|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-632 |
0e+00 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 599.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 19 DDRSLPfSIFKKANNPVTLKFENLVYTVKL--KDSQGCFGK------------NDKTEERTILKGLTGIVKPGEILAMLG 84
Cdd:PLN03211 23 DSRDLP-SLLLSSCYPITLKFMDVCYRVKFenMKNKGSNIKrilghkpkisdeTRQIQERTILNGVTGMASPGEILAVLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 85 PSGSGKTSLLTALGGRVgEGKGkLTGNISYNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKQEKI 164
Cdd:PLN03211 102 PSGSGKSTLLNALAGRI-QGNN-FTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 165 KQAKAVMTELGLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTV 244
Cdd:PLN03211 180 LVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 245 VTTIHQPSSRLFYMFDKLLLLSEGNPVYFGLGSNAMDYFASVGYSPLVErINPSDFLLDIANGV----GSDESQRPEaMK 320
Cdd:PLN03211 260 VTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFP-MNPADFLLDLANGVcqtdGVSEREKPN-VK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 321 AALVAFYKTnLLDSVINEVKGQDDLCNKPRE-----SSRVATNTYGDWPTTWWQQFCVLLKRGLKQRRHDSFSGMKVAQI 395
Cdd:PLN03211 338 QSLVASYNT-LLAPKVKAAIEMSHFPQANARfvgsaSTKEHRSSDRISISTWFNQFSILLQRSLKERKHESFNTLRVFQV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 396 FIVSFLCGLLWWQTKISRLQDQIGLLFFISSFWAFFPLFQQIFTFPQERAMLQKERSSGMYRLSPYFLSRVVGDLPMELI 475
Cdd:PLN03211 417 IAAALLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELI 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 476 LPTCFLVITYWMAGLNHNLANFFVTLLVLLVHVLVSGGLGLALGALVMDQKSATTLGSVIMLTFLLAGGYYVQHVPVFIS 555
Cdd:PLN03211 497 LPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHKLPSCMA 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 556 WIKYVSIGYYTYKLLILGQYTANE----LYPCGDNgklrcHVGDFEGIKHI-----GFNSGLVSALALTAMLVVYRVIAY 626
Cdd:PLN03211 577 WIKYISTTFYSYRLLINVQYGEGKrissLLGCSLP-----HGSDRASCKFVeedvaGQISPATSVSVLIFMFVGYRLLAY 651
|
....*.
gi 334186960 627 IALTRI 632
Cdd:PLN03211 652 LALRRI 657
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
53-631 |
2.03e-130 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 396.73 E-value: 2.03e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 53 GCFGKndKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKgKLTGNISYNNKPL-SKAVKRTTGFVT 131
Cdd:TIGR00955 29 GCFCR--ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV-KGSGSVLLNGMPIdAKEMRAISAYVQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QDDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGP-FLRGVSGGERKRVSIGQEILINP 210
Cdd:TIGR00955 106 QDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFGLGSNAMDYFASVGYsP 290
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGH-P 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 291 LVERINPSDFLLDIANGVGSDESQRPEAMKAALVAFYKTNL---LDSVINEVKGQDDLCNKPRESsrvatNTYGDWPTTW 367
Cdd:TIGR00955 265 CPENYNPADFYVQVLAVIPGSENESRERIEKICDSFAVSDIgrdMLVNTNLWSGKAGGLVKDSEN-----MEGIGYNASW 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 368 WQQFCVLLKRG-LKQRRHDSFSGMKVAQIFIVSFLCGLLWWQTKISRL--QDQIGLLFFISSFWAFFPLFQQIFTFPQER 444
Cdd:TIGR00955 340 WTQFYALLKRSwLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKgvQNINGALFLFLTNMTFQNVFPVINVFTAEL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 445 AMLQKERSSGMYRLSPYFLSRVVGDLPMELILPTCFLVITYWMAGLNHNLANFFVTLLVLLVHVLVSGGLGLALGALVMD 524
Cdd:TIGR00955 420 PVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSS 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 525 QKSATTLGSVIMLTFLLAGGYYVQ--HVPVFISWIKYVSIGYYTYKLLILGQYTANELYPCGD-NGKLRCHVGDFEGIKH 601
Cdd:TIGR00955 500 TSMALTVGPPFVIPFLLFGGFFINsdSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSaNTTGPCPSSGEVILET 579
|
570 580 590
....*....|....*....|....*....|..
gi 334186960 602 IGFNSGLVSA--LALTAMLVVYRVIAYIALTR 631
Cdd:TIGR00955 580 LSFRNADLYLdlIGLVILIFFFRLLAYFALRI 611
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
44-274 |
2.29e-78 |
|
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: 248.34 E-value: 2.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 44 YTVKLKDSQGCFGKNDKTeeRTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgEGKGKLTGNISYNNKPLSKA- 122
Cdd:cd03234 2 RVLPWWDVGLKAKNWNKY--ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQILFNGQPRKPDq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 123 VKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKqekiKQAKAVMTELGLDRCKDTIIGGPFLRGVSGGERKRVSI 202
Cdd:cd03234 79 FQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSD----AIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 203 GQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-274 |
1.08e-76 |
|
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: 242.84 E-value: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 34 PVTLKFENLVYTVKLKDSQGCfgkndkteeRTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKgkLTGNIS 113
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSG---------KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 114 YNNKPLSK-AVKRTTGFVTQDDALYPNLTVTETLVFTALLRlpnsfkkqekikqakavmtelgldrckdtiiggpflrGV 192
Cdd:cd03213 70 INGRPLDKrSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVY 272
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIY 192
|
..
gi 334186960 273 FG 274
Cdd:cd03213 193 FG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
55-586 |
5.19e-74 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 258.89 E-value: 5.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 55 FGKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFV---T 131
Cdd:TIGR00956 65 LKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVvynA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QDDALYPNLTVTETLVFTALLRLPNS----FKKQEKIKQAKAV-MTELGLDRCKDTIIGGPFLRGVSGGERKRVSIGQEI 206
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVyMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 207 LINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVT-TIHQPSSRLFYMFDKLLLLSEGNPVYFGLGSNAMDYFAS 285
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 286 VGYS-PlvERINPSDFLLDIAN--------GVGSDESQRPEAMK---------AAL---VAFYKTNLLDSVINEVKGQDD 344
Cdd:TIGR00956 305 MGFKcP--DRQTTADFLTSLTSpaerqikpGYEKKVPRTPQEFEtywrnspeyAQLmkeIDEYLDRCSESDTKEAYRESH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 345 LCNKPRESSRVATNTygdwpTTWWQQFCVLLKRG-LKQRRHDSFSGMKVAQIFIVSFLCGLLWWQTKI--SRLQDQIGLL 421
Cdd:TIGR00956 383 VAKQSKRTRPSSPYT-----VSFSMQVKYCLARNfLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKntSDFYSRGGAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 422 FFISSFWAFFPLFqQIFTFPQERAMLQKERSSGMYRLSPYFLSRVVGDLPMELILPTCFLVITYWMAGLNHNLANFFVTL 501
Cdd:TIGR00956 458 FFAILFNAFSSLL-EIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 502 LVLLVHVLVSGGLGLALGALVMDQKSATTLGSVIMLTFLLAGGYYVQ--HVPVFISWIKYVSIGYYTYKLLILGQYTA-- 577
Cdd:TIGR00956 537 LILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPrpSMLGWSKWIYYVNPLAYAFESLMVNEFHGrr 616
|
570
....*....|..
gi 334186960 578 ---NELYPCGDN 586
Cdd:TIGR00956 617 fecSQYVPSGGG 628
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-495 |
5.77e-70 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 247.33 E-value: 5.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 8 MDVETPiAKTNDDRSLPFSIFkkanNPVTLKFENLVYTVKLKDSQG---------CFGKNDKTEERTILKGLTGIVKPGE 78
Cdd:TIGR00956 716 AGETSA-SNKNDIEAGEVLGS----TDLTDESDDVNDEKDMEKESGedifhwrnlTYEVKIKKEKRVILNNVDGWVKPGT 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 79 ILAMLGPSGSGKTSLLTALGGRVGegKGKLTGNISY-NNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNS 157
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLvNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKS 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 158 FKKQEKIKQAKAVMTELGLDRCKDTIIGGPFlRGVSGGERKRVSIGQEILINP-SLLFLDEPTSGLDSTTAQRIVSILWE 236
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEMESYADAVVGVPG-EGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRK 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 237 LARGGRTVVTTIHQPSSRLFYMFDKLLLLSEG-NPVYFG-LGSNA---MDYFASVGYSPLVERINPSDFLLD-IANGVGS 310
Cdd:TIGR00956 948 LADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGdLGENShtiINYFEKHGAPKCPEDANPAEWMLEvIGAAPGA 1027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 311 D----------ESQRPEAMKaalvafyktNLLDSVINEVKGQDDLcNKPRESSRVAtntygdwpTTWWQQFCVLLKRGLK 380
Cdd:TIGR00956 1028 HanqdyhevwrNSSEYQAVK---------NELDRLEAELSKAEDD-NDPDALSKYA--------ASLWYQFKLVLWRTFQ 1089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 381 Q--RRHD----SFSGMKVAQIFIvsflcGLLWWQTKISR--LQDQIGLLFfiSSFWAFFPLFQQIF-TFPQERAMLQ-KE 450
Cdd:TIGR00956 1090 QywRTPDylysKFFLTIFAALFI-----GFTFFKVGTSLqgLQNQMFAVF--MATVLFNPLIQQYLpPFVAQRDLYEvRE 1162
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 334186960 451 RSSGMYRLSPYFLSRVVGDLPMELILPTCFLVITYWMAGLNHNLA 495
Cdd:TIGR00956 1163 RPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNAS 1207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-274 |
2.25e-60 |
|
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: 199.78 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 34 PVTLKFENLVYTVklkdsqgcfgkNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgEGKGKLTGNIS 113
Cdd:cd03232 1 GSVLTWKNLNYTV-----------PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR--KTAGVITGEIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 114 YNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRlpnsfkkqekikqakavmtelgldrckdtiiggpflrGVS 193
Cdd:cd03232 68 INGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 194 GGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSE-GNPVY 272
Cdd:cd03232 111 VEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVY 190
|
..
gi 334186960 273 FG 274
Cdd:cd03232 191 FG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-498 |
1.26e-58 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 213.94 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 23 LPFSifkkannPVTLKFENLVYTVKLKD---SQGCfgkndkTEER-TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALG 98
Cdd:PLN03140 861 LPFT-------PLAMSFDDVNYFVDMPAemkEQGV------TEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 99 GRvgEGKGKLTGNISYNNKP-LSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQAKAVMTELGLD 177
Cdd:PLN03140 928 GR--KTGGYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELD 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 178 RCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFY 257
Cdd:PLN03140 1006 NLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFE 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 258 MFDKLLLLSEGNPV-YFG-LGSNA---MDYFASV-GYSPLVERINPSDFLLDIAN-----GVGSDESqrpEAMKAALVAF 326
Cdd:PLN03140 1086 AFDELLLMKRGGQViYSGpLGRNShkiIEYFEAIpGVPKIKEKYNPATWMLEVSSlaaevKLGIDFA---EHYKSSSLYQ 1162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 327 YKTNLLDSVINEVKGQDDLcnkpRESSRVATNTYGDWPTTWWQQFCVLLkrglkqrRHDSFSGMKVAQIFIVSFLCGLLW 406
Cdd:PLN03140 1163 RNKALVKELSTPPPGASDL----YFATQYSQSTWGQFKSCLWKQWWTYW-------RSPDYNLVRFFFTLAAALMVGTIF 1231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 407 WQ--TKISRLQDqigLLFFISSFWA--FFPLFQQIFTFPQ----ERAMLQKERSSGMYRLSPYFLSRVVGDLPMELILPT 478
Cdd:PLN03140 1232 WKvgTKRSNAND---LTMVIGAMYAavLFVGINNCSTVQPmvavERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTT 1308
|
490 500
....*....|....*....|
gi 334186960 479 CFLVITYWMAGLNHNLANFF 498
Cdd:PLN03140 1309 YYTLIVYAMVAFEWTAAKFF 1328
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
60-274 |
5.08e-50 |
|
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: 172.45 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgEGKGKLTGNISYNNKPLSKAVKRTTG---FVTQDDAL 136
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT-EGNVSVEGDIHYNGIPYKEFAEKYPGeiiYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETLVFTAllrlpnsfkkqekikqakavmtelgldRCKdtiiGGPFLRGVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:cd03233 95 FPTLTVRETLDFAL---------------------------RCK----GNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
53-581 |
1.45e-44 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 171.57 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 53 GCFGKN-DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgEGKGKLTGNISYNNKPLSKAVKR-TTGFV 130
Cdd:PLN03140 166 GMLGINlAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKL-DPSLKVSGEITYNGYRLNEFVPRkTSAYI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 TQDDALYPNLTVTETLVFTALLR-------LPNSFKKQEK----IKQA------KAVMTE--------------LGLDRC 179
Cdd:PLN03140 245 SQNDVHVGVMTVKETLDFSARCQgvgtrydLLSELARREKdagiFPEAevdlfmKATAMEgvksslitdytlkiLGLDIC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 180 KDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSSRLFYM 258
Cdd:PLN03140 325 KDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 259 FDKLLLLSEGNPVYFGLGSNAMDYFASVGYS-PlvERINPSDFLLDIANgvGSDESQ------RP----------EAMKA 321
Cdd:PLN03140 405 FDDIILLSEGQIVYQGPRDHILEFFESCGFKcP--ERKGTADFLQEVTS--KKDQEQywadrnKPyryisvsefaERFKS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 322 ALVAFYKTNLLDSVINEVKGQDDLCNKPRESSRVATNTYGDWPTTWwqqfcvllkrgLKQRRHDSFSGMKVAQIFIVSFL 401
Cdd:PLN03140 481 FHVGMQLENELSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEW-----------LLMKRNAFVYVFKTVQIIIVAAI 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 402 CGLLWWQTKISRLQDQ-----IGLLFF---ISSFWAFFPLFQQIFTFPqeraMLQKERSSGMYRLSPYFLSRVVGDLPME 473
Cdd:PLN03140 550 ASTVFLRTEMHTRNEEdgalyIGALLFsmiINMFNGFAELALMIQRLP----VFYKQRDLLFHPPWTFTLPTFLLGIPIS 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 474 LILPTCFLVITYWMAGLNHNLANFFVTLLVLLVHVLVSGGLGLALGALVMDQKSATTLGSVIMLTFLLAGGYYV--QHVP 551
Cdd:PLN03140 626 IIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILpkGEIP 705
|
570 580 590
....*....|....*....|....*....|
gi 334186960 552 VFISWIKYVSIGYYTYKLLilgqyTANELY 581
Cdd:PLN03140 706 NWWEWAYWVSPLSYGFNAL-----AVNEMF 730
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
64-274 |
6.55e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.98 E-value: 6.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPL---SKAVKRTTGFVTQDDALYPN 139
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-----RPTsGEVRVLGEDVardPAEVRRRIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:COG1131 88 LTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKV-----GTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQPsSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
374-571 |
1.31e-34 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 130.09 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 374 LLKRGLKQRRHDSFSG-MKVAQIFIVSFLCGLLWWQTK-ISRLQDQIGLLFFISSFWAFFPLFQQIFTFPQERAMLQKER 451
Cdd:pfam01061 1 LLKREFLRRWRDPSLGlWRLIQPILMALIFGTLFGNLGnQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 452 SSGMYRLSPYFLSRVVGDLPMELILPTCFLVITYWMAGLNHNLANFFVTLLVLLVHVLVSGGLGLALGALVMDQKSATTL 531
Cdd:pfam01061 81 ASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 532 GSVIMLTFLLAGGYYV--QHVPVFISWIKYVSIGYYTYKLLI 571
Cdd:pfam01061 161 GPLVLLPLLLLSGFFIpiDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
37-269 |
1.96e-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: 130.30 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTVKLKDsqgcfgkndktEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTG-NIS 113
Cdd:cd03255 1 IELKNLSKTYGGGG-----------EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSGEVRVDGtDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 114 -YNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgV 192
Cdd:cd03255 70 kLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----L 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPssRLFYMFDKLLLLSEGN 269
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
37-272 |
3.02e-33 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 127.67 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTvklkdsqgcFGKNdkteerTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNN 116
Cdd:COG4555 2 IEVENLSKK---------YGKV------PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGS----ILIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 117 KPLSK---AVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQakaVMTELGLDRCKDTIIGGpflrgVS 193
Cdd:COG4555 63 EDVRKeprEARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEE---LIELLGLEEFLDRRVGE-----LS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 194 GGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPS--SRLfymFDKLLLLSEGNPV 271
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQevEAL---CDRVVILHKGKVV 211
|
.
gi 334186960 272 Y 272
Cdd:COG4555 212 A 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
63-267 |
2.50e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 123.74 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSK---AVKRTTGFVTQDDALYPN 139
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP----PSAGEVLWNGEPIRDareDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTALLRlpnsfKKQEKIKQAKAVMTELGLDRCKDTIIGgpFLrgvSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:COG4133 90 LTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVR--QL---SAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQPssrLFYMFDKLLLLSE 267
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
65-274 |
3.89e-32 |
|
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: 123.40 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLSK--AVKRTTGFVTQDDALYPNL 140
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGE------ILIDGRDVTGvpPERRNIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTalLRLpNSFKKQEKIKQAKAVMTELGLDRckdtiIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:cd03259 88 TVAENIAFG--LKL-RGVPKAEIRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 221 GLDSTTAQRIVSILWEL-ARGGRTVVTTIHQPSSRLFyMFDKLLLLSEGNPVYFG 274
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALA-LADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
60-268 |
4.26e-32 |
|
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: 123.35 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLS----KAVKRTTGFVTQD-D 134
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL----LGPTSGEVLVDGKDLTklslKELRRKVGLVFQNpD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYPNLTVTETLVFTallrLPNSFKKQEKIKQ-AKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLL 213
Cdd:cd03225 86 DQFFGPTVEEEVAFG----LENLGLPEEEIEErVEEALELVGLEGLRDR-----SPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPsSRLFYMFDKLLLLSEG 268
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
60-249 |
1.11e-31 |
|
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: 122.61 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLS---KAVKRTTGFVTQDDA 135
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-----RPTsGTAYINGYSIRtdrKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:cd03263 86 LFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRA-----RTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 334186960 216 DEPTSGLDSTTaQRIVsilWEL---ARGGRTVVTTIH 249
Cdd:cd03263 158 DEPTSGLDPAS-RRAI---WDLileVRKGRSIILTTH 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
67-220 |
2.41e-31 |
|
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: 119.29 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----KAVKRTTGFVTQDDALYPNLTV 142
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT----ILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 143 TETLVFTALLRLPNSFKKQEkikQAKAVMTELGLDRCKDTIIGGPFlRGVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDA---RAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
37-271 |
4.66e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.92 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTvklkdsqgcFGKNDktEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISY 114
Cdd:COG1136 5 LELRNLTKS---------YGTGE--GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTSGE------VLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 115 NNKPLSK-------AVKRTT-GFVTQDDALYPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTiigg 186
Cdd:COG1136 68 DGQDISSlserelaRLRRRHiGFVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDH---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 187 pFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPssRLFYMFDKLLLL 265
Cdd:COG1136 141 -RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDP--ELAARADRVIRL 217
|
....*.
gi 334186960 266 SEGNPV 271
Cdd:COG1136 218 RDGRIV 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
64-274 |
7.80e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 7.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSKAVKRTtGFVTQD---DALYPn 139
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL-----KPTsGSIRVFGKPLEKERKRI-GYVPQRrsiDRDFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTEtLVFTALLRLPNSFKKQ-----EKIKQA-KAV-MTELgLDRCkdtiiggpfLRGVSGGERKRVSIGQEILINPSL 212
Cdd:cd03235 85 ISVRD-VVLMGLYGHKGLFRRLskadkAKVDEAlERVgLSEL-ADRQ---------IGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYmFDKLLLLsEGNPVYFG 274
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEY-FDRVLLL-NRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
37-274 |
1.95e-29 |
|
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: 116.28 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTVklkdsqgcfgkndkTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNN 116
Cdd:COG1122 1 IELENLSFSY--------------PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGE----VLVDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 117 KPLSK----AVKRTTGFVTQ--DDALYpNLTVTETLVFtALLRLpnSFKKQEKIKQAKAVMTELGLDRCKDTIiggPFLr 190
Cdd:COG1122 63 KDITKknlrELRRKVGLVFQnpDDQLF-APTVEEDVAF-GPENL--GLPREEIRERVEEALELVGLEHLADRP---PHE- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 191 gVSGGERKRVSI-GqeILI-NPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEG 268
Cdd:COG1122 135 -LSGGQKQRVAIaG--VLAmEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDG 210
|
....*.
gi 334186960 269 NPVYFG 274
Cdd:COG1122 211 RIVADG 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
64-268 |
2.18e-29 |
|
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: 114.42 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSK---AVKRTTGFVTQDDALYPN 139
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-----KPDsGEIKVLGKDIKKepeEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFtallrlpnsfkkqekikqakavmtelgldrckdtiiggpflrgvSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03230 88 LTVRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEG 268
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
62-274 |
6.71e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSKAvKRTTGFVTQD---DALY 137
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL-----PPTsGTVRLFGKPPRRA-RRRIGYVPQRaevDWDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PnLTVTEtLVFTALLR---LPNSFKKQEKiKQAKAVMTELGLDRCKDTIIGGpfLrgvSGGERKRVSIGQEILINPSLLF 214
Cdd:COG1121 91 P-ITVRD-VVLMGRYGrrgLFRRPSRADR-EAVDEALERVGLEDLADRPIGE--L---SGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH--QPSSRLfymFDKLLLLSEGnPVYFG 274
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHdlGAVREY---FDRVLLLNRG-LVAHG 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
63-274 |
1.16e-28 |
|
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: 115.14 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLS----KAVKRTTGFVTQDDALYP 138
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK----PSSGEVLLDGRDLAslsrRELARRIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTEtLVftALLRLP--NSFKK--QEKIKQAKAVMTELGLDRCKDtiiggpflRGV---SGGERKRVSIGQEILINPS 211
Cdd:COG1120 89 GLTVRE-LV--ALGRYPhlGLFGRpsAEDREAVEEALERTGLEHLAD--------RPVdelSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSsrLFYMF-DKLLLLSEGNPVYFG 274
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLN--LAARYaDRLVLLKDGRIVAQG 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
64-274 |
1.47e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 114.20 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV----GEGKGKLTGNISYNNKPLsKAVKRTTGFVTQDDALYPN 139
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVeptsGSVLIDGTDINKLKGKAL-RQLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTET-----LVFTALLR-LPNSFKKQEKIKqAKAVMTELGLD-----RCKDtiiggpflrgVSGGERKRVSIGQEILI 208
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRsLFGLFPKEEKQR-ALAALERVGLLdkayqRADQ----------LSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 209 NPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSRLFYmFDKLLLLSEGNPVYFG 274
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREY-ADRIVGLKDGRIVFDG 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
64-239 |
1.72e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.35 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKgKLTGNISYNNKPLSK--AVKRTTGFVTQDDALYPNLT 141
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAF-SASGEVLLNGRRLTAlpAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFTallrLPNSFKKQEKIKQAKAVMTELGL----DRCKDTIiggpflrgvSGGERKRVSIGQEILINPSLLFLDE 217
Cdd:COG4136 93 VGENLAFA----LPPTIGRAQRRARVEQALEEAGLagfaDRDPATL---------SGGQRARVALLRALLAEPRALLLDE 159
|
170 180
....*....|....*....|..
gi 334186960 218 PTSGLDSTTAQRIVSILWELAR 239
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIR 181
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
63-268 |
1.14e-27 |
|
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: 109.58 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPL------SKAVKRTTGFVTQDDA 135
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDsGSILIDGEDLtdledeLPPLRRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFtallrlpnsfkkqekikqakavmtelgldrckdtiiggpflrGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:cd03229 87 LFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 334186960 216 DEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHQPSSrLFYMFDKLLLLSEG 268
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDG 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
60-269 |
1.28e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.68 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLSK----AVKRTTGFVT 131
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD--------LdpptSGEIYLDGKPLSAmpppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QDDALYPNlTVTETLVFTALLRlpnsfKKQEKIKQAKAVMTELGLDrckDTIIGGPFLRgVSGGERKRVSIGQEILINPS 211
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLR-----ERKFDRERALELLERLGLP---PDILDKPVER-LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHQP--SSRlfyMFDKLLLLSEGN 269
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPeqIER---VADRVLTLEAGR 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
63-274 |
2.95e-27 |
|
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: 109.68 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSKAVKRTTGFVTQDDALYPNLTV 142
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE----VLFDGKPLDIAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:cd03269 88 IDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMEL-VEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
54-260 |
3.24e-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: 109.27 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 54 CFGKNDKTEertILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSKAVK-RTTGFVTQ 132
Cdd:cd03226 6 SFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS----ILLNGKPIKAKERrKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 133 D--DALYPNlTVTETLvftaLLRLPNSFKKQEKIKQakaVMTELGLDRCKDTiigGPFlrGVSGGERKRVSIGQEILINP 210
Cdd:cd03226 79 DvdYQLFTD-SVREEL----LLGLKELDAGNEQAET---VLKDLDLYALKER---HPL--SLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQP------SSRLFYMFD 260
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYeflakvCDRVLLLAN 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
60-268 |
7.64e-27 |
|
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: 106.56 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFVTQddalypn 139
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 ltvtetlvftallrlpnsfkkqekikqakavmtelgldrckdtiiggpflrgVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEG 268
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDG 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
76-274 |
2.69e-26 |
|
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: 107.00 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 76 PGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNI---SYNNKPLSKAvKRTTGFVTQDDALYPNLTVTETLVFtA 150
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVLNGTVlfdSRKKINLPPQ-QRKIGLVFQQYALFPHLNVRENLAF-G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 151 LLRLPNSFKKQekikQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRI 230
Cdd:cd03297 100 LKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334186960 231 VSILWEL-ARGGRTVVTTIHQPsSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03297 171 LPELKQIkKNLNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
62-274 |
3.50e-26 |
|
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: 107.20 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSK-------AVKRTTGFVTQDD 134
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR----PDSGEVLIDGEDISGlseaelyRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYPNLTVTETLVFtaLLRLPNSFKKQEKIKQAKAVMTELGLdrckdtiiggpflRGV--------SGGERKRVSIGQEI 206
Cdd:cd03261 87 ALFDSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGL-------------RGAedlypaelSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 207 LINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
74-249 |
2.00e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 105.11 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS--KAVKRTTGFVTQDDALYPNLTVTETLVFTAL 151
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGK----ILLNGKDITnlPPEKRDISYVPQNYALFPHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 LRLPNSFKKQEKIKQAKAVM--TELgLDRCKDTIiggpflrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQR 229
Cdd:cd03299 98 KRKVDKKEIERKVLEIAEMLgiDHL-LNRKPETL---------SGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|.
gi 334186960 230 IVSilwELARGGRTV-VTTIH 249
Cdd:cd03299 168 LRE---ELKKIRKEFgVTVLH 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
63-274 |
3.76e-25 |
|
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: 102.51 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----KAVKRTTGFVTQddalyp 138
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE----ILLDGKDLAslspKELARKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 nltvtetlvftallrlpnsfkkqekikqakaVMTELGLDRCKDtiiggpflRGV---SGGERKRVSIGQEILINPSLLFL 215
Cdd:cd03214 81 -------------------------------ALELLGLAHLAD--------RPFnelSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSsrLFYMF-DKLLLLSEGNPVYFG 274
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLN--LAARYaDRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
63-274 |
4.52e-25 |
|
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: 104.29 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLSK-------AVKRTTGFVT 131
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG--------LlrpdSGEILVDGQDITGlsekelyELRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QDDALYPNLTVTETLVFtALLRLPNsFKKQEKIKQAKAVMTELGLdrckdtiiggpflRGV--------SGGERKRVSIG 203
Cdd:COG1127 89 QGGALFDSLTVFENVAF-PLREHTD-LSEAEIRELVLEKLELVGL-------------PGAadkmpselSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 204 QEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVYFG 274
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEG 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-268 |
5.77e-25 |
|
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: 109.46 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLVYTvklkdsqgcfgkndKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTG 110
Cdd:COG4988 331 AAGPPSIELEDVSFS--------------YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 111 NISYNNKPLS----KAVKRTTGFVTQDDALyPNLTVTETLVFTAllrlPNSfkKQEKIKQA--KAVMTEL------GLDr 178
Cdd:COG4988 393 SILINGVDLSdldpASWRRQIAWVPQNPYL-FAGTIRENLRLGR----PDA--SDEELEAAleAAGLDEFvaalpdGLD- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 179 ckdTIIG--GpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSSRLF 256
Cdd:COG4988 465 ---TPLGegG---RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ 537
|
250
....*....|..
gi 334186960 257 YmfDKLLLLSEG 268
Cdd:COG4988 538 A--DRILVLDDG 547
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
59-245 |
9.74e-25 |
|
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: 102.55 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 59 DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEgkgkltGNISYNNKPLSkAVKRTTGFVTQDDAL 136
Cdd:cd03293 12 GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRPTS------GEVLVDGEPVT-GPGPDRGYVFQQDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRckdtiiggpFLRG----VSGGERKRVSIGQEILINPSL 212
Cdd:cd03293 85 LPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLSG---------FENAyphqLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARG-GRTVV 245
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWREtGKTVL 186
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
37-239 |
9.94e-25 |
|
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: 102.97 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLvyTVKLKDSQGcfgkndkteERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrVGEGKgKLTGNISYNN 116
Cdd:cd03257 2 LEVKNL--SVSFPTGGG---------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI---LGLLK-PTSGSIIFDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 117 KPLSKAVK-------RTTGFVTQD--DALYPNLTVTETLVFTALLRLPNSfKKQEKIKQAKAVMTELGLDRckdtiiggP 187
Cdd:cd03257 67 KDLLKLSRrlrkirrKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLPE--------E 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 188 FLR----GVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR 239
Cdd:cd03257 138 VLNryphELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQE 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
46-250 |
1.10e-24 |
|
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: 102.22 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNdkteerTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPLSKAV 123
Cdd:cd03262 1 IEIKNLHKSFGDF------HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDSGTIIIDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 124 KRTTGFVTQDDALYPNLTVTE--TLVFTALLRLPnsfkKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVS 201
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLEniTLAPIKVKGMS----KAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQ 250
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
62-268 |
1.46e-24 |
|
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: 108.31 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLS----KAVKRTTGFVTQD 133
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--------FldpqSGSITLGGVDLRdldeDDLRRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DALYpNLTVTETLvftaLLRLPNSfkKQEKIKQA-KAVmtELG--LDRCK---DTIIG--GpflRGVSGGERKRVSIGQE 205
Cdd:COG4987 418 PHLF-DTTLRENL----RLARPDA--TDEELWAAlERV--GLGdwLAALPdglDTWLGegG---RRLSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 206 ILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDG 545
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
64-252 |
1.68e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTAL-------GGRVGEGKGKLTGNISYN-NKPLSKAVKRTTGFVTQDDA 135
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDITIDTARSLSqQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTALLrlPNSFKKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK11264 96 LFPHRTVLENIIEGPVI--VKGEPKEEATARARELLAKVGLAGKETS-----YPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPS 252
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
59-268 |
1.84e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 102.04 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 59 DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSKAVK--------RTTGFV 130
Cdd:TIGR02211 13 EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL----DNPTSGEVLFNGQSLSKLSSneraklrnKKLGFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 TQDDALYPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLdrcKDTIIGGPflRGVSGGERKRVSIGQEILINP 210
Cdd:TIGR02211 89 YQFHHLLPDFTALENVAMPLLIG---KKSVKEAKERAYEMLEKVGL---EHRINHRP--SELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARGGRT---VVTtiHQPssRLFYMFDKLLLLSEG 268
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsflVVT--HDL--ELAKKLDRVLEMKDG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
62-274 |
1.92e-24 |
|
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: 107.30 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkGKLTGNISYNNKPLSKAVK----RTTGFVTQD--DA 135
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG-GRISGEVLLDGRDLLELSEalrgRRIGMVFQDpmTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPnLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTiigGPFLrgVSGGERKRVSIGQEILINPSLLFL 215
Cdd:COG1123 96 LNP-VTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDR---YPHQ--LSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPsSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDG 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
67-274 |
1.98e-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: 101.68 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLskAVKRTTGFVTQDDALYPNLTVTET 145
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvDGFDVVKEPA--EARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALLrlpNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDST 225
Cdd:cd03266 99 LEYFAGL---YGLKGDELTARLEELADRLGMEELLDRRVGG-----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334186960 226 TAQRIVSILWELARGGRTVVTTIH--QPSSRLfymFDKLLLLSEGNPVYFG 274
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
60-268 |
3.27e-24 |
|
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: 101.80 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLS----KAVKRTTGFVT 131
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG--------LerpwSGEVTFDGRPVTrrrrKAFRRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QD--DALYPNLTVTETLvfTALLRLPNSFKKQEKIKQAkavMTELGLDrckdtiiggPFLRG-----VSGGERKRVSIGQ 204
Cdd:COG1124 86 QDpyASLHPRHTVDRIL--AEPLRIHGLPDREERIAEL---LEQVGLP---------PSFLDryphqLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 205 EILINPSLLFLDEPTSGLD-STTAQrIVSILWEL-ARGGRTVVTTIHQPsSRLFYMFDKLLLLSEG 268
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvSVQAE-ILNLLKDLrEERGLTYLFVSHDL-AVVAHLCDRVAVMQNG 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
65-251 |
5.08e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrVGEGKgklTGNISYNNKPLSKAVK--------RTTGFVTQDDAL 136
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGS---SGEVSLVGQPLHQMDEearaklraKHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETLVFTALLRLPNSFKKQEkikQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQSRN---GAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQP 251
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
62-274 |
7.65e-24 |
|
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: 100.93 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV-----------GEGKGKLtgNISynnkplskAVKRTTGFV 130
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvrlfGERRGGE--DVW--------ELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 TQD--DALYPNLTVTETLV--FTALLRLPNSFKKQEkIKQAKAVMTELGLDRCKDTiiggPFlRGVSGGERKRVSIGQEI 206
Cdd:COG1119 84 SPAlqLRFPRDETVLDVVLsgFFDSIGLYREPTDEQ-RERARELLELLGLAHLADR----PF-GTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 207 LINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTV---VTtiHQ----PSSrlfymFDKLLLLSEGNPVYFG 274
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTlvlVT--HHveeiPPG-----ITHVLLLKDGRVVAAG 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
63-274 |
1.04e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLL-TALGgrvgegkgkLT----GNISYNNKPLSKAVKRTTGFVTQDDALY 137
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILG---------ILapdsGEVLWDGEPLDPEDRRRIGYLPEERGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGL-DRCKDTIiggpflRGVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:COG4152 84 PKMKVGEQLVYLARLK---GLSKAEAKRRADEWLERLGLgDRANKKV------EELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSS--RLfymFDKLLLLSEGNPVYFG 274
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELveEL---CDRIVIINKGRKVLSG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
66-274 |
1.09e-23 |
|
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: 99.57 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGeILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN-ISYNNKPlsKAVKRTTGFVTQDDALYPNLTVTE 144
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgQDVLKQP--QKLRRRIGYLPQEFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFTALLRLPNSfkKQEKiKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDS 224
Cdd:cd03264 92 FLDYIAWLKGIPS--KEVK-ARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 225 ttAQRIV--SILWELARgGRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVYFG 274
Cdd:cd03264 164 --EERIRfrNLLSELGE-DRIVILSTHIVED-VESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
67-249 |
1.21e-23 |
|
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: 99.40 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSK-------AVKRTTGFVTQDDALYPN 139
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE----ELPTSGTIRVNGQDVSDlrgraipYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTalLRLPNSfKKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03292 93 RNVYENVAFA--LEVTGV-PPREIRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
60-245 |
1.70e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.16 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLSKAVKRtTGFVTQDDA 135
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG--------LekptSGEVLVDGKPVTGPGPD-RGVVFQEPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:COG1116 91 LLPWLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFEDA-----YPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190
....*....|....*....|....*....|.
gi 334186960 216 DEPTSGLDSTTAQRIVSILWEL-ARGGRTVV 245
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLwQETGKTVL 193
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
64-249 |
2.16e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSK-------AVKRTTGFVTQDDA 135
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE-----RPTsGQVLVNGQDLSRlkrreipYLRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTalLRLpnSFKKQEKIKQ-AKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLF 214
Cdd:COG2884 90 LLPDRTVYENVALP--LRV--TGKSRKEIRRrVREVLDLVGLSDKAKA-----LPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
58-270 |
3.12e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 58 NDKTEertILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGN-ISYNNKPLSKaVKRTTGFVTQ-- 132
Cdd:PRK13639 12 PDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilKPTSGEVLIKGEpIKYDKKSLLE-VRKTVGIVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 133 DDALYPNlTVTETLVFTAL-LRLPnsfkKQEKIKQAKAVMTELGLDRCKDTiigGPflRGVSGGERKRVSIGQEILINPS 211
Cdd:PRK13639 88 DDQLFAP-TVEEDVAFGPLnLGLS----KEEVEKRVKEALKAVGMEGFENK---PP--HHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQ----P--SSRLFYMFDKlLLLSEGNP 270
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPvyADKVYVMSDG-KIIKEGTP 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
65-252 |
3.64e-23 |
|
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: 98.66 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTG-NIS-YNNKPLSKAVKRTTGFVTQDDALYPNL 140
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPTSGTVRLAGqDLFaLDEDARARLRARHVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTALLR-LPNSFKkqekikQAKAVMTELGL-DRCKDTiiggPflRGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:COG4181 106 TALENVMLPLELAgRRDARA------RARALLERVGLgHRLDHY----P--AQLSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 219 TSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPS 252
Cdd:COG4181 174 TGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
67-249 |
7.59e-23 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 99.39 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGnisYNNKPLSKAVKRTTGFVTQDDALYPNLTVTE 144
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRPTSGTARVAG---YDVVREPRKVRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLV-FTALLRLPnsfkKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:TIGR01188 86 NLEmMGRLYGLP----KDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180
....*....|....*....|....*.
gi 334186960 224 STTAQRIVSILWELARGGRTVVTTIH 249
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
62-268 |
1.07e-22 |
|
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: 95.14 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLSK----AVKRTTGFVTQD 133
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--------LydptSGEILIDGVDLRDldleSLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DALYpNLTVTETLVftallrlpnsfkkqekikqakavmtelgldrckdtiiggpflrgvSGGERKRVSIGQEILINPSLL 213
Cdd:cd03228 85 PFLF-SGTIRENIL---------------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELaRGGRTVVTTIHQPSSRLfyMFDKLLLLSEG 268
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR--DADRIIVLDDG 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
75-258 |
1.09e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 75 KPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLtgNISYNNKPLSK--------AVKRTTGFVTQDDALYPNLTVTETL 146
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL--NIAGNHFDFSKtpsdkairELRRNVGMVFQQYNLWPHLTVQQNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 VfTALLRLpNSFKKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD-ST 225
Cdd:PRK11124 104 I-EAPCRV-LGLSKDQALARAEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 334186960 226 TAQrIVSILWELARGGRTVVTTIHQ------PSSRLFYM 258
Cdd:PRK11124 177 TAQ-IVSIIRELAETGITQVIVTHEvevarkTASRVVYM 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
67-249 |
1.53e-22 |
|
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: 96.28 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGnisYNNKPLSKAVKRTTGFVTQDDALYPNLTVTE 144
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSGRATVAG---HDVVREPREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TL-VFTALLRLPNSfKKQEKIKQAKAVMtelGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:cd03265 93 NLyIHARLYGVPGA-ERRERIDELLDFV---GLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180
....*....|....*....|....*..
gi 334186960 224 STTAQRIVSILWEL-ARGGRTVVTTIH 249
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
54-268 |
2.24e-22 |
|
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: 96.53 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 54 CFGKNDkteERTILKGLTGIVKPGEILAMLGPSGSGKTSLLtalggrvgegkgKL--------TGNISYNNKPLSK---- 121
Cdd:cd03253 7 TFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIL------------RLlfrfydvsSGSILIDGQDIREvtld 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 122 AVKRTTGFVTQDDAL----------YPNLTVTEtlvftallrlpnsfkkQEKIKQAKAVMTE---LGLDRCKDTIIGGpf 188
Cdd:cd03253 72 SLRRAIGVVPQDTVLfndtigynirYGRPDATD----------------EEVIEAAKAAQIHdkiMRFPDGYDTIVGE-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 189 lRGV--SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSSrlFYMFDKLLLLS 266
Cdd:cd03253 134 -RGLklSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLST--IVNADKIIVLK 209
|
..
gi 334186960 267 EG 268
Cdd:cd03253 210 DG 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
63-254 |
2.37e-22 |
|
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: 101.21 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLS----KAVKRTTGFVTQDDALYP 138
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT----EGSIAVNGVPLAdadaDSWRDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NlTVTETLvftaLLRLPNSfkKQEKIKQAkavMTELGLDRC-------KDTIIG--GpflRGVSGGERKRVSIGQEILIN 209
Cdd:TIGR02857 410 G-TIAENI----RLARPDA--SDAEIREA---LERAGLDEFvaalpqgLDTPIGegG---AGLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334186960 210 PSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSSR 254
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
64-251 |
3.50e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgkltgnisynnKPLSKAVKRTTG----FVTQ----DDA 135
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL---------------RPTSGTVRRAGGarvaYVPQrsevPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LyPnLTVTETLvftALLRLPNSFKKQEKIKQAKAV----MTELGLDRckdtiIGGPFLRGVSGGERKRVSIGQEILINPS 211
Cdd:NF040873 70 L-P-LTVRDLV---AMGRWARRGLWRRLTRDDRAAvddaLERVGLAD-----LAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQP 251
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
67-245 |
4.32e-22 |
|
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: 95.58 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS--KAVKRTT-GFV-T-QDDALYPNLT 141
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS----VLFDGEDITglPPHEIARlGIGrTfQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFTALLRLPNSF-------KKQEKIKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINPSLLF 214
Cdd:cd03219 92 VLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG-----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190
....*....|....*....|....*....|.
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARGGRTVV 245
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
64-274 |
4.55e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.95 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrVGEGKGKlTGNISYNNKPLSK------AVKRttGFVTQDDALY 137
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLL---TGELTPS-SGEVRLNGRPLAAwspwelARRR--AVLPQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTEtLVftALLRLPNSFKKQEKIKQAKAVMTELGL----DRckdtiiggpFLRGVSGGERKRVS-------IGQEI 206
Cdd:COG4559 88 FPFTVEE-VV--ALGRAPHGSSAAQDRQIVREALALVGLahlaGR---------SYQTLSGGEQQRVQlarvlaqLWEPV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 207 LINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSsrLFYMF-DKLLLLSEGNPVYFG 274
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
75-258 |
5.13e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.46 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 75 KPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT--GN-ISYNNKPLSKAV---KRTTGFVTQDDALYPNLTVTETLVF 148
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaGHqFDFSQKPSEKAIrllRQKVGMVFQQYNLWPHLTVMENLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 149 TALLRLPNSfkKQEKIKQAKAVMTELGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD-STTA 227
Cdd:COG4161 106 APCKVLGLS--KEQAREKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEITA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 334186960 228 QrIVSILWELARGGRTVVTTIHQPS------SRLFYM 258
Cdd:COG4161 179 Q-VVEIIRELSQTGITQVIVTHEVEfarkvaSQVVYM 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
63-249 |
1.01e-21 |
|
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: 94.17 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKG-KLTGNISYNNKPLSK------AVKRTTGFVTQDDA 135
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGaPDEGEVLLDGKDIYDldvdvlELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPnLTVTETLVFTalLRLPNSFKKQEKIKQAKAVMTELGL-DRCKDTIIGgpflRGVSGGERKRVSIGQEILINPSLLF 214
Cdd:cd03260 92 PFP-GSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALwDEVKDRLHA----LGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIH 249
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
64-249 |
1.53e-21 |
|
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: 93.76 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGK-LTGNISYNNKPLSKAVKRTTGFVTQDDALYPNLTV 142
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKiLLDGQDITKLPMHKRARLGIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVftALLRLPNsFKKQEKIKQAKAVMTELGLDRCKDTIigGPFLrgvSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:cd03218 93 EENIL--AVLEIRG-LSKKEREEKLEELLEEFHITHLRKSK--ASSL---SGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180
....*....|....*....|....*..
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
66-249 |
2.16e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 92.10 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN---ISYNNKPLSKaVKRTTGFVTQ--DDALYPNl 140
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgepLDYSRKGLLE-RRQRVGLVFQdpDDQLFAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTAL-LRLPNSfKKQEKIKQAkavMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:TIGR01166 85 DVDQDVAFGPLnLGLSEA-EVERRVREA---LTAVGASGLRERPT-----HCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
66-245 |
2.30e-21 |
|
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: 92.88 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLSKA-----VKRTTGFVTQDDALYP 138
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGS------IRFDGRDITGLppherARAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFTALLRLPNSFKkqEKIKQAKAVMTELGlDRCKDtiiggpflRG--VSGGERKRVSIGQEILINPSLLFLD 216
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRK--ARLERVYELFPRLK-ERRKQ--------LAgtLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180
....*....|....*....|....*....
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARGGRTVV 245
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
46-271 |
4.02e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.85 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNdkteerTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG-RVGEGKGKLTGNISYN-NKPLSKAV 123
Cdd:PRK09493 2 IEFKNVSKHFGPT------QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKlEEITSGDLIVDGLKVNdPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 124 KRTTGFVTQDDALYPNLTVTETLVFTAL-LRlpnSFKKQEKIKQAKAVMTELGL-DRckdtiiGGPFLRGVSGGERKRVS 201
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLrVR---GASKEEAEKQARELLAKVGLaER------AHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH------QPSSRLFYMfDKLLLLSEGNPV 271
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHeigfaeKVASRLIFI-DKGRIAEDGDPQ 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-245 |
4.41e-21 |
|
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: 96.90 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLVYTVKLKdsqgcfgkndKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL-- 108
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVR----------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG--------Llr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 109 --TGNISYNNKPLSKAVKRTT-------GFVTQD--DALYPNLTVTETLVFTalLRLPNSFKKQEKIKQAKAVMTELGLD 177
Cdd:COG1123 317 ptSGSILFDGKDLTKLSRRSLrelrrrvQMVFQDpySSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLP 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 178 RckdtiiggPFLR----GVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVV 245
Cdd:COG1123 395 P--------DLADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
66-255 |
1.05e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSK---AVK-----RTTGFVTQDDALY 137
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL----DTPTSGDVIFNGQPMSKlssAAKaelrnQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLvftALLRLPNSFKKQEKIKQAKAVMTELGLDRckdtiiggpflRG------VSGGERKRVSIGQEILINPS 211
Cdd:PRK11629 100 PDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEH-----------RAnhrpseLSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARGGRT---VVTTIHQPSSRL 255
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTaflVVTHDLQLAKRM 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
62-268 |
1.64e-20 |
|
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: 96.06 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLtalggrvgegkgKL--------TGNISYNNKPLSK----AVKRTTGF 129
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL------------KLllglyeptSGRILIDGIDLRQidpaSLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 130 VTQDDALYP-----NLTVTETLVftallrlpnsfkKQEKIKQAkAVMTEL---------GLdrckDTIIG--GpflRGVS 193
Cdd:COG2274 554 VLQDVFLFSgtireNITLGDPDA------------TDEEIIEA-ARLAGLhdfiealpmGY----DTVVGegG---SNLS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 194 GGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKG 685
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
65-223 |
1.92e-20 |
|
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: 90.76 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisYNNKPLSK--AVKRTTGFVTQDDALYPNLTV 142
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL----LDGKDITNlpPHKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVFTalLRLpnsfKKQEKIKQAKAVMTELGLDRCKDtiIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:cd03300 90 FENIAFG--LRL----KKLPKAEIKERVAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
.
gi 334186960 223 D 223
Cdd:cd03300 162 D 162
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
62-268 |
3.26e-20 |
|
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: 89.98 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----KAVKRTTGFVTQDDALY 137
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ----ILIDGIDIRdisrKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNlTVTETLvftallRLPNSFKKQEKIKQA-KAV-MTELGLDRCK--DTIIGgPFLRGVSGGERKRVSIGQEILINPSLL 213
Cdd:cd03254 90 SG-TIMENI------RLGRPNATDEEVIEAaKEAgAHDFIMKLPNgyDTVLG-ENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELaRGGRTVVTTIHQPSSRLFYmfDKLLLLSEG 268
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDG 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
62-274 |
4.13e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT---GNISYnnKPLSKAVKRTTGFVTQDDALYP 138
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddEDISL--LPLHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVftALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIiggpfLRGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK10895 92 RLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLfYMFDKLLLLSEGNPVYFG 274
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
63-249 |
5.13e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.08 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLSK--AVKRTTGFVTQDDALYP 138
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDSGR------ILLDGRDVTGlpPEKRNVGMVFQDYALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFTalLRLPNsFKKQEKIKQAKAVMTELGLDRCKDtiiggpflRGV---SGGERKRVSIGQEILINPSLLFL 215
Cdd:COG3842 91 HLTVAENVAFG--LRMRG-VPKAEIRARVAELLELVGLEGLAD--------RYPhqlSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 216 DEPTSGLDsttAQRIVSILWELARGGRTV-VTTIH 249
Cdd:COG3842 160 DEPLSALD---AKLREEMREELRRLQRELgITFIY 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
63-250 |
6.21e-20 |
|
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: 88.43 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKpLSKAVKRTtGFVTQDDALYPNLTV 142
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRI-GALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVFTALLRLpnsfKKQEKIKQakaVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:cd03268 90 RENLRLLARLLG----IRKKRIDE---VLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....*...
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTIHQ 250
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
60-274 |
1.09e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.54 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPlsKAVKRTTGFVTQDDALY 137
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPTSGEVRVAGLVPWKRRK--KFLRRIGVVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVF-TALLRLPNS-FKKQekikqakavmtelgLDRCKDTIIGGPFL----RGVSGGERKRVSIGQEILINPS 211
Cdd:cd03267 108 WDLPVIDSFYLlAAIYDLPPArFKKR--------------LDELSELLDLEELLdtpvRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHqpssrlfYMFD------KLLLLSEGNPVYFG 274
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSH-------YMKDiealarRVLVIDKGRLLYDG 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
62-268 |
1.24e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.92 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLS----KAVKRTTGFVTQDDA 135
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTSGR------ILIDGVDIRdltlESLRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 L----------YPNLTVTETLVFTALlrlpnsfkkqeKIKQAKAVMTEL--GLdrckDTIIGGpflRGV--SGGERKRVS 201
Cdd:COG1132 425 LfsgtirenirYGRPDATDEEVEEAA-----------KAAQAHEFIEALpdGY----DTVVGE---RGVnlSGGQRQRIA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSS-RlfyMFDKLLLLSEG 268
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTiR---NADRILVLDDG 550
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
62-223 |
1.41e-19 |
|
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: 87.70 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL-TGNISYNNKPlskAVKRTTGFVTQDDALYPNL 140
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyIGGRDVTDLP---PKDRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELG----LDRCKDTIiggpflrgvSGGERKRVSIGQEILINPSLLFLD 216
Cdd:cd03301 88 TVYDNIAFGLKLR---KVPKDEIDERVREVAELLQiehlLDRKPKQL---------SGGQRQRVALGRAIVREPKVFLMD 155
|
....*..
gi 334186960 217 EPTSGLD 223
Cdd:cd03301 156 EPLSNLD 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
63-223 |
1.81e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.13 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkL----TGNISYNNKPLSK--AVKRTTGFVTQDDAL 136
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--------LedptSGEILIGGRDVTDlpPKDRNIAMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETLVFTalLRLpNSFKKQEKIKQAKAVMTELGLDrckdtiiggPFL----RGVSGGERKRVSIGQEILINPSL 212
Cdd:COG3839 87 YPHMTVYENIAFP--LKL-RKVPKAEIDRRVREAAELLGLE---------DLLdrkpKQLSGGQRQRVALGRALVREPKV 154
|
170
....*....|.
gi 334186960 213 LFLDEPTSGLD 223
Cdd:COG3839 155 FLLDEPLSNLD 165
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
62-268 |
3.30e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.61 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSK-AVKRttGFVTQDDALYPNL 140
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA----PSSGEITLDGVPVTGpGADR--GVVFQKDALLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTalLRLpNSFKKQEKIKQAKAVMTELGLDRckdtiIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:COG4525 92 NVLDNVAFG--LRL-RGVPKAERRARAEELLALVGLAD-----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 221 GLDSTTAQRIVSILWEL-ARGGRTVVTTIHQPSSRLFyMFDKLLLLSEG 268
Cdd:COG4525 164 ALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALF-LATRLVVMSPG 211
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
63-249 |
5.78e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 86.56 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKAVKRTTGFVTQDDALYPNLT 141
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILiDGQDITHLPMHERARLGIGYLPQEASIFRKLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVftALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:TIGR04406 93 VEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180
....*....|....*....|....*...
gi 334186960 222 LDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
74-268 |
6.05e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLS-KAVKRttGFVTQDDALYPNLTVTETLVFTALL 152
Cdd:PRK11248 24 LESGELLVVLGPSGCGKTTLLNLIAGFVPYQ----HGSITLDGKPVEgPGAER--GVVFQNEGLLPWRNVQDNVAFGLQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RlpnSFKKQEKIKQAKAVMTELGLDRckdtiIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVS 232
Cdd:PRK11248 98 A---GVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 334186960 233 ILWEL-ARGGRTVVTTIHQPSSRLFyMFDKLLLLSEG 268
Cdd:PRK11248 170 LLLKLwQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
55-246 |
6.07e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.59 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 55 FGKNdkteerTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkLT----GNISYNNKPLS------KAVK 124
Cdd:COG1126 11 FGDL------EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL--------LEepdsGTITVDGEDLTdskkdiNKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 125 RTTGFVTQDDALYPNLTVTE--TLVFTALLRLPnsfkKQEKIKQAKAVMTELGL-DRCKDtiiggpFLRGVSGGERKRVS 201
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLEnvTLAPIKVKKMS----KAEAEERAMELLERVGLaDKADA------YPAQLSGGQQQRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRT--VVT 246
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTmvVVT 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
62-269 |
6.37e-19 |
|
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: 84.58 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISynNKPLSKAVKRTTGFVTQDDALYPN 139
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTSGRVRLDGADI--SQWDPNELGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 lTVTEtlvftallrlpNSFkkqekikqakavmtelgldrckdtiiggpflrgvSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03246 91 -SIAE-----------NIL----------------------------------SGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQPSsrLFYMFDKLLLLSEGN 269
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
62-268 |
9.98e-19 |
|
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: 84.29 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisYNNKPLS---KAVKRTTGFVTQDDALYp 138
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT----LDGVPVSdleKALSSLISVLNQRPYLF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLvftallrlpnsfkkqekikqakavmtelgldrckdtiiGGPFlrgvSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:cd03247 88 DTTLRNNL--------------------------------------GRRF----SGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 219 TSGLDSTTAQRIVSILWELARgGRTVVTTIHqpssRLFYM--FDKLLLLSEG 268
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK-DKTLIWITH----HLTGIehMDKILFLENG 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
63-251 |
1.08e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkGKLTGNISYNNKP--LSKAVKRTTgFVTQDDALYPNL 140
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGGDidDPDVAEACH-YLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTAllrlpnSFKKQEKIkQAKAVMTELGLDRckdtIIGGPFlRGVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:PRK13539 89 TVAENLEFWA------AFLGGEEL-DIAAALEAVGLAP----LAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|..
gi 334186960 221 GLDSTTAQRIVSILWE-LARGGRTVVTTiHQP 251
Cdd:PRK13539 157 ALDAAAVALFAELIRAhLAQGGIVIAAT-HIP 187
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
37-251 |
1.14e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.89 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTVklkdsqgcfgkndktEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEgkgKLT-GNISYN 115
Cdd:COG0396 1 LEIKNLHVSV---------------EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKY---EVTsGSILLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 116 NKPL--------SKAvkrttG-FVT-QDDALYPNLTVTEtlvftaLLRLPNSFKKQEKI------KQAKAVMTELGLDrc 179
Cdd:COG0396 63 GEDIlelspderARA-----GiFLAfQYPVEIPGVSVSN------FLRTALNARRGEELsareflKLLKEKMKELGLD-- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 180 KDtiiggpFL-RGV----SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQP 251
Cdd:COG0396 130 ED------FLdRYVnegfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
74-245 |
1.21e-18 |
|
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: 85.86 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSKA---------VKRTtgFvtQDDALYPNLTVT 143
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTLFNLITGFY-----RPTsGRILFDGRDITGLpphriarlgIART--F--QNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETL-----------VFTALLRLPnSFKKQEK--IKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINP 210
Cdd:COG0411 98 ENVlvaaharlgrgLLAALLRLP-RARREEReaRERAEELLERVGLADRADEPAG-----NLSYGQQRRLEIARALATEP 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVV 245
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDErGITIL 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
74-230 |
1.34e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.85 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkLT----GNISYNNKPLSKAVKRTT--------GFVTQDDALYPNLT 141
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAG--------LErpdsGRIRLGGEVLQDSARGIFlpphrrriGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFtALLRLPnsfKKQEKIKQAKAV-MTELG--LDRckdtiigGPflRGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:COG4148 94 VRGNLLY-GRKRAP---RAERRISFDEVVeLLGIGhlLDR-------RP--ATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170
....*....|..
gi 334186960 219 TSGLDSTTAQRI 230
Cdd:COG4148 161 LAALDLARKAEI 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
74-281 |
1.52e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGG-----RVGEGKGKLTGNISYNNKPLSKAVKRT---TGFVTQDDALYPNLTVTET 145
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGlitgdKSAGSHIELLGRTVQREGRLARDIRKSranTGYIFQQFNLVNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALLRLP------NSFKKQEKiKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:PRK09984 107 VLIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQRVS-----TLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 220 SGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSRLFYMfDKLLLLSEGNpVYFGLGSNAMD 281
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYC-ERIVALRQGH-VFYDGSSQQFD 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
67-255 |
2.35e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGE--GKGKLTGNISYNNK----PLSKAV--KRTTGFVTQDDALYP 138
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-RMNDlnPEVTITGSIVYNGHniysPRTDTVdlRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 nLTVTETLVFTalLRLpNSFKKQEKIKQA-------KAVMTELGlDRCKDTIIGgpflrgVSGGERKRVSIGQEILINPS 211
Cdd:PRK14239 100 -MSIYENVVYG--LRL-KGIKDKQVLDEAvekslkgASIWDEVK-DRLHDSALG------LSGGQQQRVCIARVLATSPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELaRGGRTVVTTIH--QPSSRL 255
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRsmQQASRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
64-271 |
2.47e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----------KAVKRttgfvtQD 133
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE----VRLNGRPLAdwspaelarrRAVLP------QH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DAL-YPnLTVTETLvftALLRLPNSFKKQEKIKQAKAVMTELGLDRckdtiIGGPFLRGVSGGERKRV----------SI 202
Cdd:PRK13548 85 SSLsFP-FTVEEVV---AMGRAPHGLSRAEDDALVAAALAQVDLAH-----LAGRDYPQLSGGEQQRVqlarvlaqlwEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 203 GQEilinPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSsrLFYMF-DKLLLLSEGNPV 271
Cdd:PRK13548 156 DGP----PRWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLN--LAARYaDRIVLLHQGRLV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
63-251 |
3.19e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkGKLTGNISYNNKPLSKAVK---RTTGFVTQDDALYPN 139
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPLAEQRDephENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTALLRLPnsfkKQEKIKQAkavMTELGLDRCKDTIIGgpFLrgvSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:TIGR01189 88 LSALENLHFWAAIHGG----AQRTIEDA---LAAVGLTGFEDLPAA--QL---SAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 220 SGLDSTTAQRIVSILWE-LARGGRTVVTTiHQP 251
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
66-251 |
3.76e-18 |
|
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: 88.19 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkGKLTGNISYNNKPLSK----AVKRTTGFVTQDDALYpNLT 141
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL----DPLQGEVTLDGVPVSSldqdEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFTAllrlPNSfKKQEKIKQAKAVMTELGLDRCKD---TIIGGPFLRgVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:TIGR02868 425 VRENLRLAR----PDA-TDEELWAALERVGLADWLRALPDgldTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 219 TSGLDSTTAQRIVSILWElARGGRTVVTTIHQP 251
Cdd:TIGR02868 499 TEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
62-274 |
4.24e-18 |
|
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: 87.88 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKP--LSKAVkrttGFVTQDDALY 137
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwPPTAGSVRLDGADLSQWDReeLGRHI----GYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNlTVTETLvftALLRLPNSfkkqEKIKQA--KAVMTE--LGLDRCKDTIIG--GPFLrgvSGGERKRVSIGQEILINPS 211
Cdd:COG4618 419 DG-TIAENI---ARFGDADP----EKVVAAakLAGVHEmiLRLPDGYDTRIGegGARL---SGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSsrLFYMFDKLLLLSEGNPVYFG 274
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFG 548
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
76-268 |
6.05e-18 |
|
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: 85.93 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 76 PG-EILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNI--SYNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTa 150
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGltRPDEGEIVLNGRTlfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 151 llrLPNSFKKQEKIKQAKaVMTELGLdrckdtiigGPFL-RGV---SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:TIGR02142 100 ---MKRARPSERRISFER-VIELLGI---------GHLLgRLPgrlSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 227 AQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEG 268
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-251 |
9.10e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 24 PFSIFKKannpVTLKFENLVY-TVKLKDSQGCFGKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVG 102
Cdd:COG2401 6 PFFVLMR----VTKVYSSVLDlSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 103 EGKGKLTGNIsynnkplskavkrttgfvtQDDALYPNLTVTEtlvftALLRLPNsfkkqekIKQAKAVMTELGLDrckDT 182
Cdd:COG2401 82 GTPVAGCVDV-------------------PDNQFGREASLID-----AIGRKGD-------FKDAVELLNAVGLS---DA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 183 IIggpFLRGV---SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQP 251
Cdd:COG2401 128 VL---WLRRFkelSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGITLVVATHHY 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-259 |
1.05e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLVYTVKLKdsQGCFGKndKTEERTILKGLTGIVKPGEILAMLGPSGSGKTS----LLTALGGRvgegkg 106
Cdd:PRK15134 270 EPASPLLDVEQLQVAFPIR--KGILKR--TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 107 kltGNISYNNKPLSK-------AVKRTTGFVTQD--DALYPNLTVtETLVFTALLRLPNSFKKQEKIKQAKAVMTELGLD 177
Cdd:PRK15134 340 ---GEIWFDGQPLHNlnrrqllPVRHRIQVVFQDpnSSLNPRLNV-LQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 178 rckdtiiggPFLR-----GVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELarggrtvvttihQPS 252
Cdd:PRK15134 416 ---------PETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL------------QQK 474
|
....*..
gi 334186960 253 SRLFYMF 259
Cdd:PRK15134 475 HQLAYLF 481
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
62-249 |
2.20e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.03 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrvgegkgklTGNISYnnkplskavKRTTGFVTQDDALYPNLT 141
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI-----------MGHPKY---------EVTEGEILFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETlvftALLRLPNSFKKQEKIKQAKAVMtelgldrckdtiiggpFLRGV----SGGERKRVSIGQEILINPSLLFLDE 217
Cdd:cd03217 71 PEER----ARLGIFLAFQYPPEIPGVKNAD----------------FLRYVnegfSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|..
gi 334186960 218 PTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-274 |
2.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 44 YTVKLKDSqgCFGKNDKTEErtiLKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSKAV 123
Cdd:PRK13636 4 YILKVEEL--NYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK----PSSGRILFDGKPIDYSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 124 K------RTTGFVTQD-DALYPNLTVTETLVFTAL-LRLPnsfkKQEKIKQAKAVMTELGLDRCKDTiiggPfLRGVSGG 195
Cdd:PRK13636 75 KglmklrESVGMVFQDpDNQLFSASVYQDVSFGAVnLKLP----EDEVRKRVDNALKRTGIEHLKDK----P-THCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 196 ERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSRLFYMfDKLLLLSEGNPVYFG 274
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYC-DNVFVMKEGRVILQG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
66-245 |
2.89e-17 |
|
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: 81.57 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSKA-----VKRTTGFVTQDDALYPNL 140
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLpphriARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTALLRlpnsfKKQEKIKQAKAVMTELgldrckdtiiggpF-----LRGV-----SGGERKRVSIGQEILINP 210
Cdd:COG0410 94 TVEENLLLGAYAR-----RDRAEVRADLERVYEL-------------FprlkeRRRQragtlSGGEQQMLAIGRALMSRP 155
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVV 245
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTIL 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
74-274 |
9.47e-17 |
|
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: 79.46 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKavkRTTGFVTQDDALYPNLTVTETLvftALL 152
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLiNGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNV---GLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RLPN---SFKKQEKIKQAKAVMTELGLD-RCKDTIiggpflrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQ 228
Cdd:cd03298 95 LSPGlklTAEDRQAIEVALARVGLAGLEkRLPGEL---------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334186960 229 RIVSILWELAR-GGRTVVTTIHQPSSRLfYMFDKLLLLSEGNPVYFG 274
Cdd:cd03298 166 EMLDLVLDLHAeTKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
74-269 |
1.11e-16 |
|
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: 79.69 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLtalggRVGEGKGKLT-GNISYNNKPLSK--AVKRTTGFVTQDDALYPNLTVTETLVFTA 150
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLL-----RLIAGLERPDsGTILFGGEDATDvpVQERNVGFVFQHYALFRHMTVFDNVAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 151 LLR----LPNSFKKQEKIKQAKAVMTELGL-DRckdtiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDST 225
Cdd:cd03296 100 RVKprseRPPEAEIRAKVHELLKLVQLDWLaDR---------YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334186960 226 TAQRIVSILWELA-RGGRTVVTTIHQPSSRLfYMFDKLLLLSEGN 269
Cdd:cd03296 171 VRKELRRWLRRLHdELHVTTVFVTHDQEEAL-EVADRVVVMNKGR 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-268 |
1.25e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLvytvklkdsqgCFGKNDktEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrvgegkgklT- 109
Cdd:PRK11160 333 AADQVSLTLNNV-----------SFTYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL-----------Tr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 110 ------GNISYNNKPLS----KAVKRTTGFVTQDDALYpNLTVTETLvftaLLRLPNSFKKQ-----EKIKQAKAVMTEL 174
Cdd:PRK11160 389 awdpqqGEILLNGQPIAdyseAALRQAISVVSQRVHLF-SATLRDNL----LLAAPNASDEAlievlQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 175 GLDrckdTIIG--GpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHqps 252
Cdd:PRK11160 464 GLN----AWLGegG---RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH--- 532
|
250
....*....|....*...
gi 334186960 253 sRLFYM--FDKLLLLSEG 268
Cdd:PRK11160 533 -RLTGLeqFDRICVMDNG 549
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
62-268 |
1.30e-16 |
|
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: 79.17 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGK-LTGNISYNNKPLSKaVKRTTGFVTQDDALYpNL 140
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvLLDGTDIRQLDPAD-LRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVftalLRLPNSfKKQEKIKQAK-AVMTEL------GLDRckdtIIG--GpflRGVSGGERKRVSIGQEILINPS 211
Cdd:cd03245 93 TLRDNIT----LGAPLA-DDERILRAAElAGVTDFvnkhpnGLDL----QIGerG---RGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELArGGRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
63-251 |
1.73e-16 |
|
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: 78.30 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSK---AVKRTTGFVTQDDALYPN 139
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL----SPPLAGRVLLNGGPLDFqrdSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTAllrlpnSFKKQEKIKQAKAvmtELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03231 88 LSVLENLRFWH------ADHSDEQVEEALA---RVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|..
gi 334186960 220 SGLDSTTAQRIVSILWELARGGRTVVTTIHQP 251
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
56-271 |
2.05e-16 |
|
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: 79.46 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 56 GKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLltalgGRVGEGKGKLT-GNISYNNKPLS-------KAVKRTT 127
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTL-----ARLLLGLEKPAqGTVSFRGQDLYqldrkqrRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 128 GFVTQD--DALYPNLTVTETLvfTALLRLPNSFKKQEKIKQAKAVMTELGLDrckdTIIGGPFLRGVSGGERKRVSIGQE 205
Cdd:TIGR02769 91 QLVFQDspSAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 206 ILINPSLLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHqpSSRLFYMF-DKLLLLSEGNPV 271
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITH--DLRLVQSFcQRVAVMDKGQIV 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
62-252 |
2.18e-16 |
|
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: 78.81 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLtALGGR---VGEGKGKLTG----NISYNNkplskaVKRTTGFVTQDD 134
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLV-NLIPRfydVDSGRILIDGhdvrDYTLAS------LRRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYpNLTVTETLVFTAllrlPNSFKKQ--EKIKQAKAVMTELGLDRCKDTIIGGpflRGV--SGGERKRVSIGQEILINP 210
Cdd:cd03251 86 FLF-NDTVAENIAYGR----PGATREEveEAARAANAHEFIMELPEGYDTVIGE---RGVklSGGQRQRIAIARALLKDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPS 252
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLS 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
74-269 |
2.28e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL-TGNISYNNKPLSKavkRTTGFVTQDDALYPNLTVTETLVFTalL 152
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfIGEKRMNDVPPAE---RGVGMVFQSYALYPHLSVAENMSFG--L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RLPNSFKK--QEKIKQAKAVMtELG--LDRckdtiigGPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSttAQ 228
Cdd:PRK11000 101 KLAGAKKEeiNQRVNQVAEVL-QLAhlLDR-------KP--KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA--AL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334186960 229 RiVSILWELA----RGGRTVVTTIHQPSSRLfYMFDKLLLLSEGN 269
Cdd:PRK11000 169 R-VQMRIEISrlhkRLGRTMIYVTHDQVEAM-TLADKIVVLDAGR 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-251 |
2.92e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGE--GKGKLTGNISYNNKPLSKA----VKRTTGFVTQDDALYPN 139
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN-RLIElyPEARVSGEVYLDGQDIFKMdvieLRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVF-TALLRLPNSFKK-QEKIKQA--KAVMTELGLDRckdtiIGGPFLRgVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK14247 97 LSIFENVALgLKLNRLVKSKKElQERVRWAleKAQLWDEVKDR-----LDAPAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQP 251
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-252 |
3.64e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.73 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALG--------GRVgEGKGKLTGNISYNNKPLSKAVKRTTGFVTQDDALY 137
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneeARV-EGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVFTalLRLPNSFKKQEKIKQ------AKAVMTELGLDRCKDtiiggpFLRGVSGGERKRVSIGQEILINPS 211
Cdd:PRK14267 98 PHLTIYDNVAIG--VKLNGLVKSKKELDErvewalKKAALWDEVKDRLND------YPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELaRGGRTVVTTIHQPS 252
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPA 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
63-268 |
4.05e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPL---SKAVKRTTGFVTQDDALYPN 139
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD----AGSISLCGEPVpsrARHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETL-VFTALLRLPNSfkkqekikQAKAVMTELgLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK13537 95 FTVRENLlVFGRYFGLSAA--------AARALVPPL-LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIH--QPSSRLfymFDKLLLLSEG 268
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEG 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-239 |
4.58e-16 |
|
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: 79.71 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgEGKGKLTGNISYNNKPLSKAVK--------RTTGFVTQD--DALYPNLTVT 143
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGLL-PPPGITSGEILFDGEDLLKLSEkelrkirgREIQMIFQDpmTSLNPVMTVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTalLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGPF-LrgvSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:COG0444 107 DQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHeL---SGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
170
....*....|....*..
gi 334186960 223 DSTTAQRIVSILWELAR 239
Cdd:COG0444 182 DVTIQAQILNLLKDLQR 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
64-224 |
5.30e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.74 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RT-ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLtgniSYNNKPLSK--AVKRTTGFVTQDDALYPNL 140
Cdd:PRK10851 14 RTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDVSRlhARDRKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFtALLRLPNsfKKQEKIKQAKAVMTELgLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:PRK10851 90 TVFDNIAF-GLTVLPR--RERPNAAAIKAKVTQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
....
gi 334186960 221 GLDS 224
Cdd:PRK10851 166 ALDA 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
63-268 |
6.62e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPL----SKAVKRTTGFVTQDDALYP 138
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT----AGTVLVAGDDVealsARAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLvftALLRLPNS--FKKQEKIKQAkAV---MTELGLDRCKDTIIggpflRGVSGGERKRV----SIGQEiliN 209
Cdd:PRK09536 91 EFDVRQVV---EMGRTPHRsrFDTWTETDRA-AVeraMERTGVAQFADRPV-----TSLSGGERQRVllarALAQA---T 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 210 PSLLfLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMfDKLLLLSEG 268
Cdd:PRK09536 159 PVLL-LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYC-DELVLLADG 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
74-245 |
6.87e-16 |
|
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: 75.93 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPL-----SKAVKRTTGFVTQD---DALYPNLTVTET 145
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGL----RPPASGEITLDGKPVtrrspRDAIRAGIAYVPEDrkrEGLVLDLSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALLrlpnsfkkqekikqakavmtelgldrckdtiiggpflrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDST 225
Cdd:cd03215 99 IALSSLL----------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180
....*....|....*....|
gi 334186960 226 TAQRIVSILWELARGGRTVV 245
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVL 158
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
58-268 |
7.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 58 NDKTEER-TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL----------TGNISYNNKPLSKAVK-- 124
Cdd:PRK13631 32 DEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELITNPYSKKIKnf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 125 ----RTTGFVTQddalYPNLTVTETLVFTALLRLPNSF--KKQEKIKQAKAVMTELGLDrcKDTIIGGPFlrGVSGGERK 198
Cdd:PRK13631 112 kelrRRVSMVFQ----FPEYQLFKDTIEKDIMFGPVALgvKKSEAKKLAKFYLNKMGLD--DSYLERSPF--GLSGGQKR 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 199 RVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLfYMFDKLLLLSEG 268
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
65-254 |
8.02e-16 |
|
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: 77.09 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGI---VKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNK----PLSKAV--------KRTT 127
Cdd:COG4778 22 KRLPVLDGVsfsVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGS------ILVRHDggwvDLAQASpreilalrRRTI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 128 GFVTQddalypNLTV-----TETLVFTALLRLpnSFKKQEKIKQAKAVMTELGLDrckdtiiggPFLRGV-----SGGER 197
Cdd:COG4778 96 GYVSQ------FLRViprvsALDVVAEPLLER--GVDREEARARARELLARLNLP---------ERLWDLppatfSGGEQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 198 KRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSR 254
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
74-224 |
9.09e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.04 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPlskAVKRTTGFVTQDDALYPNLTVTETLVFTAL 151
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAGleTPDSGRIVLNGRDLFTNLP---PRERRVGFVFQHYALFPHMTVAENIAFGLR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 152 LRLPNSFKKQEKIKQ-AKAV-MTELGlDRckdtiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDS 224
Cdd:COG1118 102 VRPPSKAEIRARVEElLELVqLEGLA-DR---------YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
62-232 |
1.68e-15 |
|
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: 76.53 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG----RVGEGKGKLTGNISYNNKPLSKAvkRTTGFVT-QDDAL 136
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyEVTSGTILFKGQDLLELEPDERA--RAGLFLAfQYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETL--VFTALLRLPNS-------FKKQEKIKQAKAVMTELGLDRCKDTiiggpflrGVSGGERKRVSIGQEIL 207
Cdd:TIGR01978 89 IPGVSNLEFLrsALNARRSARGEepldlldFEKLLKEKLALLDMDEEFLNRSVNE--------GFSGGEKKRNEILQMAL 160
|
170 180
....*....|....*....|....*
gi 334186960 208 INPSLLFLDEPTSGLDsTTAQRIVS 232
Cdd:TIGR01978 161 LEPKLAILDEIDSGLD-IDALKIVA 184
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
46-250 |
2.72e-15 |
|
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: 75.70 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGknDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTG--NISYNNKPLSK 121
Cdd:cd03258 2 IELKNVSKVFG--DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRPTSGSVLVDGtdLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 122 AvKRTTGFVTQDDALYPNLTVTETLVFTalLRLPNSfKKQEKIKQAKAVMTELGL-DRCKDtiiggpFLRGVSGGERKRV 200
Cdd:cd03258 80 A-RRRIGMIFQHFNLLSSRTVFENVALP--LEIAGV-PKAEIEERVLELLELVGLeDKADA------YPAQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334186960 201 SIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHQ 250
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
62-251 |
2.82e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALG--GRVGEGKGKLTG-NIS-YNNKPLSKAVKRTTGFVTQDDALY 137
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDKPTSGTYRVAGqDVAtLDADALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDrckDTIIGGPflRGVSGGERKRVSIGQEILINPSLLFLDE 217
Cdd:PRK10535 99 SHLTAAQNVEVPAVYA---GLERKQRLLRAQELLQRLGLE---DRVEYQP--SQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190
....*....|....*....|....*....|....
gi 334186960 218 PTSGLDSTTAQRIVSILWELARGGRTVVTTIHQP 251
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
63-235 |
3.63e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisynnkpLSKAVKrtTGFVTQDDALYPNLTV 142
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---------IPKGLR--IGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETL--VFTALLRLPNSFKK------------------QEKIK---------QAKAVMTELGLDrckdtiiGGPFLRGV- 192
Cdd:COG0488 79 LDTVldGDAELRALEAELEEleaklaepdedlerlaelQEEFEalggweaeaRAEEILSGLGFP-------EEDLDRPVs 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334186960 193 --SGGERKRVSIGQEILINPSLLFLDEPTSGLDsttaqrIVSILW 235
Cdd:COG0488 152 elSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEW 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
63-255 |
4.23e-15 |
|
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: 78.71 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLltalggrvgegkGKL--------TGNISYNNKPLS----KAVKRTTGFV 130
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTL------------ARLlfrfydvtSGRILIDGQDIRdvtqASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 TQDDAL----------YPNLTVTETLVFTA---------LLRLPNSFkkqekikqakavmtelgldrckDTIIGGpflRG 191
Cdd:COG5265 438 PQDTVLfndtiayniaYGRPDASEEEVEAAaraaqihdfIESLPDGY----------------------DTRVGE---RG 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 192 V--SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHqpssRL 255
Cdd:COG5265 493 LklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH----RL 553
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
74-288 |
4.97e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL-TGNI---SYNNKPLSKAVKRTTGFVTQddalYPNLTVTETLVFT 149
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIvvsSTSKQKEIKPVRKKVGVVFQ----FPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 ALLRLPNSF--KKQEKIKQAKAVMTELGLDrcKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTA 227
Cdd:PRK13643 105 DVAFGPQNFgiPKEKAEKIAAEKLEMVGLA--DEFWEKSPF--ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 228 QRIVSILWELARGGRTVVTTIHQPSSRLFYMfDKLLLLSEGNPVYFGLGSnamDYFASVGY 288
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYA-DYVYLLEKGHIISCGTPS---DVFQEVDF 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
46-249 |
6.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNDKTEeRTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLtgNISYNNKPLSKAVKR 125
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTE-LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI--EWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 126 TTGFVTQDDALYPNL---------------------------TVTETLVFTallrlPNSF--KKQEKIKQAKAVMTELGL 176
Cdd:PRK13651 80 KEKVLEKLVIQKTRFkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFG-----PVSMgvSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 177 DrcKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK13651 155 D--ESYLQRSPF--ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
63-250 |
6.57e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-------------GNISYNNKPLSKAVKRTTGF 129
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvrdkdGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 130 VTQDDALYPNLTVTETLVFTALLRLpnSFKKQEKIKQAKAVMTELGLDRCKDtiigGPFLRGVSGGERKRVSIGQEILIN 209
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQ----GKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334186960 210 PSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQ 250
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
63-234 |
7.45e-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: 77.54 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNIS------YNNKPLSKA-VKRTTGFVTQ 132
Cdd:TIGR03269 293 DRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmTKPGPDGRGrAKRYIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 133 DDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQAKAVmtelGLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSL 212
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMV----GFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180
....*....|....*....|...
gi 334186960 213 LFLDEPTSGLDSTTAQRIV-SIL 234
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVThSIL 471
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-251 |
7.94e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPLSK----AVKRTTGFVTQDDA 135
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRliEIYDSKIKVDGKVLYFGKDIFQidaiKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTalLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGPFLRgVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK14246 101 PFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELaRGGRTVVTTIHQP 251
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
64-268 |
8.00e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPL---SKAVKRTTGFVTQDDALYPNL 140
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD----AGKITVLGVPVparARLARARIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETL-VFTALLRLpnsfkkqeKIKQAKAVMTEL----GLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK13536 130 TVRENLlVFGRYFGM--------STREIEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 216 DEPTSGLDSTTAQRIvsilWE-----LARgGRTVVTTIH--QPSSRLfymFDKLLLLSEG 268
Cdd:PRK13536 197 DEPTTGLDPHARHLI----WErlrslLAR-GKTILLTTHfmEEAERL---CDRLCVLEAG 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
60-271 |
9.04e-15 |
|
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: 74.06 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnISYNNKPL--SKAVKRTTGFVTQDDALY 137
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL--VDGHDLALadPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 pNLTVTETLvftALLRLPNSFKKQE---KIKQAKAVMTELGLDRckDTIIGGpflRGV--SGGERKRVSIGQEILINPSL 212
Cdd:cd03252 89 -NRSIRDNI---ALADPGMSMERVIeaaKLAGAHDFISELPEGY--DTIVGE---QGAglSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELArGGRTVVTTIHQPSSrlFYMFDKLLLLSEGNPV 271
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIV 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
64-240 |
1.11e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.91 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTS-------LLTALGGRV---GEgkgkltgNISynNKPLSKAVKRTTGFVTQD 133
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGRIfldGE-------DIT--HLPMHKRARLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DALYPNLTVTETLvfTALLRLpNSFKKQEKIKQAKAVMTELGLDRCKDTiiggpflRG--VSGGERKRVSIGQEILINPS 211
Cdd:COG1137 87 ASIFRKLTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS-------KAysLSGGERRRVEIARALATNPK 156
|
170 180 190
....*....|....*....|....*....|
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELA-RG 240
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKeRG 186
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
63-271 |
1.36e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGEGKgklTGNISYNNKPLS----KAVKRTTGFVTQDDALYP 138
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQ---SGTVFLGDKPISmlssRQLARRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTEtLVftALLRLP-NSF------KKQEKIKQAkavMTELGLDRCKDTIiggpfLRGVSGGERKRVSIGQEILINPS 211
Cdd:PRK11231 90 GITVRE-LV--AYGRSPwLSLwgrlsaEDNARVNQA---MEQTRINHLADRR-----LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH--QPSSRlfYMfDKLLLLSEGNPV 271
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlNQASR--YC-DHLVVLANGHVM 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
63-253 |
1.41e-14 |
|
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: 77.06 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLtALGGRVGEGKGkltGNISYNNKPLS----KAVKRTTGFVTQDDALYp 138
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLV-NLIPRFYEPDS---GQILLDGHDLAdytlASLRRQVALVSQDVVLF- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFTALLRLPnsfkkQEKIKQA--KAVMTEL--GLDRCKDTIIGGPFLRgVSGGERKRVSIGQEILINPSLLF 214
Cdd:TIGR02203 419 NDTIANNIAYGRTEQAD-----RAEIERAlaAAYAQDFvdKLPLGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPILI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSS 253
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLST 530
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
64-268 |
2.24e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTG-NISYNNKPLSKAVKRTTGFVTQDDALYPNL 140
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGieRPSAGKIWFSGhDITRLKNREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTALLrlpnSFKKQEKIKQ-AKAVMTELGL-DRCKDTIIGgpflrgVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK10908 95 TVYDNVAIPLII----AGASGDDIRRrVSAALDKVGLlDKAKNFPIQ------LSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIHQPS--SRLFYmfdKLLLLSEG 268
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGliSRRSY---RMLTLSDG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-237 |
2.47e-14 |
|
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: 75.88 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLV--YTVKlkdsQGCFGKndKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgkl 108
Cdd:COG4172 270 PDAPPLLEARDLKvwFPIK----RGLFRR--TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 109 tGNISYNNKPLS-------KAVKRTTGFVTQD--DALYPNLTV----TETLvftALLRLPNSfkKQEKIKQAKAVMTELG 175
Cdd:COG4172 340 -GEIRFDGQDLDglsrralRPLRRRMQVVFQDpfGSLSPRMTVgqiiAEGL---RVHGPGLS--AAERRARVAEALEEVG 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 176 LDrckdtiiggPFLRG-----VSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWEL 237
Cdd:COG4172 414 LD---------PAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
62-274 |
2.50e-14 |
|
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: 72.53 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGEGKGkltGNISYNNKPLSK----AVKRTTGFVTQDdaly 137
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVELSS---GSILIDGVDISKiglhDLRSRISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 pnltvteTLVFTALLRL---PNSFKKQEKIKQA-------KAVMTELGLDrckDTII--GGPFLrgvSGGERKRVSIGQE 205
Cdd:cd03244 87 -------PVLFSGTIRSnldPFGEYSDEELWQAlervglkEFVESLPGGL---DTVVeeGGENL---SVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 206 ILINPSLLFLDEPTSGLDSTTAQRIVSILWElARGGRTVVTTIHqpssRLFYM--FDKLLLLSEGNPVYFG 274
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLDTIidSDRILVLDKGRVVEFD 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
63-253 |
2.89e-14 |
|
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: 72.57 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTAL-------GGRVgegkgkLTGNISYNNKPLsKAVKRTTGFVTQDDA 135
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEI------LLDGVDIRDLNL-RWLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNlTVTETLVFTAllrlPNSFKKQEK--IKQAKAVMTELGLDRCKDTIIGGpflRGV--SGGERKRVSIGQEILINPS 211
Cdd:cd03249 88 LFDG-TIAENIRYGK----PDATDEEVEeaAKKANIHDFIMSLPDGYDTLVGE---RGSqlSGGQKQRIAIARALLRNPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILwELARGGRTVVTTIHQPSS 253
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLST 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
76-239 |
3.18e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 76 PGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNK--------PLSKAVKRTT-----GFVTQD--DALYPNL 140
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD----AGEVHYRMRdgqlrdlyALSEAERRRLlrtewGFVHQHprDGLRMQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 T----VTETLvftallrLPNSFKKQEKIKQAKA-----VmtELGLDRCKDTiiggPflRGVSGGERKRVSIGQEILINPS 211
Cdd:PRK11701 107 SaggnIGERL-------MAVGARHYGDIRATAGdwlerV--EIDAARIDDL----P--TTFSGGMQQRLQIARNLVTHPR 171
|
170 180
....*....|....*....|....*...
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELAR 239
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVR 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
74-274 |
4.14e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLSKAV--KRTTGFVTQDDALYPNLTVTETLvftAL 151
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPD----SGRILWNGQDLTALPpaERPVSMLFQENNLFPHLTVAQNI---GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 -----LRLpnSFKKQEKIKQAKAvmtELGLDRCKDtiiggpFLRG-VSGGERKRVSIGQEILINPSLLFLDEPTSGLDST 225
Cdd:COG3840 95 glrpgLKL--TAEQRAQVEQALE---RVGLAGLLD------RLPGqLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 226 TAQRIVSILWELARG-GRTVVTTIHQPS--SRLfymFDKLLLLSEGNPVYFG 274
Cdd:COG3840 164 LRQEMLDLVDELCRErGLTVLMVTHDPEdaARI---ADRVLLVADGRIAADG 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
62-251 |
4.64e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgegkgkLT----GNISYNNKPLSKavkrttgfvtQDDALY 137
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG--------LArpdaGEVLWQGEPIRR----------QRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 -------------PNLTVTETLVFTALLRLPNSfkkQEKIKQAKAVMtelGLDRCKDTIIggpflRGVSGGERKRVSIGQ 204
Cdd:PRK13538 74 qdllylghqpgikTELTALENLRFYQRLHGPGD---DEALWEALAQV---GLAGFEDVPV-----RQLSAGQQRRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334186960 205 EILINPSLLFLDEPTSGLDSTTAQRIVSILWE-LARGGRTVVTTiHQP 251
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTT-HQD 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
65-253 |
4.73e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGkltgNISYNNKPLSKAVKRT-TGFVTQD---DALYPNL 140
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG----KISILGQPTRQALQKNlVAYVPQSeevDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TvtETLVFTA------LLRLPNSFKKQekikQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLF 214
Cdd:PRK15056 97 V--EDVVMMGryghmgWLRRAKKRDRQ----IVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSS 253
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
64-285 |
5.05e-14 |
|
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: 71.95 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALgGRVGEGKgklTGNISYNNKPLSK----AVKRTTGFVTQDDALYPN 139
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIEPT---SGEIFIDGEDIREqdpvELRRKIGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETlvfTALLRLPNSFKKQEKIKQAKAVMTELGLDRCKdtiIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03295 90 MTVEEN---IALVPKLLKWPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 220 SGLDSTTAQRIVSILWELARG-GRTVVTTIH--QPSSRLfymFDKLLLLSEGNPVYFG-----LGSNAMDYFAS 285
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQElGKTIVFVTHdiDEAFRL---ADRIAIMKNGEIVQVGtpdeiLRSPANDFVAE 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
64-243 |
5.89e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLtALGGRVGE---GKGKLTG-NISYNNKplsKAVKRTTGFVTQDDALY-- 137
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDpqsGRILIDGtDIRTVTR---ASLRRNIAVVFQDAGLFnr 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 ---PNLTV-----TETLVFTALlrlpnsfkkqeKIKQAKAVMteLGLDRCKDTIIGGpflRG--VSGGERKRVSIGQEIL 207
Cdd:PRK13657 424 sieDNIRVgrpdaTDEEMRAAA-----------ERAQAHDFI--ERKPDGYDTVVGE---RGrqLSGGERQRLAIARALL 487
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 208 INPSLLFLDEPTSGLDSTTAQRIVSILWELaRGGRT 243
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRT 522
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
74-249 |
1.16e-13 |
|
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: 71.52 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLSK-------AVKRTT-GFVTQDDALYPNLTVTE 144
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLI-----EPTsGKVLIDGQDIAAmsrkelrELRRKKiSMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFTALLRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDS 224
Cdd:cd03294 122 NVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180
....*....|....*....|....*.
gi 334186960 225 TTAQRIVSILWEL-ARGGRTVVTTIH 249
Cdd:cd03294 194 LIRREMQDELLRLqAELQKTIVFITH 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-281 |
1.17e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 33 NPVTLKFENLVYTVKLKDSQgcFGKNDKTEeRTILKGLTGIVKPGEILAMLGPSGSGKTSLLtALGGRVGEGKGkltGNI 112
Cdd:TIGR00958 466 LTGTLAPLNLEGLIEFQDVS--FSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQNLYQPTG---GQV 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 113 SYNNKPLS----KAVKRTTGFVTQDDALYpNLTVTETLVFtALLRLPNSfKKQEKIKQAKAVMTELGLDRCKDTIIG--G 186
Cdd:TIGR00958 539 LLDGVPLVqydhHYLHRQVALVGQEPVLF-SGSVRENIAY-GLTDTPDE-EIMAAAKAANAHDFIMEFPNGYDTEVGekG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 187 PFLrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDSttaqRIVSILWEL-ARGGRTVVTTIHQPSsrLFYMFDKLLLL 265
Cdd:TIGR00958 616 SQL---SGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESrSRASRTVLLIAHRLS--TVERADQILVL 686
|
250
....*....|....*.
gi 334186960 266 SEGNPVYFGLGSNAMD 281
Cdd:TIGR00958 687 KKGSVVEMGTHKQLME 702
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
63-274 |
1.28e-13 |
|
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: 73.97 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTAL-------GGRVgegkgkLTGNIsyNNKPLSKAVKRTT-GFVTQDD 134
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLlrfydpqSGRI------LLDGV--DLRQLDPAELRARmALVPQDP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYPNlTVTETLVFTAllrlPNSFKKQEKIKQAKAVMTE--LGLDRCKDTIIGGpflRGV--SGGERKRVSIGQEILINP 210
Cdd:TIGR02204 424 VLFAA-SVMENIRYGR----PDATDEEVEAAARAAHAHEfiSALPEGYDTYLGE---RGVtlSGGQRQRIAIARAILKDA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSSRLfyMFDKLLLLSEGNPVYFG 274
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETLMK-GRTTLIIAHRLATVL--KADRIVVMDQGRIVAQG 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
68-249 |
1.32e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 68 KGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT---GNISYN--NKPLsKAVKRTTGFVTQ--DDALY 137
Cdd:PRK13641 21 KGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPEtgNKNL-KKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNlTVTETLVFTALlrlpN-SFKKQEKIKQAKAVMTELGLDrcKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:PRK13641 100 EN-TVLKDVEFGPK----NfGFSEDEAKEKALKWLKKVGLS--EDLISKSPF--ELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
63-250 |
1.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GN--IS--YNNKPLsKAVKRTTGFVTQddalY 137
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTiGErvITagKKNKKL-KPLRKKVGIVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVFTALLRLPNSF--KKQEKIKQAKAVMTELGLDrcKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK13634 94 PEHQLFEETVEKDICFGPMNFgvSEEDAKQKAREMIELVGLP--EELLARSPF--ELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQ 250
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS 205
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
70-268 |
1.89e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 70 LTGIVKPGEILAMLGPSGSGKTSLLTALGGrVGEGKGKltgnISYNNKPLSK------AVKRttGFVTQDDALYPNLTVT 143
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGS----IQFAGQPLEAwsaaelARHR--AYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVftalLRLPNSFKKQEKIKQAKAVMTELGLD----RCKDTIiggpflrgvSGGERKRVSIGQEIL-----INPS--L 212
Cdd:PRK03695 88 QYLT----LHQPDKTRTEAVASALNEVAEALGLDdklgRSVNQL---------SGGEWQRVRLAAVVLqvwpdINPAgqL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMfDKLLLLSEG 268
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
67-249 |
2.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFVTQD--DALYPNlTVTE 144
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFSS-TVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFTAL-LRLpnsfKKQEKIKQAKAVMTELGLDRCKDTiigGPFlrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:PRK13647 100 DVAFGPVnMGL----DKDEVERRVEEALKAVRMWDFRDK---PPY--HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180
....*....|....*....|....*.
gi 334186960 224 STTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
74-245 |
2.19e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLS-----KAVKRTTGFVTQDDALYPNLTVTETL 146
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGvyQPDSGE------ILLDGEPVRfrsprDAQAAGIAIIHQELNLVPNLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 VFTALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpfLrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD--L---SVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170
....*....|....*....
gi 334186960 227 AQRIVSILWELARGGRTVV 245
Cdd:COG1129 176 VERLFRIIRRLKAQGVAII 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
62-223 |
2.25e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSK--AVKRTTGFVTQDDALYPN 139
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF----ETPDSGRIMLDGQDITHvpAENRHVNTVFQSYALFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTalLRLpnsfKKQEKIKQAKAVMTELGLDRCKDTIIGGPflRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:PRK09452 101 MTVFENVAFG--LRM----QKTPAAEITPRVMEALRMVQLEEFAQRKP--HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
....
gi 334186960 220 SGLD 223
Cdd:PRK09452 173 SALD 176
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
64-247 |
2.47e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTAL-------GGRVGEGKGKLTGNISYNNKPLSKaVKRTTGFVTQDDAL 136
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSGDVLLGGRSIFNYRDVLE-FRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPnLTVTETLVftALLRLPNSFKKQEKIKQAKAVMTELGL-DRCKDTIIGGPFLrgVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK14271 113 FP-MSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFR--LSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|..
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELARGGRTVVTT 247
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
74-268 |
3.02e-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: 72.55 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALggrVGEGKGKLTGNISYNNKPLS-----KAVKRTTGFVTQD---DALYPNLTVTET 145
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQAL---FGAYPGKFEGNVFINGKPVDirnpaQAIRAGIAMVPEDrkrHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALlrlpNSFKKQEKIKQAKAVMTEL-GLDRCKdTIIGGPFL--RGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:TIGR02633 360 ITLSVL----KSFCFKMRIDAAAELQIIGsAIQRLK-VKTASPFLpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTihqpSSRL---FYMFDKLLLLSEG 268
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVV----SSELaevLGLSDRVLVIGEG 479
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
59-268 |
3.91e-13 |
|
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: 68.65 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 59 DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrVGEGKgKLTGNISYNNkplskavkrTTGFVTQddalYP 138
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL---LGELE-KLSGSVSVPG---------SIAYVSQ----EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 ---NLTVTETLVFTALLRlpnsfkkQEKIKQAkavmtelgLDRC---KD---------TIIGGpflRGV--SGGERKRVS 201
Cdd:cd03250 76 wiqNGTIRENILFGKPFD-------EERYEKV--------IKACalePDleilpdgdlTEIGE---KGInlSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDSTTAQRIV-SILWELARGGRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNG 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
79-223 |
3.94e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 79 ILAMLGPSGSGKTSLLTALGGrvgegkgkLT----GNISYNNKPLSKAV--------KRTTGFVTQDDALYPNLTVTETL 146
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISG--------LTrpqkGRIVLNGRVLFDAEkgiclppeKRRIGYVFQDARLFPHYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 VFtallrlpnSFKKQEKiKQAKAVMTELG----LDRckdtiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:PRK11144 98 RY--------GMAKSMV-AQFDKIVALLGieplLDR---------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
.
gi 334186960 223 D 223
Cdd:PRK11144 160 D 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
74-245 |
4.62e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLS-----KAVKRTTGFVTQD---DALYPNLTVTET 145
Cdd:COG1129 275 VRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRirsprDAIRAGIAYVPEDrkgEGLVLDLSIREN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALLRLPNSF---KKQEKiKQAKAVMTELGLdRCK--DTIIGgpFLrgvSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:COG1129 351 ITLASLDRLSRGGlldRRRER-ALAEEYIKRLRI-KTPspEQPVG--NL---SGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180
....*....|....*....|....*
gi 334186960 221 GLDSTTAQRIVSILWELARGGRTVV 245
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
74-249 |
4.72e-13 |
|
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: 72.74 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNkplSKAVKRTTGFVTQDDALYPNLTVTETLVFTAL 151
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGdtTVTSGDATVAGKSILTN---ISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 LRlpnSFKKQEKIKQAKAVMTELGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIV 231
Cdd:TIGR01257 2039 LR---GVPAEEIEKVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170
....*....|....*...
gi 334186960 232 SILWELARGGRTVVTTIH 249
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSH 2128
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
74-239 |
7.23e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN-ISYNNKPLSkavKRTTGFVTQDDALYPNLTVTETLvftAL- 151
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDHTTTPPS---RRPVSMLFQENNLFSHLTVAQNI---GLg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 ----LRLpNSFKKQEKIKQAKAVMTELGLDRckdtiiggpfLRG-VSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:PRK10771 96 lnpgLKL-NAAQREKLHAIARQMGIEDLLAR----------LPGqLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170
....*....|...
gi 334186960 227 AQRIVSILWELAR 239
Cdd:PRK10771 165 RQEMLTLVSQVCQ 177
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
77-249 |
9.61e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSKA--VKRTTGFVTQDDALYPNLTVTETLVFTAllrl 154
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQ----IMLDGVDLSHVppYQRPINMMFQSYALFPHMTVEQNIAFGL---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 155 pnsfkKQEKIKQAKA---VMTELGLDRCKDTIIGGPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQR-- 229
Cdd:PRK11607 117 -----KQDKLPKAEIasrVNEMLGLVHMQEFAKRKP--HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmq 189
|
170 180
....*....|....*....|..
gi 334186960 230 --IVSIlweLARGGRTVVTTIH 249
Cdd:PRK11607 190 leVVDI---LERVGVTCVMVTH 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
64-270 |
1.17e-12 |
|
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: 66.41 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnisynnkpLSKAVKRTTGFVTQDdALYPNLT 141
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwPWGSGR-------------IGMPEGEDLLFLPQR-PYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFtallrlpnsfkkqekikqakavmtelgldrckdtiiggPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:cd03223 80 LREQLIY--------------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334186960 222 LDSTTAQRIVSILWELargGRTVVTTIHQPSSRLFymFDKLLLLS-EGNP 270
Cdd:cd03223 122 LDEESEDRLYQLLKEL---GITVISVGHRPSLWKF--HDRVLDLDgEGGW 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
74-268 |
1.26e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALggrVGEGKGKLTGNISYNNKPLS-----KAVKRTTGFVTQD---DALYPNLTVTET 145
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCL---FGAYPGRWEGEIFIDGKPVKirnpqQAIAQGIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTALlrlpNSFKKQEKIKQAKAVMT-ELGLDRCKdTIIGGPFLR--GVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:PRK13549 362 ITLAAL----DRFTGGSRIDDAAELKTiLESIQRLK-VKTASPELAiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTihqpSSRL---FYMFDKLLLLSEG 268
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVI----SSELpevLGLSDRVLVMHEG 481
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
62-223 |
1.33e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgkltgnisynnKPLSKAVKR----TTGFVTQD-DAL 136
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL---------------EPDSGTVKLgetvKIGYFDQHqEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 YPNLTVTETLVftallrlpnSFKKQEKIKQAKAVMTELGL--DRCKDTIiggpflrGV-SGGERKRVSIGQEILINPSLL 213
Cdd:COG0488 391 DPDKTVLDELR---------DGAPGGTEQEVRGYLGRFLFsgDDAFKPV-------GVlSGGEKARLALAKLLLSPPNVL 454
|
170
....*....|
gi 334186960 214 FLDEPTSGLD 223
Cdd:COG0488 455 LLDEPTNHLD 464
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
67-274 |
1.78e-12 |
|
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: 67.49 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgegKGKLTGNISYNNKPLSK-AVKRTTGFvtQDDALYPNLTVTET 145
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL----AQPTSGGVILEGKQITEpGPDRMVVF--QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 --LVFTALLRLPNSFKKQEKIKQAKAVmteLGLDRCKDTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:TIGR01184 75 iaLAVDRVLPDLSKSERRAIVEEHIAL---VGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 224 STTAQRIVSILWELARGGR-TVVTTIHQPSSRLFyMFDKLLLLSEGNPVYFG 274
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRvTVLMVTHDVDEALL-LSDRVVMLTNGPAANIG 197
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
37-232 |
2.21e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYTVKlkdsqgcfgkndkteERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgEGKGKLTGNISYNN 116
Cdd:CHL00131 8 LEIKNLHASVN---------------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILEGDILFKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 117 KPLSK--AVKRTT-----GF--------VTQDDAL---------YPNLTVTETLVFTALLRlpnsfkkqEKIKQAKavMT 172
Cdd:CHL00131 71 ESILDlePEERAHlgiflAFqypieipgVSNADFLrlaynskrkFQGLPELDPLEFLEIIN--------EKLKLVG--MD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 173 ELGLDRCKDtiiggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDsTTAQRIVS 232
Cdd:CHL00131 141 PSFLSRNVN--------EGFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKIIA 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
63-237 |
2.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLS-KAVKRTTGFVTQddalYPNL 140
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIiDGVDITDKKVKlSDIRKKVGLVFQ----YPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 141 TVTETLVFTALLRLPNSF--KKQEKIKQAKAVMTELGLDR--CKDTiigGPFlrGVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:PRK13637 95 QLFEETIEKDIAFGPINLglSEEEIENRVKRAMNIVGLDYedYKDK---SPF--ELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180
....*....|....*....|.
gi 334186960 217 EPTSGLDSTTAQRIVSILWEL 237
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKEL 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
61-270 |
2.49e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 61 TEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSKA----VKRTTGFVTQ--DD 134
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGS----VLIRGEPITKEnireVRKFVGLVFQnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYpNLTVTETLVFTALlrlpNSFKKQEKIK-QAKAVMTELGLDRCKDTIiggPflRGVSGGERKRVSIGQEILINPSLL 213
Cdd:PRK13652 90 QIF-SPTVEQDIAFGPI----NLGLDEETVAhRVSSALHMLGLEELRDRV---P--HHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELA-RGGRTVVTTIHQPS-----SRLFYMFDKLLLLSEGNP 270
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDlvpemADYIYVMDKGRIVAYGTV 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
60-237 |
2.65e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLltalgGRVGEGKGKLT-GNISYNNKPLS-------KAVKRTTGFVT 131
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL-----ARLLVGLESPSqGNVSWRGEPLAklnraqrKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 QD--DALYPNLTVTETLvfTALLRLPNSFKKQEKIKQAKAVMTELGL-----DRCKDTiiggpflrgVSGGERKRVSIGQ 204
Cdd:PRK10419 96 QDsiSAVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLddsvlDKRPPQ---------LSGGQLQRVCLAR 164
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 205 EILINPSLLFLDEPTSGLDSTTAQRIVSILWEL 237
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKL 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
63-253 |
3.18e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLtALGGR---VGEGKgkltgnISYNNKPLSK----------AVKRTTGF 129
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRhfdVSEGD------IRFHDIPLTKlqldswrsrlAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 130 VTQDdalypnlTVTETLvftALLRlPNSfkKQEKIKQAK--AVMTE--LGLDRCKDTIIGGpflRGV--SGGERKRVSIG 203
Cdd:PRK10789 400 LFSD-------TVANNI---ALGR-PDA--TQQEIEHVArlASVHDdiLRLPQGYDTEVGE---RGVmlSGGQKQRISIA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 204 QEILINPSLLFLDEPTSGLDSTTAQRIVSIL--WelaRGGRTVVTTIHQPSS 253
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLrqW---GEGRTVIISAHRLSA 512
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
63-269 |
4.23e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNisynNKPLSKAvKRTTGFVTQDDALYPNLTV 142
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEA-REDTRLMFQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVftalLRLPNSFKKQekikqAKAVMTELGL-DRCKDtiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:PRK11247 99 IDNVG----LGLKGQWRDA-----ALQALAAVGLaDRANE------WPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334186960 222 LDSTT---AQRIVSILWElaRGGRTVVTTIHQPSSRLfYMFDKLLLLSEGN 269
Cdd:PRK11247 164 LDALTrieMQDLIESLWQ--QHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
74-271 |
4.98e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNiSYNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTAL 151
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLCGdpRATSGRIVFDGK-DITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 LRLPNSFkkQEKIKQAKAVMTELGLDRCKDTiiggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIV 231
Cdd:PRK11614 107 FAERDQF--QERIKWVYELFPRLHERRIQRA-------GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334186960 232 SILWELARGGRTVVtTIHQPSSRLFYMFDKLLLLSEGNPV 271
Cdd:PRK11614 178 DTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
74-250 |
5.12e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLTGNISYNNKPLS----KAVKRTTGFVTQDDALyPNLTVTETLvft 149
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFL-----PYQGSLKINGIELReldpESWRKHLSWVGQNPQL-PHGTLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 aLLRLPNSfkKQEKIKQA--KAVMTE------LGLDrckdTIIGGPFLrGVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:PRK11174 444 -LLGNPDA--SDEQLQQAleNAWVSEflpllpQGLD----TPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180
....*....|....*....|....*....
gi 334186960 222 LDSTTAQRIVSILWELARGGRTVVTTiHQ 250
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMVT-HQ 543
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
62-232 |
1.00e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgEGKGKLTGNISYNNKPLSkavkrttgfvtqddALYPNLT 141
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR--EDYEVTGGTVEFKGKDLL--------------ELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTET--LVFTALLRLP---NSFKKQEKIKQAKAVMTELGLDRC--------KDTIIGGP---FLR----GVSGGERKRVS 201
Cdd:PRK09580 76 AGEGifMAFQYPVEIPgvsNQFFLQTALNAVRSYRGQEPLDRFdfqdlmeeKIALLKMPedlLTRsvnvGFSGGEKKRND 155
|
170 180 190
....*....|....*....|....*....|.
gi 334186960 202 IGQEILINPSLLFLDEPTSGLDsTTAQRIVS 232
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLD-IDALKIVA 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
74-247 |
1.13e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSKAVK-RTTGFVTQDDALYPNLTVTETLVFTALL 152
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ----IQIDGKTATRGDRsRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 ------RLPNSfkkqekikqakaVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDS-- 224
Cdd:PRK13543 110 hgrrakQMPGS------------ALAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLeg 172
|
170 180
....*....|....*....|....
gi 334186960 225 -TTAQRIVSIlwELARGGRTVVTT 247
Cdd:PRK13543 173 iTLVNRMISA--HLRGGGAALVTT 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
62-230 |
1.15e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLSK--AVKRTT--GFVTQDDAL- 136
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS----ILIDGKDVTKlpEYKRAKyiGRVFQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 137 -YPNLTVTETLVFTAL------LRLPNSFKKQEKIKQAKAVMtELGLDRCKDTIIGgpFLrgvSGGERKRVSIGQEILIN 209
Cdd:COG1101 93 tAPSMTIEENLALAYRrgkrrgLRRGLTKKRRELFRELLATL-GLGLENRLDTKVG--LL---SGGQRQALSLLMATLTK 166
|
170 180
....*....|....*....|.
gi 334186960 210 PSLLFLDEPTSGLDSTTAQRI 230
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALV 187
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
63-249 |
1.16e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKAVK---RTTGFVTQddalYP 138
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvDDTLITSTSKNKDIKqirKKVGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFTALLRLPNSF--KKQEKIKQAKAVMTELGLDrcKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLD 216
Cdd:PRK13649 95 ESQLFEETVLKDVAFGPQNFgvSQEEAEALAREKLALVGIS--ESLFEKNPF--ELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 217 EPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
64-249 |
1.48e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgrvgEGKGKLTGNISYNNKPL----SKAVKRTTGFVTQDDALYPN 139
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG----RHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTEtLVftALLRLP-------NSFKKQEKIKQAkavMTELGL----DRCKDTIiggpflrgvSGGERKRVSIGQEILI 208
Cdd:PRK10575 100 MTVRE-LV--AIGRYPwhgalgrFGAADREKVEEA---ISLVGLkplaHRLVDSL---------SGGERQRAWIAMLVAQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 209 NPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIH 249
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
78-268 |
1.59e-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: 67.73 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 78 EILAMLGPSGSGKTSLLTALGGRVGEGKGK-LTG--NISYNnkplSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRl 154
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTvLVGgkDIETN----LDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 155 pnsFKKQEKIK-QAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSI 233
Cdd:TIGR01257 1032 ---GRSWEEAQlEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 234 LWELaRGGRTVVTTIHQPSSRLFyMFDKLLLLSEG 268
Cdd:TIGR01257 1104 LLKY-RSGRTIIMSTHHMDEADL-LGDRIAIISQG 1136
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
64-268 |
2.28e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.75 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnisynnkplskaVKRTTG----FVTQ----- 132
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPYGSGR-----------------IARPAGarvlFLPQrpylp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 133 ----DDAL-YPNLtvtetlvftallrlPNSFKKQEkikqAKAVMTELGLDRCKDTI-IGGPFLRGVSGGERKRVSIGQEI 206
Cdd:COG4178 439 lgtlREALlYPAT--------------AEAFSDAE----LREALEAVGLGHLAERLdEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 207 LINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGrTVVTTIHQPSSRLFymFDKLLLLSEG 268
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAF--HDRVLELTGD 559
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
77-271 |
2.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSK---AVKRTTGFVTQddalYPNLTVTETLVFTALL 152
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvDDITITHKTKDKyirPVRKRIGMVFQ----FPESQLFEDTVEREII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RLPNSFKKQ-EKIK-QAKAVMTELGLDRckDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRI 230
Cdd:PRK13646 109 FGPKNFKMNlDEVKnYAHRLLMDLGFSR--DVMSQSPF--QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 231 VSILWEL-ARGGRTVVTTIHQPSSRLFYMfDKLLLLSEGNPV 271
Cdd:PRK13646 185 MRLLKSLqTDENKTIILVSHDMNEVARYA-DEVIVMKEGSIV 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
60-268 |
2.97e-11 |
|
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: 66.36 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvgEGKGKLTGNISYN------------------------ 115
Cdd:TIGR03269 9 KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIIYHvalcekcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 116 -------------NKPLSKAVKRTTGFVTQDD-ALYPNLTVTETlVFTALLRLpnSFKKQEKIKQAKAVMTELGLDRcKD 181
Cdd:TIGR03269 87 gtlepeevdfwnlSDKLRRRIRKRIAIMLQRTfALYGDDTVLDN-VLEALEEI--GYEGKEAVGRAVDLIEMVQLSH-RI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 182 TIIGgpflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIHQPSSrLFYMFD 260
Cdd:TIGR03269 163 THIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSD 237
|
....*...
gi 334186960 261 KLLLLSEG 268
Cdd:TIGR03269 238 KAIWLENG 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
67-250 |
3.46e-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: 66.00 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVGEgkGKLTGNISYNNKPLSKAVKRTT-----GFVTQDDALYP 138
Cdd:TIGR02633 14 VKALDGIdleVRPGECVGLCGENGAGKSTLMKILSGVYPH--GTWDGEIYWSGSPLKASNIRDTeragiVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFTALLRLPNS-FKKQEKIKQAKAVMTELGLDRCKDTIIGGPFlrgvSGGERKRVSIGQEILINPSLLFLDE 217
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 218 PTSGLDSTTAQRIVSILWELARGGRTVVTTIHQ 250
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
64-274 |
4.21e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKG----KLTGNISYNNKPLS-----KAVKRTTGFVTQDD 134
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgaRVTGDVTLNGEPLAaidapRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ALYPnLTVTETLVftaLLRLPNSFKKQEKIKQAKAVMTElGLDRCKDTIIGGPFLRGVSGGERKRVSIGQ---------E 205
Cdd:PRK13547 94 PAFA-FSAREIVL---LGRYPHARRAGALTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQFARvlaqlwpphD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 206 ILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRT-VVTTIHQPSSRLFYMfDKLLLLSEGNPVYFG 274
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHA-DRIAMLADGAIVAHG 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
46-224 |
4.23e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.74 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNdkteerTILKGLTGIVKPGEILAMLGPSGSGKTSLLtalggRVGEGKGKLT-GNISYNNKPLSKAV- 123
Cdd:PRK11432 7 VVLKNITKRFGSN------TVIDNLNLTIKQGTMVTLLGPSGCGKTTVL-----RLVAGLEKPTeGQIFIDGEDVTHRSi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 124 -KRTTGFVTQDDALYPNLTVTETLVF-TALLRLPNSFKKQeKIKQAKAVMTELGL-DRCKDTIiggpflrgvSGGERKRV 200
Cdd:PRK11432 76 qQRDICMVFQSYALFPHMSLGENVGYgLKMLGVPKEERKQ-RVKEALELVDLAGFeDRYVDQI---------SGGQQQRV 145
|
170 180
....*....|....*....|....
gi 334186960 201 SIGQEILINPSLLFLDEPTSGLDS 224
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDA 169
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
77-290 |
4.57e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSL------LTALGGRVGeGKGKLTGN--ISYNNKPLSKAVKRTTGFVTQD--DALYPNLTVTETL 146
Cdd:PRK09473 42 GETLGIVGESGSGKSQTafalmgLLAANGRIG-GSATFNGReiLNLPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 vfTALLRLPNSFKKQ----EKIKQAKAV-MTELgldRCKDTIIGGPFlrgvSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:PRK09473 121 --MEVLMLHKGMSKAeafeESVRMLDAVkMPEA---RKRMKMYPHEF----SGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 222 LDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFGlgsNAMDYFasvgYSP 290
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG---NARDVF----YQP 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
66-267 |
5.69e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKAVKRTTGFVTQDDALYPNLTVTE 144
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiGGNPCARLTPAKAHQLGIYLVPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFtallRLPNSFKKQEKIKQAKAVM-TELGLDrckdtiiggpflrgVSGG-----ERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK15439 106 NILF----GLPKRQASMQKMKQLLAALgCQLDLD--------------SSAGslevaDRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIH------QPSSRLFYMFDKLLLLSE 267
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHklpeirQLADRISVMRDGTIALSG 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
63-274 |
5.83e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFVTQDDALYPNLTV 142
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TEtlvFTALLRLPNS-----FKKQEKIKQAKAvMTELGLdrckdTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDE 217
Cdd:PRK10253 99 QE---LVARGRYPHQplftrWRKEDEEAVTKA-MQATGI-----THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 218 PTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSSRLFYMfDKLLLLSEGNPVYFG 274
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYA-SHLIALREGKIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
57-268 |
6.24e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 57 KNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGrvgeGKGKLTGNISYNNKPLS-----KAVKRTTGFVT 131
Cdd:PRK09700 269 RNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG----VDKRAGGEIRLNGKDISprsplDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 132 Q---DDALYPNLTVTETLVFTALLRLPN--------SFKKQEKIKQAKAVMTELGLDRCKDTIiggpflRGVSGGERKRV 200
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTAENQRELLALKCHSVNQNI------TELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 201 SIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTihqpSSRL---FYMFDKLLLLSEG 268
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELpeiITVCDRIAVFCEG 485
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
66-223 |
6.97e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPlskaVKRTTGFVTQDDALYPNLTVT 143
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRITSGEIWIGGRVVNELEP----ADRDIAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTALLRlpnSFKKQE---KIKQAkAVMTELG--LDRcKdtiiggPflRGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK11650 95 ENMAYGLKIR---GMPKAEieeRVAEA-ARILELEplLDR-K------P--RELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
....*
gi 334186960 219 TSGLD 223
Cdd:PRK11650 162 LSNLD 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
67-270 |
7.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGK-LTGNISYNNKPLSKAVKRTTGFVTQD-DALYPNLTVTE 144
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFTAL-LRLPNSfkkqEKIKQAKAVMTELGLDRCKDTiigGPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:PRK13644 98 DLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHR---SP--KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334186960 224 STTAQRIVSILWELARGGRTVVTTIH-----QPSSRLFYMfDKLLLLSEGNP 270
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHnleelHDADRIIVM-DRGKIVLEGEP 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
46-282 |
8.41e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNDKTEERTILKGL--------TGI----------VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGK 107
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAFKYIEQGLskeqilekTGLslgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 108 LTGN----ISYNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQAkavMTELGLDRCKDti 183
Cdd:PRK10070 85 VLIDgvdiAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAH-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 184 iGGPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHQPSSRLfYMFDKL 262
Cdd:PRK10070 160 -SYP--DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAM-RIGDRI 235
|
250 260
....*....|....*....|....*
gi 334186960 263 LLLSEGNPVYFG-----LGSNAMDY 282
Cdd:PRK10070 236 AIMQNGEVVQVGtpdeiLNNPANDY 260
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
63-268 |
8.45e-11 |
|
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: 62.10 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALggrvgEGKGKLT-GNISYNNKPLS----KAVKRTTGFVTQDDALY 137
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-----ENFYQPQgGQVLLDGKPISqyehKYLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNlTVTETLVFTallrLPNsfKKQEKIKQAK------AVMTELGLDRCKDTIIGGPFLrgvSGGERKRVSIGQEILINPS 211
Cdd:cd03248 101 AR-SLQDNIAYG----LQS--CSFECVKEAAqkahahSFISELASGYDTEVGEKGSQL---SGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 212 LLFLDEPTSGLDSTTAQRIVSILWELARgGRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
68-249 |
8.50e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 68 KGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLskAVKRTT-------GFVTQDDALY 137
Cdd:PRK11288 18 KALDDIsfdCRAGQVHALMGENGAGKSTLLKILSGNYQPD----AGSILIDGQEM--RFASTTaalaagvAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVftaLLRLPNSF---KKQEKIKQAKAVMTELGLDRCKDTiiggPfLRGVSGGERKRVSIGQEILINPSLLF 214
Cdd:PRK11288 92 PEMTVAENLY---LGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDT----P-LKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190
....*....|....*....|....*....|....*
gi 334186960 215 LDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
63-272 |
1.23e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGI---VKPGEILAMLGPSGSGKTSLLTALGG---------RVGegkgkltGNISYNNKplsKAVKRTTGFV 130
Cdd:COG4586 31 EYREVEAVDDIsftIEPGEIVGFIGPNGAGKSTTIKMLTGilvptsgevRVL-------GYVPFKRR---KEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 ----TQddaLYPNLTVTETL-VFTALLRLPnsfkkQEKIKQAKAVMTE-LGLdrckdtiigGPFL----RGVSGGERKRV 200
Cdd:COG4586 101 fgqrSQ---LWWDLPAIDSFrLLKAIYRIP-----DAEYKKRLDELVElLDL---------GELLdtpvRQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 201 SIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHqpssrlfYMFD------KLLLLSEGNPVY 272
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIY 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
74-245 |
1.30e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRV----GEgkgkltgnISYNNKPLS-----KAVKRTTGFVTQDDALYPNLTVTE 144
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGLYqpdsGE--------ILIDGKPVRirsprDAIALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLVFTALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSI------GQEILInpsllfLDEP 218
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVE-----DLSVGEQQRVEIlkalyrGARILI------LDEP 168
|
170 180 190
....*....|....*....|....*....|
gi 334186960 219 TSGLdstTAQRIVS---ILWELARGGRTVV 245
Cdd:COG3845 169 TAVL---TPQEADElfeILRRLAAEGKSII 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
55-239 |
1.31e-10 |
|
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: 64.32 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 55 FGKNDKTeeRTILKGLTGIVKPGEILAMLGPSGSGKTslLTALG--GRVGEGKGKLTGNISYNNKPLSKAVKRTT----- 127
Cdd:COG4172 16 FGQGGGT--VEAVKGVSFDIAAGETLALVGESGSGKS--VTALSilRLLPDPAAHPSGSILFDGQDLLGLSERELrrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 128 ---GFVTQD--DALYPNLTV----TETLvftallRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGPF-LrgvSGGER 197
Cdd:COG4172 92 nriAMIFQEpmTSLNPLHTIgkqiAEVL------RLHRGLSGAAARARALELLERVGIPDPERRLDAYPHqL---SGGQR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334186960 198 KRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR 239
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQR 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-274 |
1.33e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 32 NNPVTLKFENLVYTVKlkdsqgcfgkndkTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLT 109
Cdd:PRK13632 3 NKSVMIKVENVSFSYP-------------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQSGEIKID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 110 GN-ISYNNKplsKAVKRTTGFVTQD-DALYPNLTVTETLVFTallrLPNSFKKQEKIKQ-----AKAVMTELGLDRckdt 182
Cdd:PRK13632 70 GItISKENL---KEIRKKIGIIFQNpDNQFIGATVEDDIAFG----LENKKVPPKKMKDiiddlAKKVGMEDYLDK---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 183 iigGP-FLrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSSRLfyMFD 260
Cdd:PRK13632 139 ---EPqNL---SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITHDMDEAI--LAD 210
|
250
....*....|....
gi 334186960 261 KLLLLSEGNPVYFG 274
Cdd:PRK13632 211 KVIVFSEGKLIAQG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
66-274 |
1.60e-10 |
|
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: 64.55 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV--GEGKGKLTGNISYNnkplskavkrttgfvTQDDALYPNlTVT 143
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELepSEGKIKHSGRISFS---------------PQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTALLrlpNSFKKQEKIKqAKAVMTELGLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:TIGR01271 505 DNIIFGLSY---DEYRYTSVIK-ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 224 STTAQRIV-SILWEL-ARGGRTVVTtihqpsSRLFYM--FDKLLLLSEGNPVYFG 274
Cdd:TIGR01271 581 VVTEKEIFeSCLCKLmSNKTRILVT------SKLEHLkkADKILLLHEGVCYFYG 629
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
63-249 |
2.69e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL---TGNISYNNKPLSKAVKRTTGFVTQDDALYPN 139
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdGENIPAMSRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTalLR----LPNSFKKQEKIKQAKAVMtelgldrckdtiiggpfLRG--------VSGGERKRVSIGQEIL 207
Cdd:PRK11831 99 MNVFDNVAYP--LRehtqLPAPLLHSTVMMKLEAVG-----------------LRGaaklmpseLSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334186960 208 INPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIH 249
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSH 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
67-275 |
2.87e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKAVKRTTGFVTQDDALYPNLTVTET 145
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNINYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTallRLP-------NSFKKQEKIKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK09700 101 LYIG---RHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVA-----NLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIHQpSSRLFYMFDKLLLLSEGNPVYFGL 275
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
63-223 |
3.01e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLtgnisynnkplSKAVKRTTGFVTQDDALYPNLTV 142
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TetlvFTALLRLPNSFKKQEKIKQAKAVMTELGLDRckdtiiggPfLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:PRK09544 85 T----VNRFLRLRPGTKKEDILPALKRVQAGHLIDA--------P-MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
.
gi 334186960 223 D 223
Cdd:PRK09544 152 D 152
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
67-230 |
3.45e-10 |
|
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: 63.43 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 67 LKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisynnkplskaVKRTTGFVTQDdALYPNLTVTETL 146
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-------------MKGSVAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 VFTALLRlPNSFKKqekIKQAKAVMTEL----GLDRckdTIIGGpflRGV--SGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:TIGR00957 720 LFGKALN-EKYYQQ---VLEACALLPDLeilpSGDR---TEIGE---KGVnlSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170
....*....|
gi 334186960 221 GLDSTTAQRI 230
Cdd:TIGR00957 790 AVDAHVGKHI 799
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
62-235 |
4.44e-10 |
|
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: 58.23 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisynnkpLSKAVKrtTGFVTQddalypnlt 141
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVK--IGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 vtetlvftallrlpnsfkkqekikqakavmtelgldrckdtiiggpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170
....*....|....
gi 334186960 222 LDsttaqrIVSILW 235
Cdd:cd03221 101 LD------LESIEA 108
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-245 |
4.91e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 21 RSLPFSIFKKANNP--VTLKFENLVytvkLKDSQGcfgkndkteeRTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALG 98
Cdd:COG3845 240 REVLLRVEKAPAEPgeVVLEVENLS----VRDDRG----------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 99 G--RVGEGKgkltgnISYNNKPLSKA-----VKRTTGFVTQD---DALYPNLTVTETLVFTALLRLPNS---FKKQEKI- 164
Cdd:COG3845 306 GlrPPASGS------IRLDGEDITGLsprerRRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPPFSrggFLDRKAIr 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 165 KQAKAVMTELGLdRCkdtiiGGPFL--RGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGR 242
Cdd:COG3845 380 AFAEELIEEFDV-RT-----PGPDTpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGA 453
|
...
gi 334186960 243 TVV 245
Cdd:COG3845 454 AVL 456
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
60-239 |
6.72e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----KAVKRTTGFVTQDDA 135
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGT----LLFEGEDIStlkpEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNlTVTETLVFTALLRlpnsfKKQEKIKQAKAVMTELGLDrckDTIIGGPfLRGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK10247 92 LFGD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALP---DTILTKN-IAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180
....*....|....*....|....
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELAR 239
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVR 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
60-270 |
8.57e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPL--SK----AVKRTTGFVTQD 133
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA----VLWQGKPLdySKrgllALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DALYPNLTVTETLVFTALLRLpnSFKKQEKIKQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINPSLL 213
Cdd:PRK13638 86 PEQQIFYTDIDSDIAFSLRNL--GVPEAEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPS-----SRLFYMFDKLLLLSEGNP 270
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDliyeiSDAVYVLRQGQILTHGAP 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
66-274 |
1.19e-09 |
|
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: 59.87 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV--GEGKGKLTGNISynnkplskavkrttgFVTQDDALYPNlTVT 143
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELepSEGKIKHSGRIS---------------FSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTAllrlpnSFKKQEKIKQAKAVMTELGLDRC--KDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:cd03291 116 ENIIFGV------SYDEYRYKSVVKACQLEEDITKFpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 222 LDSTTAQRIV-SILWEL-ARGGRTVVTTIHQPSSRLfymfDKLLLLSEGNPVYFG 274
Cdd:cd03291 190 LDVFTEKEIFeSCVCKLmANKTRILVTSKMEHLKKA----DKILILHEGSSYFYG 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
77-250 |
1.26e-09 |
|
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: 58.88 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGegkgKLTGNISYNNKPLSKAVKRTTGFVTQDDALYP-------NLTVTETLVFT 149
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAaqkpwllNATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 AllrlPNSFKKQEKIKQAKAVMTELGLDRCKD-TIIGGpflRGV--SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:cd03290 103 S----PFNKQRYKAVTDACSLQPDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180
....*....|....*....|....*.
gi 334186960 227 AQRIVS--ILWELARGGRTVVTTIHQ 250
Cdd:cd03290 176 SDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
66-274 |
1.51e-09 |
|
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: 58.19 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 66 ILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGEGKgklTGNISYNNKPLSK----AVKRTTGFVTQDDALYPNlT 141
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF-RFLEAE---EGKIEIDGIDISTipleDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLvftallrlpNSFKKQ--EKIKQAKAVmTELGLDrckdtiiggpflrgVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:cd03369 98 IRSNL---------DPFDEYsdEEIYGALRV-SEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 220 SGLDSTTAQRIVSILWELARGGrTVVTTIHQPSSRLFYmfDKLLLLSEGNPVYFG 274
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIIDY--DKILVMDAGEVKEYD 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
64-268 |
1.59e-09 |
|
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: 60.91 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLSK----AVKRTTGFVTQDDALYPN 139
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR----SGEILLNGFSLKDidrhTLRQFINYLPQEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 lTVTETLVFTAllrlpNSFKKQEKIKQAkavmteLGLDRCKDTIIGGPFLRG---------VSGGERKRVSIGQEILINP 210
Cdd:TIGR01193 563 -SILENLLLGA-----KENVSQDEIWAA------CEIAEIKDDIENMPLGYQtelseegssISGGQKQRIALARALLTDS 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334186960 211 SLLFLDEPTSGLDSTTAQRIVSILWELARggRTVVTTIHQPSsrLFYMFDKLLLLSEG 268
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHG 684
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
62-239 |
2.87e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKT-SLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFVTQDD------ 134
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQTLRGVRGNKiamifq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 135 ----ALYPNLTVTETLVftALLRLPNSFKKQEK------------IKQAKavmtelglDRCKDtiiggpFLRGVSGGERK 198
Cdd:PRK15134 100 epmvSLNPLHTLEKQLY--EVLSLHRGMRREAArgeilncldrvgIRQAA--------KRLTD------YPHQLSGGERQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334186960 199 RVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR 239
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
74-223 |
2.94e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkgKLT-GNISYNNKPLS---------KAVKRTtgFvtQDDALYPNLTVT 143
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFY-----KPTgGTILLRGQHIEglpghqiarMGVVRT--F--QHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETL-----------VFTALLRLPnSFKK--QEKIKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINP 210
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLKTP-AFRRaeSEALDRAATWLERVGLLEHANRQAG-----NLAYGQQRRLEIARCMVTQP 172
|
170
....*....|...
gi 334186960 211 SLLFLDEPTSGLD 223
Cdd:PRK11300 173 EILMLDEPAAGLN 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
35-274 |
3.14e-09 |
|
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: 57.54 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 35 VTLKFENLVYTVKLKDSQGCFGKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNI 112
Cdd:cd03220 6 VSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiyPPDSGTVTVRGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 113 SYnnkPLSKAVkrttGFVtqddalyPNLTVTETLVFTALLrLPNSFKKQEKIKQAKAVMTELGldRCKDTiiggPfLRGV 192
Cdd:cd03220 86 SS---LLGLGG----GFN-------PELTGRENIYLNGRL-LGLSRKEIDEKIDEIIEFSELG--DFIDL----P-VKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVY 272
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRF 222
|
..
gi 334186960 273 FG 274
Cdd:cd03220 223 DG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
53-268 |
3.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 53 GCFGKNDKTEERTiLKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnisynnkplSKAVKRTTGFVTQ 132
Cdd:PLN03232 620 GYFSWDSKTSKPT-LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS------------SVVIRGSVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 133 DDALYpNLTVTETLVFTAllrlpnSFKKQE--KIKQAKAVMTELGLDRCKD-TIIGGpflRGV--SGGERKRVSIGQEIL 207
Cdd:PLN03232 687 VSWIF-NATVRENILFGS------DFESERywRAIDVTALQHDLDLLPGRDlTEIGE---RGVniSGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 208 INPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQpsSRLFYMFDKLLLLSEG 268
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-239 |
3.26e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 31 ANNPVTLKFENLVYTVKLKDSQGCFGKNDKTeertiLKGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVgegkgK 107
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKQWFWQPPKT-----LKAVDGVtlrLYEGETLGVVGESGCGKSTFARAIIGLV-----K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 108 LT-GNISYNNKPLSK-------AVKRTTGFVTQDD--ALYPNLTVTETLVFTALLRLPNsFKKQEKIKQAKAVMTELGLd 177
Cdd:PRK15079 73 ATdGEVAWLGKDLLGmkddewrAVRSDIQMIFQDPlaSLNPRMTIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGL- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186960 178 rCKDTIIGGP--FlrgvSGGERKRVSIGQEILINPSLLFLDEPTSGLD-STTAQrIVSILWELAR 239
Cdd:PRK15079 151 -LPNLINRYPheF----SGGQCQRIGIARALILEPKLIICDEPVSALDvSIQAQ-VVNLLQQLQR 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
59-268 |
3.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 59 DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgkltgnisynnKPLSKA---VKRTTGFVTQDDA 135
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL---------------PPRSDAsvvIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYpNLTVTETLVFTAllrlPNSFKKQEKIKQAKAVMTELGLDRCKD-TIIGGpflRGV--SGGERKRVSIGQEILINPSL 212
Cdd:PLN03130 690 IF-NATVRDNILFGS----PFDPERYERAIDVTALQHDLDLLPGGDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 213 LFLDEPTSGLDSTTAQRIVS--ILWELARGGRTVVTT-IHQPSSrlfymFDKLLLLSEG 268
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNqLHFLSQ-----VDRIILVHEG 815
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-228 |
4.59e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 33 NPVTLKFENL--VYTVKlkdsQGCFGKndkteERTiLKGLTGI---VKPGEILAMLGPSGSGKTSLltalgGRV------ 101
Cdd:PRK11308 2 QQPLLQAIDLkkHYPVK----RGLFKP-----ERL-VKALDGVsftLERGKTLAVVGESGCGKSTL-----ARLltmiet 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 102 -GEGKGKLTG-NISYNNKPLSKAVKRTTGFVTQD--DALYPNLTVTETLvfTALLRLPNSFKKQEKIKQAKAVMTELGL- 176
Cdd:PRK11308 67 pTGGELYYQGqDLLKADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLr 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 177 ----DRCkdtiiggPFLrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLD-STTAQ 228
Cdd:PRK11308 145 pehyDRY-------PHM--FSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQ 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
74-253 |
4.66e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.26 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKT---SLLTalggR---VGEGKGKLTG-NI-SYNNKPLSKAVkrttGFVTQDDALYpNLTVTET 145
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKStiaNLLT----RfydIDEGEILLDGhDLrDYTLASLRNQV----ALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTAllrlPNSFKKQEKIKQAK-AVMTEL--GLDRCKDTIIG--GPFLrgvSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:PRK11176 437 IAYAR----TEQYSREQIEEAARmAYAMDFinKMDNGLDTVIGenGVLL---SGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 221 GLDSTTAQRIVSILWELARgGRTVVTTIHQPSS 253
Cdd:PRK11176 510 ALDTESERAIQAALDELQK-NRTSLVIAHRLST 541
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-249 |
4.76e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGgRVGE--GKGKLTGNISYNNKPLSKA------VKRTTGFVTQD 133
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNEleSEVRVEGRVEFFNQNIYERrvnlnrLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 DALYPnLTVTETLVFTALLRLPNSFKKQEKIKQAKAVMTELgLDRCKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLL 213
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADL-WDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 334186960 214 FLDEPTSGLDSTTAQRIVSILWELA-RGGRTVVTTIH 249
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSH 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
63-270 |
6.01e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLSKA----VKRTTGFVTQD-DALY 137
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE----AGTITVGGMVLSEEtvwdVRRQVGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 PNLTVTETLVFTallrLPNS-FKKQEKIKQAKAVMTELGLDrckdtiiggPFLR----GVSGGERKRVSIGQEILINPSL 212
Cdd:PRK13635 95 VGATVQDDVAFG----LENIgVPREEMVERVDQALRQVGME---------DFLNrephRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGR-TVVTTIHQ-----PSSRLFYMfDKLLLLSEGNP 270
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDldeaaQADRVIVM-NKGEILEEGTP 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
64-239 |
6.97e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKR--TTGFVTQD--DALYPN 139
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRgrKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVT----ETLVftALLRLPNSfkkqekiKQAKAVMTELGLDRCKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFL 215
Cdd:PRK10418 96 HTMHtharETCL--ALGKPADD-------ATLTAALEAVGLENAARVLKLYPF--EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180
....*....|....*....|....
gi 334186960 216 DEPTSGLDSTTAQRIVSILWELAR 239
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQ 188
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
37-237 |
7.62e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.82 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLV--YTVKlkdsQGCFGKNDKTeertiLKGLTGI---VKPGEILAMLGPSGSGKTSLltalgGRVgegkgkLT-- 109
Cdd:COG4608 8 LEVRDLKkhFPVR----GGLFGRTVGV-----VKAVDGVsfdIRRGETLGLVGESGCGKSTL-----GRL------LLrl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 110 -----GNISYNNKPLS-------KAVKRTTGFVTQD--DALYPNLTVTETLvfTALLRLPNSFKKQEKIKQAKAVMTELG 175
Cdd:COG4608 68 eeptsGEILFDGQDITglsgrelRPLRRRMQMVFQDpyASLNPRMTVGDII--AEPLRIHGLASKAERRERVAELLELVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 176 LDRckdtiiggPFLR----GVSGGERKRVSIGQEILINPSLLFLDEPTSGLD-STTAQrIVSILWEL 237
Cdd:COG4608 146 LRP--------EHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQ-VLNLLEDL 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
64-249 |
1.34e-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: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNIsynnkplskavkrTTGFVTQDDALYPNLT 141
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdKDFNGEARPQPGI-------------KVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETlVFTALLRLPNSFKK-------------------------QEKIKQAKAVMTELGLD------RC--KDTIIGGpf 188
Cdd:TIGR03719 85 VREN-VEEGVAEIKDALDRfneisakyaepdadfdklaaeqaelQEIIDAADAWDLDSQLEiamdalRCppWDADVTK-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 189 lrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTtaqrivSILW---ELARGGRTVVTTIH 249
Cdd:TIGR03719 162 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE------SVAWlerHLQEYPGTVVAVTH 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
60-250 |
1.38e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 60 KTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKgkltgnISYNNKPLSK-------AVKRTTGFV 130
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRPTSGS------VLVDGVDLTAlserelrAARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 131 TQDDALYPNLTVTETLvftAL-LRLpNSFKKQEKIKQAKAVMTELGL-DRCKDtiiggpFLRGVSGGERKRVSIGQEILI 208
Cdd:COG1135 88 FQHFNLLSSRTVAENV---ALpLEI-AGVPKAEIRKRVAELLELVGLsDKADA------YPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334186960 209 NPSLLFLDEPTSGLDSTTAQRIVSILWEL-ARGGRTVVTTIHQ 250
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHE 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
76-239 |
1.53e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 76 PGEILAMLGPSGSGKTSLLTALGgRVGEGKGkltGNISYNNKPLS-------KAVKRTTGFVTQDD--ALYPNLTVTETL 146
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALL-RLVESQG---GEIIFNGQRIDtlspgklQALRRDIQFIFQDPyaSLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 147 VftALLRLPNSFKKQEKIKQAKAVMTELGLDrckdtiiggP-----FLRGVSGGERKRVSIGQEILINPSLLFLDEPTSG 221
Cdd:PRK10261 425 M--EPLRVHGLLPGKAAAARVAWLLERVGLL---------PehawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170
....*....|....*...
gi 334186960 222 LDSTTAQRIVSILWELAR 239
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQR 511
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
249-308 |
1.68e-08 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 57.22 E-value: 1.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 249 HQPSSRLFYMFDKLLLLSEGN-PVYFGLGSNAMDYFASVGYS-PlvERINPSDFLLDIANGV 308
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGlTVYHGPVKKVEEYFAGLGINvP--ERVNPPDHFIDILEGI 60
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
55-268 |
2.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 55 FGKNDKTEERTIL--KGLTGIVKP-----------GEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYNNKPL 119
Cdd:PRK10982 239 FPDKENKPGEVILevRNLTSLRQPsirdvsfdlhkGEILGIAGLVGAKRTDIVETLFGirEKSAGTITLHGKKINNHNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 120 sKAVKRTTGFVTQD---DALYPNLTVTetlvFTALLRLPNSFK------KQEKIKQAkavmTELGLD--RCK----DTII 184
Cdd:PRK10982 319 -EAINHGFALVTEErrsTGIYAYLDIG----FNSLISNIRNYKnkvgllDNSRMKSD----TQWVIDsmRVKtpghRTQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 185 GGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVtTIHQPSSRLFYMFDKLLL 264
Cdd:PRK10982 390 GS-----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILV 463
|
....
gi 334186960 265 LSEG 268
Cdd:PRK10982 464 MSNG 467
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
78-254 |
6.69e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 78 EILAMLGPSGSGKTSLLTAL--------GGRVgEGKGKLTGNISYNNKPLSKAVKRTTGFVTQDDALYPNlTVTETLVFT 149
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRCFnrlndlipGFRV-EGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 ALLrlpNSFKK------QEKIKQAkAVMTELGlDRCKDTIIGgpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:PRK14243 115 ARI---NGYKGdmdelvERSLRQA-ALWDEVK-DKLKQSGLS------LSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 224 STTAQRIVSILWELARgGRTVVTTIH--QPSSR 254
Cdd:PRK14243 184 PISTLRIEELMHELKE-QYTIIIVTHnmQQAAR 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
68-249 |
6.75e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 68 KGLTGI---VKPGEILAMLGPSGSGKTSLLTALGGRVGEgkGKLTGNISYNNKPL-SKAVKRT--TGFVT--QDDALYPN 139
Cdd:PRK13549 19 KALDNVslkVRAGEIVSLCGENGAGKSTLMKVLSGVYPH--GTYEGEIIFEGEELqASNIRDTerAGIAIihQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 140 LTVTETLVFTALLrLPNSFKKQEKIKQ-AKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:PRK13549 97 LSVLENIFLGNEI-TPGGIMDYDAMYLrAQKLLAQLKLDINPATPVG-----NLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
74-274 |
7.83e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTslLTALG-GRVGEGKGkltGNISYNNKPLSKAVKRTTGFVTQDDA----------------- 135
Cdd:PRK10261 39 LQRGETLAIVGESGSGKS--VTALAlMRLLEQAG---GLVQCDKMLLRRRSRQVIELSEQSAAqmrhvrgadmamifqep 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 ---LYPNLTVTETLVFTalLRLPNSFKKQEKIKQAKAVMTELGLDRCKDtiIGGPFLRGVSGGERKRVSIGQEILINPSL 212
Cdd:PRK10261 114 mtsLNPVFTVGEQIAES--IRLHQGASREEAMVEAKRMLDQVRIPEAQT--ILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-237 |
8.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 37 LKFENLVYtvklkdsqgcfgKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKG-------KLT 109
Cdd:PRK13642 5 LEVENLVF------------KYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 110 GNISYNnkplskaVKRTTGFVTQD-DALYPNLTVTETLVFTallrLPNS-FKKQEKIKQAKAVMTELGLdrcKDTIIGGP 187
Cdd:PRK13642 73 AENVWN-------LRRKIGMVFQNpDNQFVGATVEDDVAFG----MENQgIPREEMIKRVDEALLAVNM---LDFKTREP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334186960 188 flRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWEL 237
Cdd:PRK13642 139 --ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
74-239 |
9.04e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKT-SLLTALG-----GRVGEGKGKLTGN--ISYNNKPLSKAVKRTTGFVTQD--DALYPNLTVT 143
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvSSLAIMGlidypGRVMAEKLEFNGQdlQRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVftALLRLPNSFKKQEKIKQAKAVMTELGldrckdtiIGGPFLR------GVSGGERKRVSIGQEILINPSLLFLDE 217
Cdd:PRK11022 110 FQIM--EAIKVHQGGNKKTRRQRAIDLLNQVG--------IPDPASRldvyphQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180
....*....|....*....|..
gi 334186960 218 PTSGLDSTTAQRIVSILWELAR 239
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQ 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
73-249 |
1.13e-07 |
|
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: 53.52 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 73 IVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNkplskAVKRTTGFVTQDdalypnltvtetlVFTALL 152
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDE-----ILDEFRGSELQN-------------YFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 --------------RLPNSFK--------KQEKIKQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILINP 210
Cdd:cd03236 84 egdvkvivkpqyvdLIPKAVKgkvgellkKKDERGKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334186960 211 SLLFLDEPTSGLDstTAQRI--VSILWELARGGRTVVTTIH 249
Cdd:cd03236 159 DFYFFDEPSSYLD--IKQRLnaARLIRELAEDDNYVLVVEH 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
77-223 |
1.20e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGK-------TSLLTAlggrvGEGKGKLTGnisynnKPL---SKAVKRTTGFVTQDDALYPNLTVTETL 146
Cdd:NF033858 292 GEIFGFLGSNGCGKsttmkmlTGLLPA-----SEGEAWLFG------QPVdagDIATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 147 VFTA-LLRLPnsfkkQEKIKQA-KAVMTELGLDRCKDTIIGGPFLrgvsgGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:NF033858 361 ELHArLFHLP-----AAEIAARvAEMLERFDLADVADALPDSLPL-----GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
186-253 |
1.50e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 186 GPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELA-RGGRTVVTTIHQPSS 253
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIAS 1421
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
63-245 |
2.28e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.35 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTAL--------GGRVgegkgklTGNISYNNKPLSK------AVKRTTG 128
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGARV-------EGEILLDGEDIYDpdvdvvELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 129 FVTQddalYPN---LTVTETLVFtaLLRLpNSFKKQEKI--------KQAkavmtelGL-----DRCKDtiiggPFLrGV 192
Cdd:COG1117 96 MVFQ----KPNpfpKSIYDNVAY--GLRL-HGIKSKSELdeiveeslRKA-------ALwdevkDRLKK-----SAL-GL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELaRGGRTVV 245
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIV 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
64-235 |
2.31e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNIsynnkplskavkrTTGFVTQDDALYPNLT 141
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdKEFEGEARPAPGI-------------KVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETL------VFTALLRL----------PNSFKK--------QEKIKQAKAVMTELGLD------RC--KDTIIGGpfl 189
Cdd:PRK11819 87 VRENVeegvaeVKAALDRFneiyaayaepDADFDAlaaeqgelQEIIDAADAWDLDSQLEiamdalRCppWDAKVTK--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334186960 190 rgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTtaqrivSILW 235
Cdd:PRK11819 164 --LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE------SVAW 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
74-274 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.70 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGK-LTGN--ISYNNKPLS--KAVKRTTGFVTQddalYPNL-----TVT 143
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDyaIPANLKKIKevKRLRKEIGLVFQ----FPEYqlfqeTIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTALLRLPNsfkKQEKIKQAKAVMTELGLDRckDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:PRK13645 110 KDIAFGPVNLGEN---KQEAYKKVPELLKLVQLPE--DYVKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334186960 224 STTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFG 274
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
72-231 |
2.89e-07 |
|
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: 53.63 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 72 GIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN--ISYnnKPlskavkrttGFVTQDDalypNLTVTETLVFT 149
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkISY--KP---------QYISPDY----DGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 ALLRLPNSFKKQEKIKQakavmteLGLDRCKDTIiggpfLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTtaQR 229
Cdd:COG1245 426 NTDDFGSSYYKTEIIKP-------LGLEKLLDKN-----VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QR 491
|
..
gi 334186960 230 IV 231
Cdd:COG1245 492 LA 493
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
64-278 |
2.93e-07 |
|
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: 52.22 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT-GNISYNNKPLSKAVKRTTgFVTQDDALY----- 137
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIViDGIDISKLPLHTLRSRLS-IILQDPILFsgsir 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 ----PNLTVTETLVFTALlrlpnsfkkqeKIKQAKAVMTEL--GLDRCkdTIIGGpflRGVSGGERKRVSIGQEILINPS 211
Cdd:cd03288 113 fnldPECKCTDDRLWEAL-----------EIAQLKNMVKSLpgGLDAV--VTEGG---ENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186960 212 LLFLDEPTSGLDSTTaQRIVSILWELARGGRTVVTTIHQPSSRLfyMFDKLLLLSEGNPVYFGLGSN 278
Cdd:cd03288 177 ILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTIL--DADLVLVLSRGILVECDTPEN 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
62-250 |
5.31e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGnisynnkplskavKRTTGFVTQDdALYPNLT 141
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQ-AWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 142 VTETLVFtallrlpnsFKKQEKIKQAKAV-MTELGLDRCK-----DTIIGGpflRGV--SGGERKRVSIGQEILINPSLL 213
Cdd:PTZ00243 737 VRGNILF---------FDEEDAARLADAVrVSQLEADLAQlggglETEIGE---KGVnlSGGQKARVSLARAVYANRDVY 804
|
170 180 190
....*....|....*....|....*....|....*....
gi 334186960 214 FLDEPTSGLDSTTAQRIVS--ILWELArgGRTVVTTIHQ 250
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEecFLGALA--GKTRVLATHQ 841
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
77-223 |
5.76e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT--GNISYNNKPlSKAVKRTTGFVTQD---DALYPNLTVTETLVFTAL 151
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldGHEVVTRSP-QDGLANGIVYISEDrkrDGLVLGMSVKENMSLTAL 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186960 152 LRLPNSFKKQEKIKQAKAVMTELGLDRCK----DTIIGGpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLD 223
Cdd:PRK10762 357 RYFSRAGGSLKHADEQQAVSDFIRLFNIKtpsmEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
74-249 |
6.56e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkGKLTGNISYNNKPLSKAVKRTT-----GFVTQDDALYPNLTVTETlVF 148
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIY----TRDAGSILYLGKEVTFNGPKSSqeagiGIIHQELNLIPQLTIAEN-IF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 149 taLLRLP-NSFKK---QEKIKQAKAVMTELGLDRCKDTIIGgpflrGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDS 224
Cdd:PRK10762 102 --LGREFvNRFGRidwKKMYAEADKLLARLNLRFSSDKLVG-----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180
....*....|....*....|....*
gi 334186960 225 TTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK10762 175 TETESLFRVIRELKSQGRGIVYISH 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-268 |
7.77e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 32 NNPVTLKFENLVYtvklKDSqgcfgkndkteERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV---GEGKGKL 108
Cdd:PRK13640 3 DNIVEFKHVSFTY----PDS-----------KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 109 T-GNISYNNKPLSKaVKRTTGFVTQD-DALYPNLTVTETLVFTallrLPN-SFKKQEKIKQAKAVMTELGLdrcKDTIIG 185
Cdd:PRK13640 68 TvDGITLTAKTVWD-IREKVGIVFQNpDNQFVGATVGDDVAFG----LENrAVPRPEMIKIVRDVLADVGM---LDYIDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 186 GPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELAR-GGRTVVTTIHQPSSRLfyMFDKLLL 264
Cdd:PRK13640 140 EP--ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEAN--MADQVLV 215
|
....
gi 334186960 265 LSEG 268
Cdd:PRK13640 216 LDDG 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
46-270 |
8.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 46 VKLKDSQGCFGKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKL-TGNISYNNKPLSKAVK 124
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 125 RTTGFVTQDdalyPNLTVTETLVFTALLRLP-NSFKKQEKI-KQAKAVMTELGLDRCKDTiigGPFLrgVSGGERKRVSI 202
Cdd:PRK13633 85 NKAGMVFQN----PDNQIVATIVEEDVAFGPeNLGIPPEEIrERVDESLKKVGMYEYRRH---APHL--LSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 203 GQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARG-GRTVVTTIH-----QPSSRLFYMfDKLLLLSEGNP 270
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHymeeaVEADRIIVM-DSGKVVMEGTP 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
72-231 |
8.79e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 72 GIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN--ISYnnKPlskavkrttGFVTQDdalyPNLTVTETLVFT 149
Cdd:PRK13409 360 GEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkISY--KP---------QYIKPD----YDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 150 AlLRLPNSFKKQEKIKQakavmteLGLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTtaQR 229
Cdd:PRK13409 425 T-DDLGSSYYKSEIIKP-------LQLERLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QR 489
|
..
gi 334186960 230 IV 231
Cdd:PRK13409 490 LA 491
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
62-223 |
9.95e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRV--GEGKGKLTGNISynnkplskavkrtTGFVTQDDAL-YP 138
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELepDSGTVKWSENAN-------------IGYYAQDHAYdFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 N-LTVT------------ETLVFTALLRLPNSfkkQEKIKqaKAVmtelgldrckdtiiggpflRGVSGGERKRVSIGQE 205
Cdd:PRK15064 397 NdLTLFdwmsqwrqegddEQAVRGTLGRLLFS---QDDIK--KSV-------------------KVLSGGEKGRMLFGKL 452
|
170
....*....|....*...
gi 334186960 206 ILINPSLLFLDEPTSGLD 223
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD 470
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-249 |
1.30e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 136 LYPNLTVTETLVFTALlRLPNSFKKQEKIKQAKAVMTELGLDRCKdtiIGGPfLRGVSGGERKRVSIGQEILI---NPSL 212
Cdd:PRK00635 759 RYKGKNIADILEMTAY-EAEKFFLDEPSIHEKIHALCSLGLDYLP---LGRP-LSSLSGGEIQRLKLAYELLApskKPTL 833
|
90 100 110
....*....|....*....|....*....|....*..
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:PRK00635 834 YVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
65-269 |
1.33e-06 |
|
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: 50.24 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 65 TILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVG-EGKGKLTGnISYNNKPLSKAvKRTTGFVTQddalypnltvt 143
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNtEGDIQIDG-VSWNSVPLQKW-RKAFGVIPQ----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETLVFTALLRL---PNSFKKQEKIKQakaVMTELGL--------DRCKDTIIGGPFLrgVSGGERKRVSIGQEILINPSL 212
Cdd:cd03289 85 KVFIFSGTFRKnldPYGKWSDEEIWK---VAEEVGLksvieqfpGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWElARGGRTVVTTIHqpssRLFYMFD--KLLLLSEGN 269
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEH----RIEAMLEcqRFLVIEENK 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
165-247 |
1.35e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 165 KQAKAVMTELgLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTV 244
Cdd:NF000106 119 KDARARADEL-LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
...
gi 334186960 245 VTT 247
Cdd:NF000106 198 LLT 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
63-268 |
1.79e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRvGEGKgKLTGNISYNNKPL-----SKAVKRTTGFVTQDDALY 137
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR-SYGR-NISGTVFKDGKEVdvstvSDAIDAGLAYVTEDRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 138 P-NL--TVTETLVFTAL--------------LRLPNSFKKQEKIKqAKAVMTELGldrckdtiiggpflrGVSGGERKRV 200
Cdd:NF040905 350 GlNLidDIKRNITLANLgkvsrrgvideneeIKVAEEYRKKMNIK-TPSVFQKVG---------------NLSGGNQQKV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186960 201 SIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTihqpSS---RLFYMFDKLLLLSEG 268
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI----SSelpELLGMCDRIYVMNEG 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
47-226 |
2.00e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 47 KLKDSQGCFGKN-----DKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLS- 120
Cdd:PTZ00265 376 KLKDIKKIQFKNvrfhyDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINl 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 121 KAVKRTTGFVTQDDALYPNLT------------------------------------------------VTETLVFTALL 152
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RLP---NSFKKQEKIKQAKAVMTE---LGLDRCKDTIIGGPFLRgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:PTZ00265 536 EMRknyQTIKDSEVVDVSKKVLIHdfvSALPDKYETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
73-249 |
3.07e-06 |
|
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: 50.17 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 73 IVKPGEILAMLGPSGSGKTSLLTALGGRvgegkgkLTGNISYNNKPLSK--AVKRTTGFVTQDdalYpnltvtetlvFTA 150
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGE-------LKPNLGDYDEEPSWdeVLKRFRGTELQD---Y----------FKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 151 LL--------------RLPNSFK---KQ--EKI---KQAKAVMTELGLDRCKDTIIggpflRGVSGGERKRVSIGQEILI 208
Cdd:COG1245 155 LAngeikvahkpqyvdLIPKVFKgtvREllEKVderGKLDELAEKLGLENILDRDI-----SELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334186960 209 NPSLLFLDEPTSGLDSTtaQRI--VSILWELARGGRTVVTTIH 249
Cdd:COG1245 230 DADFYFFDEPSSYLDIY--QRLnvARLIRELAEEGKYVLVVEH 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
64-230 |
3.22e-06 |
|
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: 50.68 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 64 RTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVG-EGKGKLTGnISYNNKPLSKAvKRTTGFVTQddalypnltv 142
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLStEGEIQIDG-VSWNSVTLQTW-RKAFGVIPQ---------- 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 tETLVFTALLRLPNSFKKQEKIKQAKAVMTELGL--------DRCKDTIIGGPFLrgVSGGERKRVSIGQEILINPSLLF 214
Cdd:TIGR01271 1300 -KVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLksvieqfpDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILL 1376
|
170
....*....|....*.
gi 334186960 215 LDEPTSGLDSTTAQRI 230
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQII 1392
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
193-245 |
3.24e-06 |
|
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: 47.42 E-value: 3.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVV 245
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVI 136
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
188-263 |
4.66e-06 |
|
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: 46.97 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 188 FLRGVSGGERKRVSIG---QEILINP-SLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPssRLFYMFDKLL 263
Cdd:cd03227 74 TRLQLSGGEKELSALAlilALASLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
77-234 |
7.47e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.36 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGEgKGKLTGN-ISYNNKPLS--------KAVKRTTGFVTQDDA--LYPNLTVTET 145
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADrFRWNGIDLLklsprerrKIIGREIAMIFQEPSscLDPSAKIGDQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 146 LVFTallrLPNSF-------KKQEKIKQAKAVMTELGLDRCKDTIIGGPFlrGVSGGERKRVSIGQEILINPSLLFLDEP 218
Cdd:COG4170 112 LIEA----IPSWTfkgkwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPH--ELTEGECQKVMIAMAIANQPRLLIADEP 185
|
170
....*....|....*.
gi 334186960 219 TSGLDSTTAQRIVSIL 234
Cdd:COG4170 186 TNAMESTTQAQIFRLL 201
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
77-237 |
1.04e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.44 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALggrVGEGKGKlTGNISYNNKPLS----KAVKRTTGFVTQDDAlypNLTVTETLVFTALL 152
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLM---IGIEKVK-SGEIFYNNQAITddnfEKLRKHIGIVFQNPD---NQFVGSIVKYDVAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 153 RLPNSFKKQEKIKQ-AKAVMTELG-LDRCKDTiiggPflRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRI 230
Cdd:PRK13648 108 GLENHAVPYDEMHRrVSEALKQVDmLERADYE----P--NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
....*..
gi 334186960 231 VSILWEL 237
Cdd:PRK13648 182 LDLVRKV 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
74-250 |
3.06e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.72 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTAL-------GGRV---GEgkgKLTgniSYNNKPLSKAvKRTTGFVTQddalYPNLTVT 143
Cdd:PRK11153 28 IPAGEIFGVIGASGAGKSTLIRCInllerptSGRVlvdGQ---DLT---ALSEKELRKA-RRQIGMIFQ----HFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 144 ETlVF--TAL-LRLPNsfKKQEKIKQAKAVMTEL-GLDRCKDTiiggpFLRGVSGGERKRVSIGQEILINPSLLFLDEPT 219
Cdd:PRK11153 97 RT-VFdnVALpLELAG--TPKAEIKARVTELLELvGLSDKADR-----YPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190
....*....|....*....|....*....|..
gi 334186960 220 SGLDSTTAQRIVSILWELARG-GRTVVTTIHQ 250
Cdd:PRK11153 169 SALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-245 |
4.13e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 47 KLKDSQGCFGKNDKteeRT-ILKGLTgiVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGN------ISY----- 114
Cdd:PRK10938 3 SLQISQGTFRLSDT---KTlQLPSLT--LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrLSFeqlqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 115 ---------NNKPLSKAVK---RTTGFVTQDDALYPNLTvtetlvftalLRLPNSFKkqekikqakavMTELgLDRckdt 182
Cdd:PRK10938 78 lvsdewqrnNTDMLSPGEDdtgRTTAEIIQDEVKDPARC----------EQLAQQFG-----------ITAL-LDR---- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186960 183 iiggPFlRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVV 245
Cdd:PRK10938 132 ----RF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
63-223 |
4.34e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTgnisynnkpLSKAVKrtTGFVTQDDALYpnLTV 142
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG---------LAKGIK--LGYFAQHQLEF--LRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVfTALLRLpnsfKKQEKIKQAKAVMTELGLDRCKDTIIGGPFlrgvSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:PRK10636 391 DESPL-QHLARL----APQELEQKLRDYLGGFGFQGDKVTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
.
gi 334186960 223 D 223
Cdd:PRK10636 462 D 462
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
72-277 |
7.31e-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: 43.71 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 72 GIVKPGEILAMLGPSGSGKTSLLTALGGRVgegkgkltgnisynnKPlskavkrttgfvTQDDALYPNLTVtetlvftal 151
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQL---------------IP------------NGDNDEWDGITP--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 152 lrlpnSFKKQeKIKqakavmtelgldrckdtiiggpflrgVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIV 231
Cdd:cd03222 64 -----VYKPQ-YID--------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334186960 232 SILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLsEGNPVYFGLGS 277
Cdd:cd03222 112 RAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIAS 156
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
139-250 |
1.11e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 139 NLTVTETLVFtallrlpnsFKKQEKIKQAKAVMTELGLDRCKdtiIG--GPFLrgvSGGERKRVSIGQEiLINPS----L 212
Cdd:cd03271 130 DMTVEEALEF---------FENIPKIARKLQTLCDVGLGYIK---LGqpATTL---SGGEAQRIKLAKE-LSKRStgktL 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 334186960 213 LFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQ 250
Cdd:cd03271 194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
62-253 |
1.52e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.71 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 62 EERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKltgnISYNNKPLS----KAVKRTTGFVTQD---- 133
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE----IRLDGRPLSslshSVLRQGVAMVQQDpvvl 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 -DALYPNLT----VTETLVFTALlrlpnsfkkqEKIKQAKAV--MTElGLdrckDTIIG--GPFLrgvSGGERKRVSIGQ 204
Cdd:PRK10790 428 aDTFLANVTlgrdISEEQVWQAL----------ETVQLAELArsLPD-GL----YTPLGeqGNNL---SVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334186960 205 EILINPSLLFLDEPTSGLDSTTAQRIVSILwELARGGRTVVTTIHQPSS 253
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLST 537
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
77-249 |
2.48e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 77 GEILAMLGPSGSGKTSLLTALGGRVGEGKGKLT--GNISynnkplskavkrttgFVTQDDALYPNLTVTETLVFTALLRl 154
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrnGEVS---------------VIAISAGLSGQLTGIENIEFKMLCM- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 155 pnSFKKqekiKQAKAVM------TELGldrckdTIIGGPfLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQ 228
Cdd:PRK13546 114 --GFKR----KEIKAMTpkiiefSELG------EFIYQP-VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180
....*....|....*....|.
gi 334186960 229 RIVSILWELARGGRTVVTTIH 249
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSH 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
193-252 |
3.31e-04 |
|
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: 41.92 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186960 193 SGGERKRVSIGQEILINP--SLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPS 252
Cdd:cd03238 89 SGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
74-248 |
3.89e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGrVgEGKGKLTGNISYNNKPL-------SKAVkrttGFVT--QDDALYPNLTVTE 144
Cdd:NF040905 24 VREGEIHALCGENGAGKSTLMKVLSG-V-YPHGSYEGEILFDGEVCrfkdirdSEAL----GIVIihQELALIPYLSIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 145 TLvFtallrLPNSFKK------QEKIKQAKAVMTELGLDRCKDTIIGGpflRGVsgGERKRVSIGQEILINPSLLFLDEP 218
Cdd:NF040905 98 NI-F-----LGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTD---IGV--GKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190
....*....|....*....|....*....|
gi 334186960 219 TSGLDSTTAQRIVSILWELARGGrtvVTTI 248
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQG---ITSI 193
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
56-274 |
1.98e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.45 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 56 GKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGG--RVGEGKGKLTGNISYnnkPLSKAvkrtTGFVtqd 133
Cdd:COG1134 31 RRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGilEPTSGRVEVNGRVSA---LLELG----AGFH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 134 dalyPNLTVTETLVFTALLrlpNSFKKQEkikqAKAVM------TELG--LDRckdtiiggPfLRGVSGGERKRVSIGQE 205
Cdd:COG1134 101 ----PELTGRENIYLNGRL---LGLSRKE----IDEKFdeivefAELGdfIDQ--------P-VKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186960 206 ILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSrLFYMFDKLLLLSEGNPVYFG 274
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
74-268 |
2.78e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 74 VKPGEILAMLGPSGSGKTSLLTALGGRVgegkGKLTGNISYNNKPL----SK-AVKRTTGFVTQDDALYPNLTVTETLvf 148
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIY----QKDSGSILFQGKEIdfksSKeALENGISMVHQELNLVLQRSVMDNM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 149 tALLRLPNS--FKKQEKI-KQAKAVMTELGLD---RCKdtiiggpfLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGL 222
Cdd:PRK10982 95 -WLGRYPTKgmFVDQDKMyRDTKAIFDELDIDidpRAK--------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334186960 223 DSTTAQRIVSILWELARGGRTVVTTIHQpSSRLFYMFDKLLLLSEG 268
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
193-235 |
3.86e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 334186960 193 SGGERKRVSIGQEILINPSLLFLDEPTSGLDsttaqrIVSILW 235
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD------LHAVLW 382
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
63-253 |
4.51e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 63 ERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGkgklTGNISYNNKPLSKAVKRTTGFVTQDDALYPNLTV 142
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS----SGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 143 TETLVFTALLrlpnsFKKQEKIKQAKAV--MTELGLDRCKDtiiggpflrgVSGGERKRVSIGQEILINPSLLFLDEPTS 220
Cdd:PRK13541 88 FENLKFWSEI-----YNSAETLYAAIHYfkLHDLLDEKCYS----------LSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|...
gi 334186960 221 GLDSTTAQRIVSILWELARGGRTVVTTIHQPSS 253
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGIVLLSSHLESS 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
163-226 |
4.62e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 4.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186960 163 KIKQakaVMTELGLDrcKDTIiggpfLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTT 226
Cdd:PRK11147 138 RINE---VLAQLGLD--PDAA-----LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
193-249 |
4.84e-03 |
|
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: 40.00 E-value: 4.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186960 193 SGGERKRVSIGQEIL---INPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIH 249
Cdd:TIGR00630 831 SGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
76-107 |
6.89e-03 |
|
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: 37.74 E-value: 6.89e-03
10 20 30
....*....|....*....|....*....|..
gi 334186960 76 PGEILAMLGPSGSGKTSLLTALGGRVGEGKGK 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG 32
|
|
| |
