR-AEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELME 693
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRErgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
469-650 |
1.07e-36 |
|
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: 137.22 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyqhkyLHSKV 547
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFS-GTVRDNIAYGLQgcsMERVKEAASKANAHSFISKlekgydtdVGERGNL------LSGGEKQRIAIAR 620
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLE---LQGVPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190
....*....|....*....|....*....|
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
470-681 |
1.81e-36 |
|
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: 134.29 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAM 549
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQepvlfsgtvrdniayglqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIREPQVL 629
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 630 ILDEVTSSLDTESEQMVQQALS--CCPTQTLLVIAHRLKTIERA-DQIVVIDSGE 681
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRelAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
472-693 |
3.27e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.84 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRPDHnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:PRK13635 9 EHISFRYPDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEP-VLFSG-TVRDNIAYGLQGCSM------ERVKEAASKANAHSFISklekgydtdvgERGNLLSGGEKQRIAIARALI 623
Cdd:PRK13635 88 QNPdNQFVGaTVQDDVAFGLENIGVpreemvERVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 624 REPQVLILDEVTSSLDTESEQMV---------QQALsccptqTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVletvrqlkeQKGI------TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
469-717 |
3.48e-36 |
|
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: 137.18 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG-KPLQDYQHKYLHSKV 547
Cdd:TIGR04520 1 IEVENVSFSYPESEK-PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEP--VLFSGTVRDNIAYGL--QGCSME----RVKEAASKANAHSFISKlekgydtdvgeRGNLLSGGEKQRIAIA 619
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenLGVPREemrkRVDEALKLVGMEDFRDR-----------EPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMV---------QQALsccptqTLLVIAHRLKTIERADQIVVIDSGELVEKGT--- 687
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVletirklnkEEGI------TVISITHDMEEAVLADRVIVMNKGKIVAEGTpre 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 29561855 688 ---HEELMEKKG-----SY---YKLRERLFSDDKTTKQEKE 717
Cdd:TIGR04520 223 ifsQVELLKEIGldvpfITelaKALKKRGIPLPPDILTEEE 263
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
469-695 |
5.28e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.04 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEP-VLFSG-TVRDNIAYGLQGCSMER------VKEAASKANAHSFISKlekgydtdvgERGNlLSGGEKQRIAIAR 620
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGLENKKVPPkkmkdiIDDLAKKVGMEDYLDK----------EPQN-LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQ---ALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKimvDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
469-681 |
9.72e-36 |
|
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: 133.75 E-value: 9.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHN--VLKDFSLELKPGQITALVGMSGGGKSTCVSLL--ErfYQPQQGTIlldgkplqdyqhkYLH 544
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEPVLFSGTVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIR 624
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 625 EPQVLILDEVTSSLDTES-----EQMVQQALSCCptQTLLVIAHRLKTIERADQIVVIDSGE 681
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgrhifENCILGLLLNN--KTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
469-684 |
1.09e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPR-RPDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYL- 543
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 ---HSKVAMVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSFISKLekgydtDVGERGNL----LSGGEKQR 615
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPLL---LAGVSRKERRERARELLERV------GLGDRLDHrpsqLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTESEQMVQQAL-SCC--PTQTLLVIAHRLKTIERADQIVVIDSGELVE 684
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLrELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
468-639 |
1.21e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.60 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 468 HVKFQKLTFSYPRRP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyqhkyLHSK 546
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFs-gTVRDNIAYGLQgcsMERVKEAASKANAHSFISKlekgydtdVG--ERGNL----LSGGEKQRIAIA 619
Cdd:COG1116 82 RGVVFQEPALLpwlTVLDNVALGLE---LRGVPKAERRERARELLEL--------VGlaGFEDAyphqLSGGMRQRVAIA 150
|
170 180
....*....|....*....|
gi 29561855 620 RALIREPQVLILDEVTSSLD 639
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
469-681 |
2.40e-35 |
|
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: 131.93 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY--QHKYLHSK 546
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSG-TVRDNIAYGlqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIRE 625
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGE 681
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
486-686 |
3.97e-35 |
|
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: 132.64 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKylhSKVAMVGQEPVLFSG-TVRD 563
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNIGMVFQDYALFPHlTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLqgcSMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTES- 642
Cdd:cd03259 92 NIAFGL---KLRGVPKAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLr 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29561855 643 EQM------VQQALSCCptqTLLVIAHRLKTIERADQIVVIDSGELVEKG 686
Cdd:cd03259 167 EELreelkeLQRELGIT---TIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
468-691 |
4.85e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 468 HVKFQKLTFSYPRRP-DHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYL 543
Cdd:COG1135 1 MIELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 H---SKVAMVGQEPVLFSG-TVRDNIAYGLQGCSMERvKEAASKAN-----------AHSFISKlekgydtdvgergnlL 608
Cdd:COG1135 78 RaarRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPK-AEIRKRVAellelvglsdkADAYPSQ---------------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESeqmvqqalsccpTQ---------------TLLVIAHRLKTIER-AD 672
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPET------------TRsildllkdinrelglTIVLITHEMDVVRRiCD 209
|
250
....*....|....*....
gi 29561855 673 QIVVIDSGELVEKGTHEEL 691
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDV 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
469-682 |
1.56e-34 |
|
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: 131.07 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPD-HNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDY----QH 540
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekeLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 541 KYLHSKVAMVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSFISKLekgydtDVGERGNL----LSGGEKQR 615
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELPLL---LAGVPKKERRERAEELLERV------GLGDRLNHypseLSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTESEQMVQ---QALSCCPTQTLLVIAHRLKTIERADQIVVIDSGEL 682
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMellRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
469-693 |
7.49e-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: 129.71 E-value: 7.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY---QHKYLHS 545
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSG-TVRDNIAYGLQ---GCSMERVKEAAskanahsfISKLEKgydtdVGERG--NL----LSGGEKQR 615
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLRehtDLSEAEIRELV--------LEKLEL-----VGLPGaaDKmpseLSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLD----TESEQMV---QQALSCcptqTLLVIAHRLKTIER-ADQIVVIDSGELVEKGT 687
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpitsAVIDELIrelRDELGL----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
....*.
gi 29561855 688 HEELME 693
Cdd:COG1127 226 PEELLA 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
470-692 |
9.48e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.10 E-value: 9.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRRPdhnvlKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHS-KVA 548
Cdd:COG3840 3 RLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTALPPAErPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAYGLQ-GCSM-----ERVKEAASKANAHSFISKLEkgydtdvGErgnlLSGGEKQRIAIARA 621
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLRpGLKLtaeqrAQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 622 LIREPQVLILDEVTSSLD----TESEQMVQQAlsCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGlTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
469-694 |
1.85e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.76 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQD---YQHKylhs 545
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 kVAMVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSFISKLE-KGY-DTDVGErgnlLSGGEKQRIAIARAL 622
Cdd:COG3842 79 -VGMVFQDYALFPHlTVAENVAFGLR---MRGVPKAEIRARVAELLELVGlEGLaDRYPHQ----LSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 623 IREPQVLILDEVTSSLDTES-EQM------VQQALSCcptqTLLVIAH------RLktierADQIVVIDSGELVEKGTHE 689
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLrEEMreelrrLQRELGI----TFIYVTHdqeealAL-----ADRIAVMNDGRIEQVGTPE 221
|
....*
gi 29561855 690 ELMEK 694
Cdd:COG3842 222 EIYER 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
469-692 |
2.07e-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: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK--YLHSK 546
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVlfsgTVRDNIAYGLQGCS----------MERVKEAASKANAHSFISKLekgydtdVGErgnlLSGGEKQRI 616
Cdd:COG1121 84 AEVDWDFPI----TVRDVVLMGRYGRRglfrrpsradREAVDEALERVGLEDLADRP-------IGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTESEQMVQQALsccpTQ------TLLVIAHRLKTIER-ADQIVVIDsGELVEKGTHE 689
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELL----RElrregkTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPE 223
|
...
gi 29561855 690 ELM 692
Cdd:COG1121 224 EVL 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
153-414 |
3.78e-33 |
|
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: 129.46 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRS-AIIFMGLFSLGSSFSAGcrGGLFMCAI-NSFTCRVKVQL 230
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLvPLAIIGLFLLRGLASYL--QTYLMAYVgQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNI 310
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 311 YDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAiylLIRRMTE----L 386
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA---LSSPLMEllgaI 235
|
250 260
....*....|....*....|....*...
gi 29561855 387 GMkVAMLYYGRLFIQYGQMSTGNLVSFI 414
Cdd:cd18552 236 AI-ALVLWYGGYQVISGELTPGEFISFI 262
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
469-691 |
4.75e-33 |
|
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: 127.23 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS--- 545
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSG-TVRDNIAYGLQ---GCSMERVKEAAskanahsfISKLEKgydtdVGERG--NL----LSGGEKQR 615
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLRehtRLSEEEIREIV--------LEKLEA-----VGLRGaeDLypaeLSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLD----TESEQMV---QQALSCcptqTLLVIAHRLKTIER-ADQIVVIDSGELVEKGT 687
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIrslKKELGL----TSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
....
gi 29561855 688 HEEL 691
Cdd:cd03261 221 PEEL 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
153-444 |
1.29e-32 |
|
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: 127.93 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFG 232
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 233 SLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYD 312
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 313 THYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDgrlmeTHNLKTRRDTVRAIYLLIRRM------TEL 386
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFD-----KENEEYRDLNIKLAKLLAKYWplmdflSGL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 387 GMkVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18542 236 QI-VLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
465-699 |
4.11e-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: 125.41 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 465 LKGHVKFQKLTFSYprrpDHN---VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK 541
Cdd:cd03288 16 LGGEIKIHDLCVRY----ENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 542 YLHSKVAMVGQEPVLFSGTVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARA 621
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMVQQ-ALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYY 699
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKvVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
469-691 |
5.35e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDyqhkyLHS 545
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLED---PTSGEILIGGRDVTD-----LPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 K---VAMVGQEPVLF-SGTVRDNIAYGLQGCSM------ERVKEAASkanahsfISKLEKGYDTDVGErgnlLSGGEKQR 615
Cdd:COG3839 73 KdrnIAMVFQSYALYpHMTVYENIAFPLKLRKVpkaeidRRVREAAE-------LLGLEDLLDRKPKQ----LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTES-EQM------VQQALSccpTQTLLViahrlkT---IER---ADQIVVIDSGEL 682
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLrVEMraeikrLHRRLG---TTTIYV------ThdqVEAmtlADRIAVMNDGRI 212
|
....*....
gi 29561855 683 VEKGTHEEL 691
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
483-682 |
1.13e-31 |
|
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: 122.64 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPL--QDYQHKYLHSKVAMVGQEPVLF 557
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SG-TVRDNIAYGLqgcsMERVKEAASKANAHSfISKLEKgydtdVG--ERGNL----LSGGEKQRIAIARALIREPQVLI 630
Cdd:cd03262 89 PHlTVLENITLAP----IKVKGMSKAEAEERA-LELLEK-----VGlaDKADAypaqLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 631 LDEVTSSLDTES-----EQMVQQALSccpTQTLLVIAHRLKTI-ERADQIVVIDSGEL 682
Cdd:cd03262 159 FDEPTSALDPELvgevlDVMKDLAEE---GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
472-639 |
2.14e-31 |
|
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: 120.62 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QepvlfsgtvrdniayglqgcSMERVKeaaskanahsfISKL-EKGYDTdvgergnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:cd03214 80 Q--------------------ALELLG-----------LAHLaDRPFNE--------LSGGERQRVLLARALAQEPPILL 120
|
....*....
gi 29561855 631 LDEVTSSLD 639
Cdd:cd03214 121 LDEPTSHLD 129
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
469-682 |
3.02e-31 |
|
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: 120.20 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHsKVA 548
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIayglqgcsmervkeaaskanahsfisklekgydtdvgergnLLSGGEKQRIAIARALIREPQ 627
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 628 VLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGEL 682
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEgkTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
469-686 |
4.58e-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: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHnvlkdFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHSK-V 547
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRpV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSG-TVRDNIAYGLQ-GCSMERV-KEAASKANAHSFISKLEKgydtdvgERGNLLSGGEKQRIAIARALIR 624
Cdd:cd03298 73 SMLFQENNLFAHlTVEQNVGLGLSpGLKLTAEdRQAIEVALARVGLAGLEK-------RLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 625 EPQVLILDEVTSSLD-TESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03298 146 DKPVLLLDEPFAALDpALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
170-444 |
5.80e-31 |
|
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: 123.04 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 170 IPLYTGEVIDILG---SHYQWDNFRS----AIIFMGLFSLGSSFSAGCRGGLFMCAINsFTCRVKVQLFGSLIRQDIGFF 242
Cdd:cd18574 15 IPLLLGDLVNVISrslKETNGDFIEDlkkpALKLLGLYLLQSLLTFAYISLLSVVGER-VAARLRNDLFSSLLRQDIAFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 243 ETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEV 322
Cdd:cd18574 94 DTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 323 QDSMAQANDAAGEAVSGIRTVKSFKTElgeahrydGRLMETHNLKTRRDTVRAIYL-----LIRRMTEL---GMKVAMLY 394
Cdd:cd18574 174 QAQVAKATGVADEALGNIRTVRAFAME--------DRELELYEEEVEKAAKLNEKLglgigIFQGLSNLalnGIVLGVLY 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 29561855 395 YGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18574 246 YGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
486-692 |
6.55e-31 |
|
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: 121.39 E-value: 6.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQ-----GCSMERV--KEAASKANAHSFIS--KLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEV 634
Cdd:cd03219 95 NVMVAAQartgsGLLLARArrEEREARERAEELLErvGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 635 TSSL-DTESEQMVQ--QALScCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:cd03219 171 AAGLnPEETEELAEliRELR-ERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
487-686 |
9.87e-31 |
|
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: 120.09 E-value: 9.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELK---PGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYLHS----KVAMVGQEPVL 556
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSG-TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYdtdVGErgnlLSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:cd03297 87 FPHlNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRY---PAQ----LSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 636 SSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlniPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
472-692 |
1.38e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.03 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVL-FSGTVRDNIAYGLQ--GCSMERVKEAASKAnahsfiskLEKgydTDVGE-RGNL---LSGGEKQRIAIARALIR 624
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAA--------LAQ---VDLAHlAGRDypqLSGGEQQRVQLARVLAQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 625 ------EPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIA--HRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVvlHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
474-678 |
1.79e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.18 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHkylhsKVAMVGQE 553
Cdd:cd03235 5 LTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVL---FSGTVRDNIAYGLQGcsmervkeaasKANAHSFISK---------LEKGYDTDVGER--GNlLSGGEKQRIAIA 619
Cdd:cd03235 77 RSIdrdFPISVRDVVLMGLYG-----------HKGLFRRLSKadkakvdeaLERVGLSELADRqiGE-LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMV------QQALSCcptqTLLVIAHRLKTIER-ADQIVVID 678
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIyellreLRREGM----TILVVTHDLGLVLEyFDRVLLLN 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
480-693 |
2.25e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.95 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGK------PLQDyqhkylhSKVAMV 550
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRdlftnlPPRE-------RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 GQEPVLFSG-TVRDNIAYGLqgcSMERVKEAASKANAHSFISK-----LEKGYDTDvgergnlLSGGEKQRIAIARALIR 624
Cdd:COG1118 81 FQHYALFPHmTVAENIAFGL---RVRPPSKAEIRARVEELLELvqlegLADRYPSQ-------LSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 625 EPQVLILDEVTSSLDT----ESEQMVQQALSCCPTQTLLVI-----AHRLktierADQIVVIDSGELVEKGTHEELME 693
Cdd:COG1118 151 EPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
469-684 |
2.70e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.00 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK---YLHS 545
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQE-PVLFSGTVRDNIAYGLQ--GCSMERVKEAASKAnahsfiskLEKgydtdVG--ERGNL----LSGGEKQRI 616
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLRvtGKSRKEIRRRVREV--------LDL-----VGlsDKAKAlpheLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTE-SEQMVQ--QALSCcpTQTLLVIA-HRLKTIERADQ-IVVIDSGELVE 684
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEINR--RGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
470-695 |
2.80e-30 |
|
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: 119.60 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLH---SK 546
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSG-TVRDNIAYGLQGC-----SMERVKEAASKANAhsfISKLEK-GYDTDVGERGNLLSGGEKQRIAIA 619
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGRrstwrSLFGLFPKEEKQRA---LAALERvGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIA--HRLKTIER-ADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVslHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
153-416 |
1.84e-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: 118.69 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYqwDNFRSAIIFMGLFSLGSSFSAGcrgGLFMCAI--NSFTCRVKVQL 230
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG--SSGGLLALLVALFLLQAVLSAL---SSYLLGRtgERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNI 310
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 311 YDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKV 390
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALL 235
|
250 260
....*....|....*....|....*.
gi 29561855 391 AMLYYGRLFIQYGQMSTGNLVSFILY 416
Cdd:cd18551 236 VVLGVGGARVASGALTVGTLVAFLLY 261
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
153-416 |
2.22e-29 |
|
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: 118.28 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHyqwDNFRSAIIFMGLFSLGSSF-SAGCRGG---LFMCAINSFTCRVKV 228
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAG---TLTASQLLRYALLILLLALlIGIFRFLwryLIFGASRRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQ 308
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 309 NIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDG--RLMETHNLKTRRdtVRAIYL-LIRRMTE 385
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKlnEEYVEKNLRLAR--VDALFFpLIGLLIG 235
|
250 260 270
....*....|....*....|....*....|.
gi 29561855 386 LGMKVAMLYYGRLFIQyGQMSTGNLVSFILY 416
Cdd:cd18541 236 LSFLIVLWYGGRLVIR-GTITLGDLVAFNSY 265
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
486-694 |
2.58e-29 |
|
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: 116.57 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKylhSKVAMVGQEPVLFSG-TVRD 563
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQgcsMERVKEAASKANAHSFIS--KLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDTE 641
Cdd:cd03300 92 NIAFGLR---LKKLPKAEIKERVAEALDlvQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 642 SEQMVQQALSCCPTQ---TLLVIAH-RLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:cd03300 165 LRKDMQLELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
152-412 |
2.98e-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: 118.35 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 152 LLFGAFvflaLAVLCEMFIPLYT---GEVIDILGSHYQW----DNFRS-----AIIFMGLFsLGSSFSAGCRGGLFMCAI 219
Cdd:cd18577 1 LIIGLL----AAIAAGAALPLMTivfGDLFDAFTDFGSGesspDEFLDdvnkyALYFVYLG-IGSFVLSYIQTACWTITG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 220 NSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLM 299
Cdd:cd18577 76 ERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 300 ETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLL 379
Cdd:cd18577 156 TLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLG 235
|
250 260 270
....*....|....*....|....*....|...
gi 29561855 380 IRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVS 412
Cdd:cd18577 236 LLFFIIFAMYALAFWYGSRLVRDGEISPGDVLT 268
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
469-687 |
3.61e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQHKYLH 544
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 S---KVAMVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSF-----ISKLEKGYDTDvgergnlLSGGEKQR 615
Cdd:PRK11153 79 KarrQIGMIFQHFNLLSSrTVFDNVALPLE---LAGTPKAEIKARVTELlelvgLSDKADRYPAQ-------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTESEQMVQQALSccptQ-------TLLVIAHRLKTIER-ADQIVVIDSGELVEKGT 687
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLK----DinrelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
143-454 |
5.84e-29 |
|
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: 117.94 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 143 IRLYRPDYILLFGAFVFlalAVLCEMFIPLY---TGEVIDILGSHYQwDNFRS-----AIIFMGLfSLGSSFSAGCRGGL 214
Cdd:cd18578 1 LKLNKPEWPLLLLGLIG---AIIAGAVFPVFailFSKLISVFSLPDD-DELRSeanfwALMFLVL-AIVAGIAYFLQGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 215 FMCAINSFTCRVKVQLFGSLIRQDIGFF--ETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWK 292
Cdd:cd18578 76 FGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 293 LTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDT 372
Cdd:cd18578 156 LALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 373 VRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNL--VSFILYQ--QDLGdniRTLIYIfGDMLNSVGAAGKVFEYQ 448
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFfiVFMALIFgaQSAG---QAFSFA-PDIAKAKAAAARIFRLL 311
|
....*.
gi 29561855 449 DRKSEV 454
Cdd:cd18578 312 DRKPEI 317
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
469-692 |
1.37e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.11 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK11231 3 LRTENLTVGYG---TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAYG------LQGCSMERVKEAASKANAHSFISKLEKGYDTDvgergnlLSGGEKQRIAIARA 621
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGrspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTD-------LSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 622 LIREPQVLILDEVTSSLDTESE-------QMVQQAlsccpTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQvelmrlmRELNTQ-----GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
480-692 |
3.16e-28 |
|
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: 116.74 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVlkDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQDYQ-------HKylhSKVAM 549
Cdd:COG4148 10 RRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEVLQDSArgiflppHR---RRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEPVLFSG-TVRDNIAYGlqgcsMERVKEAASKANAHSFISKLEKGydtDVGERG-NLLSGGEKQRIAIARALIREPQ 627
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLYG-----RKRAPRAERRISFDEVVELLGIG---HLLDRRpATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 628 VLILDEVTSSLDTESEQ-------MVQQALScCPtqtLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:COG4148 154 LLLMDEPLAALDLARKAeilpyleRLRDELD-IP---ILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
478-686 |
4.08e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 112.35 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 478 YPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKylHSKVAMVGQEPVLF 557
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SG-TVRDNIAYGLQGCSM------ERVKEAASKANahsfISKLEKGYDTDvgergnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:cd03301 85 PHmTVYDNIAFGLKLRKVpkdeidERVREVAELLQ----IEHLLDRKPKQ-------LSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 631 LDEVTSSLDTE-SEQM------VQQALSccpTQTLLVIAHRLKTIERADQIVVIDSGELVEKG 686
Cdd:cd03301 154 MDEPLSNLDAKlRVQMraelkrLQQRLG---TTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
486-691 |
6.82e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdyQHKYLHSK---VAMVGQEPVLFSG-TV 561
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQaagIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYGLQGCSMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSL-DT 640
Cdd:COG1129 97 AENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLtER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 641 ESE-------QMVQQALSCcptqtlLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:COG1129 175 EVErlfriirRLKAQGVAI------IYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
486-690 |
9.79e-28 |
|
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: 112.82 E-value: 9.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQ------------GCSMERVKEAASKANAHSFIS--KLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVL 629
Cdd:COG0411 99 NVLVAAHarlgrgllaallRLPRARREEREARERAEELLErvGLADRADEPAGN----LSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 630 ILDEVTSSL-DTESEQMVQ--QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEE 690
Cdd:COG0411 175 LLDEPAAGLnPEETEELAEliRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
469-692 |
1.19e-27 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 112.01 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRpdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQ 627
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVPK---LLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 628 VLILDEVTSSLD-----TESEQMV--QQALSccptQTLLVIAHRL-KTIERADQIVVIDSGELVEKGTHEELM 692
Cdd:cd03295 156 LLLMDEPFGALDpitrdQLQEEFKrlQQELG----KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
480-693 |
1.46e-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: 117.48 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDH-NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFyQPQQGTILLDGKPLQDYQHKYLH---SKVAMVGQEPv 555
Cdd:COG4172 294 RTVGHvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDP- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 lFSG-----TVRDNIAYGLQ----GCS----MERVKEAaskanahsfiskLEK-GYDTDVGER-GNLLSGGEKQRIAIAR 620
Cdd:COG4172 372 -FGSlsprmTVGQIIAEGLRvhgpGLSaaerRARVAEA------------LEEvGLDPAARHRyPHEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 621 ALIREPQVLILDEVTSSLD-TESEQMVQ-----QA---LSCcptqtlLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEE 690
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDvSVQAQILDllrdlQRehgLAY------LFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQ 512
|
...
gi 29561855 691 LME 693
Cdd:COG4172 513 VFD 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
469-694 |
1.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYP--RRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ---QGTILLDGKPLQDYQHKYL 543
Cdd:PRK13640 6 VEFKHVSFTYPdsKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEP-VLFSG-TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLekgyDTDVGERGNLlSGGEKQRIAIARA 621
Cdd:PRK13640 83 REKVGIVFQNPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML----DYIDSEPANL-SGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 622 LIREPQVLILDEVTSSLDTES-EQMVQ--QALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGkEQILKliRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
467-678 |
1.79e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.60 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFsypRRPDHNVL-KDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplqdyqhkylHS 545
Cdd:COG4178 361 GALALEDLTL---RTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSGTVRDNIAYGLQGCSM--ERVKEAASKANAHSFISKLEKGYDTDvgergNLLSGGEKQRIAIARALI 623
Cdd:COG4178 427 RVLFLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLDEEADWD-----QVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQAL-SCCPTQTLLVIAHRLKTIERADQIVVID 678
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
486-693 |
1.91e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.60 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGCSMERVKEAaskanahsfiskLEKGYDT--DVGER----GNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:cd03224 95 NLLLGAYARRRAKRKAR------------LERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 638 LdteSEQMVQQALSCCPT-----QTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELME 693
Cdd:cd03224 163 L---APKIVEEIFEAIRElrdegVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
469-692 |
2.04e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.21 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHnvlkdFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHSK-V 547
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRpV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSG-TVRDNIAYG------LQGCSMERVKEAASKANAHSFISKLEkgydtdvGErgnlLSGGEKQRIAIAR 620
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNIGLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQ-MVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQeMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
487-694 |
2.59e-27 |
|
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: 111.97 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS----KVAMVGQEPVLFSG-TV 561
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYGL--QGCSMERVKEAASKAnahsfiskLEKgydtdVGERG------NLLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:cd03294 120 LENVAFGLevQGVPRAEREERAAEA--------LEL-----VGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 634 VTSSLD------TESEQMVQQALSccpTQTLLVIAHRL-KTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:cd03294 187 AFSALDplirreMQDELLRLQAEL---QKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
473-683 |
2.60e-27 |
|
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: 110.04 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 473 KLTFSYPRRPdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdyqHKYLHSKVAMVGQ 552
Cdd:cd03226 4 NISFSYKKGT--EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 553 EP--VLFSGTVRDNIAYGLqgcsmervKEAASKANAHSFISKLEKGYDTDvgERGNL-LSGGEKQRIAIARALIREPQVL 629
Cdd:cd03226 79 DVdyQLFTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 630 ILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELV 683
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQgkAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
480-697 |
2.69e-27 |
|
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: 110.89 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGK-----PLQDYQhkylhskVAMVGQEP 554
Cdd:cd03296 11 RFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvPVQERN-------VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 VLFSG-TVRDNIAYGLQ-GCSMERVKEAASKANAHSFI-----SKLEKGYDTDvgergnlLSGGEKQRIAIARALIREPQ 627
Cdd:cd03296 84 ALFRHmTVFDNVAFGLRvKPRSERPPEAEIRAKVHELLklvqlDWLADRYPAQ-------LSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 628 VLILDEVTSSLDT----ESEQMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGS 697
Cdd:cd03296 157 VLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
483-694 |
2.87e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFY--QPQQ---GTILLDGKPLqdYQHKY----LHSKVAMVGQE 553
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDI--YDPDVdvveLRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFSGTVRDNIAYGL--QGCS-----MERVKEAASKANahsfiskLekgYDtDVGER----GNLLSGGEKQRIAIARAL 622
Cdd:COG1117 101 PNPFPKSIYDNVAYGLrlHGIKskselDEIVEESLRKAA-------L---WD-EVKDRlkksALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 623 IREPQVLILDEVTSSLDTES----EQMVQQaLSccpTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEK 694
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPIStakiEELILE-LK---KDyTIVIVTHNMQQAARvSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
486-698 |
7.59e-27 |
|
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: 109.35 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKylHSKVAMVGQEPVLFSG-TVRDN 564
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 565 IAYGLQGCSM------ERVKEAASKAN-AHSFISKLEKgydtdvgergnlLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:cd03299 92 IAYGLKKRKVdkkeieRKVLEIAEMLGiDHLLNRKPET------------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 638 LDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEKKGSY 698
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEfgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
487-692 |
8.21e-27 |
|
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: 112.51 E-value: 8.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELK---PGQ-ITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS----KVAMVGQEPVLFS 558
Cdd:TIGR02142 9 LGDFSLDADftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 559 G-TVRDNIAYGlqgcsMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:TIGR02142 89 HlSVRGNLRYG-----MKRARPSERRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 638 LDTESEQMVQQALSCCPTQT---LLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
474-693 |
1.35e-26 |
|
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: 110.91 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ---QGTILLDGKPLQDYQHK----YLHS 545
Cdd:COG0444 7 LKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKelrkIRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQE------PVLfsgTVRDNIAYGLQGCSMERVKEAASKAnahsfISKLEKgydtdVG-----ERGNL----LSG 610
Cdd:COG0444 87 EIQMIFQDpmtslnPVM---TVGDQIAEPLRIHGGLSKAEARERA-----IELLER-----VGlpdpeRRLDRypheLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 611 GEKQRIAIARALIREPQVLILDEVTSSLDTeSEQM--------VQQALSCcptqTLLVIAHRLKTIER-ADQIVVIDSGE 681
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqilnllkdLQRELGL----AILFITHDLGVVAEiADRVAVMYAGR 228
|
250
....*....|..
gi 29561855 682 LVEKGTHEELME 693
Cdd:COG0444 229 IVEEGPVEELFE 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
469-641 |
1.59e-26 |
|
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: 107.88 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK---YLHS 545
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEPVLFSG-TVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGErgnlLSGGEKQRIAIARALIR 624
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVN 153
|
170
....*....|....*..
gi 29561855 625 EPQVLILDEVTSSLDTE 641
Cdd:cd03292 154 SPTILIADEPTGNLDPD 170
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-416 |
3.92e-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: 109.16 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDIL-GSHYQWDNFRS-AIIFMGLFSLGSSFSAGcRGGLFMCAINSFTCRVKVQL 230
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGlALLLLGAYLLRALLNFL-RIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNI 310
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 311 YDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRydgrlMETHNLKTRRDTVRAIYL------LIRRMT 384
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKR-----FEALSRRYRKAQLRAMKLwaifhpLMEFLT 234
|
250 260 270
....*....|....*....|....*....|..
gi 29561855 385 ELGMkVAMLYYGRLFIQYGQMSTGNLVSFILY 416
Cdd:cd18778 235 SLGT-VLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
153-444 |
7.45e-26 |
|
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: 108.34 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFG 232
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 233 SLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALnVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYD 312
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 313 THYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYL-LIRRMTELGMKVA 391
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWpLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 29561855 392 MLYYGRLFIQyGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18543 240 LALGGWLVAN-GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
469-691 |
7.68e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.90 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEP-VLFSG-TVRDNIAYGL--QGCSM----ERVKEAASKANAHSFISKlekgydtdvgeRGNLLSGGEKQRIAIAR 620
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLenKGIPHeemkERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
469-650 |
1.14e-25 |
|
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: 105.25 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTcvsLLeR----FYQPQQGTILLDGKPLQDYQHKYlH 544
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LL-RilagLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEPVLFSG-TVRDNIAY--GLQGC--SMERVKEAASKANahsfiskLEKGYDTDVGErgnlLSGGEKQRIAIA 619
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFwaALYGLraDREAIDEALEAVG-------LAGLADLPVRQ----LSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|.
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
468-660 |
1.23e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 468 HVKFQKLTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ----DYqhky 542
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 lhskvAMVGQEPVLFSG-TVRDNIAYGLQgcsMERVKEAASKANAHSFISK--LEKGYDTDVGErgnlLSGGEKQRIAIA 619
Cdd:COG4525 79 -----GVVFQKDALLPWlNVLDNVAFGLR---LRGVPKAERRARAEELLALvgLADFARRRIWQ----LSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29561855 620 RALIREPQVLILDEVTSSLDTES-EQMvqqalsccptQTLLV 660
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTrEQM----------QELLL 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
487-689 |
1.67e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdyqhkyLHS-------KVAMVGQEPVLFSG 559
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR------IRSprdaialGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 -TVRDNIAYGLQGCSMERV--KEAASKanahsfISKLEKGY------DTDVGErgnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRLdrKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 631 LDEVTSSLdTESE---------QMVQQALsccptqTLLVIAHRLKTIER-ADQIVVIDSGELVekGTHE 689
Cdd:COG3845 165 LDEPTAVL-TPQEadelfeilrRLAAEGK------SIIFITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
469-691 |
2.22e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.89 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdYQHKYLHSKVA 548
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAY--GLQGCSmerVKEAASKANAHSFISKLEKGYDTDVGErgnlLSGGEKQRIAIARALIRE 625
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyaRLKGLP---KSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCCPTQTLLVIA-HRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTtHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
482-683 |
3.80e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 102.12 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 482 PDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ--DYQHKyLHSKVAMVGQepvlfsg 559
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaSPRDA-RRAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 tvrdniayglqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIREPQVLILDEVTSSL- 638
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29561855 639 DTESEQM-------VQQALSCcptqtlLVIAHRLKTIER-ADQIVVIDSGELV 683
Cdd:cd03216 115 PAEVERLfkvirrlRAQGVAV------IFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
469-705 |
5.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLqDYQHK---YLHS 545
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 KVAMVGQEP--VLFSGTVRDNIAYGLQGCSM--ERVKEAASKANAHSFISKLEKgydtdvgERGNLLSGGEKQRIAIARA 621
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 622 LIREPQVLILDEVTSSLDTE--SEQM-----VQQALSCcptqTLLVIAHRLKTIE-RADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMgvSEIMkllveMQKELGL----TIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
250
....*....|..
gi 29561855 694 KKGSYYKLRERL 705
Cdd:PRK13636 232 EKEMLRKVNLRL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
469-694 |
5.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSY-PRRP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI----LLDGKPLQDYQHKY 542
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LHSKVAMVGQEP--VLFSGTVRDNIAYGLQGCSMErvKEAASKANAHsfisKLEK-GYDTDVGERGNL-LSGGEKQRIAI 618
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIP--KEKAEKIAAE----KLEMvGLADEFWEKSPFeLSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 619 ARALIREPQVLILDEVTSSLDTESE-QMVQQALSCCPT-QTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
469-695 |
6.92e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSY-PRRP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ----DYQHKY 542
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LHSKVAMVGQ--EPVLFSGTVRDNIAYGLQ--GCSMERVKEAASKANAhsfisklEKGYDTDVGERGNL-LSGGEKQRIA 617
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEEDAKQKAREMIE-------LVGLPEELLARSPFeLSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 618 IARALIREPQVLILDEVTSSLD----TESEQMVQQaLSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYK-LHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234
|
...
gi 29561855 693 EKK 695
Cdd:PRK13634 235 ADP 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
474-686 |
8.99e-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: 102.66 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRpdhNVLKDFSLELKPGqITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyQHKYLHSKVAMVGQE 553
Cdd:cd03264 6 LTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFSG-TVRDNIAY--GLQGCSMERVKEAASKAnahsfiskLEKGYDTDVG-ERGNLLSGGEKQRIAIARALIREPQVL 629
Cdd:cd03264 81 FGVYPNfTVREFLDYiaWLKGIPSKEVKARVDEV--------LELVNLGDRAkKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 630 ILDEVTSSLDTESEQMVQQALSCCPTQTLLVIA-HRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILStHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
461-699 |
9.16e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 461 MPKDLKGHVKFQKLTFSYP-------RRPDHN-VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYqPQQGTILLDG 532
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPirkgilkRTVDHNvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 533 KPLQDYQHKYL---HSKVAMVGQEPvlFSG-----TVRDNIAYGLQ--------GCSMERVKEAASkanahsfisklEKG 596
Cdd:PRK15134 347 QPLHNLNRRQLlpvRHRIQVVFQDP--NSSlnprlNVLQIIEEGLRvhqptlsaAQREQQVIAVME-----------EVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 597 YDTDVGER-GNLLSGGEKQRIAIARALIREPQVLILDEVTSSLD-TESEQMVQQALSCCPTQTL--LVIAHRLKTIeRA- 671
Cdd:PRK15134 414 LDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDkTVQAQILALLKSLQQKHQLayLFISHDLHVV-RAl 492
|
250 260
....*....|....*....|....*....
gi 29561855 672 -DQIVVIDSGELVEKGTHEELMEKKGSYY 699
Cdd:PRK15134 493 cHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-684 |
1.05e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.38 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY---QHKYLHSKVAMVGQEP-- 554
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 -VLFSGTVRDNIAYGLQgcSMERVKEAASKANAHSFISKLEKGyDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:PRK10419 101 aVNPRKTVREIIREPLR--HLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 634 VTSSLDTESEQMVQQALSCCPTQT---LLVIAHRLKTIER-ADQIVVIDSGELVE 684
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
475-686 |
1.13e-24 |
|
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: 102.83 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 475 TFSYPRRPDHnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG-----KPLQDYQHKYLHSkvAM 549
Cdd:cd03266 10 RFRDVKKTVQ-AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARRRLGFVS--DS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEPVLfsgTVRDNIAY-----GLQGCSME-RVKEAASKANAHSFISKlekgydtdvgeRGNLLSGGEKQRIAIARALI 623
Cdd:cd03266 87 TGLYDRL---TARENLEYfaglyGLKGDELTaRLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALS--CCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRqlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
474-691 |
1.29e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLqDYQHKYL---HSKVAMV 550
Cdd:PRK13639 7 LKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 GQEP--VLFSGTVRDNIAYGLQ--GCSME----RVKEAASKANAHSFISKLEkgydtdvgergNLLSGGEKQRIAIARAL 622
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLnlGLSKEevekRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
469-691 |
1.72e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.02 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEP--VLFSGTVRDNIAYGL--QGCSME----RVKEAASKANAHSFISKlekgydtdvgeRGNLLSGGEKQRIAIAR 620
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMenQGIPREemikRVDEALLAVNMLDFKTR-----------EPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
469-716 |
1.96e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEP--VLFSGTVRDNIAYGLQGCSM------ERVKEAASKANAHSFISKLEKGydtdvgergnlLSGGEKQRIAIAR 620
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLdkdeveRRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLK-TIERADQIVVIDSGELVEKG-----THEELM 692
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgkTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260
....*....|....*....|....
gi 29561855 693 EKKGSYYKLRERLFSDDKTTKQEK 716
Cdd:PRK13647 232 EQAGLRLPLVAQIFEDLPELGQSK 255
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
153-444 |
2.12e-24 |
|
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: 104.02 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDIL------GSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRV 226
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIieglggGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 227 KVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGL 306
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 307 LQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDgrlmeTHNLKTRRDTVRAIYL------LI 380
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFD-----EINEELYKASFKAQFYsgllmpIM 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 381 RRMTELGMkVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18547 236 NFINNLGY-VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
469-694 |
2.36e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYprRPDHN-VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKV 547
Cdd:PRK13648 8 IVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPV-LFSG-TVRDNIAYGLQgcsmervKEAASKANAHSFISKLEKgyDTDVGERGNL----LSGGEKQRIAIARA 621
Cdd:PRK13648 86 GIVFQNPDnQFVGsIVKYDVAFGLE-------NHAVPYDEMHRRVSEALK--QVDMLERADYepnaLSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQ----MVQQaLSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQnlldLVRK-VKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
486-675 |
3.03e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNI 565
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYGLQgCSMERVKEAASKANAHSF---ISKLEKGYdtdvgergNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTES 642
Cdd:PRK10247 102 IFPWQ-IRNQQPDPAIFLDDLERFalpDTILTKNI--------AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 29561855 643 EQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIV 675
Cdd:PRK10247 173 KHNVNEIIHRYVREqniAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
486-691 |
3.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI-----LLDGKPLQDYQHKYLHSK-----------VAM 549
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELITNPYSKkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEP--VLFSGTVRDNIAYGLQGCSMERVkEAASKANAHsfiskLEK-GYDTDVGERGNL-LSGGEKQRIAIARALIRE 625
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFY-----LNKmGLDDSYLERSPFgLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQAL--SCCPTQTLLVIAHRL-KTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLIldAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
461-684 |
3.29e-24 |
|
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: 101.74 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 461 MPKDLKGHVKFQKLTFSYPRrPDH--NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPL--- 535
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGT-GAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 536 -QDYQHKYLHSKVAMVGQ-EPVLFSGTVRDNIAYGLQgcsMERVKEAASKANAHsfiskLEK-GydtdVGERG----NLL 608
Cdd:COG4181 80 dEDARARLRARHVGFVFQsFQLLPTLTALENVMLPLE---LAGRRDARARARAL-----LERvG----LGHRLdhypAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL--------SccptqTLLVIAHRLKTIERADQIVVIDSG 680
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnrergT-----TLVLVTHDPALAARCDRVLRLRAG 222
|
....
gi 29561855 681 ELVE 684
Cdd:COG4181 223 RLVE 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
474-693 |
3.31e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRpdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQE 553
Cdd:PRK10575 17 VSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 -PVLFSGTVRDNIAYG----------LQGCSMERVKEAASKANAHSFISKLekgYDTdvgergnlLSGGEKQRIAIARAL 622
Cdd:PRK10575 94 lPAAEGMTVRELVAIGrypwhgalgrFGAADREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQ---QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLalvHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
486-684 |
3.70e-24 |
|
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: 102.58 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY---QHKYLHSKVAMVGQE-PVLFSG-- 559
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIAYGLQgcSMERVKEAASKANAHSFISklEKGYDTDVGER-GNLLSGGEKQRIAIARALIREPQVLILDEVTSSL 638
Cdd:TIGR02769 106 TVRQIIGEPLR--HLTSLDESEQKARIAELLD--MVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29561855 639 DTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVE 684
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAfgtAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
491-694 |
4.53e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 103.66 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 491 SLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYL---HSKVAMVGQEPvlFSG-----TVR 562
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--YASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAYGLQ-------GCSMERVKEAaskanahsfiskLEK-GYDTDVGER-GNLLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:COG4608 116 DIIAEPLRihglaskAERRERVAEL------------LELvGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 634 VTSSLDTeSEQM--------VQQALSCcptqTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEK 694
Cdd:COG4608 184 PVSALDV-SIQAqvlnlledLQDELGL----TYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
486-697 |
5.98e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.33 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNI 565
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYGLQGCSMErVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLIL-DEVTSSLDTESEQ 644
Cdd:PTZ00243 1405 DPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDR 1483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 645 MVQQA-LSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGS 697
Cdd:PTZ00243 1484 QIQATvMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
487-699 |
6.65e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS----KVAMVGQEPVLFSG-TV 561
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYGLQ--GCSMERVKEAASKANAHSFISKLEKGYDTDvgergnlLSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:PRK10070 124 LDNTAFGMElaGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 640 TESEQMVQQ---ALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEKKGSYY 699
Cdd:PRK10070 197 PLIRTEMQDelvKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
469-705 |
6.95e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.94 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLErfyQPQQGTILLDGKPLQD--YQHKYL 543
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDGLKVNDpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSG-TVRDNIAYGLQgcsmeRVKeAASKANAHsfisKLEKGYDTDVG--ERGN----LLSGGEKQRI 616
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPL-----RVR-GASKEEAE----KQARELLAKVGlaERAHhypsELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
250
....*....|..
gi 29561855 694 KKGSyYKLRERL 705
Cdd:PRK09493 226 NPPS-QRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
483-691 |
1.36e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.59 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLErfyQPQQGTI-----LLDG-KPL--QDYQHKYLHSKVAMVG 551
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLE---QPEAGTIrvgdiTIDTaRSLsqQKGLIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVLFSG-TVRDNIAYGlqGCSMERVKEAASKANAHSFISKLE-KGYDTDVGERgnlLSGGEKQRIAIARALIREPQVL 629
Cdd:PRK11264 92 QNFNLFPHrTVLENIIEG--PVIVKGEPKEEATARARELLAKVGlAGKETSYPRR---LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 630 ILDEVTSSLDTEseqMVQQALSCC-----PTQTLLVIAHRLK-TIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK11264 167 LFDEPTSALDPE---LVGEVLNTIrqlaqEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
469-695 |
1.67e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPR-RP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPL----QDYQHKY 542
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LHSKVAMVGQ--EPVLFSGTVRDNIAYGLQGCSMErVKEAasKANAHSFIskLEKGYDTDVGERGNL-LSGGEKQRIAIA 619
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLL--MDLGFSRDVMSQSPFqMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenkTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
483-693 |
2.13e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY--QHKYLHSkvamVGQEPVLFSG- 559
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRHVNT----VFQSYALFPHm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIAYGL--QGCS----MERVKEAASkanahsfISKLEkgydtDVGERGNL-LSGGEKQRIAIARALIREPQVLILD 632
Cdd:PRK09452 102 TVFENVAFGLrmQKTPaaeiTPRVMEALR-------MVQLE-----EFAQRKPHqLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 633 EVTSSLDTESEQMVQQALSCCPTQ---TLLVIAH-RLKTIERADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
484-689 |
2.49e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG------KPLQDYQHKYLHSKVAMVGQE---- 553
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLfsgTVRDNIAYG---LQGCSmervKEAAsKANAHSFISKLEKgydTDVGERGNL-LSGGEKQRIAIARALIREPQVL 629
Cdd:COG4161 95 PHL---TVMENLIEApckVLGLS----KEQA-REKAMKLLARLRL---TDKADRFPLhLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 630 ILDEVTSSLDTE-SEQMVQQALSCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:COG4161 164 LFDEPTAALDPEiTAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
153-427 |
2.57e-23 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 100.93 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVID--ILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQL 230
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTlmgravALN---VNVL---LRTLVKTLGMLYLMVSLSWKLTLLMLMETPLT 304
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTE------ALNelfTSGLvtlIGDLLLLIGILIAMFLLNWRLALISLLVLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 305 GLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMEthNLKTRRDTVRaIYLLIRRMT 384
Cdd:cd18544 155 LLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE--YRKANLKSIK-LFALFRPLV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29561855 385 ELGMKVAM---LYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTL 427
Cdd:cd18544 232 ELLSSLALalvLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDL 277
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
480-692 |
5.29e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.14 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ--DYQHKYLHskVAMVGQEPVLf 557
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKYRCKH--IRMIFQDPNT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SGTVRDNIAyglqgcsmeRVKEAASKANAH-SFISKLEKGYDT--DVGERG-------NLLSGGEKQRIAIARALIREPQ 627
Cdd:COG4167 99 SLNPRLNIG---------QILEEPLRLNTDlTAEEREERIFATlrLVGLLPehanfypHMLSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 628 VLILDEVTSSLD-TESEQMVQQALSCCPTQTL--LVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:COG4167 170 IIIADEALAALDmSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
471-686 |
6.80e-23 |
|
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: 96.85 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYPRRPDHN---VLKDFSLELKPGQITALVGMSGGGKSTCVSLL--ERFYQPQQGTILLDGKPLQDYQHKYLhs 545
Cdd:cd03213 6 FRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRKI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 kVAMVGQEPVLFSG-TVRDNIayglqgcsmervkeaaskanahSFISKLekgydtdvgeRGnlLSGGEKQRIAIARALIR 624
Cdd:cd03213 84 -IGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 625 EPQVLILDEVTSSLDTESEQMVQQALS--CCPTQTLLVIAHRLKT--IERADQIVVIDSGELVEKG 686
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRrlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
469-686 |
7.64e-23 |
|
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: 97.29 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyqhkyLHSKVA 548
Cdd:cd03268 1 LKTNDLTKTYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVG---QEPVLFSG-TVRDNIAYG--LQGCSMERVKEAASKANAHSFISKLEKGYdtdvgergnllSGGEKQRIAIARAL 622
Cdd:cd03268 73 RIGaliEAPGFYPNlTARENLRLLarLLGIRKKRIDEVLDVVGLKDSAKKKVKGF-----------SLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgiTVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
483-691 |
9.59e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.03 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdyqhkylHSKVAMVG---QEPVLFSG 559
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRIGylpEERGLYPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 -TVRDNIAY--GLQGcsmerVKEAASKANAHSFISKLEkgydtdVGERGNL----LSGGEKQRIAIARALIREPQVLILD 632
Cdd:COG4152 86 mKVGEQLVYlaRLKG-----LSKAEAKRRADEWLERLG------LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 633 EVTSSLDTESEQMVQQALsccpTQ------TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:COG4152 155 EPFSGLDPVNVELLKDVI----RElaakgtTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
469-717 |
1.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.97 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSY-PRRP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKY--LH 544
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEP--VLFSGTVRDNIAYGLQ--GCSME----RVKEAASkanahsfISKLEkgYDTDVGERGNLLSGGEKQRI 616
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPInlGLSEEeienRVKRAMN-------IVGLD--YEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTESEQMVQ---QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL- 691
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILnkiKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVf 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 29561855 692 -----MEKKG------SYY--KLRERLF--SDDK-TTKQEKE 717
Cdd:PRK13637 234 kevetLESIGlavpqvTYLvrKLRKKGFniPDDIfTIEEAKE 275
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
485-699 |
1.48e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 485 NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQD---YQHkylhsKVAMVGQEPVLFSG-T 560
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppYQR-----PINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGydtdvGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDT 640
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-----KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 641 E-SEQM---VQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYY 699
Cdd:PRK11607 183 KlRDRMqleVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
469-695 |
2.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSY-PRRP-DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ----DYQHKY 542
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LHSKVAMVGQ--EPVLFSGTVRDNIAYGLQ--GCSMERVKEAASKanahsFISKLekGYDTDVGERGNL-LSGGEKQRIA 617
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfGFSEDEAKEKALK-----WLKKV--GLSEDLISKSPFeLSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 618 IARALIREPQVLILDEVTSSLDTES-EQMVQ-----QALSccptQTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEE 690
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQlfkdyQKAG----HTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*
gi 29561855 691 LMEKK 695
Cdd:PRK13641 232 IFSDK 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
487-695 |
2.77e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.77 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERF--YQPQ---QGTILLDGK----PLQDYQHkyLHSKVAMVGQEPVLF 557
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHniysPRTDTVD--LRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SGTVRDNIAYGLqgcsmeRVKEAASKANAHSFISKLEKG-----------YDTDVGergnlLSGGEKQRIAIARALIREP 626
Cdd:PRK14239 99 PMSIYENVVYGL------RLKGIKDKQVLDEAVEKSLKGasiwdevkdrlHDSALG-----LSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKG-THEELMEKK 695
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMNPK 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
486-693 |
3.75e-22 |
|
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: 95.82 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGcsmeRVKEAASKANahsfiskLEKGYDT--DVGER----GNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:COG0410 98 NLLLGAYA----RRDRAEVRAD-------LERVYELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 638 LdteSEQMVQQalsccptqtllvIAHRLKTI------------------ERADQIVVIDSGELVEKGTHEELME 693
Cdd:COG0410 167 L---APLIVEE------------IFEIIRRLnregvtillveqnarfalEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
469-691 |
5.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPDHN---VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKY-LH 544
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEP--VLFSGTVRDNIAYGLQGCSM------ERVKEAASKANAHSFiskleKGYDTdvgergNLLSGGEKQRI 616
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIppeeirERVDESLKKVGMYEY-----RRHAP------HLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
472-693 |
6.00e-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: 95.30 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHSKvAMVG 551
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITKLPMHKR-ARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 -----QEPVLFSG-TVRDNIAYGLQGCSMERvKEAASKANA--HSF-ISKLEKgydtdvgERGNLLSGGEKQRIAIARAL 622
Cdd:cd03218 77 igylpQEASIFRKlTVEENILAVLEIRGLSK-KEREEKLEEllEEFhITHLRK-------SKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQalsccptqtllvIAHRLK---------------TIERADQIVVIDSGELVEKGT 687
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQK------------IIKILKdrgigvlitdhnvreTLSITDRAYIIYEGKVLAEGT 216
|
....*.
gi 29561855 688 HEELME 693
Cdd:cd03218 217 PEEIAA 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
475-720 |
6.72e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 101.74 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 475 TFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSllerfyqpqqgTILLDGKPLQDyQHKYLHSKVAMVGQEP 554
Cdd:PLN03130 621 YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS-----------AMLGELPPRSD-ASVVIRGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 VLFSGTVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEV 634
Cdd:PLN03130 689 WIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 635 TSSLDTeseQMVQQALSCC-----PTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLRERLFSDD 709
Cdd:PLN03130 768 LSALDA---HVGRQVFDKCikdelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKME 844
|
250
....*....|.
gi 29561855 710 KTTKQEKEKSD 720
Cdd:PLN03130 845 EYVEENGEEED 855
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
476-722 |
7.47e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.59 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 476 FSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVS-LLERFYQPQQGTILLDGKplqdyqhkylhskVAMVGQEP 554
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 VLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFisKLEKGYD-TDVGERGNLLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:PLN03232 689 WIFNATVRENILFGSDFESERYWRAIDVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 634 VTSSLDTeseQMVQQALSCC-----PTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLRERLFSD 708
Cdd:PLN03232 767 PLSALDA---HVAHQVFDSCmkdelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM 843
|
250
....*....|....
gi 29561855 709 DKTTKqEKEKSDTV 722
Cdd:PLN03232 844 DATQE-VNTNDENI 856
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-691 |
1.22e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKY------LHSKVAMVGQEPVL 556
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaikLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSG-TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 636 SSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
469-693 |
1.22e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHkYLHSKVA 548
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQ----EPVLfsgTVRDNIA-----YGLQGcsmervkeAASKANAHSFI--SKLEKGYDTDVGErgnlLSGGEKQRIA 617
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSA--------AAARALVPPLLefAKLENKADAKVGE----LSGGMKRRLT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 618 IARALIREPQVLILDEVTSSLDTESEQMVQQALSC--CPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-420 |
1.26e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 96.01 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDilgshyqwdnfrSAIIF--MGLFSL--GSSFSAGCRGGLFMCAINSFTCRV-- 226
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIID------------DALPQgdLGLLVLlaLGMVAVAVASALLGVVQTYLSARIgq 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 227 ------KVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAV---ALNV--NVLlrTLVKTLGMlylMVSLSWKLTL 295
Cdd:cd18550 69 gvmydlRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVtgtLTSVvsNVV--TLVATLVA---MLALDWRLAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 296 LMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGE--AVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTV 373
Cdd:cd18550 144 LSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29561855 374 RAIYLLIRRMTeLGMKVAMLYY--GRLFIQyGQMSTGNLVSFILYQQDL 420
Cdd:cd18550 224 GRWFFAALGLF-TAIGPALVYWvgGLLVIG-GGLTIGTLVAFTALLGRL 270
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
483-691 |
1.65e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHSK-VAMVGQEPVLFSG-T 560
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFPHmS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDNIAYGL--QGCSME----RVKEAASKANAHSFisklEKGYdtdVGErgnlLSGGEKQRIAIARALIREPQVLILDEV 634
Cdd:PRK11432 95 LGENVGYGLkmLGVPKEerkqRVKEALELVDLAGF----EDRY---VDQ----ISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 635 TSSLDT-------ESEQMVQQALSCcptqTLLVIAH-RLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK11432 164 LSNLDAnlrrsmrEKIRELQQQFNI----TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
486-682 |
2.15e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQhkylhSKVAMVGQEPVLFS-GTVRDN 564
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 565 IAYGLQGcsmeRVKEAASKAnahsfiskLEKgydtdVG--ERGN----LLSGGEKQRIAIARALIREPQVLILDEVTSSL 638
Cdd:PRK11247 102 VGLGLKG----QWRDAALQA--------LAA-----VGlaDRANewpaALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29561855 639 DTESEQMVQQALSCCPTQ---TLLVIAHRL-KTIERADQIVVIDSGEL 682
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
480-696 |
2.89e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLqDYQHK---YLHSKVAMVGQEP-- 554
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 VLFSGTVRDNIAYGLQGCSM------ERVKEAASKANAHSFISKLEKgydtdvgergnLLSGGEKQRIAIARALIREPQV 628
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVpeaeitRRVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 629 LILDEVTSSLDTESE-QMVQQALSCCPTQTLLVI-AHRLKTI-ERADQIVVIDSGELVEKG------THEELMEKKG 696
Cdd:PRK13638 158 LLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
469-692 |
3.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPR-RPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQH-KYLHSK 546
Cdd:PRK13644 2 IRLENVSYSYPDgTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEP-VLFSG-TVRDNIAYGLQGCSME--RVKEAASKANAHSFISKLEKgydtdvgERGNLLSGGEKQRIAIARAL 622
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRH-------RSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALSCC--PTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
484-689 |
3.67e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG------KPLQDYQHKYLHSKVAMVGQE---- 553
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLfsgTVRDNIAYGlqGCSMERVKEAASKANAHSFISKLEKgydTDVGERGNL-LSGGEKQRIAIARALIREPQVLILD 632
Cdd:PRK11124 95 PHL---TVQQNLIEA--PCRVLGLSKDQALARAEKLLERLRL---KPYADRFPLhLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 633 EVTSSLDTE-SEQMVQQALSCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:PRK11124 167 EPTAALDPEiTAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
474-659 |
4.88e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.23 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQD--------YQHkylhs 545
Cdd:PRK11248 7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvFQN----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 kvamvgqEPVLFSGTVRDNIAYGLQGCSMERvkeAASKANAHSFISKLekgydtDVGERGN----LLSGGEKQRIAIARA 621
Cdd:PRK11248 79 -------EGLLPWRNVQDNVAFGLQLAGVEK---MQRLEIAHQMLKKV------GLEGAEKryiwQLSGGQRQRVGIARA 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 29561855 622 LIREPQVLILDEVTSSLDT-ESEQMvqqalsccptQTLL 659
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAfTREQM----------QTLL 171
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-416 |
4.92e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 94.11 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVID------ILGSHYQWdnFRSAIIFMGLFSLGSSFSAGCRGglFMCAI--NSFTC 224
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvliqlGPGGNTSL--LLLLVLGLAGAYVLSALLGILRG--RLLARlgERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 225 RVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLT 304
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 305 GLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRlmethNLKTRRDTVRAIYL------ 378
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEA-----NQELLDANIRAEKLwatffp 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 29561855 379 LIRRMTELGMkVAMLYYGRLFIQYGQMSTGNLVSFILY 416
Cdd:cd18563 232 LLTFLTSLGT-LIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
469-686 |
5.16e-21 |
|
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: 91.96 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRrpdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLqDYQHKylhSKVA 548
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR---NRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSG-TVRDNIAY--GLQGcsmerVKEAASKANAHSFISKLEkgydtdVGERGNL----LSGGEKQRIAIARA 621
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlaQLKG-----LKKEEARRRIDEWLERLE------LSEYANKrveeLSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgkTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
469-664 |
6.85e-21 |
|
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: 90.29 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSyprRPDHNVL-KDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTIlldgkplqdyqHKYLHSKV 547
Cdd:cd03223 1 IELENLSLA---TPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSGTVRDNIAYGLQgcsmervkeaaskanahsfisklekgydtDVgergnlLSGGEKQRIAIARALIREPQ 627
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIYPWD-----------------------------DV------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29561855 628 VLILDEVTSSLDTESE----QMVQQALSccptqTLLVIAHR 664
Cdd:cd03223 112 FVFLDEATSALDEESEdrlyQLLKELGI-----TVISVGHR 147
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
469-691 |
7.54e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRpdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQpQQGTILLDGKPLQDYQHKY------ 542
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 --LHSKVAMVGQEPVLFSGTVRDNIAYGLQ------GCSMERVKEAASKAnahsfiSKLEKGYDTDVGERGNLLSGGEKQ 614
Cdd:PRK14258 84 nrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 615 RIAIARALIREPQVLILDEVTSSLDTESEQMVQ---QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDS-----GELVEK 685
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVEsliQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
....*.
gi 29561855 686 GTHEEL 691
Cdd:PRK14258 238 GLTKKI 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
482-680 |
9.30e-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: 91.24 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 482 PDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSK----VAMVGQEPVLF 557
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SGTVRDNIAYGlQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:cd03290 92 NATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29561855 638 LDTE-SEQMVQQALSCC---PTQTLLVIAHRLKTIERADQIVVIDSG 680
Cdd:cd03290 171 LDIHlSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
486-691 |
1.18e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHkyLHSK---VAMVGQEPVLFSG-TV 561
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSR--LHARdrkVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYGLqgcSM----ERVKEAASKANAHSFISKLEKGYdtdVGER-GNLLSGGEKQRIAIARALIREPQVLILDEVTS 636
Cdd:PRK10851 92 FDNIAFGL---TVlprrERPNAAAIKAKVTQLLEMVQLAH---LADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 637 SLDT----ESEQMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK10851 166 ALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
487-702 |
1.22e-20 |
|
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: 91.37 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLhskvaMVGQEPVLFSG-TVRDNI 565
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYglqgcSMERVKEAASKANAHSFISK------LEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:TIGR01184 76 AL-----AVDRVLPDLSKSERRAIVEEhialvgLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 640 TESEQMVQ-QALSCCPTQ--TLLVIAHRL-KTIERADQIVVIDSGELVEKGT-----------HEELMEKKgSYYKLR 702
Cdd:TIGR01184 147 ALTRGNLQeELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQilevpfprprdRLEVVEDP-SYYDLR 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
480-692 |
1.47e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKST---CVSLLERfyqPQQGTILLDGKPLQ-------------DYQHKYL 543
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSG-TVRDNIAYG---LQGCSMERVKEAASKANAHSFISKLEKG-YDTDvgergnlLSGGEKQRIAI 618
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHmTVLENVMEApiqVLGLSKQEARERAVKYLAKVGIDERAQGkYPVH-------LSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 619 ARALIREPQVLILDEVTSSLDTE--------SEQMVQQAlsccptQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPElvgevlriMQQLAEEG------KTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPE 237
|
...
gi 29561855 690 ELM 692
Cdd:PRK10619 238 QLF 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
486-695 |
1.81e-20 |
|
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: 90.66 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGCsmervkeAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESE 643
Cdd:TIGR03410 95 NLLTGLAAL-------PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 644 QMVQQALSCCPTQT----LLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:TIGR03410 168 KDIGRVIRRLRAEGgmaiLLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-441 |
3.11e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 92.19 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVID-ILGSH-----------YQWDNFR----SAIIFMGLFSLGSSFSAGcrgGLFM 216
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKplpgllglaplLGPDPLAllllAAAALVGIALLRGLASYA---GTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 217 CAI--NSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLT 294
Cdd:cd18564 78 TALvgQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 295 LLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYdgrlmETHNLKTRRDTVR 374
Cdd:cd18564 158 LIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRF-----ARENRKSLRAGLR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 375 AIYL--LIRRMTELGMKVA---MLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLiyifGDMLNSVGAA 441
Cdd:cd18564 233 AARLqaLLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDL----AKLTGRIAKA 300
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-420 |
4.49e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 91.47 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDI---------------LGSHYQWDNF-RSAIIFMGLFSLGSSFSagcrgGLFM 216
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAvfngeasflplvpasLGPADPRGQLwLLGGLTVAAFLLESLFQ-----YLSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 217 CAINSFTCRV----KVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWK 292
Cdd:cd18565 76 VLWRRFAQRVqhdlRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 293 LTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDT 372
Cdd:cd18565 156 LALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 373 VRAIYLLIRRM-TELGMKVAMLYYGRLFIQ-----YGQMSTGNLVSFILYQQDL 420
Cdd:cd18565 236 LRAAFFPVIRLvAGAGFVATFVVGGYWVLDgpplfTGTLTVGTLVTFLFYTQRL 289
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
153-428 |
4.55e-20 |
|
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: 91.36 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAV-LCEMFIPLYTGEVIDILGSHYQWDN-FRSAIIFMGLFslgssfsagcrggLFMCAINSFTCR----- 225
Cdd:cd18549 3 LFFLDLFCAVLIaALDLVFPLIVRYIIDDLLPSKNLRLiLIIGAILLALY-------------ILRTLLNYFVTYwghvm 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 226 -VKVQ------LFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLML 298
Cdd:cd18549 70 gARIEtdmrrdLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 299 METPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDgRLMETHnLKTRRDTVRA--- 375
Cdd:cd18549 150 ALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFD-EGNDRF-LESKKKAYKAmay 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 376 ----IYLLIRRMTelgmkVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLI 428
Cdd:cd18549 228 ffsgMNFFTNLLN-----LVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLV 279
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
487-695 |
5.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPL----QDYQHKYLHSKVAMVGQ--EPVLFSGT 560
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDNIAYGLQ--GCSMERVKEAASKANAHSFISklEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSL 638
Cdd:PRK13649 103 VLKDVAFGPQnfGVSQEEAEALAREKLALVGIS--ESLFEKNPFE----LSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 639 D--------TESEQMVQQALsccptqTLLVIAHRLKTI-ERADQIVVIDSGELVEKGT------HEELMEKK 695
Cdd:PRK13649 177 DpkgrkelmTLFKKLHQSGM------TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKpkdifqDVDFLEEK 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-691 |
5.38e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQ--PQ---QGTILLDGKPLQDYQHKYLHSKVAMVGQEP-VL 556
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSGTVRDNIAYGLQGCSM--------ERVKEAASKANahsFISKLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQV 628
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLvkskkelqERVRWALEKAQ---LWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 629 LILDEVTSSLDTESEQMVQQA-LSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLfLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
469-695 |
7.02e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyQHKYLHSKVA 548
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVL-FSGTVRDN-IAYGlQGCSMERVKEAASKANAHSFiSKLEKGYDTDVGErgnlLSGGEKQRIAIARALIREP 626
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARgkTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
485-691 |
9.34e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 485 NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHS-KVAMVGQEPVLFSG-TVR 562
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAYGLQgcsmervKEAASKANAHSFISKLEKGYDTDVgeRGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLD-TE 641
Cdd:PRK15439 105 ENILFGLP-------KRQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 642 SEQMVQQalsccpTQTLLV-------IAHRLKTI-ERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK15439 176 TERLFSR------IRELLAqgvgivfISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
472-691 |
9.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:PRK13652 7 RDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEP--VLFSGTVRDNIAYGlqGCSMERVKEAAskanAHSFISKLEKGYDTDVGERG-NLLSGGEKQRIAIARALIREPQV 628
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAFG--PINLGLDEETV----AHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 629 LILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
480-641 |
1.06e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.92 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ---QGTILLDGKPLQDYQhkYLHSKVAMVGQEPVL 556
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP--AEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSG-TVRDNIAYGLQgcsmERVKEAASKANAHSFISKLEKG--YDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:COG4136 88 FPHlSVGENLAFALP----PTIGRAQRRARVEQALEEAGLAgfADRDPAT----LSGGQRARVALLRALLAEPRALLLDE 159
|
....*...
gi 29561855 634 VTSSLDTE 641
Cdd:COG4136 160 PFSKLDAA 167
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
471-717 |
1.36e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplqdyqhkylHSKVAMV 550
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 GQEPVLFSG-TVRDNIAYGLQG-CSMERVKEAASKA---------------------NAHSFISKLEK----------GY 597
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElRALEAELEELEAKlaepdedlerlaelqeefealGGWEAEARAEEilsglgfpeeDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 598 DTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDTES----EQMVQQAlsccpTQTLLVIAH-R--LKTIer 670
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNY-----PGTVLVVSHdRyfLDRV-- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29561855 671 ADQIVVIDSGELVE-KGTHEELMEKKGSYYKLRERLFSddkttKQEKE 717
Cdd:COG0488 216 ATRILELDRGKLTLyPGNYSAYLEQRAERLEQEAAAYA-----KQQKK 258
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
153-416 |
1.41e-19 |
|
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: 89.77 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAgcrgglfmcAINSFTCRVKVQLFG 232
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAG---------ILAGYFAAKASQGFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 233 SLIRQDI-----GF----FETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPL 303
Cdd:cd18548 72 RDLRKDLfekiqSFsfaeIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 304 TGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYD---GRLMEThNLKTRRDTVR---AIY 377
Cdd:cd18548 152 LALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDkanDDLTDT-SLKAGRLMALlnpLMM 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 29561855 378 LLIrrmtELGMkVAMLYYGRLFIQYGQMSTGNLVSFILY 416
Cdd:cd18548 231 LIM----NLAI-VAILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
484-691 |
1.79e-19 |
|
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: 92.44 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNVLKDFSLELKPGQITALVGMSGGGKS-TCVS---LLERFYQPQQGTILLDGKPLQDYQHKYLH----SKVAMVGQEPV 555
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSilrLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 -----LFsgTVRDNIAYGL---QGCS-----------MERV--KEAASKANA--HSfisklekgydtdvgergnlLSGGE 612
Cdd:COG4172 103 tslnpLH--TIGKQIAEVLrlhRGLSgaaararalelLERVgiPDPERRLDAypHQ-------------------LSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 613 KQRIAIARALIREPQVLILDEVTSSLD-TESEQMV------QQALSccptQTLLVIAHRLKTIER-ADQIVVIDSGELVE 684
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDvTVQAQILdllkdlQRELG----MALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
....*..
gi 29561855 685 KGTHEEL 691
Cdd:COG4172 238 QGPTAEL 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
477-633 |
2.40e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 477 SYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCvsllerFY------QPQQGTILLDGKPLQDYQ-HK-------Y 542
Cdd:COG1137 12 SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPmHKrarlgigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LhskvamvGQEPVLFSG-TVRDNIAYGLQGCSMERvKEAASKANA--HSF-ISKLEKgydtdvgERGNLLSGGEKQRIAI 618
Cdd:COG1137 83 L-------PQEASIFRKlTVEDNILAVLELRKLSK-KEREERLEEllEEFgITHLRK-------SKAYSLSGGERRRVEI 147
|
170
....*....|....*
gi 29561855 619 ARALIREPQVLILDE 633
Cdd:COG1137 148 ARALATNPKFILLDE 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
487-691 |
2.68e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdYQH--KYLHSKVAMVGQE----PVLfsgT 560
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASttAALAAGVAIIYQElhlvPEM---T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDNIAYGLQGCSMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDT 640
Cdd:PRK11288 96 VAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 641 -ESEQM--VQQALScCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEkgTHEEL 691
Cdd:PRK11288 174 rEIEQLfrVIRELR-AEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
483-687 |
3.67e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKST---CVS----LLERFYQpqQGTILLDGKPL--QDYQHKYLHSKVAMVGQE 553
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNrlndLIPGFRV--EGKVTFHGKNLyaPDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFSGTVRDNIAYG-----LQGcSMERVKEAASKANAhsfiskLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQV 628
Cdd:PRK14243 100 PNPFPKSIYDNIAYGaringYKG-DMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 629 LILDEVTSSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIERADQIVVIDSGELVEKGT 687
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQyTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
469-694 |
4.51e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLdGKPLQ----DYQHKYLH 544
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKigyfDQHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SkvamvgqepvlfSGTVRDNIAyglqgcsmeRVKEAASKANAHSFISK-LEKGYDTD--VGErgnlLSGGEKQRIAIARA 621
Cdd:COG0488 392 P------------DKTVLDELR---------DGAPGGTEQEVRGYLGRfLFSGDDAFkpVGV----LSGGEKARLALAKL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMVQQALsccptQ----TLLVIAH-R--LKTIerADQIVVIDSGELVEK-GTHEELME 693
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEAL-----DdfpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLE 519
|
.
gi 29561855 694 K 694
Cdd:COG0488 520 K 520
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
475-692 |
5.07e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 475 TFSYP----RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMV 550
Cdd:PRK15112 13 TFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 GQEPVLfSGTVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEK-GYDTD-VGERGNLLSGGEKQRIAIARALIREPQV 628
Cdd:PRK15112 93 FQDPST-SLNPRQRISQILD-FPLRLNTDLEPEQREKQIIETLRQvGLLPDhASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 629 LILDEVTSSLD-TESEQMVQQALSCCPTQT---LLVIAH--RLKTIerADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK15112 171 IIADEALASLDmSMRSQLINLMLELQEKQGisyIYVTQHlgMMKHI--SDQVLVMHQGEVVERGSTADVL 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
469-694 |
7.76e-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: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRrpDHNVLKDFSLELKPGQITALVGMSGGGKSTC---VSLLERFyqpQQGTILLDGKPLQDyqhkyLHS 545
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNE-----LEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 K---VAMVGQEPVLFSG-TVRDNIAYGLQGCSM------ERVKEAASkanahsfISKLEKGYDtdvgERGNLLSGGEKQR 615
Cdd:PRK11650 74 AdrdIAMVFQNYALYPHmSVRENMAYGLKIRGMpkaeieERVAEAAR-------ILELEPLLD----RKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTESE-QM------VQQALSccpTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTH 688
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRvQMrleiqrLHRRLK---TTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*.
gi 29561855 689 EELMEK 694
Cdd:PRK11650 220 VEVYEK 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
460-691 |
8.87e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.10 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 460 LMPKDLKGHVKFQKLTFSYPRRPdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ 539
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLFKPERLV--KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 540 H---KYLHSKVAMVGQEPvlFSG-----TVRDNIAYGLQ-GCSMERvkeAASKANAHSFISKlekgydtdVGERG----- 605
Cdd:PRK11308 84 PeaqKLLRQKIQIVFQNP--YGSlnprkKVGQILEEPLLiNTSLSA---AERREKALAMMAK--------VGLRPehydr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 606 --NLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMV-------QQALSCcptqTLLVIAHRLKTIER-ADQIV 675
Cdd:PRK11308 151 ypHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQELGL----SYVFISHDLSVVEHiADEVM 226
|
250
....*....|....*.
gi 29561855 676 VIDSGELVEKGTHEEL 691
Cdd:PRK11308 227 VMYLGRCVEKGTKEQI 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
487-691 |
1.02e-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: 85.50 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyQHKYLHSKVAMVGQEPVLFSG-TVRDNI 565
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 A-----YGLQGCSM-ERVKEAASKANAHSFISKLEKGYdtdvgergnllSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:cd03265 95 YiharlYGVPGAERrERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 640 TESEQMVQ---QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:cd03265 164 PQTRAHVWeyiEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
486-686 |
1.16e-18 |
|
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: 85.40 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTcvsLLERFYQPQQ------GTILLDGKPLQDYQHKYlhsKVAMVGQEPVLFSG 559
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT---LLDAISGRVEgggttsGQILFNGQPRKPDQFQK---CVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 -TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKgyDTDVGerGNL---LSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:cd03234 96 lTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIG--GNLvkgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 636 SSLDTESEQMVQQALSCCPTQTLLVIAhrlkTIERA--------DQIVVIDSGELVEKG 686
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVIL----TIHQPrsdlfrlfDRILLLSSGEIVYSG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
486-646 |
1.55e-18 |
|
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: 85.18 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILldgkplqdYQHKYlhSKVAMVGQEPVlfsgTV---- 561
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG--GWVDLAQASPR----EIlalr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYglqgCS-----------MERVKEAAskanahsfiskLEKGYDTDVGER--GNLL-----------------SGG 611
Cdd:COG4778 92 RRTIGY----VSqflrviprvsaLDVVAEPL-----------LERGVDREEARAraRELLarlnlperlwdlppatfSGG 156
|
170 180 190
....*....|....*....|....*....|....*
gi 29561855 612 EKQRIAIARALIREPQVLILDEVTSSLDTESEQMV 646
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
486-696 |
2.27e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLL---ERfYQPQQGTILLDGKPLqdyqhkyLHSKV----------AMvgQ 552
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI-------LELSPderaragiflAF--Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 553 EPVLFSG-TVRD--NIAYGLQGCS-------MERVKEAASKAN-AHSFISKlekgyDTDVGergnlLSGGEKQRIAIARA 621
Cdd:COG0396 85 YPVEIPGvSVSNflRTALNARRGEelsarefLKLLKEKMKELGlDEDFLDR-----YVNEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMV----QQALSccPTQTLLVIAH--RLKTIERADQIVVIDSGELVEKGTHE--ELME 693
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVaegvNKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElaLELE 232
|
...
gi 29561855 694 KKG 696
Cdd:COG0396 233 EEG 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
487-690 |
2.78e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELK---PGQ-ITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK-YL---HSKVAMVGQEPVLFS 558
Cdd:PRK11144 10 LGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 559 G-TVRDNIAYGLqgcsmervkeaASKANAHsF--------ISKLEKGYDTDvgergnlLSGGEKQRIAIARALIREPQVL 629
Cdd:PRK11144 90 HyKVRGNLRYGM-----------AKSMVAQ-FdkivallgIEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 630 ILDEVTSSLDTESEQMVQQALsccptQTL--------LVIAHRLKTIER-ADQIVVIDSGELVEKGTHEE 690
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYL-----ERLareinipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
486-695 |
2.94e-18 |
|
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: 89.97 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhskVAMVGQEPVLFSGTVRDNI 565
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQM 645
Cdd:TIGR01271 508 IFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29561855 646 VQQALSC--CPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKK 695
Cdd:TIGR01271 587 IFESCLCklMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
486-691 |
5.06e-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: 84.91 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhskVAMVGQEPVLFSGTVRDNI 565
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQM 645
Cdd:cd03291 119 IFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29561855 646 VQQALSC--CPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:cd03291 198 IFESCVCklMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
488-691 |
1.26e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 488 KDFSLELKPGQITALVGMSGGGKST---CVSLLERFyqpQQGTILLDGKPLQDYQHKylHSKVAMVGQEPVLFSG-TVRD 563
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLEDI---TSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHlSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGCSMERvKEAASKANAHSFISKLEKGYDtdvgERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESE 643
Cdd:PRK11000 95 NMSFGLKLAGAKK-EEINQRVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 644 -QM------VQQALSCcptqTLLVIAH-RLKTIERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK11000 170 vQMrieisrLHKRLGR----TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-687 |
1.77e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 485 NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKylhSKVAMVGQE--------PVL 556
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA---AKAELRNQKlgfiyqfhHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSGTVRDNIAYGLQgcsMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTS 636
Cdd:PRK11629 100 PDFTALENVAMPLL---IGKKKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 637 SLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIVVIDSGELVEKGT 687
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLqgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
486-691 |
2.44e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQP-----QQGTILLDGKPLQDYQHKY-LHSKVAMVGQEPVLFSG 559
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 640 -TESEQMVQQALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK14271 196 pTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
477-677 |
2.68e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 477 SYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplqdyqhkylHSKVAMVGQ---E 553
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFSGTVRDNIAYGLQGcsmERVKEAASKANAHSFISK-LEK-GYDTDVGERGNLLSGGEKQRIAIARALIREPQVLIL 631
Cdd:NF040873 67 PDSLPLTVRDLVAMGRWA---RRGLWRRLTRDDRAAVDDaLERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29561855 632 DEVTSSLDTESEQMVQQALS--CCPTQTLLVIAHRLKTIERADQIVVI 677
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAeeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
467-698 |
3.80e-17 |
|
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: 82.21 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYpRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQpQQGTILLDG-----KPLQDYQHK 541
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 542 YlhskvAMVGQEPVLFSGTVRDNI-AYGLQgcSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIAR 620
Cdd:cd03289 79 F-----GVIPQKVFIFSGTFRKNLdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 621 ALIREPQVLILDEVTSSLDTESEQMV----QQALSCCptqTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKG 696
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIrktlKQAFADC---TVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
..
gi 29561855 697 SY 698
Cdd:cd03289 229 HF 230
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
150-414 |
3.86e-17 |
|
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: 82.49 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 150 YILLFGAFVFLALAVLCEMFIPLYTGEVID-ILGSHYQwDNFRSAIIFMGLFSLGSSFSAGCRGGLfmcaINSFTCRVKV 228
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDdIIPSGDI-NLLNIISIGLILLYLFQSLLSYIRSYL----LLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QL----FGSLIRQDIGFFETIKTGDITSRLStDTTLMGRAVA-LNVNVLLRTLVkTLGMLYLMVSLSWKLTLLMLMETPL 303
Cdd:cd18570 76 RLilgyFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISsTTISLFLDLLM-VIISGIILFFYNWKLFLITLLIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 304 TGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRM 383
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250 260 270
....*....|....*....|....*....|.
gi 29561855 384 TELGMKVAMLYYGRLFIQYGQMSTGNLVSFI 414
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
462-691 |
4.04e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 462 PKDLKGHVKFQKLTFSyPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLErFYQPQ----QGTILLDGKPLQD 537
Cdd:TIGR00955 17 DGSWKQLVSRLRGCFC-RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 538 YQhkyLHSKVAMVGQEPVLF-SGTVRDNiaygLQGCSMERVKEAASKANAHSFISK------LEKGYDTDVGERGNL--L 608
Cdd:TIGR00955 95 KE---MRAISAYVQQDDLFIpTLTVREH----LMFQAHLRMPRRVTKKEKRERVDEvlqalgLRKCANTRIGVPGRVkgL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVqqalsccpTQTLLVIAHRLKTI------------ERADQIVV 676
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV--------VQVLKGLAQKGKTIictihqpsselfELFDKIIL 239
|
250
....*....|....*
gi 29561855 677 IDSGELVEKGTHEEL 691
Cdd:TIGR00955 240 MAEGRVAYLGSPDQA 254
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
486-693 |
4.98e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.99 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDgkplqdyqhkylhSKVAMVGQEPVLFSGTVRDNI 565
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYgLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTE-SEQ 644
Cdd:PTZ00243 742 LF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29561855 645 MVQQ----ALSCcptQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELME 693
Cdd:PTZ00243 821 VVEEcflgALAG---KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
472-692 |
1.08e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRrpdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVG 551
Cdd:PRK10253 11 EQLTLGYGK---YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVLFSG-TVRDNIAYG------LQGCSMERVKEAASKANAHSFISKLekgydtdVGERGNLLSGGEKQRIAIARALIR 624
Cdd:PRK10253 88 QNATTPGDiTVQELVARGryphqpLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 625 EPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREkgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-691 |
1.33e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKS-TCVSLLERFYQPQ----QGTILLDGKPLQDYQHKYLH----SKVAMVGQE 553
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLfSGTVRDNIAYGL-QGCSMER--VKEAASKanahSFISKLEKgydtdVGER---GNL------LSGGEKQRIAIARA 621
Cdd:PRK15134 101 PMV-SLNPLHTLEKQLyEVLSLHRgmRREAARG----EILNCLDR-----VGIRqaaKRLtdyphqLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 622 LIREPQVLILDEVTSSLD-TESEQMVQ------QALSccptQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK15134 171 LLTRPELLIADEPTTALDvSVQAQILQllrelqQELN----MGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
472-723 |
1.41e-16 |
|
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: 83.45 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGtillDGKPLQDYqhkylhsKVAMVG 551
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----EARPQPGI-------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVL-FSGTVRDNIAYGLQ--------------------------GCSMERVKEAASKANAHSFISKLEKG-------- 596
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAeikdaldrfneisakyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEIAmdalrcpp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 597 YDTDVgergNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTqTLLVIAHrlktiER------ 670
Cdd:TIGR03719 155 WDADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG-TVVAVTH-----DRyfldnv 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 671 ADQIVVIDSGELVE-KGTHEELMEKKgsyyklRERLFSDDkttKQEKEKSDTVK 723
Cdd:TIGR03719 225 AGWILELDRGRGIPwEGNYSSWLEQK------QKRLEQEE---KEESARQKTLK 269
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
483-639 |
1.91e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVL-FSGTV 561
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYG---------LQGCSMER-VKEAASKANAHSFIsklekgyDTDVGErgnlLSGGEKQRIAIARALIREPQVLIL 631
Cdd:PRK09536 95 RQVVEMGrtphrsrfdTWTETDRAaVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARALAQATPVLLL 163
|
....*...
gi 29561855 632 DEVTSSLD 639
Cdd:PRK09536 164 DEPTASLD 171
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
153-441 |
2.01e-16 |
|
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: 80.59 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVID--ILGSHYqWDNFRSAIIFMGLFsLGSSFSAGCRGGLFMCAINSFTCRVKVQL 230
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDeyIPNGDL-SGLLIIALLFLALN-LVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 231 FGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNI 310
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 311 YDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGrlmetHNLKTRRDTVRAIYL------LIRRMT 384
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDE-----LNRENRKANMRAVRLnalfwpLVELIS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 385 ELGMkVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAA 441
Cdd:cd18545 235 ALGT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASA 290
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
463-691 |
2.05e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.91 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 463 KDLKGHVKFqKLTFSYPRRPDHNV--LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQH 540
Cdd:PRK15079 12 ADLKVHFDI-KDGKQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 541 KYLH---SKVAMVGQEPvLFS----GTVRDNIAYGLQ--------GCSMERVKEAASKanahsfisklekgydtdVGERG 605
Cdd:PRK15079 91 DEWRavrSDIQMIFQDP-LASlnprMTIGEIIAEPLRtyhpklsrQEVKDRVKAMMLK-----------------VGLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 606 NLL-------SGGEKQRIAIARALIREPQVLILDEVTSSLDTESE-QMVQ--QALSCCPTQTLLVIAHRLKTIER-ADQI 674
Cdd:PRK15079 153 NLInryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaQVVNllQQLQREMGLSLIFIAHDLAVVKHiSDRV 232
|
250
....*....|....*..
gi 29561855 675 VVIDSGELVEKGTHEEL 691
Cdd:PRK15079 233 LVMYLGHAVELGTYDEV 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
475-698 |
2.42e-16 |
|
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: 83.84 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 475 TFSYPRrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhskVAMVGQEP 554
Cdd:TIGR00957 643 TFTWAR-DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 555 VLFSGTVRDNIaygLQGCSMERvKEAASKANAHSFISKLE---KGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLIL 631
Cdd:TIGR00957 709 WIQNDSLRENI---LFGKALNE-KYYQQVLEACALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 632 DEVTSSLDTESEQMVQQAL----SCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSY 698
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVigpeGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
487-641 |
2.72e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKP---LQDYQHKYLHSKVAMVGQEP-VLFSGTVR 562
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAYGL--QGCSMERVKEAASKANAHsfISKLEKGYDTDVGergnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDT 640
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRRRVSAALDK--VGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
.
gi 29561855 641 E 641
Cdd:PRK10908 171 A 171
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
488-691 |
2.92e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 488 KDFSLELKPGQITALVGMSGGGKS-TCVSLLERF---YQPQQGTILLDGKPLQDYQHKYLHskVAMVGQEPVLFSGTVRD 563
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNPRSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGLQGCsmervKEAASKANAHSFISKLEkgydtDVG--ERGNLL-------SGGEKQRIAIARALIREPQVLILDEV 634
Cdd:PRK10418 98 MHTHARETC-----LALGKPADDATLTAALE-----AVGleNAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 635 TSSLDTESEQ---------MVQQALSccptqtLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK10418 168 TTDLDVVAQArildllesiVQKRALG------MLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
491-691 |
4.02e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 491 SLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLF-SGTVRDN---- 564
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMGVVRTFQHVRLFrEMTVIENllva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 565 --------IAYGLQGCSMERVKEAASKANAHSFiskLEKGYDTDVGER--GNLlSGGEKQRIAIARALIREPQVLILDEV 634
Cdd:PRK11300 105 qhqqlktgLFSGLLKTPAFRRAESEALDRAATW---LERVGLLEHANRqaGNL-AYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 635 TSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhnvTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
469-681 |
4.18e-16 |
|
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: 75.56 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhSKVA 548
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQepvlfsgtvrdniayglqgcsmervkeaaskanahsfisklekgydtdvgergnlLSGGEKQRIAIARALIREPQV 628
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 629 LILDEVTSSLDTESEQMVQQALSCCPtQTLLVIAH-R--LKTIerADQIVVIDSGE 681
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
470-686 |
5.14e-16 |
|
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: 77.57 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 470 KFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPlqdyqhkylHSKVAM 549
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 -VGQEPVLfsgTVRDNIAYG--LQGCSmerVKEAASKANA-HSFiSKLEKGYDTDVGErgnlLSGGEKQRIAIARALIRE 625
Cdd:cd03220 92 gGGFNPEL---TGRENIYLNgrLLGLS---RKEIDEKIDEiIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 626 PQVLILDEVTSSLDTESEQMVQQALSCC--PTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELlkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
487-686 |
5.29e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKyLHSK--VAMVGQE-PVLFSGTVRD 563
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYG------LQGCSMERVKEAASKANAHSFISKLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:PRK09700 100 NLYIGrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 638 L-DTESEQM---VQQALSccPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:PRK09700 176 LtNKEVDYLfliMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
467-678 |
5.40e-16 |
|
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: 82.65 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 467 GHVKFQKLTFSYPRrPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQpQQGTILLDGKPLQDYQHKYLHSK 546
Cdd:TIGR01271 1216 GQMDVQGLTAKYTE-AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPVLFSGTVRDNIAYGLQgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREP 626
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDPYEQ-WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 627 QVLILDEVTSSLDTESEQMV----QQALSCCptqTLLVIAHRLKTIERADQIVVID 678
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIrktlKQSFSNC---TVILSEHRVEALLECQQFLVIE 1425
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
476-686 |
5.46e-16 |
|
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: 78.14 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 476 FSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPV 555
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 L-FSGTVRDNIAYgLQgcSMERVKEAASKANAHSFISKLEKGYDTDVGERGnlLSGGEKQRIAIARALIREPQVLILDEV 634
Cdd:cd03267 106 LwWDLPVIDSFYL-LA--AIYDLPPARFKKRLDELSELLDLEELLDTPVRQ--LSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 635 TSSLDTESEQMVQQALS--CCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKG 686
Cdd:cd03267 181 TIGLDVVAQENIRNFLKeyNRERGtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-693 |
6.73e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQ-----GTILLDGKPL--QDYQHKYLHSKVAMVGQEPV 555
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 LFSG-TVRDNIAYGLQGCSM--------ERVKEAASKANAHSFISKLEKGYDTDvgergnlLSGGEKQRIAIARALIREP 626
Cdd:PRK14267 96 PFPHlTIYDNVAIGVKLNGLvkskkeldERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 627 QVLILDEVTSSLDTESEQMVQQALSCCPTQ-TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEyTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
487-681 |
9.65e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.74 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYqPQ---QGTILLDGKPLQ-----DYQHKylhsKVAMVGQEPVLFS 558
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQasnirDTERA----GIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 559 G-TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:PRK13549 96 ElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 638 LdTESEQMV---------QQALSCcptqtlLVIAHRLKTIER-ADQIVVIDSGE 681
Cdd:PRK13549 174 L-TESETAVlldiirdlkAHGIAC------IYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
477-683 |
1.10e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 477 SYPRRPDH-NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGT--------ILLDGKPL------------ 535
Cdd:PRK10535 13 SYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALaqlrrehfgfif 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 536 QDYqHKYLHSKVAMVGQEPVLFSGTVRdniayglqgcsmervkeAASKANAHSFISKLekGYDTDVGERGNLLSGGEKQR 615
Cdd:PRK10535 93 QRY-HLLSHLTAAQNVEVPAVYAGLER-----------------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 616 IAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIVVIDSGELV 683
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
469-639 |
1.18e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRpdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVA 548
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 M---VGQEPVLFSGTVRDNIAYGLqgcsmERVKEAaskanaHSFISKLEKgydtdvgergnlLSGGEKQRIAIARALIRE 625
Cdd:PRK09544 82 LpltVNRFLRLRPGTKKEDILPAL-----KRVQAG------HLIDAPMQK------------LSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 29561855 626 PQVLILDEVTSSLD 639
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
480-692 |
1.22e-15 |
|
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: 77.05 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQG-TILLDGKPL-----QDyqhkyLHSKVAMVG-- 551
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggedvWE-----LRKRIGLVSpa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 -QEPVLFSGTVRDNIAYGLQGcSMERVKE--AASKANAHSFI------SKLEKGYDTdvgergnlLSGGEKQRIAIARAL 622
Cdd:COG1119 87 lQLRFPRDETVLDVVLSGFFD-SIGLYREptDEQRERARELLellglaHLADRPFGT--------LSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 623 IREPQVLILDEVTSSLDTES-EQMVQ--QALSCCPTQTLLVIAHRL----KTIERAdqiVVIDSGELVEKGTHEELM 692
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGArELLLAllDKLAAEGAPTLVLVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
483-694 |
1.47e-15 |
|
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: 80.23 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERF--YQPQQGTIL----------------LDGKP---------- 534
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 535 -------LQDYQHKYLHSKVAMVGQEPVLFSG--TVRDNIAYGLQGCSMErVKEAASKAnahsfiskLEKGYDTDVGER- 604
Cdd:TIGR03269 92 eevdfwnLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYE-GKEAVGRA--------VDLIEMVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 605 ---GNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVI 677
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgiSMVLTSHWPEVIEDlSDKAIWL 242
|
250
....*....|....*..
gi 29561855 678 DSGELVEKGTHEELMEK 694
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
144-537 |
1.65e-15 |
|
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: 80.23 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 144 RLYRPDYILLFGAFVFLALAVLCEMFIpLYTgeVIDILGSHYQwDNFRSAIIFMGL--FSLGSSFSAGCrggLFMCAINS 221
Cdd:COG4615 6 LLLRESRWLLLLALLLGLLSGLANAGL-IAL--INQALNATGA-ALARLLLLFAGLlvLLLLSRLASQL---LLTRLGQH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 222 FTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNvLLRTLVKTLGMLYLMVSLSWKLTLLMLMET 301
Cdd:COG4615 79 AVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQSVALVLGCLAYLAWLSPPLFLLTLVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 302 PLTGLLqniydthYQKLSKEVQDSMAQANDAAGEAVSGIRTV-KSFKtEL----GEAHRYDGRLMETHNLKTRRDTVRA- 375
Cdd:COG4615 158 GLGVAG-------YRLLVRRARRHLRRAREAEDRLFKHFRALlEGFK-ELklnrRRRRAFFDEDLQPTAERYRDLRIRAd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 376 -IYLLIRRMTELGMKVAM---LYygrLFIQYGQMSTGNLVSFILyqqdlgdnirTLIYIFGDMLNSVG----------AA 441
Cdd:COG4615 230 tIFALANNWGNLLFFALIgliLF---LLPALGWADPAVLSGFVL----------VLLFLRGPLSQLVGalptlsranvAL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 442 GKVFE-----YQDRKSEVSIDGNLMPKDLKgHVKFQKLTFSYPRRPDHN--VLKDFSLELKPGQITALVGMSGGGKSTCV 514
Cdd:COG4615 297 RKIEElelalAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
410 420
....*....|....*....|...
gi 29561855 515 SLLERFYQPQQGTILLDGKPLQD 537
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTA 398
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
153-416 |
3.87e-15 |
|
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: 76.76 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVID--ILGSHYqwdnfrSAIIFMGLFSLGSSFSAGCRGGLFMCAIN----SFTCRV 226
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGDL------GVLLLAAAAYLAVVLAGWVAQRAQTRLTGrtgeRLLYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 227 KVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGL 306
Cdd:cd18546 75 RLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 307 LQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGrlmetHNLKTRRDTVRAIYLL------I 380
Cdd:cd18546 155 ATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAE-----LSDDYRDARLRAQRLVaiyfpgV 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 29561855 381 RRMTELGMkVAMLYYGRLFIQYGQMSTGNLVSFILY 416
Cdd:cd18546 230 ELLGNLAT-AAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
160-428 |
3.98e-15 |
|
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: 76.73 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 160 LALAVLCEMFI---PLYTGEVID-ILGSHyqwD-NFRSAI-IFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGS 233
Cdd:cd18567 8 LLLSLALELFAlasPLYLQLVIDeVIVSG---DrDLLTVLaIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 234 LIRQDIGFFETIKTGDITSRL-STDT---TLMGRAVALNVNVLLrtlvkTLGMLYLMVSLSWKLTLLMLMETPLTGLLQN 309
Cdd:cd18567 85 LLRLPLSYFEKRHLGDIVSRFgSLDEiqqTLTTGFVEALLDGLM-----AILTLVMMFLYSPKLALIVLAAVALYALLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 310 IYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMK 389
Cdd:cd18567 160 ALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLEN 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 29561855 390 VAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLI 428
Cdd:cd18567 240 ILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLI 278
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
486-692 |
7.81e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG-TVRD 563
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYGlqGCSMERVKEAASKANAHSFISKLekgYDTDVgERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSL----- 638
Cdd:PRK11614 100 NLAMG--GFFAERDQFQERIKWVYELFPRL---HERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLapiii 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 639 ----DTeSEQMVQQALSccptqTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK11614 174 qqifDT-IEQLREQGMT-----IFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
464-691 |
7.84e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 464 DLKGHVKFQKLTFSYPRRP--DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQG-TILLDGKPLQDYQH 540
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 541 ----KYLHSKVAMVGQEP--VLFSGTVRDNIAYGlqgcsmeRVKEAASKANAHSFISKLEK--GYDTDVGERGNL-LSGG 611
Cdd:PRK13645 82 ikevKRLRKEIGLVFQFPeyQLFQETIEKDIAFG-------PVNLGENKQEAYKKVPELLKlvQLPEDYVKRSPFeLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 612 EKQRIAIARALIREPQVLILDEVTSSLDTESEQ---MVQQALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGT 687
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
....
gi 29561855 688 HEEL 691
Cdd:PRK13645 235 PFEI 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
486-696 |
8.50e-15 |
|
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: 73.72 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERF--YQPQQGTILLDGKPLQDYQhKYLHSK--VAMVGQEPVLFSG-T 560
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARlgIFLAFQYPPEIPGvK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 561 VRDniayglqgcsmervkeaaskanahsFISKLEKGydtdvgergnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDT 640
Cdd:cd03217 94 NAD-------------------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 641 ESEQMVQQALSCC--PTQTLLVIAHRLKTIE--RADQIVVIDSGELVEKGTHE--ELMEKKG 696
Cdd:cd03217 138 DALRLVAEVINKLreEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
484-682 |
9.24e-15 |
|
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: 72.85 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMV----GQEPVLFS 558
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 559 GTVRDNIAYGlqgcsmervkeaaskanahsfisklekgydtdvgergNLLSGGEKQRIAIARALIREPQVLILDEVTSSL 638
Cdd:cd03215 93 LSVAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29561855 639 DTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGEL 682
Cdd:cd03215 136 DVGAKAEIYRLIRELADAgkAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
191-415 |
2.42e-14 |
|
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: 74.62 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 191 RSAIIFMGLfSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVN 270
Cdd:cd18558 60 LYAYYYLII-GAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 271 VLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTEL 350
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQ 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 351 GEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFIL 415
Cdd:cd18558 219 KEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFF 283
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
435-693 |
3.13e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 435 LNSVGAAGKVFEYQDRKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPDHNVlKDFSLELKPGQITALVGMSGGGKSTCV 514
Cdd:PRK10261 289 LISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 515 SLLERFYQPQQGTILLDGK---PLQDYQHKYLHSKVAMVGQEPVLfSGTVRDNIAYGLqgcsME--RVKEAASKANAHSF 589
Cdd:PRK10261 368 RALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYA-SLDPRQTVGDSI----MEplRVHGLLPGKAAAAR 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 590 ISKLEkgydtdvgERGNLL-----------SGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMV-------QQALS 651
Cdd:PRK10261 443 VAWLL--------ERVGLLpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIinllldlQRDFG 514
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 29561855 652 CcptqTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK10261 515 I----AYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
483-696 |
4.71e-14 |
|
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: 72.29 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLL--ERFYQPQQGTILLDGKPL-----QDYQHKYLHskVAMvgQEPV 555
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLlelepDERARAGLF--LAF--QYPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 LFSG-TVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEK--GYDTDVGERG-NL-LSGGEKQRIAIARALIREPQVLI 630
Cdd:TIGR01978 88 EIPGvSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRSvNEgFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 631 LDEVTSSLDTESEQMVQQALSCCPTQT--LLVIAHRLKTIE--RADQIVVIDSGELVEKGTHE--ELMEKKG 696
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLREPDrsFLIITHYQRLLNyiKPDYVHVLLDGRIVKSGDVElaKELEAKG 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
486-646 |
5.44e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHK----YLHSKVAMvgqEPVLfsgTV 561
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAY--GLQGCSMERVkEAASKANAHSFISKLEKGYdtdvgergnlLSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:PRK13539 91 AENLEFwaAFLGGEELDI-AAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
....*..
gi 29561855 640 TESEQMV 646
Cdd:PRK13539 160 AAAVALF 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
487-678 |
6.88e-14 |
|
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: 72.06 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPG-----QITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQdYQHKYLHSKvamvgqepvlFSGTV 561
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIayglqgcsMERVKEAASKANAHSFISK---LEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSL 638
Cdd:cd03237 79 RDLL--------SSITKDFYTHPYFKTEIAKplqIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29561855 639 DTESEQMVQQA---LSCCPTQTLLVIAHRLKTIER-ADQIVVID 678
Cdd:cd03237 147 DVEQRLMASKVirrFAENNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
480-633 |
7.82e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGK--PLQDYQHKY-LHSKVAMVGQEPVL 556
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYtVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSG-TVRDNIAYGLqgcsmeRVKEAASKANAHSFI-SKLEKgydtdVGERG--NL----LSGGEKQRIAIARALIREPQV 628
Cdd:PRK11831 96 FTDmNVFDNVAYPL------REHTQLPAPLLHSTVmMKLEA-----VGLRGaaKLmpseLSGGMARRAALARAIALEPDL 164
|
....*
gi 29561855 629 LILDE 633
Cdd:PRK11831 165 IMFDE 169
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
153-414 |
8.34e-14 |
|
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: 72.59 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCemfIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLfmcaINSFTCRVKVQLFG 232
Cdd:cd18568 7 ILLASLLLQLLGLA---LPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYL----LDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 233 SLIRQ----DIGFFETIKTGDITSRLSTDTT----LMGRAVALNVNVLlrTLVKTLGmlyLMVSLSWKLTLLMLMETPLT 304
Cdd:cd18568 80 DFYKHllslPLSFFASRKVGDIITRFQENQKirrfLTRSALTTILDLL--MVFIYLG---LMFYYNLQLTLIVLAFIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 305 GLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTElgeaHRYDGRLME--THNLKTR-RDTVRAIYL--L 379
Cdd:cd18568 155 VLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNTRfRGQKLSIVLqlI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 29561855 380 IRRMTELGmKVAMLYYGRLFIQYGQMSTGNLVSFI 414
Cdd:cd18568 231 SSLINHLG-TIAVLWYGAYLVISGQLTIGQLVAFN 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
487-693 |
8.35e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKylHSKVAMVG---QEPVLFSG-TVR 562
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQEAGIGiihQELNLIPQlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAYGLQGCS-MERVKEAASKANAHSFISKLEKGYDTD--VGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSL- 638
Cdd:PRK10762 98 ENIFLGREFVNrFGRIDWKKMYAEADKLLARLNLRFSSDklVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 639 DTESEQMVQ-----QALSCcptqTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELME 693
Cdd:PRK10762 174 DTETESLFRvirelKSQGR----GIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
473-635 |
8.79e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 473 KLTFSYPRRP--------------DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLerF--YQPQQGTILLDGKPLQ 536
Cdd:COG1129 240 ELEDLFPKRAaapgevvleveglsVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 537 dyqhkyLHS-------KVAMV----GQEPVLFSGTVRDNIAYGLQG--CSMERVKEAASKANAHSFISKLE---KGYDTD 600
Cdd:COG1129 318 ------IRSprdairaGIAYVpedrKGEGLVLDLSIRENITLASLDrlSRGGLLDRRRERALAEEYIKRLRiktPSPEQP 391
|
170 180 190
....*....|....*....|....*....|....*
gi 29561855 601 VGErgnlLSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:COG1129 392 VGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
486-651 |
9.90e-14 |
|
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: 70.60 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLqDYQHKYLHSKVAMVGQEPVLFSG-TVRDN 564
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 565 IAYGLQGCSMERVKEAASKANAHSFisklekgYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQ 644
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-------EDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*..
gi 29561855 645 MVQQALS 651
Cdd:cd03231 163 RFAEAMA 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
496-668 |
1.99e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 496 PGQITALVGMSGGGKSTCVSLLERFYQPQ--QGTILLDGKPLQdyqhKYLHSKVAMVGQEPVLFSG-TVRDNIAYglqgC 572
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVF----C 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 573 SMERVKEAASKAN----AHSFISKL--EKGYDTDVGE---RGnlLSGGEKQRIAIARALIREPQVLILDEVTSSLD-TES 642
Cdd:PLN03211 165 SLLRLPKSLTKQEkilvAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAA 242
|
170 180
....*....|....*....|....*.
gi 29561855 643 EQMVqqalsccptQTLLVIAHRLKTI 668
Cdd:PLN03211 243 YRLV---------LTLGSLAQKGKTI 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
490-692 |
2.06e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 490 FSLELKPGQITALVGMSGGGKSTcvsLLERF--YQPQQGTILLDGKPLQDYQHKYL-HSKVAMVGQEPVLFSGTVRDNIA 566
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 567 YGLQGCSMERVKEAASKANAHSFisKLEKGYDTDVGErgnlLSGGEKQRIAIARALIR-------EPQVLILDEVTSSLD 639
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 640 TESEQMVQQALSCCPTQTLLVI--AHRL-KTIERADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVmsSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
479-683 |
2.76e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.21 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 479 PRRPDHNVLKDFSLELKPGQITALVGMSGGGKST----CVSLLERFYQPQqGTILLDGKPLQDYQHKYlHSKVAMVGQE- 553
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 ---PVLfsgTVRDNIayglqgcsmervkEAASKANAHSFIsklekgydtdvgeRGnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:cd03233 93 vhfPTL---TVRETL-------------DFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 631 LDEVTSSLDTESeqmvqqALSCcpTQTLLVIAHRLKTI-------------ERADQIVVIDSGELV 683
Cdd:cd03233 142 WDNSTRGLDSST------ALEI--LKCIRTMADVLKTTtfvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
475-710 |
5.04e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 475 TFsYPRRPDHN-VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKP---LQDYQH-KYlhskVAM 549
Cdd:COG1101 10 TF-NPGTVNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRaKY----IGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VGQEPVL---FSGTVRDN--IAY------GLqgcsmervKEAASKANAHSFISK-------LEKGYDTDVGergnLLSGG 611
Cdd:COG1101 85 VFQDPMMgtaPSMTIEENlaLAYrrgkrrGL--------RRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 612 EKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAlsccpTQ--------TLLVIAHRLK-TIERADQIVVIDSGEL 682
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEL-----TEkiveennlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 29561855 683 V--------EKGTHEELMEKkgsYYKLRERLFSDDK 710
Cdd:COG1101 228 IldvsgeekKKLTVEDLLEL---FEEIRGEELADDR 260
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
472-692 |
5.66e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPRRpdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplQDYQHKYLHSK----V 547
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISLLPLHARarrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQEPVLFSG-TVRDNIAYGLQ---GCSMERVKEAASKANAHSFISKLEKGYdtdvgerGNLLSGGEKQRIAIARALI 623
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQirdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQALSCCPTQTL--LVIAHRLK-TIERADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgvLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
481-692 |
6.89e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 481 RPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLE-RFYQPQ-------QGTILLDGKPLQDYQHKYLHSKVAMVGQ 552
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 553 --EPVlFSGTVRDNIAYGL------QGCSMERVKEAASKANAHSfisklekGYDTDVGERGNLLSGGEKQRIAIARAL-- 622
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGRypharrAGALTHRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 623 -------IREPQVLILDEVTSSLDTESEQMVQ---QALSCCPTQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLdtvRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADV 242
|
.
gi 29561855 692 M 692
Cdd:PRK13547 243 L 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
487-683 |
9.05e-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: 71.39 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYqPQ---QGTILLDGKPLQDYQHKYLHSK-VAMVGQEPVLFSG-TV 561
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYG----LQGCSMErvkEAASKANAHSFISKLEKGYDTD---VGERGnllsGGEKQRIAIARALIREPQVLILDEV 634
Cdd:TIGR02633 96 AENIFLGneitLPGGRMA---YNAMYLRAKNLLRELQLDADNVtrpVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 635 TSSLdTESEQMV---------QQALSCcptqtlLVIAHRLKTIER-ADQIVVIDSGELV 683
Cdd:TIGR02633 169 SSSL-TEKETEIlldiirdlkAHGVAC------VYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
481-722 |
9.14e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 481 RPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLH--------------SK 546
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 547 VAMVGQEPV-----LFsgTVRDNIAYGL---QGCSMERVKEAASKANAHSFISKLEkgydTDVGERGNLLSGGEKQRIAI 618
Cdd:PRK10261 106 MAMIFQEPMtslnpVF--TVGEQIAESIrlhQGASREEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 619 ARALIREPQVLILDEVTSSLD-TESEQMVQ--QALSCCPTQTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEE---- 690
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQifha 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29561855 691 ---------------LMEKKGSYYKLRERLFSDDKTTKQEKE-KSDTV 722
Cdd:PRK10261 260 pqhpytrallaavpqLGAMKGLDYPRRFPLISLEHPAKQEPPiEQDTV 307
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
473-677 |
1.09e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 473 KLTFSYprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLhskVAMVGQ 552
Cdd:PRK15056 11 DVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 553 E-------PVLfsgtVRDNIAYGLQG-CSMERVKEAASKA---NAHSFISKLEKGYdTDVGErgnlLSGGEKQRIAIARA 621
Cdd:PRK15056 86 SeevdwsfPVL----VEDVVMMGRYGhMGWLRRAKKRDRQivtAALARVDMVEFRH-RQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTI-ERADQIVVI 677
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgkTMLVSTHNLGSVtEFCDYTVMV 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
494-639 |
1.23e-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: 70.97 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 494 LKPGQITALVGMSGGGKSTCVSLL---------------------ERFyqpqQGTILLDG-KPLQDYQHKYLHsKVAMVG 551
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlKRF----RGTELQDYfKKLANGEIKVAH-KPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVLFSGTVRDniayglqgcSMERVKEaasKANAHSFISKL--EKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVL 629
Cdd:COG1245 171 LIPKVFKGTVRE---------LLEKVDE---RGKLDELAEKLglENILDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 29561855 630 ILDEVTSSLD 639
Cdd:COG1245 235 FFDEPSSYLD 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
491-693 |
1.83e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 491 SLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI-LLDGKPLQDYQHKYLHSK------VAMVGQEPVLFS-GTVR 562
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPhRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAyglQGCSMERVKEAASKANAHSFISkleKGYDTDVGER-----GNLLSGGEKQRIAIARALIREPQVLILDEVTSS 637
Cdd:TIGR03269 384 DNLT---EAIGLELPDELARMKAVITLKM---VGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 638 LD-------TESEQMVQQALSccptQTLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELME 693
Cdd:TIGR03269 458 MDpitkvdvTHSILKAREEME----QTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
485-695 |
1.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 485 NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI---LLDGKPLQDYQH--------------------- 540
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 541 KYLHSKVAMVGQ--EPVLFSGTVRDNIAYGlqGCSMERVKEAAsKANAHSFISKLekGYDTDVGERGNL-LSGGEKQRIA 617
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFG--PVSMGVSKEEA-KKRAAKYIELV--GLDESYLQRSPFeLSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 618 IARALIREPQVLILDEVTSSLDTeseQMVQQALSCCPT-----QTLLVIAHRLKTI-ERADQIVVIDSGELVEKG-THEE 690
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDP---QGVKEILEIFDNlnkqgKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDI 252
|
....*
gi 29561855 691 LMEKK 695
Cdd:PRK13651 253 LSDNK 257
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
471-684 |
2.17e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYPRRPDHnvLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPL-----QDYQHkylhs 545
Cdd:PRK10522 325 LRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqpEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 546 kvamvgqepvLFSGTVRDniaYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDV--GERGNL-LSGGEKQRIAIARAL 622
Cdd:PRK10522 398 ----------LFSAVFTD---FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELedGRISNLkLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALscCPT-----QTLLVIAHRLKTIERADQIVVIDSGELVE 684
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVL--LPLlqemgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
472-650 |
2.33e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 472 QKLTFSYPrrPDHNVLKDFSLELKPGQITALVGMSGGGKSTcvsLLErfyqpqqgtIL--LDgkplQDYQHKYLHSKVAM 549
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LLR---------IMagVD----KEFEGEARPAPGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 550 VG---QEPVL-FSGTVRDNIAYGLQGC--------------------------SMERVKEAASKANAHSFISKLEKG--- 596
Cdd:PRK11819 72 VGylpQEPQLdPEKTVRENVEEGVAEVkaaldrfneiyaayaepdadfdalaaEQGELQEIIDAADAWDLDSQLEIAmda 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 597 -----YDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:PRK11819 152 lrcppWDAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
479-694 |
3.05e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 479 PRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGkplqdyqhkylhsKVA-----MVGQE 553
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSallelGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLfsgTVRDNI-----AYGLQGCSM-ERVKEAASKANAHSFIsklekgyDTDVGergnLLSGGEKQRIAIARALIREPQ 627
Cdd:COG1134 101 PEL---TGRENIylngrLLGLSRKEIdEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 628 VLILDEVTSSLDTE--------SEQMVQQAlsccptQTLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHEELMEK 694
Cdd:COG1134 167 ILLVDEVLAVGDAAfqkkclarIRELRESG------RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
485-684 |
8.19e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 485 NVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ---DYQHKYLHSK-VAMVGQEPVLF-SG 559
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRAKhVGFVFQSFMLIpTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIAYG--LQGCSmervkEAASKANAHSFISKLekgydtDVGERGN----LLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:PRK10584 104 NALENVELPalLRGES-----SRQSRNGAKALLEQL------GLGKRLDhlpaQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 634 VTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIERADQIVVIDSGELVE 684
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREhgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
482-643 |
1.58e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 482 PDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKY-LHSKVAMVGQE-PVLFSG 559
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNI---AYGLQGC-----SMERVKEAASKanahsfisklEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLIL 631
Cdd:PRK10982 89 SVMDNMwlgRYPTKGMfvdqdKMYRDTKAIFD----------ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170
....*....|..
gi 29561855 632 DEVTSSLdTESE 643
Cdd:PRK10982 159 DEPTSSL-TEKE 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
498-687 |
1.92e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 498 QITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDyQHKYLHSKVAMVGQEPVLFSG-TVRDNIAY--GLQGCSM 574
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyaQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 575 ErvkEAASKANAhsfisKLE-KGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQ-ALSC 652
Cdd:TIGR01257 1036 E---EAQLEMEA-----MLEdTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDlLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*.
gi 29561855 653 CPTQTLLVIAHRLKTIE-RADQIVVIDSGELVEKGT 687
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
495-665 |
1.94e-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: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 495 KPGQITALVGMSGGGKSTCVSLLE--------RFYQPQQGTILLD---GKPLQDYQHKYLHSKVAM------VGQEPVLF 557
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SGTVRDNIayglqgcsmERVKEaasKANAHSFISKLE--KGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:cd03236 104 KGKVGELL---------KKKDE---RGKLDELVDQLElrHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 29561855 636 SSLDteseqmVQQALSCC--------PTQTLLVIAHRL 665
Cdd:cd03236 168 SYLD------IKQRLNAArlirelaeDDNYVLVVEHDL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
494-639 |
1.99e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 494 LKPGQITALVGMSGGGKSTCVSLL---------------------ERFyqpqQGTILLDG-KPLQDYQHKYLHsKVAMVG 551
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQNYfKKLYNGEIKVVH-KPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 552 QEPVLFSGTVRDNIayglqgcsmERVKEaasKANAHSFISKL--EKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVL 629
Cdd:PRK13409 171 LIPKVFKGKVRELL---------KKVDE---RGKLDEVVERLglENILDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 29561855 630 ILDEVTSSLD 639
Cdd:PRK13409 235 FFDEPTSYLD 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
462-693 |
2.84e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 462 PKDLKGHV-KFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ-QGTILLDGKPLQDYQ 539
Cdd:TIGR02633 250 PHEIGDVIlEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 540 -HKYLHSKVAMVGQE-------PVLfsgTVRDNIAYG-LQG-CSMERVKEAASKANAHSFISKLE-KGYDTDVGERGnlL 608
Cdd:TIGR02633 330 pAQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSvLKSfCFKMRIDAAAELQIIGSAIQRLKvKTASPFLPIGR--L 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESE--------QMVQQALSccptqtLLVIAHRL-KTIERADQIVVIDS 679
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyeiyklinQLAQEGVA------IIVVSSELaEVLGLSDRVLVIGE 478
|
250
....*....|....*....
gi 29561855 680 GEL----VEKG-THEELME 693
Cdd:TIGR02633 479 GKLkgdfVNHAlTQEQVLA 497
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
469-691 |
2.93e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRrpdHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLL----------ERFYQPQQGTILLDGKPLQDY 538
Cdd:PRK09984 5 IRVEKLAKTFNQ---HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 539 QHKYLHSKVaMVGQEPVLFSGTVRDNIAYGLQGCS-----MERVKEAASKANAHSFISKLekGYDTDVGERGNLLSGGEK 613
Cdd:PRK09984 82 RKSRANTGY-IFQQFNLVNRLSVLENVLIGALGSTpfwrtCFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 614 QRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
|
..
gi 29561855 690 EL 691
Cdd:PRK09984 239 QF 240
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
484-686 |
6.96e-11 |
|
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: 61.57 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNVLKDFSLELKPGQITALVGMSGGGKSTCVslLERFYQPQQgtilldgKPLQDYQHKYLHSKVAMVGQepvlfsgtvrd 563
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGK-------ARLISFLPKFSRNKLIFIDQ----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 niaygLQgcsmervkeaaskanahsFISKLEKGYDTdVGERGNLLSGGEKQRIAIARALIREPQ--VLILDEVTSSLDte 641
Cdd:cd03238 68 -----LQ------------------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-- 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 642 sEQMVQQALSCCPT-----QTLLVIAHRLKTIERADQIVVI------DSGELVEKG 686
Cdd:cd03238 122 -QQDINQLLEVIKGlidlgNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
480-684 |
9.81e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQhkylhskvamvgQEPVLfsg 559
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR------------EASLI--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 tvrDNIAyglQGCSMERVKEAASKA---NAHSFISKlekgYDTdvgergnlLSGGEKQRIAIARALIREPQVLILDEVTS 636
Cdd:COG2401 104 ---DAIG---RKGDFKDAVELLNAVglsDAVLWLRR----FKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 637 SLDTESEQMVQQALSCCPTQ---TLLVIAHRlKTIERA---DQIVVIDSGELVE 684
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRagiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
147-413 |
1.23e-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: 63.00 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 147 RPDYILLFGAFVFLALAVLcemFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRV 226
Cdd:cd18782 1 RRALIEVLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 227 KVQLFGSLIRQDIGFFETIKTGDITSRLS-TDTT---LMGRAVALNVNVLLrtlvkTLGMLYLMVSLSWKLTLLMLMETP 302
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISeLDTIrgfLTGTALTTLLDVLF-----SVIYIAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 303 LTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMET--HNLKTRR--DTVRAIYL 378
Cdd:cd18782 153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSlgEGFKLTVlgTTSGSLSQ 232
|
250 260 270
....*....|....*....|....*....|....*
gi 29561855 379 LIRRMTELgmkvAMLYYGRLFIQYGQMSTGNLVSF 413
Cdd:cd18782 233 FLNKLSSL----LVLWVGAYLVLRGELTLGQLIAF 263
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
487-641 |
1.37e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQI-----TALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplQDYQHKYLHSKvamvgqepvlFSGTV 561
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPQYIKPD----------YDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAyglqgcsmervkEAASKANAHSFIS------KLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:PRK13409 418 EDLLR------------SITDDLGSSYYKSeiikplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 481
|
....*.
gi 29561855 636 SSLDTE 641
Cdd:PRK13409 482 AHLDVE 487
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
471-650 |
1.87e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYP-RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTcvsLLERFYQPQ-----QGTILLDGKPLQdyqhKYLH 544
Cdd:cd03232 6 WKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLD----KNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEPVLFSG-TVRDniayglqgcSMErvkeaaskanahsFISKLekgydtdvgeRGnlLSGGEKQRIAIARALI 623
Cdd:cd03232 79 RSTGYVEQQDVHSPNlTVRE---------ALR-------------FSALL----------RG--LSVEQRKRLTIGVELA 124
|
170 180
....*....|....*....|....*..
gi 29561855 624 REPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
147-444 |
2.52e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 62.11 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 147 RPDYILLFGAFVFLALavlCEMFIPLYTGEVID---ILGSHyqwDNFRSAIIFMGLFSLGSSFSAGcrgGLFMCA--INS 221
Cdd:cd18540 1 KKLLILLIILMLLVAL---LDAVFPLLTKYAIDhfiTPGTL---DGLTGFILLYLGLILIQALSVF---LFIRLAgkIEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 222 FTCR-VKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLME 300
Cdd:cd18540 72 GVSYdLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 301 TPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTE---LGEAhrydgrlmETHNLKTRRDTVRAIY 377
Cdd:cd18540 152 VPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREeknLREF--------KELTEEMRRASVRAAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 378 L------LIRRMTELGMKVAMLYYGRLFIQyGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18540 224 LsalflpIVLFLGSIATALVLWYGGILVLA-GAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
479-693 |
2.72e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 479 PRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ-QGTILLDGKPLQ-DYQHKYLHSKVAMV------ 550
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVpedrkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 551 -GQEPVLfsgTVRDNIAYGL--QGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLlSGGEKQRIAIARALIREPQ 627
Cdd:PRK13549 350 dGIVPVM---GVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARL-SGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 628 VLILDEVTSSLDTESE--------QMVQQALSccptqtLLVIAHRLKTI-ERADQIVVIDSGELveKG-------THEEL 691
Cdd:PRK13549 426 ILILDEPTRGIDVGAKyeiyklinQLVQQGVA------IIVISSELPEVlGLSDRVLVMHEGKL--KGdlinhnlTQEQV 497
|
..
gi 29561855 692 ME 693
Cdd:PRK13549 498 ME 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
486-693 |
3.81e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLL--ERfyQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEP-----VLf 557
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 558 SGTVRDNIAYGLQG----CSMERVKEAASKANAHSFISKlekgYD---TDVGERGNLLSGGEKQRIAIARALIREPQVLI 630
Cdd:COG3845 350 DMSVAENLILGRYRrppfSRGGFLDRKAIRAFAEELIEE----FDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 631 LDEVTSSLDTESEQMVQQALsccptqtllviahrlktIERADQ---IVVIdSGELvekgthEELME 693
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRL-----------------LELRDAgaaVLLI-SEDL------DEILA 467
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
151-413 |
4.50e-10 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 61.36 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 151 ILLFGAFV-FLALAVlcemfiPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFmcaiNSFTCRVKV- 228
Cdd:cd18588 7 VLLASLFLqLFALVT------PLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLF----SHTTNRIDAe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 ---QLFGSLIRQDIGFFETIKTGDITSRLS---------TDTTLMgravalnvnvLLRTLVKTLGMLYLMVSLSWKLTLL 296
Cdd:cd18588 77 lgaRLFRHLLRLPLSYFESRQVGDTVARVRelesirqflTGSALT----------LVLDLVFSVVFLAVMFYYSPTLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 297 MLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLmeTHNLKTRRDTVR-- 374
Cdd:cd18588 147 VLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELL--ARYVKASFKTANls 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 29561855 375 ----AIYLLIRRMTELgmkvAMLYYGRLFIQYGQMSTGNLVSF 413
Cdd:cd18588 225 nlasQIVQLIQKLTTL----AILWFGAYLVMDGELTIGQLIAF 263
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
446-642 |
5.29e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 446 EYQDRKSEVSiDGNLMPKDLKGHVKFQK-LTFSYPRRPDHNV-LKDFSLELKPGQITALVGMSGGGKSTCVSLL-ERFYQ 522
Cdd:TIGR00956 737 DLTDESDDVN-DEKDMEKESGEDIFHWRnLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTT 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 523 P--QQGTILLDGKPLQD-------Y-QHKYLHSKVAMVgQEPVLFSgtvrdniAYglqgcsMERVKEaASKANAHSFISK 592
Cdd:TIGR00956 816 GviTGGDRLVNGRPLDSsfqrsigYvQQQDLHLPTSTV-RESLRFS-------AY------LRQPKS-VSKSEKMEYVEE 880
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 593 ------LEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLI-LDEVTSSLDTES 642
Cdd:TIGR00956 881 viklleMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
474-695 |
1.18e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSyprrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLerfyqpqQGTILLDGKPLQDYQHkylhSKVAMVGQE 553
Cdd:PRK11147 11 LSFS-----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIYEQD----LIVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVL-FSGTVRDNIAYGLQGCS------------------------MERVKEAASKANAHSFISK----LEK-GYDTDvgE 603
Cdd:PRK11147 75 PPRnVEGTVYDFVAEGIEEQAeylkryhdishlvetdpseknlneLAKLQEQLDHHNLWQLENRinevLAQlGLDPD--A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 604 RGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTqTLLVIAHRLKTIER-ADQIVVIDSGEL 682
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
250
....*....|....
gi 29561855 683 VE-KGTHEELMEKK 695
Cdd:PRK11147 232 VSyPGNYDQYLLEK 245
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
483-696 |
1.18e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERF--YQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQEPVLFSG 559
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TvrDNIAYGLQGCSMERVKEAASKANAHSFI----SKLEK-GYDTDVGERgNL---LSGGEKQRIAIARALIREPQVLIL 631
Cdd:CHL00131 99 V--SNADFLRLAYNSKRKFQGLPELDPLEFLeiinEKLKLvGMDPSFLSR-NVnegFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 632 DEVTSSLDTESEQMVQQALSCCPTQT--LLVIAH--RLKTIERADQIVVIDSGELVEKGTHE--ELMEKKG 696
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSEnsIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
487-641 |
1.36e-09 |
|
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: 61.34 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQI-----TALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplQDYQHKYLHSKvamvgqepvlFSGTV 561
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--ISYKPQYISPD----------YDGTV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIayglqgcsmervkeaaSKANAHSFISK-----------LEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:COG1245 419 EEFL----------------RSANTDDFGSSyykteiikplgLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYL 478
|
170
....*....|.
gi 29561855 631 LDEVTSSLDTE 641
Cdd:COG1245 479 LDEPSAHLDVE 489
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
153-349 |
1.57e-09 |
|
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: 59.83 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFM-CAINSfTCRVKVQLF 231
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVlAGLRA-SRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 232 GSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIy 311
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRY- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29561855 312 dthYQKLSKEVQ--DSMAQA--NDAAGEAVSGIRTVKSFKTE 349
Cdd:cd18580 159 ---YLRTSRQLRrlESESRSplYSHFSETLSGLSTIRAFGWQ 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
474-686 |
1.76e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSYPRRpdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqHKYLHSKVAMVGQE 553
Cdd:PRK11701 12 LTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFS----GTVRDNIAYGLQ------GCSMERVKEAASK------ANAHSFISKLEkgYDTD-VGERGNLLSGGEKQRI 616
Cdd:PRK11701 83 RRRLLrtewGFVHQHPRDGLRmqvsagGNIGERLMAVGARhygdirATAGDWLERVE--IDAArIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 617 AIARALIREPQVLILDEVTSSLDTeSEQ----------MVQQALSccptqtLLVIAHRLkTIER--ADQIVVIDSGELVE 684
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDV-SVQarlldllrglVRELGLA------VVIVTHDL-AVARllAHRLLVMKQGRVVE 232
|
..
gi 29561855 685 KG 686
Cdd:PRK11701 233 SG 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
487-684 |
2.94e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYqPQ---QGTILLDGKPLQ-----DYQHK---YLHSKVAMVgqePV 555
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRfkdirDSEALgivIIHQELALI---PY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 LfsgTVRDNIAYGlqgcsMERVKE-----AASKANAHSFISK--LEKGYDTDVGERGNllsgGEKQRIAIARALIREPQV 628
Cdd:NF040905 93 L---SIAENIFLG-----NERAKRgvidwNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29561855 629 LILDEVTSSL-DTESEQMV-------QQALSCcptqtlLVIAHRLKTIER-ADQIVVIDSGELVE 684
Cdd:NF040905 161 LILDEPTAALnEEDSAALLdlllelkAQGITS------IIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
450-686 |
4.45e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 450 RKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPDH----NVLKDFSLELKPGQITALVGMSGGGKSTCV----SLLERFY 521
Cdd:TIGR00956 36 SAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRDtktfDILKPMDGLIKPGELTVVLGRPGSGCSTLLktiaSNTDGFH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 522 QPQQGTILLDGKPLQDYQhKYLHSKVAMVGQEPVLF-SGTVRDNIAY-------GLQGCSMERVKEAASKANAHSFISKL 593
Cdd:TIGR00956 116 IGVEGVITYDGITPEEIK-KHYRGDVVYNAETDVHFpHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 594 EKGYDTDVGE---RGnlLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPT---QTLLVIAHRL-- 665
Cdd:TIGR00956 195 SHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANildTTPLVAIYQCsq 272
|
250 260
....*....|....*....|.
gi 29561855 666 KTIERADQIVVIDSGELVEKG 686
Cdd:TIGR00956 273 DAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
229-444 |
6.82e-09 |
|
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: 57.81 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTD---------TTLMgravalnvNVLLRTLVkTLGMLYLMVSLSWKLTLLMLM 299
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDveqtkdfitTGLM--------NIWLDMIT-IIIAICIMLVLNPKLTFVSLV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 300 ETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYL- 378
Cdd:cd18554 155 IFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFs 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29561855 379 LIRRMTELGMKVAMLYYGRLFIQyGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKV 444
Cdd:cd18554 235 AVNTITDLAPLLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
491-691 |
9.05e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 491 SLELKPGQITALVGMSGGGKSTC----VSLLERFYQPQQGTILLDGKPLQDYQHK----YLHSKVAMVGQEPVlfsgtVR 562
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSVSslaiMGLIDYPGRVMAEKLEFNGQDLQRISEKerrnLVGAEVAMIFQDPM-----TS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 563 DNIAY--GLQGCSMERVKEAASKANAHS-FISKLEKGYDTDVGERGNL----LSGGEKQRIAIARALIREPQVLILDEVT 635
Cdd:PRK11022 102 LNPCYtvGFQIMEAIKVHQGGNKKTRRQrAIDLLNQVGIPDPASRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 636 SSLD-TESEQMVQQALSCCPTQ--TLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEEL 691
Cdd:PRK11022 182 TALDvTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
473-672 |
1.09e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 473 KLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYlHSKVAMVGQ 552
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 553 E----PVLfsgTVRDNIAYGLQGCSmervkeAASKANAHSFISKLEKGYDTDVGergnLLSGGEKQRIAIARALIREPQV 628
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSP------GAVGITELCRLFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29561855 629 LILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERAD 672
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKggAVLLTSHQDLPLNKAD 194
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
483-688 |
1.51e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLL--ERFYQPQQGTILLDGKPLQDYQHKYLHSK-VAMVGQEPVLFSG 559
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 -TVRDNIAYGLQGCSMERVKEAASKANAHSFISklEKGYDTDVGErgNLL--------SGGEKQRIAIARALIREPQVLI 630
Cdd:PRK09580 93 vSNQFFLQTALNAVRSYRGQEPLDRFDFQDLME--EKIALLKMPE--DLLtrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 631 LDEVTSSLDTESEQMVQQALSCC--PTQTLLVIAHRLKTIE--RADQIVVIDSGELVEKGTH 688
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLrdGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
482-663 |
1.66e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 482 PDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDY--QHKylhskvAMVGQEPvlfsg 559
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYfdQHR------AELDPEK----- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIAYGLQGCSMERVKEAAskanahsfISKLE------KGYDTDVgergNLLSGGEKQRIAIARALIREPQVLILDE 633
Cdd:PRK11147 399 TVMDNLAEGKQEVMVNGRPRHV--------LGYLQdflfhpKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|
gi 29561855 634 VTSSLDTESEQMVQQALSCCPTqTLLVIAH 663
Cdd:PRK11147 467 PTNDLDVETLELLEELLDSYQG-TVLLVSH 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
469-663 |
1.80e-08 |
|
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: 57.64 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYprrpDHNVL-KDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLdGKPLqdyqhkylhsKV 547
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQ--EPVLFSGTVRDNIAYGLqgcsmERVKEAASKANAHSFISKLE-KGYDTD--VGErgnlLSGGEKQRIAIARAL 622
Cdd:TIGR03719 388 AYVDQsrDALDPNKTVWEEISGGL-----DIIKLGKREIPSRAYVGRFNfKGSDQQkkVGQ----LSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALSCCPTqTLLVIAH 663
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNFAG-CAVVISH 498
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
480-692 |
2.09e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 480 RRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLErfyqpqQGTILLDGKPLQDYQH---------------KYLH 544
Cdd:PRK10938 12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA------GELPLLSGERQSQFSHitrlsfeqlqklvsdEWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVAMVGQEPVLFSGTVRDNIayglqgcsMERVKEAASKAN-AHSF-ISKLekgydtdVGERGNLLSGGEKQRIAIARAL 622
Cdd:PRK10938 86 NNTDMLSPGEDDTGRTTAEII--------QDEVKDPARCEQlAQQFgITAL-------LDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29561855 623 IREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTI-ERADQIVVIDSGELVEKGTHEELM 692
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
469-696 |
3.08e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTIlldgkplqdyqhKYlhSKVA 548
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW--SENA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 mvgqepvlfsgtvrdNIAYglqgCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNL----------------LSGGE 612
Cdd:PRK15064 383 ---------------NIGY----YAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVRGTLgrllfsqddikksvkvLSGGE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 613 KQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTqTLLVIAHrlktiER------ADQIVVIDSGELVE-K 685
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG-TLIFVSH-----DRefvsslATRIIEITPDGVVDfS 517
|
250
....*....|.
gi 29561855 686 GTHEELMEKKG 696
Cdd:PRK15064 518 GTYEEYLRSQG 528
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
193-413 |
4.19e-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: 55.22 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 193 AIIFMGLFSLGssfsagcRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTT----LMGRavaln 268
Cdd:cd18783 51 ALLFEGILGYL-------RRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERirqfLTGQ----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 269 vnvLLRTLVKTLGMLYL---MVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKS 345
Cdd:cd18783 119 ---LFGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 346 FKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSF 413
Cdd:cd18783 196 LALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
469-650 |
4.21e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPrrpDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTI-LLDGKPL---QDYQHKYLH 544
Cdd:PRK10636 313 LKMEKVSAGYG---DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 545 SKVA----MVGQEPVLFSGTVRDNI-AYGLQGcsmERVkeaaskanahsfisklekgydTDVGERgnlLSGGEKQRIAIA 619
Cdd:PRK10636 390 ADESplqhLARLAPQELEQKLRDYLgGFGFQG---DKV---------------------TEETRR---FSGGEKARLVLA 442
|
170 180 190
....*....|....*....|....*....|.
gi 29561855 620 RALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
486-664 |
6.81e-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: 55.91 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 486 VLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhSKVAMVGQEPVLFSGTVRDNI 565
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 566 AYGLQGCSMER--VKEAASKA---NAH-SFISKLEKGYDTdVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLD 639
Cdd:TIGR00954 536 IYPDSSEDMKRrgLSDKDLEQildNVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*
gi 29561855 640 TESEQMVQQALSCCPTqTLLVIAHR 664
Cdd:TIGR00954 615 VDVEGYMYRLCREFGI-TLFSVSHR 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
488-682 |
9.33e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 488 KDFSLELKPGQITALVGMSGGGKStcvSLLERFY---QPQQGTILLDGKPLQDYQHK--------YLHSKVAMVGqepvL 556
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTAqrlarglvYLPEDRQSSG----L 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 F-SGTVRDNI---AYGLQGCSMERVKEAASKANAHSFIS-KLEkgyDTDVGERGnlLSGGEKQRIAIARALIREPQVLIL 631
Cdd:PRK15439 353 YlDAPLAWNVcalTHNRRGFWIKPARENAVLERYRRALNiKFN---HAEQAART--LSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29561855 632 DEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGEL 682
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQnvAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
487-692 |
1.95e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ-DYQHKYLHSKVAMVGQEP----VLFSGTV 561
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 562 RDNIAYglqgCSME-------RVKEAASKANAHSFISKLE---KGYDTDVGergnLLSGGEKQRIAIARALIREPQVLIL 631
Cdd:PRK10762 348 KENMSL----TALRyfsraggSLKHADEQQAVSDFIRLFNiktPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 632 DEVTSSLDT----ESEQMV----QQALSccptqTLLVIAHRLKTIERADQIVVIDSGEL-----VEKGTHEELM 692
Cdd:PRK10762 420 DEPTRGVDVgakkEIYQLInqfkAEGLS-----IILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
608-692 |
2.30e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 LSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCC---PTQTLLVIAHRLKTIER-ADQIVVIDSGELV 683
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqnNNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
....*....
gi 29561855 684 EKGTHEELM 692
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
156-411 |
2.39e-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: 52.89 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFM--GLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGS 233
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLayGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 234 LIRQDIGFFETIKTGDITSRL-----STDTTLmgRAVALNVnvlLRTLVKTLGMLYLMVSL-SWKLTLLMLmetpLTGLL 307
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIergtrGIEFLL--RFLLFNI---LPTILELLLVCGILWYLyGWSYALITL----VTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 308 QNIYDTHYQKLSKEVQDSMAQA-NDAAGEAVSGIR---TVKSFKTELGEAHRYDGRL--METHNLKTRRD--TVRAIYLL 379
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEAdNEANAKAVDSLLnyeTVKYFNNEEYEAERYDKALakYEKAAVKSQTSlaLLNIGQAL 231
|
250 260 270
....*....|....*....|....*....|..
gi 29561855 380 IrrMTeLGMkVAMLYYGRLFIQYGQMSTGNLV 411
Cdd:cd18582 232 I--IS-LGL-TAIMLLAAQGVVAGTLTVGDFV 259
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
153-446 |
2.82e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 52.90 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 153 LFGAFVFLALAV-LCEMFIPLYTGEVID--ILGSHYQW-DNFRSAIIFMGLFSLGSSFSagcRGGLFMCAINSFTCRVKV 228
Cdd:cd18555 3 LLISILLLSLLLqLLTLLIPILTQYVIDnvIVPGNLNLlNVLGIGILILFLLYGLFSFL---RGYIIIKLQTKLDKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTT----LMGRAVALNVNVLLrtlvkTLGMLYLMVSLSWKLTLLMLMETPLT 304
Cdd:cd18555 80 DFFEHLLKLPYSFFENRSSGDLLFRANSNVYirqiLSNQVISLIIDLLL-----LVIYLIYMLYYSPLLTLIVLLLGLLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 305 GLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMT 384
Cdd:cd18555 155 VLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29561855 385 ELGMKVAMLYYGRLFIQYGQMSTGNLVSFilyqQDLGDNIRTLIYIFGDMLNSVGAAGKVFE 446
Cdd:cd18555 235 QFIAPLLILWIGAYLVINGELTLGELIAF----SSLAGSFLTPIVSLINSYNQFILLKSYLE 292
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
474-651 |
6.48e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 474 LTFSyprRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKylhSKVAMVGQE 553
Cdd:PRK13543 17 LAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 554 PVLFSG-TVRDNIAY--GLQGCsmeRVKEAASKANAhsfISKLEKGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLI 630
Cdd:PRK13543 91 PGLKADlSTLENLHFlcGLHGR---RAKQMPGSALA---IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWL 160
|
170 180
....*....|....*....|.
gi 29561855 631 LDEVTSSLDTESEQMVQQALS 651
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMIS 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
496-681 |
2.16e-06 |
|
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: 48.14 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 496 PGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLdgkplqdyqhkylhskvamvgqepvlfsgtvrdniayglqgCSME 575
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 576 RVKEAAskanahsfiskLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSC--- 652
Cdd:smart00382 40 DILEEV-----------LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29561855 653 -----CPTQTLLVIAHRLK------TIERADQIVVIDSGE 681
Cdd:smart00382 109 lllksEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
469-650 |
6.65e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYPRRPdhNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKplqdyqhkylhSKVA 548
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-----------VRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 549 MVGQEPVLFSGTVRDNIAYglqgcsMER----VKEAASKANAHSFisklekgydtdvGERGNL-------LSGGEKQRIA 617
Cdd:PLN03073 576 VFSQHHVDGLDLSSNPLLY------MMRcfpgVPEQKLRAHLGSF------------GVTGNLalqpmytLSGGQKSRVA 637
|
170 180 190
....*....|....*....|....*....|...
gi 29561855 618 IARALIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
484-691 |
6.76e-06 |
|
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: 49.63 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNvLKDFSLELKPGQITALVGMSGGGKSTCV------SLLERFYQpqQGTILLDGKPLQDYQHKylhSKVAMVGQEPV-- 555
Cdd:TIGR00630 622 NN-LKNITVSIPLGLFTCITGVSGSGKSTLIndtlypALANRLNG--AKTVPGRYTSIEGLEHL---DKVIHIDQSPIgr 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 ------------------LFSGTVRD------------NIAYG----LQG--------------------CSMER----- 576
Cdd:TIGR00630 696 tprsnpatytgvfdeireLFAETPEAkvrgytpgrfsfNVKGGrceaCQGdgvikiemhflpdvyvpcevCKGKRynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 577 -----------------VKEAASKANAHSFIS-KLEKGYDT-----DVGERGNLLSGGEKQRIAIARALIRE---PQVLI 630
Cdd:TIGR00630 776 levkykgkniadvldmtVEEAYEFFEAVPSISrKLQTLCDVglgyiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYI 855
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 631 LDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIvvID--------SGELVEKGTHEEL 691
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDKgnTVVVIEHNLDVIKTADYI--IDlgpeggdgGGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
574-663 |
8.98e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 574 MERVKEAASKANAHSFISKLEKGYDTDVgERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCC 653
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW 390
|
90
....*....|
gi 29561855 654 PtQTLLVIAH 663
Cdd:PLN03073 391 P-KTFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
487-639 |
9.19e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQ-HKYLHSKVAMVGQE----------PV 555
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 556 LFSGTVRDNIAYGlqgCSMERVKEAASKANAHSFISKLE---KGYDTDVGErgnlLSGGEKQRIAIARALIREPQVLILD 632
Cdd:PRK10982 344 GFNSLISNIRNYK---NKVGLLDNSRMKSDTQWVIDSMRvktPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
....*..
gi 29561855 633 EVTSSLD 639
Cdd:PRK10982 417 EPTRGID 423
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
608-705 |
1.41e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 LSGGEKQRIAIARALIREPQ---VLILDEVTSSLDTESEQMVQQALsccptQ-------TLLVIAHRLKTIERADQIvvI 677
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVL-----HrlvdkgnTVVVIEHNLDVIKTADWI--I 899
|
90 100 110
....*....|....*....|....*....|....*....
gi 29561855 678 D--------SGELVEKGTHEELMEKKGSY---YkLRERL 705
Cdd:COG0178 900 DlgpeggdgGGEIVAEGTPEEVAKVKASYtgrY-LKEYL 937
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
608-681 |
1.55e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 608 LSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQA---LSCCPTQTLLVIAHRLKTIERADQIVVIDSGE 681
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAirrLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
468-691 |
1.91e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 468 HVKFQKLTFSyprRPDHNV--LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQ---QGTILLDGKPLQDYQHKY 542
Cdd:PRK09473 14 DVKDLRVTFS---TPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 543 LH----SKVAMVGQEPVLfsgTVRDNIAYGLQGCSMERVKEAASKANA-HSFISKLEKGYDTDVGERGNL----LSGGEK 613
Cdd:PRK09473 91 LNklraEQISMIFQDPMT---SLNPYMRVGEQLMEVLMLHKGMSKAEAfEESVRMLDAVKMPEARKRMKMypheFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 614 QRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ---TLLVIAHRLKTIER-ADQIVVIDSGELVEKGTHE 689
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfntAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNAR 247
|
..
gi 29561855 690 EL 691
Cdd:PRK09473 248 DV 249
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
608-698 |
2.07e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 LSGGEKQRIAIARALIREP---QVLILDEVTSSLDTES--------EQMVQQAlsccptQTLLVIAHRLKTIERADQIvv 676
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDirkllevlHRLVDKG------NTVVVIEHNLDVIKTADWI-- 902
|
90 100 110
....*....|....*....|....*....|
gi 29561855 677 ID--------SGELVEKGTHEELMEKKGSY 698
Cdd:PRK00349 903 IDlgpeggdgGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
483-687 |
4.97e-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: 45.68 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 483 DHNVLKDFSLELKPGQITALVGMSGGGKSTCV------SLLERFYQPQQgtillDGKPLQDYQHKYLHSKVAMVGQEPVl 556
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHLKKE-----QPGNHDRIEGLEHIDKVIVIDQSPI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 fsG-TVRDNIA-Y-GL---------QGCSMER----------------------VKEAASKANAHSFIS-KLEK------ 595
Cdd:cd03271 81 --GrTPRSNPAtYtGVfdeirelfcEVCKGKRynretlevrykgksiadvldmtVEEALEFFENIPKIArKLQTlcdvgl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 596 GYDTdVGERGNLLSGGEKQRIAIARALIRE---PQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER 670
Cdd:cd03271 159 GYIK-LGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgnTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|....*
gi 29561855 671 ADQIvvID--------SGELVEKGT 687
Cdd:cd03271 238 ADWI--IDlgpeggdgGGQVVASGT 260
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
469-717 |
5.38e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYP--------------RRPD---HNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLD 531
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklkdlffRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 532 GKPLQDYQHKYLHSKvaMVGQEPVLFSGTvrdniaygLQGCSMERVKEAASK----ANAHSFISKLEKGYdtdvgergnl 607
Cdd:PRK13545 85 GSAALIAISSGLNGQ--LTGIENIELKGL--------MMGLTKEKIKEIIPEiiefADIGKFIYQPVKTY---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 lSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVE 684
Cdd:PRK13545 145 -SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgkTIFFISHSLSQVKSfCTKALWLHYGQVKE 223
|
250 260 270
....*....|....*....|....*....|...
gi 29561855 685 KGTHEELMEKKGSYYKLRERLFSDDKTTKQEKE 717
Cdd:PRK13545 224 YGDIKEVVDHYDEFLKKYNQMSVEERKDFREEQ 256
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
608-675 |
5.69e-05 |
|
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: 44.27 E-value: 5.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 608 LSGGEKQRIAIARAL----IREPQVLILDEVTSSLDTESeqmvQQALSC------CPTQTLLVIAHRLKTIERADQIV 675
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD----GQALAEailehlVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
471-646 |
6.52e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 471 FQKLTFSYPRRpdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDG-------KPLQDYQHKYL 543
Cdd:PRK13541 4 LHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 544 HSKVAMVGQEPVLFSGTVRDniayglqgcSMERVKEAASKANAHSFISklEKGYDtdvgergnlLSGGEKQRIAIARALI 623
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYN---------SAETLYAAIHYFKLHDLLD--EKCYS---------LSSGMQKIVAIARLIA 139
|
170 180
....*....|....*....|...
gi 29561855 624 REPQVLILDEVTSSLDTESEQMV 646
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENRDLL 162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
609-696 |
7.17e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 609 SGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIER-ADQIVVIDSGELVEK 685
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgaTVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225
|
90
....*....|.
gi 29561855 686 GTHEELMEKKG 696
Cdd:NF000106 226 GKVDELKTKVG 236
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
606-675 |
1.34e-04 |
|
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: 43.61 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 606 NLLSGGEKQRIAIAR--ALIRE---PQVlILDEVTSSLDTES--------EQMVQQalsccpTQtLLVIAHRLKTIERAD 672
Cdd:cd03278 112 SLLSGGEKALTALALlfAIFRVrpsPFC-VLDEVDAALDDANverfarllKEFSKE------TQ-FIVITHRKGTMEAAD 183
|
...
gi 29561855 673 QIV 675
Cdd:cd03278 184 RLY 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
469-650 |
1.50e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 469 VKFQKLTFSYprrpDHNVL-KDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLdGKPLqdyqhkylhsKV 547
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 548 AMVGQ-----EPvlfSGTVRDNIAYGLqgcsmERVKEAASKANAHSFISKLE-KGydTDVGERGNLLSGGEKQRIAIARA 621
Cdd:PRK11819 390 AYVDQsrdalDP---NKTVWEEISGGL-----DIIKVGNREIPSRAYVGRFNfKG--GDQQKKVGVLSGGERNRLHLAKT 459
|
170 180
....*....|....*....|....*....
gi 29561855 622 LIREPQVLILDEVTSSLDTESEQMVQQAL 650
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLDVETLRALEEAL 488
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
477-668 |
1.53e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 477 SYPRRPdhnVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYqPQ--------------QGTILLDGKplqdyQH-K 541
Cdd:PRK10938 269 SYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgysndltlfgrrrgSGETIWDIK-----KHiG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 542 YLHSKVAM---VgqepvlfSGTVRDNIAYGL-------QGCS----------MERVKEAASKANA--HSfisklekgydt 599
Cdd:PRK10938 340 YVSSSLHLdyrV-------STSVRNVILSGFfdsigiyQAVSdrqqklaqqwLDILGIDKRTADApfHS----------- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 600 dvgergnlLSGGEkQRIA-IARALIREPQVLILDEVTSSLDTESEQMVQ----QALSCCPTQTLLV----------IAHR 664
Cdd:PRK10938 402 --------LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRrfvdVLISEGETQLLFVshhaedapacITHR 472
|
....
gi 29561855 665 LKTI 668
Cdd:PRK10938 473 LEFV 476
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
487-697 |
1.70e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 487 LKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQH-KYLHSKVAMVGQ------EPVLfsg 559
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQglgknlYPTL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 560 TVRDNIA-----YGLqgcsmervkeaaSKANAHSFISKLEKgyDTDVG---ER--GNLlSGGEKQRIAIARALIREPQVL 629
Cdd:NF033858 94 SVFENLDffgrlFGQ------------DAAERRRRIDELLR--ATGLApfaDRpaGKL-SGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 630 ILDEVTSSLD---------------TESEQMvqqalsccptqTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEK 694
Cdd:NF033858 159 ILDEPTTGVDplsrrqfwelidrirAERPGM-----------SVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLAR 227
|
...
gi 29561855 695 KGS 697
Cdd:NF033858 228 TGA 230
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
156-436 |
3.04e-04 |
|
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: 43.37 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRS--AIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGS 233
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAvtLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 234 LIRQDIGFFETIKTGDITSRLSTDTtlmgRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDT 313
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGT----ESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 314 HY-----QKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHnlKTRRdTVRAIYLLIRRMTELGM 388
Cdd:cd18560 157 IKvtewrTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQ--KSSV-KVQASLSLLNVGQQLII 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 29561855 389 KVAM---LYYGRLFIQYGQMSTGNLVSFILYQQD-------LGDNIRTLIYIFGDMLN 436
Cdd:cd18560 234 QLGLtlgLLLAGYRVVDGGLSVGDFVAVNTYIFQlfqplnfLGTIYRMIIQSLTDMEN 291
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
230-414 |
3.69e-04 |
|
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: 43.30 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 230 LFGSLIRQDIGFFETIKTGDITSRLSTDTT----LMGRAVALnvnVLLRTLVktLGMLYLMVSLSWKLTLLMLmetpLTG 305
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNATirelLTSQTLSA---LLDGTLV--LGYLALLFAQSPLLGLVVL----GLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 306 LLQ--NIYDTH--YQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRD----TVRAIY 377
Cdd:cd18779 152 ALQvaLLLATRrrVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGrldaLVDALL 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 29561855 378 LLIRRMTELgmkvAMLYYGRLFIQYGQMSTGNLVSFI 414
Cdd:cd18779 232 ATLRLAAPL----VLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
588-680 |
4.00e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 588 SFISKLEK----------GYdTDVGERGNLLSGGEKQRIAIARALI---REPQVLILDEVTSSLDTESEQMVQQALSCCP 654
Cdd:PRK00635 1671 PFLKKIQKplqalidnglGY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLV 1749
|
90 100
....*....|....*....|....*...
gi 29561855 655 TQ--TLLVIAHRLKTIERADQIVVIDSG 680
Cdd:PRK00635 1750 SLghSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
611-715 |
1.17e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 611 GEKQRIAIARALIREPQVLILDEVTSSLDTES----EQMVQQALSccptqTLLVIAH-R--LKTI--ERADqivvIDSGE 681
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTirwlEDVLNERNS-----TMIIISHdRhfLNSVctHMAD----LDYGE 229
|
90 100 110
....*....|....*....|....*....|....*
gi 29561855 682 L-VEKGTHEELMEKKGsyyKLRERLFSDDKTTKQE 715
Cdd:PRK15064 230 LrVYPGNYDEYMTAAT---QARERLLADNAKKKAQ 261
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
229-368 |
1.52e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 41.36 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQ 308
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29561855 309 NiydtHYQKLSKEVQ--DSMAQAN--DAAGEAVSGIRTVKSFKTELGEAHRYDGRLmeTHNLKT 368
Cdd:cd18605 160 R----YYRATSRELKrlNSVNLSPlyTHFSETLKGLVTIRAFRKQERFLKEYLEKL--ENNQRA 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
481-692 |
1.63e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 481 RPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQ-DYQHKYLHSKVAMVGQ---EPVL 556
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 557 FSG-TVRDNIAYGLQgcsmerVKEAASKANAHSFISKLEKGYDTDVGERGNL-----------LSGGEKQRIAIARALIR 624
Cdd:PRK09700 353 FPNfSIAQNMAISRS------LKDGGYKGAMGLFHEVDEQRTAENQRELLALkchsvnqniteLSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29561855 625 EPQVLILDEVTSSLD--TESE-QMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVE------KGTHEELM 692
Cdd:PRK09700 427 CPEVIIFDEPTRGIDvgAKAEiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
484-686 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 484 HNvLKDFSLELKPGQITALVGMSGGGKSTCVsllerFyqpqqGTILLDGkplqdyQHKYLHSKVAMVGQepvLFSGTVRD 563
Cdd:cd03270 9 HN-LKNVDVDIPRNKLVVITGVSGSGKSSLA-----F-----DTIYAEG------QRRYVESLSAYARQ---FLGQMDKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 564 NIAYgLQGCSME-RVKEAASKANAHSFISKLEKGYD------------------TDVG------ER-GNLLSGGEKQRIA 617
Cdd:cd03270 69 DVDS-IEGLSPAiAIDQKTTSRNPRSTVGTVTEIYDylrllfarvgirerlgflVDVGlgyltlSRsAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29561855 618 IARALIRE-PQVL-ILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIVVI------DSGELVEKG 686
Cdd:cd03270 148 LATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLgnTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
199-378 |
2.04e-03 |
|
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: 41.05 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 199 LFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVK 278
Cdd:cd18602 58 GLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 279 TLGMLYLMVSLSWKLTLLMLmetPLTGL---LQNIydthYQKLSKEVQ--DSMAQANDAAG--EAVSGIRTVKSFktelg 351
Cdd:cd18602 138 CLSAIIVNAIVTPYFLIALI---PIIIVyyfLQKF----YRASSRELQrlDNITKSPVFSHfsETLGGLTTIRAF----- 205
|
170 180
....*....|....*....|....*..
gi 29561855 352 eahRYDGRLMETHNLKTRRDTVRAIYL 378
Cdd:cd18602 206 ---RQQARFTQQMLELIDRNNTAFLFL 229
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
608-694 |
2.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 608 LSGGEKQRIAIARALI---REPQVLILDEVTSSLDTESEQMVQQALSCCPTQ--TLLVIAHRLKTIERADQIVVID---- 678
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQghTVVIIEHNMHVVKVADYVLELGpegg 889
|
90
....*....|....*...
gi 29561855 679 --SGELVEKGTHEELMEK 694
Cdd:PRK00635 890 nlGGYLLASCSPEELIHL 907
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
156-380 |
2.34e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 40.55 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 156 AFVFLALAVLCEMFIPLYTGEVIDILGShYQWDNFRSAIIFMGLFSLGSSFSAGCRGgLFMCAINSFTCRVKVQLfGSLI 235
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSS-YPDEPLSEGYLLALALFLVSLLQSLLLH-QYFFLSFRLGMRVRSAL-SSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 236 -----RQDIGFFETIKTGDITSRLSTDTTLMGRAVaLNVNVLLRTLVKTLGMLYLMVSLSWKLTL----LMLMETPLTGL 306
Cdd:cd18579 79 yrkalRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLLGWAALaglgVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 307 LQniydthyqKLSKEVQDSMAQANDA----AGEAVSGIRTVK------SFKTELGEAhrydgRLMETHNLKTRRdTVRAI 376
Cdd:cd18579 158 LA--------KLISKLRKKLMKATDErvklTNEILSGIKVIKlyawekPFLKRIEEL-----RKKELKALRKFG-YLRAL 223
|
....
gi 29561855 377 YLLI 380
Cdd:cd18579 224 NSFL 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-674 |
2.65e-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: 41.20 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 606 NLLSGGEKQRIAIAR--ALIRE---PQVlILDEVTSSLDtES---------EQMVQQalsccpTQtLLVIAHRLKTIERA 671
Cdd:TIGR02168 1088 SLLSGGEKALTALALlfAIFKVkpaPFC-ILDEVDAPLD-DAnverfanllKEFSKN------TQ-FIVITHNKGTMEVA 1158
|
...
gi 29561855 672 DQI 674
Cdd:TIGR02168 1159 DQL 1161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
611-697 |
3.10e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 611 GEKQRIAIARALIREPQVLILDEVTSSLDTES-----EQMVQqaLSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEK 685
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfwRLLIE--LSREDGVTIFISTHFMNEAERCDRISLMHAGRVLAS 478
|
90
....*....|..
gi 29561855 686 GTHEELMEKKGS 697
Cdd:NF033858 479 DTPAALVAARGA 490
|
|
| MFS_MdtG_SLC18_like |
cd17325 |
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ... |
98-209 |
4.62e-03 |
|
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340883 [Multi-domain] Cd Length: 375 Bit Score: 39.87 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 98 FTVWLVGTVAAALACLFWeitLPDTNEESNGKERKQKARVLFIRVIrLYRPDYILLFGAFVFLALAV-LCEMFIPLYTGE 176
Cdd:cd17325 153 FLVCAALALLALVLALLL---LPEPRPPPNKRAVSAARLRSGLRLL-LRDRRLLALFLAIFVLAFAFgALEPFLPLYAAE 228
|
90 100 110
....*....|....*....|....*....|....*
gi 29561855 177 VIDilgshyqWDNFRSAIIF--MGLFSLGSSFSAG 209
Cdd:cd17325 229 LGG-------LSPAQIGLLFgaQGLASALSQPPAG 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
150-413 |
7.67e-03 |
|
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: 39.10 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 150 YILLFGAFV--FLALAVlcemfiPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVK 227
Cdd:cd18566 5 PQVLLASLFinILALAT------PLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 228 VQLFGSLIRQDIGFFETIKTGDITSRLSTDTTL----MGRAValnvnVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPL 303
Cdd:cd18566 79 NAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIreflTGQAL-----LALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29561855 304 TGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDgRLMETHNLKTRRDTVRAiyLLIRRM 383
Cdd:cd18566 154 FVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYE-RLQANAAYAGFKVAKIN--AVAQTL 230
|
250 260 270
....*....|....*....|....*....|...
gi 29561855 384 TELGMKVAM---LYYGRLFIQYGQMSTGNLVSF 413
Cdd:cd18566 231 GQLFSQVSMvavVAFGALLVINGDLTVGALIAC 263
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
229-289 |
8.07e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 38.84 E-value: 8.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29561855 229 QLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSL 289
Cdd:cd18601 97 KMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
|
| |
