|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-666 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 715.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 37 CRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLT--GDVVLNGMAMERDQMTRISSFLREFEINV 114
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKgsGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQ------LSGGERKRLSLAEELITDPIFLFCD 188
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 189 EPTTGLDSFSAYTVIKTLRHLCTRRRIAkhsltqvygedsfatpsdngssgsnsiemeivdnshesllqamkelptlgvl 268
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTI---------------------------------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 269 nnspngtqkkaaICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQAAKFFTE-GFMQPKNCNPADFYLKTLADGQGSKN 347
Cdd:TIGR00955 220 ------------ICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPCPENYNPADFYVQVLAVIPGSEN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 348 AG-ELLRAKYEHETDGLYSGSWLLARNYS----GDYMKHVQNFKKIR----WIYQVYLLVIRFMTEDLANIRSGLIGFGF 418
Cdd:TIGR00955 288 ESrERIEKICDSFAVSDIGRDMLVNTNLWsgkaGGLVKDSENMEGIGynasWWTQFYALLKRSWLSVLRDPLLLKVRLIQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 419 FMTTAVTLSLMYSGvGGLTQRTVQDVGGSIFMLSNEMIFTFSYGVTYIFPAALPIIRREVAEGTYSLSAYYVALVLSFVP 498
Cdd:TIGR00955 368 TMMTAILIGLIYLG-QGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 499 VAFFKGYMFLSVIYASIYYTRGFLLYITMGFLMSLSAIAAVGYGVFLSSLFETDKMASECAAPFDLIFLIFGGTYMNVDS 578
Cdd:TIGR00955 447 LFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 579 VP----LLKYFSLFFYSNEALMYNFWIDIDNIAC*-VNDEHPCCQTGLEVLQQASFRTADYtfWLDCASLLVVALVFHIV 653
Cdd:TIGR00955 527 IPvyfkWLSYLSWFRYGNEGLLINQWSDVDNIECTsANTTGPCPSSGEVILETLSFRNADL--YLDLIGLVILIFFFRLL 604
|
650
....*....|...
gi 2492600 654 SFTLIRRYINRSG 666
Cdd:TIGR00955 605 AYFALRIRIRRKR 617
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-310 |
1.71e-85 |
|
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: 267.60 E-value: 1.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 28 QSNYSFWNECRKQRELG----ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLR--GNLTGDVVLNGMAMERDQMT 101
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEggGTTSGQILFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 102 RISSFLREFEINVKTFTAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLL-AVGLRDAAHTRIQQLSGGERKRLSLAEELIT 180
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLrDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 181 DPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIakhsltqvygedsfatpsdngssgsnsiemeivdnshesllqamk 260
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI--------------------------------------------- 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2492600 261 elptlgvlnnspngtqkkaAICSIHQPTSDIFELFTHIILMDGGRIVYQG 310
Cdd:cd03234 196 -------------------VILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-310 |
2.77e-46 |
|
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: 162.34 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 14 LEWKQLNYYVPaqeqsnySFWNECRKQrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIS-QRLRGNLTGDVVLNG 92
Cdd:cd03213 4 LSFRNLTVTVK-------SSPSKSGKQ----LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVSGEVLING 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 93 MAMERDQMTRISSFLREFEINVKTFTAYDDLYFmshfkmhrrttksekrqavsdlllavglrdAAHtrIQQLSGGERKRL 172
Cdd:cd03213 73 RPLDKRSFRKIIGYVPQDDILHPTLTVRETLMF------------------------------AAK--LRGLSGGERKRV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 173 SLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCtrrriakhsltqvygedsfatpsdngssgsnsiemeivdnsh 252
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA------------------------------------------ 158
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2492600 253 esllqamkelptlgvlnnspngTQKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQG 310
Cdd:cd03213 159 ----------------------DTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-596 |
2.75e-40 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 156.96 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 35 NECRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN-LTGDVVLNGMAMERDQMTRISsFLREFEIN 113
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnFTGTILANNRKPTKQILKRTG-FVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHT-----RIQQLSGGERKRLSLAEELITDPIFLFCD 188
Cdd:PLN03211 152 YPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 189 EPTTGLDSFSAYTVIKTLRHLCTRrriakhsltqvygedsfatpsdngssgsnsiemeivdnshesllqamkelptlgvl 268
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQK-------------------------------------------------------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 269 nnspngtqKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQAAKFF-TEGFMQPKNCNPADFYLKtLADG----- 342
Cdd:PLN03211 256 --------GKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFeSVGFSPSFPMNPADFLLD-LANGvcqtd 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 343 ----QGSKNAGELLRAKYE-----HETDGLYSGSWLLARNYSGDYMKHVQNFKKIR-----WIYQVYLLVIRFMTEDLAN 408
Cdd:PLN03211 327 gvseREKPNVKQSLVASYNtllapKVKAAIEMSHFPQANARFVGSASTKEHRSSDRisistWFNQFSILLQRSLKERKHE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 409 IRSGLIGFGFFMtTAVTLSLMYSGVgglTQRTVQDVGGSIFMLSnemIF--TF-SYGVTYIFPAALPIIRREVAEGTYSL 485
Cdd:PLN03211 407 SFNTLRVFQVIA-AALLAGLMWWHS---DFRDVQDRLGLLFFIS---IFwgVFpSFNSVFVFPQERAIFVKERASGMYTL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 486 SAYYVALVLSFVPVAFFKGYMFLSVIYASIYYTRGFLLYITMGFLMSLSAIAAVGYGVFLSSLFETDKMASECAAPFDLI 565
Cdd:PLN03211 480 SSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLA 559
|
570 580 590
....*....|....*....|....*....|....*
gi 2492600 566 FLIFGGTYmnVDSVP----LLKYFSLFFYSNEALM 596
Cdd:PLN03211 560 FVLTGGFY--VHKLPscmaWIKYISTTFYSYRLLI 592
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-310 |
8.00e-36 |
|
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: 133.52 E-value: 8.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 12 LLLEWKQLNYYVPAQEQsnysfwnecRKQrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQR-LRGNLTGDVVL 90
Cdd:cd03232 2 SVLTWKNLNYTVPVKGG---------KRQ----LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRkTAGVITGEILI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 91 NGMAMERDqMTRISSFLREFEINVKTFTAyddlyfmshfkmhrrttksekRQAvsdLLLAVGLRDaahtriqqLSGGERK 170
Cdd:cd03232 69 NGRPLDKN-FQRSTGYVEQQDVHSPNLTV---------------------REA---LRFSALLRG--------LSVEQRK 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 171 RLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLrhlctrRRIAKHSLtqvygedsfatpsdngssgsnsiemeivdn 250
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL------KKLADSGQ------------------------------ 159
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2492600 251 shesllqamkelptlgvlnnspngtqkkAAICSIHQPTSDIFELFTHIILMD-GGRIVYQG 310
Cdd:cd03232 160 ----------------------------AILCTIHQPSASIFEKFDRLLLLKrGGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-597 |
1.19e-33 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 138.32 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 10 GSLLLEWKQLNYYVPAqeqsnysfwnecrKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNL--TGD 87
Cdd:TIGR00956 756 GEDIFHWRNLTYEVKI-------------KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 88 VVLNGMAMErDQMTRISSFLREFEINVKTFTAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRI----QQ 163
Cdd:TIGR00956 823 RLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEG 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 164 LSGGERKRLSLAEELITDP-IFLFCDEPTTGLDSFSAYTVIKTLRHLctrrriAKHSltqvygedsfatpsdngssgsns 242
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKL------ADHG----------------------- 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 243 iemeivdnshesllqamkelptlgvlnnspngtqkKAAICSIHQPTSDIFELFTHIILMD-GGRIVYQGRTEQAAKFFTE 321
Cdd:TIGR00956 953 -----------------------------------QAILCTIHQPSAILFEEFDRLLLLQkGGQTVYFGDLGENSHTIIN 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 322 GFMQ------PKNCNPADFYLKTLADGQGSK----------NAGELLRAKYE-HETDGLYSGSWLLarNYSGDYMKHVQN 384
Cdd:TIGR00956 998 YFEKhgapkcPEDANPAEWMLEVIGAAPGAHanqdyhevwrNSSEYQAVKNElDRLEAELSKAEDD--NDPDALSKYAAS 1075
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 385 FkkirwIYQVYLLVIRFMTED-----------LANIRSGL-IGFGFFMTtavtlslmysgvgGLTQRTVQDVGGSIFMls 452
Cdd:TIGR00956 1076 L-----WYQFKLVLWRTFQQYwrtpdylyskfFLTIFAALfIGFTFFKV-------------GTSLQGLQNQMFAVFM-- 1135
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 453 neMIFTFSYGVTYIFPAALPIIR----REVAEGTYSLSAYYVALVLSFVPVAFFKGYMFLSVIYASI--YYT-------- 518
Cdd:TIGR00956 1136 --ATVLFNPLIQQYLPPFVAQRDlyevRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVgfYWNasktgqvh 1213
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 519 -RGFLLYitmgFLMSLSAIAAVGYGVFLSSLFETDKMASECAAPFDLIFLIFGGTYMNVDSVPllkYFSLFFYSNEALMY 597
Cdd:TIGR00956 1214 eRGVLFW----LLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMP---GFWIFMYRCSPFTY 1286
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
45-223 |
1.28e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVVLNGMAMERDQ-----MTRISSFLREFEINVKTFTA 119
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PTSGSIRVFGKPLEKERkrigyVPQRRSIDRDFPISVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 yddLYFMSHFKMHRRTTKSEKRqAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSA 199
Cdd:cd03235 93 ---MGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180
....*....|....*....|....*..
gi 2492600 200 YTVIKTLRHLCTRRR---IAKHSLTQV 223
Cdd:cd03235 169 EDIYELLRELRREGMtilVVTHDLGLV 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-209 |
1.54e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVVLNGMAMERDQmTRI------SSFLREFEINVKTFT 118
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PTSGTVRLFGKPPRRAR-RRIgyvpqrAEVDWDFPITVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AyddLYFMSHFKMHRRTTKSEkRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:COG1121 99 L---MGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170
....*....|.
gi 2492600 199 AYTVIKTLRHL 209
Cdd:COG1121 175 EEALYELLREL 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-580 |
1.69e-27 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 119.18 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 12 LLLEWKQLNYYVPAQEQSNYSFWNECRKQrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN-LTGDVVL 90
Cdd:PLN03140 866 LAMSFDDVNYFVDMPAEMKEQGVTEDRLQ----LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRI 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 91 NGMAMERDQMTRISSFLREFEINVKTFTAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAV---GLRDA--AHTRIQQLS 165
Cdd:PLN03140 942 SGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVeldNLKDAivGLPGVTGLS 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 166 GGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHlctrrriakhsltqvygedsfatpsdngssgsnsiem 245
Cdd:PLN03140 1022 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN------------------------------------- 1064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 246 eIVDNShesllqamkelptlgvlnnspngtqkKAAICSIHQPTSDIFELFTHIILMD-GGRIVYQGRTEQAAKFFTEGFM 324
Cdd:PLN03140 1065 -TVDTG--------------------------RTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 325 Q-------PKNCNPADFYLKTladgqgSKNAGELlraKYEHETDGLYSGSWLLARN------------------YSGDYM 379
Cdd:PLN03140 1118 AipgvpkiKEKYNPATWMLEV------SSLAAEV---KLGIDFAEHYKSSSLYQRNkalvkelstpppgasdlyFATQYS 1188
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 380 KHV-QNFK----KIRWIYqvyllvirFMTEDLanirsGLIGFGFFMTTAVTLSLMYSGVGGlTQRTVQDVGGSIFMLSNE 454
Cdd:PLN03140 1189 QSTwGQFKsclwKQWWTY--------WRSPDY-----NLVRFFFTLAAALMVGTIFWKVGT-KRSNANDLTMVIGAMYAA 1254
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 455 MIFTFSYGVTYIFPAAL---PIIRREVAEGTYSLSAYYVALVLSFVPVAFFKGYMFLSVIYASIYYTRGFLLYITMGFLM 531
Cdd:PLN03140 1255 VLFVGINNCSTVQPMVAverTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFIS 1334
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2492600 532 SLSAIAAVGYGVFLSSLFETDKMASECAAPFDLIFLIFGGTYMNVDSVP 580
Cdd:PLN03140 1335 FFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIP 1383
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
45-210 |
2.03e-27 |
|
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: 110.27 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgnLT-GDVVLNGMAMERDQMTRISSFLRE--------FEInVK 115
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTsGEVRVDGTDISKLSEKELAAFRRRhigfvfqsFNL-LP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TFTAYDDLYFMSHFkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03255 96 DLTALENVELPLLL---AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170
....*....|....*
gi 2492600 196 SFSAYTVIKTLRHLC 210
Cdd:cd03255 173 SETGKEVMELLRELN 187
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
45-209 |
3.82e-27 |
|
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: 109.48 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQMTRISS------------FLREfei 112
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN-GLLGPTSGEVLVDGKDLTKLSLKELRRkvglvfqnpddqFFGP--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 nvktfTAYDDLYF-MSHFKMHRrttkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:cd03225 92 -----TVEEEVAFgLENLGLPE----EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170
....*....|....*...
gi 2492600 192 TGLDSFSAYTVIKTLRHL 209
Cdd:cd03225 163 AGLDPAGRRELLELLKKL 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
45-216 |
4.07e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.75 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGM---AMERDQMTRissfLREFEI------ 112
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG----GLDRptsGEVLIDGQdisSLSERELAR----LRRRHIgfvfqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 -N-VKTFTAYDDLYFMSHFkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:COG1136 95 fNlLPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180
....*....|....*....|....*.
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG1136 172 TGNLDSKTGEEVLELLRELNRELGTT 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
45-212 |
4.99e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.77 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMAMERDQ---MTRISSFLREFEINvKTFT 118
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL----GLLRptsGEVRVLGEDVARDPaevRRRIGYVPQEPALY-PDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYFMSHFkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:COG1131 90 VRENLRFFARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170
....*....|....
gi 2492600 199 AYTVIKTLRHLCTR 212
Cdd:COG1131 167 RRELWELLRELAAE 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
45-208 |
1.51e-26 |
|
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: 108.53 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNG---MAMERDQMTRI--------------SSfL 107
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-SGEILVDGqdiTGLSEKELYELrrrigmlfqggalfDS-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 108 REFEiNVktftayddLYFMshfKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:COG1127 98 TVFE-NV--------AFPL---REHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180
....*....|....*....|....
gi 2492600 188 DEPTTGLDSFSAYTV---IKTLRH 208
Cdd:COG1127 166 DEPTAGLDPITSAVIdelIRELRD 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-192 |
1.00e-25 |
|
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: 103.50 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGnLTGDVVLNGMAMERDQMT----RISSFLREFEINvKTFTAYD 121
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-TEGTILLDGQDLTDDERKslrkEIGYVFQDPQLF-PRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 122 DLYFMSHFKMHRRTTKSEKrqaVSDLLLAVGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
45-209 |
2.64e-25 |
|
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: 104.89 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMamERDQMTRISsfLREFEINV---------- 114
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGE--DISGLSEAE--LYRLRRRMgmlfqsgalf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFMshFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:cd03261 90 DSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170
....*....|....*
gi 2492600 195 DSFSAYTVIKTLRHL 209
Cdd:cd03261 168 DPIASGVIDDLIRSL 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
45-216 |
2.71e-25 |
|
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: 104.96 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAM-------ERDQMTRISSFLREFEInVKTF 117
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGTDInklkgkaLRQLRRQIGMIFQQFNL-IERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDD-----LYFMSHFK-MHRRTTKSEKRQAVSdLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:cd03256 94 SVLENvlsgrLGRRSTWRsLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180
....*....|....*....|....*
gi 2492600 192 TGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:cd03256 173 ASLDPASSRQVMDLLKRINREEGIT 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
56-220 |
3.52e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.12 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 56 GDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNG--MAMERDQMTRISSFLREFEINVKTFTAYDDLYFMSHFKMHR 133
Cdd:cd03263 28 GEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINGysIRTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLKGLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 134 RTtksEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:cd03263 107 KS---EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR 183
|
....*....
gi 2492600 214 RI--AKHSL 220
Cdd:cd03263 184 SIilTTHSM 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-598 |
5.40e-25 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 111.35 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNL---TGDVVLNGMAME--RDQMTRISSFLREFEI 112
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigvEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 NVKTFTAYDDLYFMSHFKM----HRRTTKSEKRQAVSDLLLAV-GLRdaaHTR--------IQQLSGGERKRLSLAEELI 179
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKTpqnrPDGVSREEYAKHIADVYMATyGLS---HTRntkvgndfVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 180 TDPIFLFCDEPTTGLDSFSAYTVIKTLRhlctrrriakhsltqvygedsfatpsdngssgsnsiemEIVDnshesllqam 259
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALK--------------------------------------TSAN---------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 260 kelptlgVLNNSPngtqkkaaICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQAAKFF-TEGFMQPKNCNPADFyLKT 338
Cdd:TIGR00956 258 -------ILDTTP--------LVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFeKMGFKCPDRQTTADF-LTS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 339 LADgqgskNAGELLRAKYEH---ETDGLYSGSWLLARNYS------GDYMKHVQNFKKIRWIYQV-------------YL 396
Cdd:TIGR00956 322 LTS-----PAERQIKPGYEKkvpRTPQEFETYWRNSPEYAqlmkeiDEYLDRCSESDTKEAYREShvakqskrtrpssPY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 397 LVIRFMTEDLANIRS-----GLIGFGFFMT-TAVTLSLMYSGVGGLTQRTVQDV---GGSIFMlsnEMIFTFSYGVTYIF 467
Cdd:TIGR00956 397 TVSFSMQVKYCLARNflrmkGNPSFTLFMVfGNIIMALILSSVFYNLPKNTSDFysrGGALFF---AILFNAFSSLLEIA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 468 P--AALPIIRREVAEGTYSLSAYYVALVLSFVPVAFFKGYMFLSVIYASIYYTR---GFLLYITMGFLMSLsaiAAVGYG 542
Cdd:TIGR00956 474 SmyEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRtagRFFFYLLILFICTL---AMSHLF 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 543 VFLSSLFETDKMASECAAPFDLIFLIFGGTYMNVDSVP----LLKYFSLFFYSNEALMYN 598
Cdd:TIGR00956 551 RSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLgwskWIYYVNPLAYAFESLMVN 610
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
45-314 |
7.21e-25 |
|
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: 103.97 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNG---MAMERDQMTRISSFLREFEINVKTFTAYD 121
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLKPSSGEVLLDGrdlASLSRRELARRIAYVPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 --DLYFMSHFKMHRRTTKsEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDsfsa 199
Cdd:COG1120 95 lvALGRYPHLGLFGRPSA-EDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 200 ytviktLRHlctrrriakhsltQVygedsfatpsdngssgsnsiemeivdnsheSLLQAMKELptlgvlnnspNGTQKKA 279
Cdd:COG1120 170 ------LAH-------------QL------------------------------EVLELLRRL----------ARERGRT 190
|
250 260 270
....*....|....*....|....*....|....*...
gi 2492600 280 AICSIHqptsDI---FELFTHIILMDGGRIVYQGRTEQ 314
Cdd:COG1120 191 VVMVLH----DLnlaARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
38-216 |
6.36e-24 |
|
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: 100.66 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMamERDQMTRISSFLREFEINV--- 114
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI-LGLLKPTSGSIIFDGK--DLLKLSRRLRKIRRKEIQMvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 -------KTFTAYDDLY--FMSHFKMHRrttKSEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGERKRLSLAEELITDPIF 184
Cdd:cd03257 90 dpmsslnPRMTIGEQIAepLRIHGKLSK---KEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190
....*....|....*....|....*....|..
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLT 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
38-310 |
1.24e-23 |
|
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: 99.26 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN--LTGDVVLNGMAM--ERDQMTRISSFLREFEIN 113
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsVEGDIHYNGIPYkeFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLYFmshfkmhrrttksekrqavsdlllAVGLRdaAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:cd03233 95 FPTLTVRETLDF------------------------ALRCK--GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 194 LDSFSAYTVIKTLRHLctrrriakhsltqvygedsfatpsdngssgsnsiemeivdnSHEsllqamkelptlgvlnnspn 273
Cdd:cd03233 149 LDSSTALEILKCIRTM-----------------------------------------ADV-------------------- 167
|
250 260 270
....*....|....*....|....*....|....*..
gi 2492600 274 gtQKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQG 310
Cdd:cd03233 168 --LKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
45-216 |
1.31e-23 |
|
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: 104.99 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLR--GNLTGDVVLNGMAM----ERDQMTRISSFLREFEINVKTFT 118
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhgGRISGEVLLDGRDLlelsEALRGRRIGMVFQDPMTQLNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYFMShfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:COG1123 101 VGDQIAEAL---ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT 177
|
170
....*....|....*...
gi 2492600 199 AYTVIKTLRHLCTRRRIA 216
Cdd:COG1123 178 QAEILDLLRELQRERGTT 195
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
45-209 |
9.97e-23 |
|
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: 97.40 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNL---TGDVVLNGMAMERDQMTRISS-----F------LreF 110
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLL----RLLNGLLkptSGEVLVDGKDITKKNLRELRRkvglvFqnpddqL--F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINVktftaYDDLYF-MSHFKMhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:COG1122 90 APTV-----EEDVAFgPENLGL----PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180
....*....|....*....|
gi 2492600 190 PTTGLDSFSAYTVIKTLRHL 209
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRL 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
45-215 |
1.40e-22 |
|
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: 97.24 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQ---MTRISSFLREFEInVKTFTAYD 121
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDVRKEPreaRRQIGVLPDERGL-YDRLTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 DLYFmshFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDP-IFLFcDEPTTGLDSFSAY 200
Cdd:COG4555 94 NIRY---FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPkVLLL-DEPTNGLDVMARR 169
|
170
....*....|....*
gi 2492600 201 TVIKTLRHLCTRRRI 215
Cdd:COG4555 170 LLREILRALKKEGKT 184
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
38-216 |
1.68e-22 |
|
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: 101.52 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLREFEI----- 112
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-SGSILFDGKDLTKLSRRSLRELRRRVQMvfqdp 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 ----NvKTFTAYDDLYFMshFKMHRRTTKSEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:COG1123 352 ysslN-PRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLIL 428
|
170 180
....*....|....*....|....*....
gi 2492600 188 DEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG1123 429 DEPTSALDVSVQAQILNLLRDLQRELGLT 457
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
45-216 |
1.20e-21 |
|
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: 92.50 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGM---AMERDQMTRISSFLRefeinvktftayd 121
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPSSGEILLDGKdlaSLSPKELARKIAYVP------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 dlyfmshfkmhrrttksekrQAVSdlllAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYT 201
Cdd:cd03214 80 --------------------QALE----LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170
....*....|....*
gi 2492600 202 VIKTLRHLCTRRRIA 216
Cdd:cd03214 136 LLELLRRLARERGKT 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-195 |
3.28e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.26 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGdLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNG---MAMeRDQMTRISSFLREfEINV-KTFTAY 120
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGqdvLKQ-PQKLRRRIGYLPQ-EFGVyPNFTVR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 121 DDLYFMSHFKmhrRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03264 91 EFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
37-216 |
4.10e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.80 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 37 CRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQMT----RIS-----SFL 107
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA-DLDPPTSGEIYLDGKPLSAMPPPewrrQVAyvpqePAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 108 reFEINVKTFTAYDDLYFMSHFKMHRrttksekrqaVSDLLLAVGLR-DAAHTRIQQLSGGERKRLSLAEELITDPIFLF 186
Cdd:COG4619 86 --WGGTVRDNLPFPFQLRERKFDRER----------ALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|
gi 2492600 187 CDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRA 183
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
37-216 |
2.48e-20 |
|
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: 89.46 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 37 CRKQRELgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGnLTGDVVLNGmameRDQMTRISSFLREF-----E 111
Cdd:COG4133 10 CRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNG----EPIRDAREDYRRRLaylghA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 INVK-TFTAYDDLYFmsHFKMHRRTTKSEkrqAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:COG4133 84 DGLKpELTVRENLRF--WAALYGLRADRE---AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|....*.
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAV 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-216 |
4.95e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 35 NECRKQRE----LGILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisqRLRGNL----TGDVVLNGMAMER-------DQ 99
Cdd:PRK11629 10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLL-----HLLGGLdtptSGDVIFNGQPMSKlssaakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 MTRISSFLREFEINVKTFTAYDDLYfMSHFKMHRRTTKSEKRqaVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELI 179
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVA-MPLLIGKKKPAEINSR--ALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2492600 180 TDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTA 198
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
411-598 |
1.73e-19 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 87.33 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 411 SGLIGFGFFMTTAVTLSLMYSGVGglTQRTVQDVGGSIFMLSNEMIFTFSYGVTYIFPAALPIIRREVAEGTYSLSAYYV 490
Cdd:pfam01061 15 LGLWRLIQPILMALIFGTLFGNLG--NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRELASPLYSPSAYVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 491 ALVLSFVPVAFFKGYMFLSVIYASIYYTRGFLLYITMGFLMSLSAIAAVGYGVFLSSLFETDKMASECAAPFDLIFLIFG 570
Cdd:pfam01061 93 AKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLS 172
|
170 180 190
....*....|....*....|....*....|..
gi 2492600 571 GTYMNVDSVPL----LKYFSLFFYSNEALMYN 598
Cdd:pfam01061 173 GFFIPIDSMPVwwqwIYYLNPLTYAIEALRAN 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
46-209 |
1.84e-19 |
|
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: 87.27 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQ--MTRISSFlrefeINVKTFtaYDDL 123
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEITFDGKSYQKNIeaLRRIGAL-----IEAPGF--YPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 YFMSHFKMHRRTTKSEKrQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSaytvI 203
Cdd:cd03268 88 TARENLRLLARLLGIRK-KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG----I 162
|
....*.
gi 2492600 204 KTLRHL 209
Cdd:cd03268 163 KELREL 168
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
45-216 |
1.86e-19 |
|
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: 87.41 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisqRLRGNL----TGDVVLNGMAMERDQMTRISS-------FLREFEIN 113
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLL-----HLLGGLdnptSGEVLFNGQSLSKLSSNERAKlrnkklgFIYQFHHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDL---YFMSHFKmhrrttKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:TIGR02211 95 LPDFTALENVampLLIGKKS------VKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180
....*....|....*....|....*.
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTS 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
45-314 |
2.97e-19 |
|
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: 87.83 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLL--------------------------------------AAISQRLRGNLTG 86
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLslitgdlpptygndvrlfgerrggedvwelrkriglvsPALQLRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 87 -DVVLNGmamerdqmtrissflrefeinvktFTAYDDLYfmshfkmhRRTTKSEKRQAVsDLLLAVGLRDAAHTRIQQLS 165
Cdd:COG1119 98 lDVVLSG------------------------FFDSIGLY--------REPTDEQRERAR-ELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 166 GGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCtrrriAKHSLTQVYgedsfatpsdngssgsnsiem 245
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLA-----AEGAPTLVL--------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 246 eiVdnSHesllqamkelptlgvlnnspngtqkkaaicsiHQptSDIFELFTHIILMDGGRIVYQGRTEQ 314
Cdd:COG1119 199 --V--TH--------------------------------HV--EEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
45-213 |
4.21e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.52 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMA---MERDQMTRISSFLRE-----FEINVKT 116
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRPladWSPAELARRRAVLPQhsslsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 FTAyddlyfMShfKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELI------TDPIFLFCDEP 190
Cdd:PRK13548 96 VVA------MG--RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180
....*....|....*....|...
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHER 190
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
42-214 |
5.96e-19 |
|
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: 86.33 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAaisqrLRGNL----TGDVVLNG---MAMERDQMTRISS------FlR 108
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLG-----LLAGLdrptSGTVRLAGqdlFALDEDARARLRArhvgfvF-Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 109 EFEInVKTFTAYDD----LYFMSHfkmhrrttkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIF 184
Cdd:COG4181 98 SFQL-LPTLTALENvmlpLELAGR---------RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190
....*....|....*....|....*....|
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTLRHLcTRRR 214
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFEL-NRER 196
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
45-215 |
8.29e-19 |
|
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: 85.26 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNG------MAMERDqmtriSSFLREFEINVKTFT 118
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGrdvtgvPPERRN-----IGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLyfmsHFKM-HRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:cd03259 89 VAENI----AFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170
....*....|....*...
gi 2492600 198 SAYTVIKTLRHLCTRRRI 215
Cdd:cd03259 165 LREELREELKELQRELGI 182
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
46-195 |
1.05e-18 |
|
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: 87.06 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTrissfLREfEINV--KTFTAYDDL 123
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT-SGTARVAGYDVVREPRK-----VRR-SIGIvpQYASVDEDL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 124 YFMSHFKMHRR---TTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:TIGR01188 82 TGRENLEMMGRlygLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
45-215 |
1.33e-18 |
|
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: 83.06 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmamerdqmtrissflrefeinvktftayddly 124
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDG-------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 fmshfkmhrRTTKSEKRQAVSDLLLAVGlrdaahtriqQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIK 204
Cdd:cd00267 61 ---------KDIAKLPLEELRRRIGYVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170
....*....|.
gi 2492600 205 TLRHLCTRRRI 215
Cdd:cd00267 122 LLRELAEEGRT 132
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
46-207 |
1.77e-18 |
|
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: 85.08 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGM-AMERDQMTRISSFLREFEINVKTFTAYDDLY 124
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDSGTILFGGEdATDVPVQERNVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 F-MSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSfsayTVI 203
Cdd:cd03296 97 FgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA----KVR 172
|
....
gi 2492600 204 KTLR 207
Cdd:cd03296 173 KELR 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
45-210 |
1.86e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGM---AMERDQMtrisSFLReFEINVkTF---- 117
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT-SGQVLVNGQdlsRLKRREI----PYLR-RRIGV-VFqdfr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 -----TAYDDLYFMshfkMH-RRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:COG2884 90 llpdrTVYENVALP----LRvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170
....*....|....*....
gi 2492600 192 TGLDSFSAYTVIKTLRHLC 210
Cdd:COG2884 166 GNLDPETSWEIMELLEEIN 184
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
46-227 |
3.56e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVvlngmamERDQMTRI------SSFLREFEINVKtfta 119
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-PTSGTV-------RRAGGARVayvpqrSEVPDSLPLTVR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 ydDLYFM---SHFKMHRRTTKsEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:NF040873 76 --DLVAMgrwARRGLWRRLTR-DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 197 FSAYTVIKTLRHLCTRRR---IAKHSLTQVYGED 227
Cdd:NF040873 153 ESRERIIALLAEEHARGAtvvVVTHDLELVRRAD 186
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
46-215 |
5.43e-18 |
|
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: 83.40 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlrgNL-----TGDVVLNGmameRDqMTRISSF-LREFEINV----K 115
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI------NGlerptSGSVLVDG----TD-LTLLSGKeLRKARRRIgmifQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TF------TAYDDLYFmsHFKMHRrTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:cd03258 90 HFnllssrTVFENVAL--PLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180
....*....|....*....|....*.
gi 2492600 190 PTTGLDSFSAYTVIKTLRHLCTRRRI 215
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRELGL 192
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
32-195 |
8.06e-18 |
|
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: 83.31 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 32 SFWNECRKQRelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERD---------QMT- 101
Cdd:COG1124 10 SYGQGGRRVP---VLKDVSLEVAPGESFGLVGESGSGKSTLLRALA-GLERPWSGEVTFDGRPVTRRrrkafrrrvQMVf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 102 -----------RISSFLREfeinvktftayddlyfmsHFKMHRRTtksEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGER 169
Cdd:COG1124 86 qdpyaslhprhTVDRILAE------------------PLRIHGLP---DREERIAELLEQVGLpPSFLDRYPHQLSGGQR 144
|
170 180
....*....|....*....|....*.
gi 2492600 170 KRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALD 170
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
45-197 |
8.25e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNL---TGDVVLNGMAMERDQMTRISSF--------Lrefein 113
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIA----GFLapsSGEITLDGVPVTGPGADRGVVFqkdallpwL------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 vktfTAYDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:COG4525 92 ----NVLDNVAF--GLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
....
gi 2492600 194 LDSF 197
Cdd:COG4525 165 LDAL 168
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
45-207 |
1.61e-17 |
|
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: 86.26 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAMERDQMTRISSFLREFEINVKTF--TAYDD 122
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATL-AGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFdtTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMshfkmhrRTTKSEkrQAVSDLLLAVGL-------RDAAHTRIQQ----LSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:TIGR02868 429 LRLA-------RPDATD--EELWAALERVGLadwlralPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPT 499
|
170
....*....|....*.
gi 2492600 192 TGLDSFSAYTVIKTLR 207
Cdd:TIGR02868 500 EHLDAETADELLEDLL 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-212 |
3.31e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTllaaISQRLRGNLTGDV----VLNGMAMERDQMTRIS-SFLREFEINVKTFTA 119
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKST----IARMILGMTSPDAgkitVLGVPVPARARLARARiGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YDDLY-FMSHFKMHRRTTKSekrqAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:PRK13536 132 RENLLvFGRYFGMSTREIEA----VIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170
....*....|....
gi 2492600 199 AYTVIKTLRHLCTR 212
Cdd:PRK13536 208 RHLIWERLRSLLAR 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-207 |
3.48e-17 |
|
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: 80.91 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLREFEINVKTF------TA 119
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFrllpdrNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YDDLYFMSHFKMHRRttkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSA 199
Cdd:cd03292 96 YENVAFALEVTGVPP---REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
....*...
gi 2492600 200 YTVIKTLR 207
Cdd:cd03292 173 WEIMNLLK 180
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-195 |
6.78e-17 |
|
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: 79.32 E-value: 6.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVVLNG--MAMERDQMTRISSFLREFEINVKTFTA 119
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR-PDSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492600 120 YDDLYFMSHFkmHRRTtksekRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:TIGR01189 91 LENLHFWAAI--HGGA-----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
48-221 |
8.09e-17 |
|
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: 80.17 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmamerdqmTRISSfLREFEIN----VKTF------ 117
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDG--------EDITG-LPPHEIArlgiGRTFqiprlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 ---TAYDDLYFMSHFKMHR-------RTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:cd03219 88 pelTVLENVMVAAQARTGSglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 188 DEPTTGLDSFSAYTVIKTLrhlctrRRIAKHSLT 221
Cdd:cd03219 168 DEPAAGLNPEETEELAELI------RELRERGIT 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
46-215 |
8.86e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 79.82 E-value: 8.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMAMERDQMTRISSFLrefeiNVKTF---TAYDD 122
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPTSGGVILEGKQITEPGPDRMVVFQ-----NYSLLpwlTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMSHFKMHRRTtKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:TIGR01184 75 IALAVDRVLPDLS-KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170
....*....|...
gi 2492600 203 IKTLRHLCTRRRI 215
Cdd:TIGR01184 154 QEELMQIWEEHRV 166
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
46-195 |
1.10e-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: 81.64 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNL--TGDVVLNG---MAMERDQMTRI-------------SSF- 106
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitSGEILFDGedlLKLSEKELRKIrgreiqmifqdpmTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 107 --------LREFeinvktftayddlyfmshFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHtRIQ----QLSGGERKRLSL 174
Cdd:COG0444 101 pvmtvgdqIAEP------------------LRIHGGLSKAEARERAIELLERVGLPDPER-RLDryphELSGGMRQRVMI 161
|
170 180
....*....|....*....|.
gi 2492600 175 AEELITDPIFLFCDEPTTGLD 195
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD 182
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
48-195 |
1.13e-16 |
|
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: 79.34 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMT---RISSFLREFEINvKTFTAYDDLY 124
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAGHDVVREPREvrrRIGIVFQDLSVD-DELTGWENLY 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492600 125 fmshfkMHRR---TTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03265 96 ------IHARlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
45-197 |
1.15e-16 |
|
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: 79.44 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMAMERDQMTRISSF----LrefeinvktF 117
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA----GLERptsGEVLVDGEPVTGPGPDRGYVFqqdaL---------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 ---TAYDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:cd03293 86 pwlTVLDNVAL--GLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
...
gi 2492600 195 DSF 197
Cdd:cd03293 163 DAL 165
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
45-209 |
1.40e-16 |
|
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: 78.23 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQmtrisSFLREFEINVKT-FTAYDDL 123
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ-SGAVLIDGEPLDYSR-----KGLLERRQRVGLvFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 YF-------MSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:TIGR01166 81 LFaadvdqdVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170
....*....|...
gi 2492600 197 FSAYTVIKTLRHL 209
Cdd:TIGR01166 161 AGREQMLAILRRL 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
45-209 |
1.51e-16 |
|
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: 77.82 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVVLNGMAMERDQmtrissflrefeINVKTFTAY--DD 122
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIKVLGKDIKKEP------------EEVKRRIGYlpEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMSHFKmhrrttksekrqaVSDLLlavglrdaahtriqQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:cd03230 82 PSLYENLT-------------VRENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
....*..
gi 2492600 203 IKTLRHL 209
Cdd:cd03230 135 WELLREL 141
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
45-213 |
1.83e-16 |
|
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: 82.89 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGM---AMERDQMTRISSF-----------LREf 110
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLDPQSGSITLGGVdlrDLDEDDLRRRIAVvpqrphlfdttLRE- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 eiNVKTftAYDDLyfmshfkmhrrtTKSEKRQAvsdlLLAVGLRDAA-------HTRI----QQLSGGERKRLSLAEELI 179
Cdd:COG4987 428 --NLRL--ARPDA------------TDEELWAA----LERVGLGDWLaalpdglDTWLgeggRRLSGGERRRLALARALL 487
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 180 TDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALAGR 521
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
45-195 |
3.89e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.53 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGmameRDqMTRISSFLRefeiNVKT----- 116
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA----GFETpdsGRILLDG----RD-VTGLPPEKR----NVGMvfqdy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 --F---TAYDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDP-IFLFcDEP 190
Cdd:COG3842 87 alFphlTVAENVAF--GLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPrVLLL-DEP 162
|
....*
gi 2492600 191 TTGLD 195
Cdd:COG3842 163 LSALD 167
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-213 |
4.03e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.14 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 32 SFWNecRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmameRDQMTRISSFLREFE 111
Cdd:cd03267 25 SLFK--RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-SGEVRVAG----LVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 I--NVKTFTAYDdLYFMSHFKMHR---RTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLF 186
Cdd:cd03267 98 VvfGQKTQLWWD-LPVIDSFYLLAaiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180
....*....|....*....|....*..
gi 2492600 187 CDEPTTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRER 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
45-210 |
4.27e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMER---DQMTRISSFLR-EFEINVKtFTAY 120
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RLLPPDSGEVLVDGLDVATtpsRELAKRLAILRqENHINSR-LTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 121 DDLYFmSHFKMHR-RTTKsEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKR----LSLAEEliTDPIFLfcDEPTTGLD 195
Cdd:COG4604 94 ELVAF-GRFPYSKgRLTA-EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafiaMVLAQD--TDYVLL--DEPLNNLD 167
|
170
....*....|....*
gi 2492600 196 SFSAYTVIKTLRHLC 210
Cdd:COG4604 168 MKHSVQMMKLLRRLA 182
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-223 |
4.36e-16 |
|
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: 77.99 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNL-----TGDVVLNGMAMERDQMTRISsfLRE-----FEI-N 113
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIpgapdEGEVLLDGKDIYDLDVDVLE--LRRrvgmvFQKpN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLYFmsHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQ--QLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:cd03260 92 PFPGSIYDNVAY--GLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 192 TGLDSFSAYTVIKTLRHLCTRRRI--AKHSLTQV 223
Cdd:cd03260 170 SALDPISTAKIEELIAELKKEYTIviVTHNMQQA 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
56-224 |
4.88e-16 |
|
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: 77.34 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 56 GDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMerdQMTRISSFL--REFEI-----NVKTF---TAYDDLYF 125
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPD-GGTIVLNGTVL---FDSRKKINLppQQRKIglvfqQYALFphlNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MShfkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKT 205
Cdd:cd03297 99 GL-----KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180
....*....|....*....|...
gi 2492600 206 LRHLCTRRRI----AKHSLTQVY 224
Cdd:cd03297 174 LKQIKKNLNIpvifVTHDLSEAE 196
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
45-209 |
1.33e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.67 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMeRDQMTRISSFLREFEINVKTF------T 118
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN-KLEEITSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQFylfphlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYFMShfkMH-RRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:PRK09493 94 ALENVMFGP---LRvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170
....*....|..
gi 2492600 198 SAYTVIKTLRHL 209
Cdd:PRK09493 171 LRHEVLKVMQDL 182
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
45-195 |
2.04e-15 |
|
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: 76.12 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGmamerDQMTRISSFLREFEI---NVKTF- 117
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETptsGEILLDG-----KDITNLPPHKRPVNTvfqNYALFp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 --TAYDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03300 86 hlTVFENIAF--GLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
39-334 |
2.67e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 80.28 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 39 KQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNL--TGDVVLNGMAMERDQMTRISSFLREFEINVKT 116
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLkvSGEITYNGYRLNEFVPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 FTAYDDLYFMSHFK------------------------------MHRRTTKSEKRQAVSDLLLAV-GLRDAAHT-----R 160
Cdd:PLN03140 254 MTVKETLDFSARCQgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDYTLKIlGLDICKDTivgdeM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 161 IQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHlctrrriakhsltqvygedsfatpsdngssgs 240
Cdd:PLN03140 334 IRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQ-------------------------------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 241 nsiemeIVDNSHESLLQamkelptlgvlnnspngtqkkaaicSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQAAKFF- 319
Cdd:PLN03140 382 ------IVHLTEATVLM-------------------------SLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFe 430
|
330
....*....|....*
gi 2492600 320 TEGFMQPKNCNPADF 334
Cdd:PLN03140 431 SCGFKCPERKGTADF 445
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
45-195 |
2.71e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLT--GDVVLNGmameRDqMTRISSFLRE----FEinvktft 118
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSasGEVLLNG----RR-LTALPAEQRRigilFQ------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 ayDDLYF--MS-----HFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:COG4136 84 --DDLLFphLSvgenlAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 2492600 192 TGLD 195
Cdd:COG4136 162 SKLD 165
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
45-224 |
4.39e-15 |
|
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: 73.76 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGmamerDQMTRISSFLREFEINVKTftAYDDLY 124
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI-AGLEEPDSGSILIDG-----EDLTDLEDELPPLRRRIGM--VFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFkmhrrttksekrQAVSDLLLAvglrdaahtriqqLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIK 204
Cdd:cd03229 87 LFPHL------------TVLENIALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180
....*....|....*....|
gi 2492600 205 TLRHLCtrrriAKHSLTQVY 224
Cdd:cd03229 142 LLKSLQ-----AQLGITVVL 156
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
45-221 |
4.59e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNL---TGDVVLNGMAMERDQMTRISSFL-REFEiNVKTFTAY 120
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA----GSLppdSGSILIDGKDVTKLPEYKRAKYIgRVFQ-DPMMGTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 121 DdlyfMS-------------HFKMHRRTTKSEK---RQAVSDLLLavGLRDAAHTRIQQLSGGERKRLSLAEELITDPIF 184
Cdd:COG1101 96 S----MTieenlalayrrgkRRGLRRGLTKKRRelfRELLATLGL--GLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTlrhlcTRRRIAKHSLT 221
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLEL-----TEKIVEENNLT 201
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
45-216 |
6.80e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.13 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMAMERDQMTRisSFLrefeinvktF---- 117
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA----GLEKptsGEVLVDGKPVTGPGPDR--GVV---------Fqepa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 -----TAYDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:COG1116 91 llpwlTVLDNVAL--GLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180
....*....|....*....|....
gi 2492600 193 GLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKT 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
46-195 |
7.52e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.27 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlrgNL-----TGDVVLNGmameRDqMTRISSF-LRE--------FE 111
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI------NLlerptSGSVLVDG----VD-LTALSEReLRAarrkigmiFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 invktftayddlyfmsHFK-MHRRT--------------TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAE 176
Cdd:COG1135 90 ----------------HFNlLSSRTvaenvalpleiagvPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170
....*....|....*....
gi 2492600 177 ELITDPIFLFCDEPTTGLD 195
Cdd:COG1135 154 ALANNPKVLLCDEATSALD 172
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
39-212 |
1.00e-14 |
|
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: 74.23 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 39 KQRElgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNG-----MAMERDQMTRISSFLREFEIn 113
Cdd:TIGR04406 12 KKRK--VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-AGKILIDGqdithLPMHERARLGIGYLPQEASI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLyfMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:TIGR04406 88 FRKLTVEENI--MAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170
....*....|....*....
gi 2492600 194 LDSFSAYTVIKTLRHLCTR 212
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKER 184
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
46-216 |
2.82e-14 |
|
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: 73.15 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmameRDqMTRissfLREFEIN----VKTF---- 117
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-SGRILFDG----RD-ITG----LPPHRIArlgiARTFqnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 -----TAYDDL----------YFMSHFKMHRRTTKSEK--RQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELIT 180
Cdd:COG0411 90 lfpelTVLENVlvaaharlgrGLLAALLRLPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2492600 181 DPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEETEELAELIRRLRDERGIT 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-194 |
3.54e-14 |
|
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: 72.08 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGmameRDqMTRISSFLRefeinVK------ 115
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIM----GLLPprsGSIRFDG----RD-ITGLPPHER-----ARagigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 --------TFTAYDDLyfmshfKMHRRTTKSEKRQAVSDLLLAV--GLRDAAHTRIQQLSGGERKRLSLAEELITDPIFL 185
Cdd:cd03224 81 pegrrifpELTVEENL------LLGAYARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
....*....
gi 2492600 186 FCDEPTTGL 194
Cdd:cd03224 155 LLDEPSEGL 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
46-210 |
4.08e-14 |
|
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: 72.02 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERD--QMTRISSFLREFEINVKTFTAYDDL 123
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFDVVKEpaEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 -YFMSHFKMHRRttksEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:cd03266 100 eYFAGLYGLKGD----ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
....*...
gi 2492600 203 IKTLRHLC 210
Cdd:cd03266 176 REFIRQLR 183
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
45-213 |
4.33e-14 |
|
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: 70.49 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGmamerdqmtrissflrefeINVKTFTayddly 124
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-RLYDPTSGEILIDG-------------------VDLRDLD------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 fmshfkmhrrttKSEKRQAVS-----DLLLAVGLRDaahtRIqqLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSA 199
Cdd:cd03228 71 ------------LESLRKNIAyvpqdPFLFSGTIRE----NI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170
....*....|....
gi 2492600 200 YTVIKTLRHLCTRR 213
Cdd:cd03228 133 ALILEALRALAKGK 146
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
46-209 |
4.55e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN--------LTGDVVLNGMAMERD-QMTRISS--FLREFEInV 114
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshieLLGRTVQREGRLARDiRKSRANTgyIFQQFNL-V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDL---------YFMSHFKMHRRTTKSEKRQAvsdlLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFL 185
Cdd:PRK09984 99 NRLSVLENVligalgstpFWRTCFSWFTREQKQRALQA----LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180
....*....|....*....|....
gi 2492600 186 FCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDI 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
45-207 |
6.66e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMAMER-DQMTRISSFLREFEINVKTFTAYDDL 123
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQTSGHIRFHGTDVSRlHARDRKVGFVFQHYALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 YF-MSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSfsayTV 202
Cdd:PRK10851 96 AFgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA----QV 171
|
....*
gi 2492600 203 IKTLR 207
Cdd:PRK10851 172 RKELR 176
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
45-209 |
7.62e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTT---LLAAISQRLRGNLT-GDVVLNGMAMERDQMTRISSFLREFEInVKTFTAY 120
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIiDDEDISLLPLHARARRGIGYLPQEASI-FRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 121 DDLyfMSHFKMhRRTTKSEKRQAVSDLLLA----VGLRDAAHtriQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:PRK10895 97 DNL--MAVLQI-RDDLSAEQREDRANELMEefhiEHLRDSMG---QSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170
....*....|...
gi 2492600 197 FSAYTVIKTLRHL 209
Cdd:PRK10895 171 ISVIDIKRIIEHL 183
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
45-223 |
8.45e-14 |
|
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: 74.41 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAME-------RDQMTRISS----F---LREf 110
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-GFLPPYSGSILINGVDLSdldpaswRRQIAWVPQnpylFagtIRE- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 eiNVktftaydDLYfmshfkmHRRTTKSEKRQAvsdlLLAVGLRD--AA-----HTRI----QQLSGGERKRLSLAEELI 179
Cdd:COG4988 430 --NL-------RLG-------RPDASDEELEAA----LEAAGLDEfvAAlpdglDTPLgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2492600 180 TD-PIFLFcDEPTTGLDSFSAYTVIKTLRHLCTRRR--IAKHSLTQV 223
Cdd:COG4988 490 RDaPLLLL-DEPTAHLDAETEAEILQALRRLAKGRTviLITHRLALL 535
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
45-198 |
9.53e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMAMERDQMTRISSFLREFEI---NVKTFT 118
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIA----GFVPyqhGSITLDGKPVEGPGAERGVVFQNEGLLpwrNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYD-DLYFMShfkmhrrttKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:PRK11248 92 AFGlQLAGVE---------KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
.
gi 2492600 198 S 198
Cdd:PRK11248 163 T 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-212 |
1.20e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisqRLRGNLT----GDVVLNGMAM-ERDQMTRIS-SFLREFEINVKTFT 118
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTL-----RMLLGLThpdaGSISLCGEPVpSRARHARQRvGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLY-FMSHFKMhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:PRK13537 97 VRENLLvFGRYFGL----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170
....*....|....*
gi 2492600 198 SAYTVIKTLRHLCTR 212
Cdd:PRK13537 173 ARHLMWERLRSLLAR 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-195 |
1.33e-13 |
|
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: 70.83 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 35 NECRKQRELgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmamerDQMTRISSFLREFEInv 114
Cdd:cd03299 5 NLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNG-----KDITNLPPEKRDISY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 ktftAYDDLYFMSHFKM---------HRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFL 185
Cdd:cd03299 76 ----VPQNYALFPHMTVykniayglkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170
....*....|
gi 2492600 186 FCDEPTTGLD 195
Cdd:cd03299 152 LLDEPFSALD 161
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-195 |
1.33e-13 |
|
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: 70.25 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQmTRISSFLREFEINVKTF------T 118
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-LLEEPDSGTIIIDGLKLTDDK-KNINELRQKVGMVFQQFnlfphlT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 119 AYDDLYF--MSHFKMhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03262 93 VLENITLapIKVKGM----SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
46-195 |
2.39e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmameRDQMTRissflrefeinvktftaydDLYF 125
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVHYRM----RDGQLR-------------------DLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKMhRRTTKSE-----------KRQAVS------DLLLAVG------LRDAAH----------TRIQQL----SGGE 168
Cdd:PRK11701 78 LSEAER-RRLLRTEwgfvhqhprdgLRMQVSaggnigERLMAVGarhygdIRATAGdwlerveidaARIDDLpttfSGGM 156
|
170 180
....*....|....*....|....*..
gi 2492600 169 RKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
45-209 |
3.01e-13 |
|
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: 69.21 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLREfeinvktfTAYDDLY 124
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-SGSILLNGKPIKAKERRKSIGYVMQ--------DVDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFKMHRRTTK--SEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:cd03226 86 TDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
....*..
gi 2492600 203 IKTLRHL 209
Cdd:cd03226 166 GELIREL 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
52-195 |
4.06e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.11 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 52 HLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLREFEINVKTFTAYDDLYFMShfKM 131
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLC--GL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492600 132 HRRttksEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK13543 110 HGR----RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
38-216 |
4.81e-13 |
|
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: 72.02 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrLRgnL---TGDVVLNGM---AMERDQMTRissFLREFE 111
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL---LR--LipsEGEIRFDGQdldGLSRRALRP---LRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 InVktftayddlyF----------MS-----------HfkmHRRTTKSEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGER 169
Cdd:COG4172 366 V-V----------FqdpfgslsprMTvgqiiaeglrvH---GPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQR 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2492600 170 KRLSLAEELITDPIFLFCDEPTTGLD-SFSAyTVIKTLRHLCTRRRIA 216
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDvSVQA-QILDLLRDLQREHGLA 478
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-195 |
5.01e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGnLTGDVVLNgmamerdQMTRISSF---LREFEINVktfTAYD 121
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP-DSGTVKLG-------ETVKIGYFdqhQEELDPDK---TVLD 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 122 DLyfmshfkmhRRTTKSEKRQAVSDLLLAVGLR-DAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:COG0488 399 EL---------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
46-223 |
6.04e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLREFEINVKTFTAY-DDLY 124
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLvEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMS---HFKMHRRTtKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYT 201
Cdd:PRK15056 102 MMGrygHMGWLRRA-KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|....*
gi 2492600 202 VIKTLRHLCTRRR---IAKHSLTQV 223
Cdd:PRK15056 181 IISLLRELRDEGKtmlVSTHNLGSV 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-215 |
6.53e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVlngmAMERDQMTRISSFLrefeinvktftayDDLY 124
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV----DVPDNQFGREASLI-------------DAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFKmhrrttksekrQAVsDLLLAVGLRDAA--HTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:COG2401 108 RKGDFK-----------DAV-ELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170
....*....|...
gi 2492600 203 IKTLRHLCTRRRI 215
Cdd:COG2401 176 ARNLQKLARRAGI 188
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
45-213 |
6.77e-13 |
|
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: 71.79 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAME-------RDQmtrISSFLREFEInvktF 117
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLL-LGLYEPTSGRILIDGIDLRqidpaslRRQ---IGVVLQDVFL----F 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 --TAYDDLYFMshfkmHRRTTKSEKRQAVSDlllaVGLRDAA-------HTRI----QQLSGGERKRLSLAEELITDPIF 184
Cdd:COG2274 562 sgTIRENITLG-----DPDATDEEIIEAARL----AGLHDFIealpmgyDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180
....*....|....*....|....*....
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKGR 661
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
45-196 |
1.11e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGnLTGDVVLNGMAMERDQMTRISSFL--REFeinVK-TFTAYD 121
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLghRNA---MKpALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492600 122 DLYFMSHFKMHRRTtksekrqAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITD-PIFLFcDEPTTGLDS 196
Cdd:PRK13539 93 NLEFWAAFLGGEEL-------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNrPIWIL-DEPTAALDA 160
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-195 |
1.11e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 40 QRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGM---AMERDQMTRISS----FLREFEI 112
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQplhQMDEEARAKLRAkhvgFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 NVKTFTAYDDLYFMShfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:PRK10584 99 LIPTLNALENVELPA---LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
...
gi 2492600 193 GLD 195
Cdd:PRK10584 176 NLD 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
45-206 |
1.35e-12 |
|
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: 66.57 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNL---TGDVVLNG--MAMERDQMTRISSFLREfeinvktfta 119
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLL----QLLTGDLkpqQGEITLDGvpVSDLEKALSSLISVLNQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 yddlyfmshfKMHrrttksekrqavsdlLLAVGLRDAAHTRiqqLSGGERKRLSLAEELITD-PIFLFcDEPTTGLDSFS 198
Cdd:cd03247 83 ----------RPY---------------LFDTTLRNNLGRR---FSGGERQRLALARILLQDaPIVLL-DEPTVGLDPIT 133
|
....*...
gi 2492600 199 AYTVIKTL 206
Cdd:cd03247 134 ERQLLSLI 141
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
45-209 |
1.42e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN-------LTGDVVLNG---MAMERDQMTRISSFLREFEINV 114
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarVTGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAyDDLYFMSHFKMHRRTTKSEKR-QAVSDLLLAVGLRDAAHTR-IQQLSGGERKRLSLAEEL---------ITDPI 183
Cdd:PRK13547 96 FAFSA-REIVLLGRYPHARRAGALTHRdGEIAWQALALAGATALVGRdVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180
....*....|....*....|....*.
gi 2492600 184 FLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
45-209 |
1.58e-12 |
|
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: 67.57 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTR-----ISSFLREFEInVKTFTA 119
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGKILLDGQDITKLPMHKrarlgIGYLPQEASI-FRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YDDLYFMSHFkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSA 199
Cdd:cd03218 93 EENILAVLEI---RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170
....*....|
gi 2492600 200 YTVIKTLRHL 209
Cdd:cd03218 170 QDIQKIIKIL 179
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
49-195 |
1.96e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNltGDVVLNGMAMER---DQMTRISSFLRE-----FEINVktFtAY 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ--GEILLNGRPLSDwsaAELARHRAYLSQqqsppFAMPV--F-QY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 121 DDLYfmshfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELIT-------DPIFLFCDEPTTG 193
Cdd:COG4138 90 LALH------QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
..
gi 2492600 194 LD 195
Cdd:COG4138 164 LD 165
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-195 |
2.10e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRL---------RGNLT----------------GDVVLNGMAMERDQ 99
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELepdsgevsiPKGLRigylpqeppldddltvLDTVLDGDAELRAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 MTRISSFLREFEINVKTFTAYDDLyfmsHFKMHRR---TTKSEkrqaVSDLLLAVGLRDAAHTR-IQQLSGGERKRLSLA 175
Cdd:COG0488 93 EAELEELEAKLAEPDEDLERLAEL----QEEFEALggwEAEAR----AEEILSGLGFPEEDLDRpVSELSGGWRRRVALA 164
|
170 180
....*....|....*....|
gi 2492600 176 EELITDPIFLFCDEPTTGLD 195
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
46-209 |
2.77e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQmtrisSFLREFEINVK-TFTAYDDLY 124
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT-SGEVLIKGEPIKYDK-----KSLLEVRKTVGiVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFK-------MHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:PRK13639 92 FAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170
....*....|..
gi 2492600 198 SAYTVIKTLRHL 209
Cdd:PRK13639 172 GASQIMKLLYDL 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
45-209 |
2.88e-12 |
|
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: 66.15 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISsFLREFEINVKTFTAYDDL- 123
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMKVIDQLv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 YFMSHFKMhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVI 203
Cdd:cd03269 93 YLAQLKGL----KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
....*.
gi 2492600 204 KTLRHL 209
Cdd:cd03269 169 DVIREL 174
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
39-195 |
4.05e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 39 KQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlrgNL-----TGDVVLNGmameRDQMTRISSFLREFEIN 113
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI------NLlerptSGRVLVDG----QDLTALSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 V----KTF------TAYDDLYF---MSHfkmhrrTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELIT 180
Cdd:PRK11153 84 IgmifQHFnllssrTVFDNVALpleLAG------TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170
....*....|....*
gi 2492600 181 DPIFLFCDEPTTGLD 195
Cdd:PRK11153 158 NPKVLLCDEATSALD 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
46-220 |
4.46e-12 |
|
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: 68.85 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAME-------RDQMTRISSFLREFEINVKTFT 118
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLL-GFVDPTEGSIAVNGVPLAdadadswRDQIAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYfmshfkmhrrTTKSEKRQAVSD---LLLAVGLRDAAHTRIQQ----LSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:TIGR02857 417 RLARPD----------ASDAEIREALERaglDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|.
gi 2492600 192 TGLDSFSAYTVIKTLRHLCTRRR--IAKHSL 220
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGRTvlLVTHRL 517
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-223 |
4.48e-12 |
|
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: 66.36 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGmameRDQMTRISSFLRE-----FEINVKTFTA 119
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI-QRFYVPENGRVLVDG----HDLALADPAWLRRqvgvvLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YDDLYFMSHFKMHRRTTKSEKRQA-----VSDLLLA----VGLRDAAhtriqqLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAgahdfISELPEGydtiVGEQGAG------LSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRRR--IAKHSLTQV 223
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTviIIAHRLSTV 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
45-198 |
5.59e-12 |
|
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: 63.62 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVvlngmamERDQMTRISsflrefeinvktftayddlY 124
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE-PDEGIV-------TWGSTVKIG-------------------Y 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492600 125 FmshfkmhrrttksekrqavsdlllavglrdaahtriQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:cd03221 68 F------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
39-212 |
7.12e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.82 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 39 KQRElgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTR-----IS------SFL 107
Cdd:COG1137 14 GKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGRIFLDGEDITHLPMHKrarlgIGylpqeaSIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 108 REFeinvktfTAYDDLyfMSHFKMHRRTtKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:COG1137 91 RKL-------TVEDNI--LAVLELRKLS-KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180
....*....|....*....|....*
gi 2492600 188 DEPTTGLDSFSAYTVIKTLRHLCTR 212
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKER 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
38-216 |
7.83e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLlaaisQRLRGNL----TGDVVLNGMAMERDQMTRISSFLRE---- 109
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL-----ARLLVGLespsQGNVSWRGEPLAKLNRAQRKAFRRDiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 110 FEINVKTFTAYDDLYFMSHFKMHRRTTKSEKRQA--VSDLLLAVGLRDA-AHTRIQQLSGGERKRLSLAEELITDPIFLF 186
Cdd:PRK10419 95 FQDSISAVNPRKTVREIIREPLRHLLSLDKAERLarASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190
....*....|....*....|....*....|
gi 2492600 187 CDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTA 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
45-195 |
8.60e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.81 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMER---DQMTRISSFLREFE-----INVKT 116
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQSGTVFLGDKPISMlssRQLARRLALLPQHHltpegITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 FTAYDDLYFMSHFKmhRRTTKSEKR--QAVSDLllavGLRDAAHTRIQQLSGGERKRLSLAEELITD-PIFLFcDEPTTG 193
Cdd:PRK11231 96 LVAYGRSPWLSLWG--RLSAEDNARvnQAMEQT----RINHLADRRLTDLSGGQRQRAFLAMVLAQDtPVVLL-DEPTTY 168
|
..
gi 2492600 194 LD 195
Cdd:PRK11231 169 LD 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
45-230 |
9.59e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI-------SQRLRgnlTGDVVLNGMAMERDQMTRISSFLREFEINVKTF 117
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIR---VGDITIDTARSLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDDLYFMSHFKMHRRTTKSEKRQAVS----DLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2492600 194 LDSFSAYTVIKTLRHLCTRRRiakhSLTQVYGEDSFA 230
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKR----TMVIVTHEMSFA 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
46-195 |
1.01e-11 |
|
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: 65.74 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMErdQMTRisSFLREfeINVKTFTayddLYF 125
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCIN-RLIEPTSGKVLIDGQDIA--AMSR--KELRE--LRRKKIS----MVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKMHRRTT--------------KSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:cd03294 109 QSFALLPHRTVlenvafglevqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
....
gi 2492600 192 TGLD 195
Cdd:cd03294 189 SALD 192
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-195 |
1.03e-11 |
|
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: 64.44 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRgNLTGDVVLNGMAMERDQMTRISSFLREFEIN-VKT-FTA 119
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-PLAGRVLLNGGPLDFQRDSIARGLLYLGHAPgIKTtLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492600 120 YDDLYFMSHFkmhrrttksEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03231 91 LENLRFWHAD---------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
52-195 |
1.07e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.16 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 52 HLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGmameRDqMTRISSFLREFEI-----NVktF---TAY 120
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIA----GFLPpdsGRILWNG----QD-LTALPPAERPVSMlfqenNL--FphlTVA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492600 121 DDLYFMSHFKMHRRttkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITD-PIFLFcDEPTTGLD 195
Cdd:COG3840 90 QNIGLGLRPGLKLT---AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKrPILLL-DEPFSALD 161
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-212 |
1.18e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLL---------AAISQRLRGNltgDVVlngmAMERDQMTRISsflRE---Fei 112
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMnilgcldkpTSGTYRVAGQ---DVA----TLDADALAQLR---REhfgF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 nvkTFTAYddlYFMSHFK---------MHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPI 183
Cdd:PRK10535 91 ---IFQRY---HLLSHLTaaqnvevpaVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180
....*....|....*....|....*....
gi 2492600 184 FLFCDEPTTGLDSFSAYTVIKTLRHLCTR 212
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
45-195 |
1.57e-11 |
|
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: 67.02 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKT-TLLAAIsqRL----RGNLTGDVVLNG---MAMERDQMTRIssflREFEINVkT 116
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALSIL--RLlpdpAAHPSGSILFDGqdlLGLSERELRRI----RGNRIAM-I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 F----TAYDDLY-----FMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAhTRIQ----QLSGGERKRLSLAEELITDPI 183
Cdd:COG4172 98 FqepmTSLNPLHtigkqIAEVLRLHRGLSGAAARARALELLERVGIPDPE-RRLDayphQLSGGQRQRVMIAMALANEPD 176
|
170
....*....|..
gi 2492600 184 FLFCDEPTTGLD 195
Cdd:COG4172 177 LLIADEPTTALD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
46-195 |
1.79e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISsFLREfEINvktftayddLYF 125
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-AGKIWFSGHDITRLKNREVP-FLRR-QIG---------MIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKMHRRT--------------TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:PRK10908 86 QDHHLLMDRTvydnvaipliiagaSGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
....
gi 2492600 192 TGLD 195
Cdd:PRK10908 166 GNLD 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
48-195 |
2.87e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMamerdQMTRISSFLREfeINVkTFTAYDDLYFMS 127
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDGV-----DLSHVPPYQRP--INM-MFQSYALFPHMT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492600 128 -----HFKMHR-RTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK11607 108 veqniAFGLKQdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-209 |
2.91e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.74 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISsFLRE----FeinvKTFTAYD 121
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-SGEVLWDGEPLDPEDRRRIG-YLPEerglY----PKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 DLYFMSHFK-MhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAY 200
Cdd:COG4152 91 QLVYLARLKgL----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVE 166
|
....*....
gi 2492600 201 TVIKTLRHL 209
Cdd:COG4152 167 LLKDVIREL 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
45-195 |
3.19e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisqRL--------RGNLT-GDVVLNGMA-MERDqmtrIS----SFlref 110
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLL-----RMiagledptSGEILiGGRDVTDLPpKDRN----IAmvfqSY---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 einvktftaydDLY-FMSHF-------KMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDP 182
Cdd:COG3839 85 -----------ALYpHMTVYeniafplKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170
....*....|....
gi 2492600 183 -IFLFcDEPTTGLD 195
Cdd:COG3839 153 kVFLL-DEPLSNLD 165
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
37-209 |
3.33e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 37 CRKQRElgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGM---AMERDQMTRIS---SFLREF 110
Cdd:PRK11831 16 TRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGEnipAMSRSRLYTVRkrmSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINVKTFTAYDDLYFmsHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:PRK11831 93 GALFTDMNVFDNVAY--PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170
....*....|....*....
gi 2492600 191 TTGLDSFSAYTVIKTLRHL 209
Cdd:PRK11831 171 FVGQDPITMGVLVKLISEL 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
45-209 |
3.39e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNG--MAMERDQMTRISSF----LREFEINVKTFT 118
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-FLEKPSEGSIVVNGqtINLVRDKDGQLKVAdknqLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYfmSHFKMHRRT----------TKSEKRQAVSDLLLAVGLRDAAHTRIQ-QLSGGERKRLSLAEELITDPIFLFC 187
Cdd:PRK10619 99 QHFNLW--SHMTVLENVmeapiqvlglSKQEARERAVKYLAKVGIDERAQGKYPvHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180
....*....|....*....|..
gi 2492600 188 DEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQL 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-195 |
3.69e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGmamerDQMTRISSFLRefeiNVKT-FTAYDDL 123
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPDSGRIMLDG-----QDITHVPAENR----HVNTvFQSYALF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 124 YFMSHF-------KMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK09452 99 PHMTVFenvafglRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
45-195 |
4.69e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.57 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKT-TLLAAISQRLRG--NLTGDVVLNGMAMERDQM--TRISSFLRefeiNVKTftA 119
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGvrQTAGRVLLDGKPVAPCALrgRKIATIMQ----NPRS--A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YDDLYFMSHfkmH-RRTTKSEKRQAVSDLLL----AVGLRDAAhtRIQQL-----SGGERKRLSLAEELITDPIFLFCDE 189
Cdd:PRK10418 92 FNPLHTMHT---HaRETCLALGKPADDATLTaaleAVGLENAA--RVLKLypfemSGGMLQRMMIALALLCEAPFIIADE 166
|
....*.
gi 2492600 190 PTTGLD 195
Cdd:PRK10418 167 PTTDLD 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
45-208 |
5.18e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAaisqrlrgnltgdVVLNGMA-----MERDQMTRISSFLREFEINVKTFTA 119
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVR-------------VVLGLVApdegvIKRNGKLRIGYVPQKLYLDTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 yddlyfMSHFKMHRRTTKSekrqavSDLLLAVGLRDAAH---TRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD- 195
Cdd:PRK09544 86 ------VNRFLRLRPGTKK------EDILPALKRVQAGHlidAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDv 153
|
170
....*....|....*
gi 2492600 196 --SFSAYTVIKTLRH 208
Cdd:PRK09544 154 ngQVALYDLIDQLRR 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-196 |
6.23e-11 |
|
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: 61.46 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNL---TGDVVLNGMAmerdqmtrISSFLRefeinvktftayd 121
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL----GLLrptSGRVRLDGAD--------ISQWDP------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 dlyfmshfkmhrrttkSEKRQAVS-----DLLLAVGLRDAAhtriqqLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:cd03246 72 ----------------NELGDHVGylpqdDELFSGSIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
45-195 |
6.33e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlRGNLT---GDVVLNGMAME----RDQMTRISSFLRE----FEIN 113
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI----NGTLTptaGTVLVAGDDVEalsaRAASRRVASVPQDtslsFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLYFMSHFKMHRRTtkseKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:PRK09536 94 VRQVVEMGRTPHRSRFDTWTET----DRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
..
gi 2492600 194 LD 195
Cdd:PRK09536 170 LD 171
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
8.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.75 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 23 VPAQEQSNYSFWNECRKqrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRlrGNLTGDVVLNGMAMERDQ--- 99
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVRVEGRVEFFNQniy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 --MTRISSFLREFEI-----NVKTFTAYDDLYFmsHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQ----LSGGE 168
Cdd:PRK14258 78 erRVNLNRLRRQVSMvhpkpNLFPMSVYDNVAY--GVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 169 RKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRR----IAKHSLTQV 223
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSEltmvIVSHNLHQV 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-227 |
8.99e-11 |
|
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: 62.25 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAME-------RDQMTRIS--SFLreFEINVK 115
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVDSGRILIDGHDVRdytlaslRRQIGLVSqdVFL--FNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TFTAYDDlyfmshfkmhRRTTKSEKRQAVSdllLA------VGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFL 185
Cdd:cd03251 94 ENIAYGR----------PGATREEVEEAAR---AAnahefiMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2492600 186 FCDEPTTGLDSFSAYTVIKTLRHLCTRRR---IAkHSLTQVYGED 227
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTtfvIA-HRLSTIENAD 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
46-209 |
1.31e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRIssfLREFEINV----KTF---T 118
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-SGRIVFDGKDITDWQTAKI---MREAVAIVpegrRVFsrmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYFMSHFKmhRRTTKSEKRQAVSDLLLAvgLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:PRK11614 97 VEENLAMGGFFA--ERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170
....*....|.
gi 2492600 199 AYTVIKTLRHL 209
Cdd:PRK11614 173 IQQIFDTIEQL 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
40-195 |
1.42e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 40 QRELGIL-HDVSGHLKTGDLIAILGGSGAGKTTLL---AAISQRlrgnLTGDVVLNGMAMERDQmtriSSFLREF----- 110
Cdd:PRK13538 10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLrilAGLARP----DAGEVLWQGEPIRRQR----DEYHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINVKT-FTAYDDLYFMShfKMHRRTTksekRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:PRK13538 82 QPGIKTeLTALENLRFYQ--RLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
....*.
gi 2492600 190 PTTGLD 195
Cdd:PRK13538 156 PFTAID 161
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
46-209 |
1.47e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNL---TGDVVLNGMAMERDQMTRISsfLRE-----FE-INVKT 116
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLF----QNLNGILkpsSGRILFDGKPIDYSRKGLMK--LREsvgmvFQdPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 FTA--YDDLYFMShfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:PRK13636 96 FSAsvYQDVSFGA---VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170
....*....|....*
gi 2492600 195 DSFSAYTVIKTLRHL 209
Cdd:PRK13636 173 DPMGVSEIMKLLVEM 187
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
45-195 |
1.79e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.55 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlrgNL-----TGDVVLNGMAMERDQmTRISSFLRE----FEinvk 115
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI------NLleepdSGTITVDGEDLTDSK-KDINKLRRKvgmvFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 tftayddlyfmsHF----------------KMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELI 179
Cdd:COG1126 85 ------------QFnlfphltvlenvtlapIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170
....*....|....*.
gi 2492600 180 TDPIFLFCDEPTTGLD 195
Cdd:COG1126 153 MEPKVMLFDEPTSALD 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
48-195 |
1.86e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNG-----------MAMERD-QMT------------RI 103
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLL-RLEEPTSGEILFDGqditglsgrelRPLRRRmQMVfqdpyaslnprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 104 SSFLRE-FEInvktftayddlyfmshfkmHRRTTKSEKRQAVSDLLLAVGLR-DAAHTRIQQLSGGERKRLSLAEELITD 181
Cdd:COG4608 115 GDIIAEpLRI-------------------HGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALN 175
|
170
....*....|....
gi 2492600 182 PIFLFCDEPTTGLD 195
Cdd:COG4608 176 PKLIVCDEPVSALD 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
45-195 |
1.88e-10 |
|
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: 61.12 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLL---AAISQRLRGNL-TGDVVLNGM-AMERDqmtrISSFLREFEInVKTFTA 119
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLrmiAGLEEPTSGRIyIGGRDVTDLpPKDRD----IAMVFQNYAL-YPHMTV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2492600 120 YDDLYFmsHFKMhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDP-IFLFcDEPTTGLD 195
Cdd:cd03301 90 YDNIAF--GLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPkVFLM-DEPLSNLD 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
49-195 |
1.91e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGnlTGDVVLNGMAMER---DQMTRISSFLREFE---INVKTFTaYDD 122
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEAwsaAELARHRAYLSQQQtppFAMPVFQ-YLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYfmshfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEE-LITDPI------FLFCDEPTTGLD 195
Cdd:PRK03695 92 LH------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPMNSLD 165
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
42-223 |
2.11e-10 |
|
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: 62.82 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTgdliAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMerdQMTRISSFL----REFEINVKTF 117
Cdd:TIGR02142 13 SLDADFTLPGQGVT----AIFGRSGSGKTTLIRLIAGLTRPD-EGEIVLNGRTL---FDSRKGIFLppekRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAV-GLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190
....*....|....*....|....*....|.
gi 2492600 197 FSAYTVIKTLRHLCTRRRI----AKHSLTQV 223
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIpilyVSHSLQEV 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
41-203 |
3.14e-10 |
|
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: 60.53 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 41 RELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrLRGNLT--GDVVL---NGM-----AMERdQMTRissfLREF 110
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCI---YGNYLPdsGSILVrhdGGWvdlaqASPR-EILA----LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINvktftayddlyFMSHF--KMHRRTTksekRQAVSDLLLAVGL-RDAAHTRIQQL------------------SGGER 169
Cdd:COG4778 94 TIG-----------YVSQFlrVIPRVSA----LDVVAEPLLERGVdREEARARARELlarlnlperlwdlppatfSGGEQ 158
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 170 KRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVI 203
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-196 |
3.65e-10 |
|
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: 60.70 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMErdQMTRISsfLREfEINVktfTAYDDLY 124
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLM-RFYDPQKGQILIDGIDIR--DISRKS--LRS-MIGV---VLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 F----MSHFKMHRRTTKSEKRQAVSDLL--------LAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:cd03254 89 FsgtiMENIRLGRPNATDEEVIEAAKEAgahdfimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
....
gi 2492600 193 GLDS 196
Cdd:cd03254 169 NIDT 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
38-209 |
3.71e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQREL-GILHDVSGHLKTGDLIAILGGSGAGKTtlLAAIS-QRLRGN-----LTGDVVLNGMAM-ERDQMT-------R 102
Cdd:PRK15134 16 RQQQTVrTVVNDVSLQIEAGETLALVGESGSGKS--VTALSiLRLLPSppvvyPSGDIRFHGESLlHASEQTlrgvrgnK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 103 ISSFLREFEINVKTF-TAYDDLYFMshFKMHRRTTKSEKRQAVSDLLLAVGLRDAAhTRI----QQLSGGERKRLSLAEE 177
Cdd:PRK15134 94 IAMIFQEPMVSLNPLhTLEKQLYEV--LSLHRGMRREAARGEILNCLDRVGIRQAA-KRLtdypHQLSGGERQRVMIAMA 170
|
170 180 190
....*....|....*....|....*....|..
gi 2492600 178 LITDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
45-215 |
4.09e-10 |
|
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: 60.18 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLlAAISQRLRGNLTGDVVLNGMAME-------RDQMTRISS----FLREFEIN 113
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTV-VALLENFYQPQGGQVLLDGKPISqyehkylHSKVSLVGQepvlFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKtftayddlYFMSHFKMHRRTTKSEKRQAVSDL-LLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:cd03248 108 IA--------YGLQSCSFECVKEAAQKAHAHSFIsELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180
....*....|....*....|...
gi 2492600 193 GLDSFSAYTVIKTLRHLCTRRRI 215
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERRTV 202
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-222 |
4.66e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQ---RLRG-NLTGDVVLNGMAM--ERDQMT---RISSFLREfeINVK 115
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmndKVSGyRYSGDVLLGGRSIfnYRDVLEfrrRVGMLFQR--PNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TFTAYDDLyfMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:PRK14271 114 PMSIMDNV--LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|...
gi 2492600 192 TGLDSFSAYTVIKTLRHLCTRRR--IAKHSLTQ 222
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTviIVTHNLAQ 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
45-195 |
5.68e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQMtriSSFLREFEINVKTFTAYD--- 121
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-RHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQLPAAEgmt 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2492600 122 --DLYFMSHFKMHRRTTK--SEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK10575 102 vrELVAIGRYPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-209 |
6.33e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 44 GILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQ-MTRISSFLREFEINV-------- 114
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN-RLIEIYDSKIKVDGKVLYFGKdIFQIDAIKLRKEVGMvfqqpnpf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFmsHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:PRK14246 103 PHLSIYDNIAY--PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170
....*....|....*....
gi 2492600 191 TTGLDSFSAYTVIKTLRHL 209
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
43-224 |
7.79e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 43 LGIlHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQMTRISSFLREfeinvKTFTAYDD 122
Cdd:PRK10070 42 LGV-KDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIEPTRGQVLIDGVDIAKISDAELREVRRK-----KIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMSHFKMHRRTT---------KSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:PRK10070 115 FALMPHMTVLDNTAfgmelaginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190
....*....|....*....|....*....|.
gi 2492600 194 LDSfsaytVIKTLRHLCTRRRIAKHSLTQVY 224
Cdd:PRK10070 195 LDP-----LIRTEMQDELVKLQAKHQRTIVF 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
46-196 |
8.03e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAMeRDqMTRISsfLRE-----FE--------- 111
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVFDPQSGRILIDGTDI-RT-VTRAS--LRRniavvFQdaglfnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 ---INVKTFTAYDDlyfmshfKMHRrttkSEKRQAVSDLLLA--VGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLF 186
Cdd:PRK13657 426 ednIRVGRPDATDE-------EMRA----AAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170
....*....|
gi 2492600 187 CDEPTTGLDS 196
Cdd:PRK13657 495 LDEATSALDV 504
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
45-194 |
8.39e-10 |
|
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: 59.61 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQ---------RLRG-NLTG----DVVLNGMAM---ERD---QMT--- 101
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllpprsgsiRFDGeDITGlpphRIARLGIGYvpeGRRifpSLTvee 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 102 --RISSFLRefeinvktftayddlyfmshfkmHRRTTKSEKRQAVSDLLLAvgLRDAAHTRIQQLSGGERKRLSLAEELI 179
Cdd:COG0410 98 nlLLGAYAR-----------------------RDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170
....*....|....*
gi 2492600 180 TDPIFLFCDEPTTGL 194
Cdd:COG0410 153 SRPKLLLLDEPSLGL 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-195 |
1.03e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMER---DQMTRISSFLREF-----EINVKT 116
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPAHGHVWLDGEHIQHyasKEVARRIGLLAQNattpgDITVQE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 117 FTAYDDLYFMSHFKMHRRttksEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRK----EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
42-209 |
1.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNL---TGDVVLNGMAMERDQMT-RISSFLREFEI----- 112
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFI----EHLNALLlpdTGTIEWIFKDEKNKKKTkEKEKVLEKLVIqktrf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 ----NVK----------TFTAY--------DDLYFMShfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQ-QLSGGER 169
Cdd:PRK13651 95 kkikKIKeirrrvgvvfQFAEYqlfeqtieKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2492600 170 KRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
56-195 |
1.45e-09 |
|
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: 58.27 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 56 GDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMAMERDQMTR--ISSFLRE--------FEINVktftaydD 122
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETpqsGRVLINGVDVTAAPPADrpVSMLFQEnnlfahltVEQNV-------G 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 123 LYFMSHFKMhrrttKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03298 93 LGLSPGLKL-----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
42-209 |
2.42e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTllaaISQRLRGNL---TGDVVLNGMAMERDQMTRISSFL--------REF 110
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKST----ISKILTGLLkpqSGEIKIDGITISKENLKEIRKKIgiifqnpdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 eINVktfTAYDDLYFMSHfkmHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDP-IFLFcDE 189
Cdd:PRK13632 97 -IGA---TVEDDIAFGLE---NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPeIIIF-DE 168
|
170 180
....*....|....*....|
gi 2492600 190 PTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDL 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
2.67e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 2 PMDEGDAQGSLLLEWKQLNYYVPAQEQSnysfwnecrkqrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLR 81
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQP---------------VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 82 GNlTGDVVLNGMAME-------RDQMT----RISSF---LREfeiNVK--TFTAYDDlyfmshfkmhrrttksekrqAVS 145
Cdd:PRK11160 392 PQ-QGEILLNGQPIAdyseaalRQAISvvsqRVHLFsatLRD---NLLlaAPNASDE--------------------ALI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 146 DLLLAVGLRDAAHT------------RiqQLSGGERKRLSLAEELITD-PIFLFcDEPTTGLD 195
Cdd:PRK11160 448 EVLQQVGLEKLLEDdkglnawlgeggR--QLSGGEQRRLGIARALLHDaPLLLL-DEPTEGLD 507
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-227 |
2.68e-09 |
|
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: 58.01 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAMERDQMTRissfLRE-----------FEIN 113
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYDVSSGSILIDGQDIREVTLDS----LRRaigvvpqdtvlFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTFTAYDDLyfmshfkmhrRTTKSEKRQA-----VSDLLLavGLRDAAHTRIQQ----LSGGERKRLSLAEELITDPIF 184
Cdd:cd03253 91 IGYNIRYGRP----------DATDEEVIEAakaaqIHDKIM--RFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTLRHLCTRRR---IAkHSLTQVYGED 227
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTtivIA-HRLSTIVNAD 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
52-220 |
2.97e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.05 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 52 HLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGM---AMERDQmtRISSFLreFEINvktftaydDLYf 125
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIA----GFLTpasGSLTLNGQdhtTTPPSR--RPVSML--FQEN--------NLF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 mSHFK--------MH---RRTtkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITD-PIFLFcDEPTTG 193
Cdd:PRK10771 84 -SHLTvaqniglgLNpglKLN--AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREqPILLL-DEPFSA 159
|
170 180 190
....*....|....*....|....*....|.
gi 2492600 194 LDSFSAYTVIKTLRHLCTRRRIA----KHSL 220
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTllmvSHSL 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-209 |
7.08e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 2 PMDEGDAQGSLLLEWKQLNYyvpaqeqSNYSFWNECRKQRElgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLR 81
Cdd:PTZ00265 366 PLVENNDDGKKLKDIKKIQF-------KNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLI-ERLY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 82 GNLTGDVVLN--------GMAMERDQMTRISS----FLREFEINVK-------------------TFTAYD--------- 121
Cdd:PTZ00265 436 DPTEGDIIINdshnlkdiNLKWWRSKIGVVSQdpllFSNSIKNNIKyslyslkdlealsnyynedGNDSQEnknkrnscr 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 -----DLYFMS---------HFKMHRRTTKSEKRQAVSDLLL----AVGLRDAAHTRI----QQLSGGERKRLSLAEELI 179
Cdd:PTZ00265 516 akcagDLNDMSnttdsneliEMRKNYQTIKDSEVVDVSKKVLihdfVSALPDKYETLVgsnaSKLSGGQKQRISIARAII 595
|
250 260 270
....*....|....*....|....*....|
gi 2492600 180 TDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
46-209 |
7.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFLRE-------------FEI 112
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-TGTVTVDDITITHKTKDKYIRPVRKrigmvfqfpesqlFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 NVKTftayDDLYFMSHFKMHRRTTKSEkrqaVSDLLLAVGL-RDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:PRK13646 102 TVER----EIIFGPKNFKMNLDEVKNY----AHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170
....*....|....*...
gi 2492600 192 TGLDSFSAYTVIKTLRHL 209
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSL 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
45-216 |
8.09e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmamerDQMTRIS--SFLREFEINVKT---F-- 117
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT-SGTLLFEG-----EDISTLKpeIYRQQVSYCAQTptlFgd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDDLYFMSHFKmhrrtTKSEKRQAVSDLLLAVGLRDAAHT-RIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:PRK10247 96 TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPDTILTkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|
gi 2492600 197 FSAYTVIKTLRHLCTRRRIA 216
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIA 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
45-230 |
8.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.12 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTllaaISQRLRGNLTGD------VVLNGMAMERDQMTRIssflRE-----FEIN 113
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKST----ISKLINGLLLPDdnpnskITVDGITLTAKTVWDI----REkvgivFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 114 VKTF---TAYDDLYFMSHfkmHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:PRK13640 94 DNQFvgaTVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2492600 191 TTGLDSFSAYTVIKTLRHLCTRRRIAKHSLTQVYGEDSFA 230
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMA 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-207 |
8.54e-09 |
|
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: 56.44 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 14 LEWKQLNYYVPAQEQSNysfwnecrkqrelgiLHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGM 93
Cdd:cd03245 3 IEFRNVSFSYPNQEIPA---------------LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA-GLYKPTSGSVLLDGT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 94 AME----RDQMTRISSFLREfeinVKTF--TAYDDLYFMSHFKMHRRTTKSEKRQAVSDLL--------LAVGLRDaaht 159
Cdd:cd03245 67 DIRqldpADLRRNIGYVPQD----VTLFygTLRDNITLGAPLADDERILRAAELAGVTDFVnkhpngldLQIGERG---- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2492600 160 riQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLR 207
Cdd:cd03245 139 --RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLR 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-224 |
9.60e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.94 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 44 GILHDVSGHLKTGdliaILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISsfLREfeiNVKT-FTAYDD 122
Cdd:PRK13638 19 GLNLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGKPLDYSKRGLLA--LRQ---QVATvFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMSH------FKMHRR-TTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK13638 89 QIFYTDidsdiaFSLRNLgVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190
....*....|....*....|....*....|..
gi 2492600 196 SFSAYTVIKTLRHLCTRRR---IAKHSLTQVY 224
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNhviISSHDIDLIY 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
49-195 |
1.03e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTL-------------------------LAAISQRLRGNLTGDVVlngmAM-ERDQMTR 102
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSslaimglidypgrvmaeklefngqdLQRISEKERRNLVGAEV----AMiFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 103 IS-SFLREFEInvktftayddlyfMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAhTRI----QQLSGGERKRLSLAEE 177
Cdd:PRK11022 102 LNpCYTVGFQI-------------MEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPA-SRLdvypHQLSGGMSQRVMIAMA 167
|
170
....*....|....*...
gi 2492600 178 LITDPIFLFCDEPTTGLD 195
Cdd:PRK11022 168 IACRPKLLIADEPTTALD 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-215 |
1.31e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 32 SFWNecRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGMamerdqmtriSSFLR 108
Cdd:COG4586 26 GLFR--REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT----GILVptsGEVRVLGY----------VPFKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 109 EFEiNVKTFTA--------YDDLYFMSHFKMHR---RTTKSEKRQAV---SDLLlavGLRDAAHTRIQQLSGGERKRLSL 174
Cdd:COG4586 90 RKE-FARRIGVvfgqrsqlWWDLPAIDSFRLLKaiyRIPDAEYKKRLdelVELL---DLGELLDTPVRQLSLGQRMRCEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2492600 175 AEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRI 215
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGT 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
38-216 |
1.84e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTT----LLAAISQRlrgnltGDVVLNGMAMERDQMTRISSFLREFEI- 112
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ------GEIWFDGQPLHNLNRRQLLPVRHRIQVv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 ------------NVKTFTAyddlyfmSHFKMHRRT-TKSEKRQAVSDLLLAVGLrDAA--HTRIQQLSGGERKRLSLAEE 177
Cdd:PRK15134 368 fqdpnsslnprlNVLQIIE-------EGLRVHQPTlSAAQREQQVIAVMEEVGL-DPEtrHRYPAEFSGGQRQRIAIARA 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 2492600 178 LITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIA 216
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLA 478
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
48-195 |
2.13e-08 |
|
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: 55.38 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGM-AMERDqmtrissflrEFEINVKTFTAYDDLYFM 126
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMIN-RLIEPTSGEIFIDGEdIREQD----------PVELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 127 SHFKMHRRTT---------KSEKRQAVSDLLLAVGLRDA--AHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03295 88 PHMTVEENIAlvpkllkwpKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
46-209 |
2.26e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.55 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGN----LTGDVVLNGMAMERDQMTRISsfLREfEI-------NV 114
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtITGSIVYNGHNIYSPRTDTVD--LRK-EIgmvfqqpNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFmsHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQ----LSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:PRK14239 98 FPMSIYENVVY--GLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170
....*....|....*....
gi 2492600 191 TTGLDSFSAYTVIKTLRHL 209
Cdd:PRK14239 176 TSALDPISAGKIEETLLGL 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-207 |
2.38e-08 |
|
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: 57.12 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRG-----NLTGDVVLNGMAMERDQMTRISSFLRE--------FE 111
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLM----HVLRGmdqyePTSGRIIYHVALCEKCGYVERPSKVGEpcpvcggtLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 INVKTFTAYDDLYFMSHFK----MHRRTTKSEKRQAVSDLLL----------------AVGLRDAAHT--RI----QQLS 165
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIRKriaiMLQRTFALYGDDTVLDNVLealeeigyegkeavgrAVDLIEMVQLshRIthiaRDLS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2492600 166 GGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLR 207
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
45-223 |
2.67e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAaisqrlrgnltgdvVLNGMAMERDQMTRI--SSFLREFEINVKT------ 116
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLR--------------VLNLLETPDSGQLNIagHQFDFSQKPSEKAirllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 -----FTAYDdlyFMSHFK-MHRRT---------TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITD 181
Cdd:COG4161 83 kvgmvFQQYN---LWPHLTvMENLIeapckvlglSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2492600 182 PIFLFCDEPTTGLDSFSAYTVIKTLRHLctrrriAKHSLTQV 223
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL------SQTGITQV 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
53-196 |
3.59e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 53 LKTGDLIAILGGSGAGKTTLLaaisqRLRGNL----TGDVVLNGmamerDQMTRISSFLREFEInvkTFTAYDDLYFMS- 127
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTVL-----RLVAGLekptEGQIFIDG-----EDVTHRSIQQRDICM---VFQSYALFPHMSl 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 128 ------HFKMHRRTtKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:PRK11432 96 genvgyGLKMLGVP-KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-195 |
3.78e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTL---LAAISQRLRGNLT---GDVVLNGMAMERD-----QMT----- 101
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETPTGGELYyqgQDLLKADPEAQKLlrqkiQIVfqnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 102 -------RISSFLRE-FEINVktftaydDLyfmshfkmhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQQL-SGGERKRL 172
Cdd:PRK11308 103 gslnprkKVGQILEEpLLINT-------SL------------SAAERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRI 163
|
170 180
....*....|....*....|...
gi 2492600 173 SLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALD 186
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-196 |
4.17e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisqRLRGNL---TGDVVLNGMAMerdqmtrissfLREfeinvktftAYD 121
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLL-----RLLAGLetpSAGELLAGTAP-----------LAE---------ARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 DLYFMshFKMHRRTT------------KSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:PRK11247 82 DTRLM--FQDARLLPwkkvidnvglglKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
....*..
gi 2492600 190 PTTGLDS 196
Cdd:PRK11247 160 PLGALDA 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-205 |
4.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAMERDQMTRIssflreFEINVKtftayDDLYF 125
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVSWI------FNATVR-----ENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKMHRRTTKSEKRQAVSDLLLAVGlRDAAHT--RIQQLSGGERKRLSLAEELITDP-IFLFcDEPTTGLDSFSAYTV 202
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLPG-RDLTEIgeRGVNISGGQKQRVSMARAVYSNSdIYIF-DDPLSALDAHVAHQV 779
|
...
gi 2492600 203 IKT 205
Cdd:PLN03232 780 FDS 782
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
48-195 |
1.05e-07 |
|
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: 54.34 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAIS--QRLRgnlTGDVVLNGMAMerdqmtrissFLREFEINVKT--------- 116
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAglERPD---SGRIRLGGEVL----------QDSARGIFLPPhrrrigyvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 --------FTAYDDLYFMshfkmHRRTTKSEKRQ---AVSDLLlavGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFL 185
Cdd:COG4148 84 qearlfphLSVRGNLLYG-----RKRAPRAERRIsfdEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170
....*....|
gi 2492600 186 FCDEPTTGLD 195
Cdd:COG4148 156 LMDEPLAALD 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-195 |
1.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRL----RGNLTGDVVLNG---MAMERDQMTRISSFLREFEINVKTF 117
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypEARVSGEVYLDGqdiFKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDDLYFmsHFKMHRRT-TKSEKRQAVSDLLLAVGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:PRK14247 98 SIFENVAL--GLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
...
gi 2492600 193 GLD 195
Cdd:PRK14247 176 NLD 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
45-223 |
1.41e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAaisqrlrgnltgdvVLNGMAMERDQMTRI--SSF----------LREFEI 112
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLR--------------VLNLLEMPRSGTLNIagNHFdfsktpsdkaIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 113 NV-KTFTAYDdlyFMSHFK-MHRRT---------TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITD 181
Cdd:PRK11124 83 NVgMVFQQYN---LWPHLTvQQNLIeapcrvlglSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2492600 182 PIFLFCDEPTTGLDSFSAYTVIKTLRHLctrrriAKHSLTQV 223
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIREL------AETGITQV 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
45-195 |
1.51e-07 |
|
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: 52.14 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLT-GDVVLNG-----MAM-ERDQMTRISSFLREFEI-NVKt 116
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTeGEILFKGeditdLPPeERARLGIFLAFQYPPEIpGVK- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 117 ftayddlyfmshfkmhrrttksekrqaVSDLLLAVGlrdaahtriQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03217 94 ---------------------------NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
45-206 |
1.57e-07 |
|
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: 52.93 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAME-------RDQMTRISsflRE---FEINV 114
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-ERFYDPTSGEILLDGVDIRdlnlrwlRSQIGLVS---QEpvlFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDlyfmshfkmHRRTTKSEKRQAVSDLLLA--VGLRDAAHTRI----QQLSGGERKRLSLAEELITDPIFLFCD 188
Cdd:cd03249 94 AENIRYGK---------PDATDEEVEEAAKKANIHDfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170
....*....|....*...
gi 2492600 189 EPTTGLDSFSAYTVIKTL 206
Cdd:cd03249 165 EATSALDAESEKLVQEAL 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-195 |
1.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIS---QRLRGNL-TGDVVLNGMAMERD---QMTRISSFLREFEINVKTFT 118
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNgllQPTEGKVtVGDIVVSSTSKQKEikpVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 119 AYDDLYF-MSHFKMhrrtTKSEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK13643 102 VLKDVAFgPQNFGI----PKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-198 |
1.88e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIS--QRLRgnlTGDV-VLNG-MA--MERDQM-TRIssflrefeinvktft 118
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ---QGRVeVLGGdMAdaRHRRAVcPRI--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AY------DDLY----------FMSHFKMHRRttkSEKRQAVSDLLLAVGL-----RDAAhtriqQLSGGERKRLSLAEE 177
Cdd:NF033858 79 AYmpqglgKNLYptlsvfenldFFGRLFGQDA---AERRRRIDELLRATGLapfadRPAG-----KLSGGMKQKLGLCCA 150
|
170 180
....*....|....*....|.
gi 2492600 178 LITDPIFLFCDEPTTGLDSFS 198
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLS 171
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
46-195 |
1.93e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.82 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIS-----QRLRGNLTGDVVlnGMAMERDQMTRISSFLREFEINVKTFTAY 120
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNgiylpQRGRVKVMGREV--NAENEKWVRSKVGLVFQDPDDQVFSSTVW 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 121 DDLYFMShfkMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK13647 99 DDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
49-195 |
1.93e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMER--DQMTRISSFLREFEiNVKTF---TAYDDL 123
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT-GGTILLRGQHIEGlpGHQIARMGVVRTFQ-HVRLFremTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 YFMSHFKMHR------------RTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPT 191
Cdd:PRK11300 102 LVAQHQQLKTglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
....
gi 2492600 192 TGLD 195
Cdd:PRK11300 182 AGLN 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
46-212 |
3.58e-07 |
|
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: 50.50 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNLT---GDVVLNGmamerdqmtrissflREFEINvktftaydd 122
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILS----GLYKpdsGEILVDG---------------KEVSFA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 lyfmshfkmhrrttksekrqavsdlllavGLRDAAHTRIQ---QLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSA 199
Cdd:cd03216 68 -----------------------------SPRDARRAGIAmvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170
....*....|...
gi 2492600 200 YTVIKTLRHLCTR 212
Cdd:cd03216 119 ERLFKVIRRLRAQ 131
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
45-223 |
3.80e-07 |
|
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: 51.38 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGmamerdqmtRISSFLrefEINV---KTFTAYD 121
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-SGTVTVRG---------RVSSLL---GLGGgfnPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 DLYFMSHFKMHRRTTKSEKRQAVSDLllaVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYT 201
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEF---SELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180
....*....|....*....|....*
gi 2492600 202 VIKTLRHLCTRRRI---AKHSLTQV 223
Cdd:cd03220 181 CQRRLRELLKQGKTvilVSHDPSSI 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
58-202 |
4.42e-07 |
|
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: 53.48 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 58 LIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMER--DQMTRISSFLREFEINVKTFTAYDDLYFMSHFKMHrrt 135
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGKDIETnlDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR--- 1033
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2492600 136 TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTV 202
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-228 |
4.55e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFMSHFkmhRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:NF000106 99 ESFSGRENLYMIGR*---LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110
....*....|....*....|....*....|....
gi 2492600 195 DSFSAYTVIKTLRHLCtrRRIAKHSLTQVYGEDS 228
Cdd:NF000106 176 DPRTRNEVWDEVRSMV--RDGATVLLTTQYMEEA 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
45-207 |
6.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFL-REFEINVKTF---TAY 120
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLTEENVWDIRHKIgMVFQNPDNQFvgaTVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 121 DDLYF------MSHFKMHRRttksekrqaVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:PRK13650 101 DDVAFglenkgIPHEEMKER---------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170
....*....|...
gi 2492600 195 DSFSAYTVIKTLR 207
Cdd:PRK13650 172 DPEGRLELIKTIK 184
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
59-209 |
7.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.34 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 59 IAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMTRISSFL----REFEINVKTFTAYDDLYFmSHFKMHRR 134
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEPITKENIREVRKFVglvfQNPDDQIFSPTVEQDIAF-GPINLGLD 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492600 135 TTKSEKRqaVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK13652 111 EETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
46-194 |
7.98e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMamERDQMTRISSFLREFEINVKTFTAYDDLYF 125
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG-IHEPTKGTITINNI--NYNKLDHKLAAQLGIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 126 MSHFKMHRRTTK----------SEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:PRK09700 98 LENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-213 |
8.41e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.09 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGmamerdqmtrissflrefeINVKTFTaYDDLy 124
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLL-RFYDPTSGRILIDG-------------------VDIRDLT-LESL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 fmshfkmhrrttksekRQAVS----DLLL---------AVGLRDA-------------AHTRIQQ--------------- 163
Cdd:COG1132 413 ----------------RRQIGvvpqDTFLfsgtireniRYGRPDAtdeeveeaakaaqAHEFIEAlpdgydtvvgergvn 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2492600 164 LSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRR 213
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR 526
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
45-210 |
8.85e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI----------------------SQRLR---GNLtgdvvlngmameRDQ 99
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriarpagarvlflPQRPYlplGTL------------REA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 MTRissflrefeinVKTFTAYDDlyfmshfkmhrrttksekrQAVSDLLLAVGLRDAAHtRI-------QQLSGGERKRL 172
Cdd:COG4178 446 LLY-----------PATAEAFSD-------------------AELREALEAVGLGHLAE-RLdeeadwdQVLSLGEQQRL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 2492600 173 SLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLC 210
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL 532
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
49-208 |
9.83e-07 |
|
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: 51.73 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTL---LAAISQRLRGNL---TGDVVLNgMA----MERDQMTRISSFLrefeinvktFT 118
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLskiIAGVLEPTSGEVnvrVGDEWVD-MTkpgpDGRGRAKRYIGIL---------HQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDdLYfmSHFKMHRRTTKS---------EKRQAVSdLLLAVGLRDAAHTRI-----QQLSGGERKRLSLAEELITDPIF 184
Cdd:TIGR03269 373 EYD-LY--PHRTVLDNLTEAiglelpdelARMKAVI-TLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRI 448
|
170 180
....*....|....*....|....
gi 2492600 185 LFCDEPTTGLDSFSAYTVIKTLRH 208
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILK 472
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
53-195 |
9.95e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 53 LKTGDLIAILGGSGAGKTTLLAAISQRLRGN--LTGDVVLNG------------------MAME-RDQMTRISSFLREFE 111
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGLLAANgrIGGSATFNGreilnlpekelnklraeqISMIfQDPMTSLNPYMRVGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 112 invktftayddlYFMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAaHTRI----QQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:PRK09473 119 ------------QLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEA-RKRMkmypHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
....*...
gi 2492600 188 DEPTTGLD 195
Cdd:PRK09473 186 DEPTTALD 193
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-209 |
1.10e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 12 LLLEWKQLNYYVPAQEQSNYsFWnecRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLN 91
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGKQW-FW---QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAII-GLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 92 G---MAMERDQMTRISSFLREF---------------EINVKTFTAYddlyfmsHFKMhrrtTKSEKRQAVSDLLLAVGL 153
Cdd:PRK15079 82 GkdlLGMKDDEWRAVRSDIQMIfqdplaslnprmtigEIIAEPLRTY-------HPKL----SRQEVKDRVKAMMLKVGL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2492600 154 RDAAHTRI-QQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD-SFSAyTVIKTLRHL 209
Cdd:PRK15079 151 LPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvSIQA-QVVNLLQQL 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
46-195 |
1.29e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.43 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNL---TGDVVLNGMAMErDQMTRISSFLREF-------EINVK 115
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLI----QHLNGLLkptSGKIIIDGVDIT-DKKVKLSDIRKKVglvfqypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TFTAYDDLYF------MSHFKMHRRTTKSEKrqavsdlllAVGL--RDAAHTRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:PRK13637 98 EETIEKDIAFgpinlgLSEEEIENRVKRAMN---------IVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
....*...
gi 2492600 188 DEPTTGLD 195
Cdd:PRK13637 169 DEPTAGLD 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-195 |
1.63e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 38 RKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAMERDQMTRISSFLREFEInvktf 117
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL-LRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQF----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 tAYDDLY------------FMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRI-QQLSGGERKRLSLAEELITDPIF 184
Cdd:PRK10261 406 -IFQDPYasldprqtvgdsIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKV 484
|
170
....*....|.
gi 2492600 185 LFCDEPTTGLD 195
Cdd:PRK10261 485 IIADEAVSALD 495
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-204 |
2.12e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 27 EQSNYSFWNECRKQRElgILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLN--------------- 91
Cdd:PRK13549 261 EVRNLTAWDPVNPHIK--RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDgkpvkirnpqqaiaq 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 92 GMAM-----ERDQMTRISSFLRefeiNVkTFTAYDDLYFMShfkmhrRTTKSEKRQAVSDLLLAVGLRDA-AHTRIQQLS 165
Cdd:PRK13549 339 GIAMvpedrKRDGIVPVMGVGK----NI-TLAALDRFTGGS------RIDDAAELKTILESIQRLKVKTAsPELAIARLS 407
|
170 180 190
....*....|....*....|....*....|....*....
gi 2492600 166 GGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIK 204
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
46-195 |
2.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNLT--------GDVVLNGMAMERDQMTrissfLRE-------- 109
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLL----QHLNGLLQptsgtvtiGERVITAGKKNKKLKP-----LRKkvgivfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 110 -----FEINVKTFTAYDDLYFmshfkmhrRTTKSEKRQAVSDLLLAVGLRDAAHTRIQ-QLSGGERKRLSLAEELITDPI 183
Cdd:PRK13634 94 pehqlFEETVEKDICFGPMNF--------GVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPE 165
|
170
....*....|..
gi 2492600 184 FLFCDEPTTGLD 195
Cdd:PRK13634 166 VLVLDEPTAGLD 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
53-195 |
2.36e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 53 LKTGDLIAILGGSGAGKTTLLaaisQRLRGNLT---GDVVLNGMAMerdqMTRISS------FLREFEINVKTFTAYDDL 123
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTF----KMLTGDTTvtsGDATVAGKSI----LTNISDvhqnmgYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 124 YFMSHFkmhrRTTKSEKRQAVSDL-LLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:TIGR01257 2034 YLYARL----RGVPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-222 |
2.74e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.26 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI--------SQRLrgnlTGDVVLNGMAMERDQMTRISsfLRE------- 109
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGARV----EGEILLDGEDIYDPDVDVVE--LRRrvgmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 110 ---------FEiNVktftAYDdlyfmshFKMHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQ----LSGGERKRLSLAE 176
Cdd:COG1117 100 kpnpfpksiYD-NV----AYG-------LRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKsalgLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2492600 177 ELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHLCTRRRIA--KHSLTQ 222
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVivTHNMQQ 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
45-207 |
4.07e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNlTGDVVLNGMAMERDQMT---RISSFLREFEINvKTFTAYD 121
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFERQSIKKDLCTyqkQLCFVGHRSGIN-PYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 122 DLYFMSHFkmhrrttkSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYT 201
Cdd:PRK13540 94 NCLYDIHF--------SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
....*.
gi 2492600 202 VIKTLR 207
Cdd:PRK13540 166 IITKIQ 171
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
46-227 |
4.84e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.59 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTT---LLAAISQRLRGNltgdVVLNGMAMERDQMTRISSFL--------REFeinV 114
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTiakLMIGIEKVKSGE----IFYNNQAITDDNFEKLRKHIgivfqnpdNQF---V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYD-----DLYFMSHFKMHRRttksekrqaVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:PRK13648 98 GSIVKYDvafglENHAVPYDEMHRR---------VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2492600 190 PTTGLDSFSAYTVIKTLRHLCTRRRIA----KHSLTQVYGED 227
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITiisiTHDLSEAMEAD 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-202 |
5.26e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLlAAISQRLRGNLTGDVVLNGMAME-------RDQMTRISSFLREFEINVKTF 117
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTV-AALLQNLYQPTGGQVLLDGVPLVqydhhylHRQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYDdlyfmshfkmhRRTTKSEKRQAVSDLLLA----VGLRDAAHTRI----QQLSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:TIGR00958 575 IAYG-----------LTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170
....*....|...
gi 2492600 190 PTTGLDSFSAYTV 202
Cdd:TIGR00958 644 ATSALDAECEQLL 656
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
54-220 |
6.17e-06 |
|
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: 48.13 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 54 KTGDLIAILGGSGAGKTTLLAAISQRLRGNLTG-------DVVLN---GMAMErDQMTRissfLREFEINVKTFTAYDDL 123
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwDEILDefrGSELQ-NYFTK----LLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 124 yFMSHFKMHRRT--TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYT 201
Cdd:cd03236 99 -IPKAVKGKVGEllKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|..
gi 2492600 202 VIKTLRHLCTRRR---IAKHSL 220
Cdd:cd03236 178 AARLIRELAEDDNyvlVVEHDL 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
39-222 |
6.60e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 39 KQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLlAAISQRLRGNLTGDVVLNGMAMERDQM----TRISSFLREFEINV 114
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTT-ARLIDGLFEEFEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFMSHfkmHRRTTKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:PRK13642 95 VGATVEDDVAFGME---NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180
....*....|....*....|....*...
gi 2492600 195 DSFSAYTVIKTLRHLCTRRRIAKHSLTQ 222
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITH 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
43-195 |
7.77e-06 |
|
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: 47.33 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 43 LGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI---SQRLRG-----NLTGDVVLNGMAMERDQMTRISSFLREFEINV 114
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIlgeMQTLEGkvhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 ktfTAYDDLYFMSHFKMHRRTTKSEKRQAVSDL-LLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:cd03290 94 ---TVEENITFGSPFNKQRYKAVTDACSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
..
gi 2492600 194 LD 195
Cdd:cd03290 171 LD 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
53-209 |
8.52e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 53 LKTGDLIAILGGSGAGKTTLLAAISQRLRGNL-------TGDVVLngmamERDQMTRISSF---LREFEINVKTFTAYDD 122
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLgdyeeepSWDEVL-----KRFRGTELQNYfkkLYNGEIKVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 123 LYFMShFKMHRRT--TKSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAY 200
Cdd:PRK13409 171 LIPKV-FKGKVREllKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
....*....
gi 2492600 201 TVIKTLRHL 209
Cdd:PRK13409 250 NVARLIREL 258
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-198 |
8.59e-06 |
|
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: 48.78 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLL---AAISQRLRG-------------------NLTGDV---VLNGMAMERDQ 99
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimAGVDKDFNGearpqpgikvgylpqepqlDPTKTVrenVEEGVAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 MTRISsflrefEINVKtFTAYDDLYfmshfkmhrrtTKSEKRQA-VSDLLLAVGLRD-------AAH--------TRIQQ 163
Cdd:TIGR03719 100 LDRFN------EISAK-YAEPDADF-----------DKLAAEQAeLQEIIDAADAWDldsqleiAMDalrcppwdADVTK 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2492600 164 LSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFS 198
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
31-195 |
9.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.92 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 31 YSFWNEcRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAisqrlrgnltgdvvLNGMAMERDQMTRISSFLREF 110
Cdd:PRK13631 28 YCVFDE-KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTH--------------FNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINVKTFTAYDDLYFMSHFKMHRRT------------------------------TKSEKRQAVSDLLLAVGLRDAAHTR 160
Cdd:PRK13631 93 KKNNHELITNPYSKKIKNFKELRRRvsmvfqfpeyqlfkdtiekdimfgpvalgvKKSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2492600 161 IQ-QLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK13631 173 SPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-195 |
1.03e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 23 VPAQEQSNYSFWNEcrkQRELGILHDVSGHLKTGDLIAILGGSGAGKT-TLLAAIsqRLRGNLTGDVVLNGMAMERDQMT 101
Cdd:PRK10261 12 VLAVENLNIAFMQE---QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQAGGLVQCDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 102 RISsfLREFE--------------INVKTFTAYDDLY-----FMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAaHTRI- 161
Cdd:PRK10261 87 VIE--LSEQSaaqmrhvrgadmamIFQEPMTSLNPVFtvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILs 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2492600 162 ---QQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK10261 164 rypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
44-195 |
1.42e-05 |
|
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: 45.89 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 44 GILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMAMERDqmtRISSFLRefeinvktftayddl 123
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG-LRPPASGEITLDGKPVTRR---SPRDAIR--------------- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2492600 124 YFMSHFkmhrrttkSEKRQAVSdLLLAVGLRDAAHTRiQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03215 75 AGIAYV--------PEDRKREG-LVLDLSVAENIALS-SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
45-195 |
1.65e-05 |
|
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: 45.61 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAmerdqmtrissflrefeinvktftaydDLY 124
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-GLWPWGSGRIGMPEGE---------------------------DLL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 125 FMShfkmhRRTtksekrqavsdlLLAVG-LRDA-AHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:cd03223 68 FLP-----QRP------------YLPLGtLREQlIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
48-212 |
1.68e-05 |
|
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: 47.90 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAME-RDQMTRISSFL--------REFEINVKTFT 118
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDiRNPAQAIRAGIamvpedrkRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 119 AYDDLYFMSHFKMHRRTTKSEKRQAVSDLLLAVGLRDAA-HTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSF 197
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170
....*....|....*
gi 2492600 198 SAYTVIKTLRHLCTR 212
Cdd:TIGR02633 438 AKYEIYKLINQLAQE 452
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-195 |
2.14e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNL---TGDVVLNGMAME----RDQMTRISSFLRE--------F 110
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLY----GALprtSGYVTLDGHEVVtrspQDGLANGIVYISEdrkrdglvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 111 EINVK---TFTAYDdlYFMshfKMHRRTTKSEKRQAVSDLLLAVGL----RDAAhtrIQQLSGGERKRLSLAEELITDPI 183
Cdd:PRK10762 344 GMSVKenmSLTALR--YFS---RAGGSLKHADEQQAVSDFIRLFNIktpsMEQA---IGLLSGGNQQKVAIARGLMTRPK 415
|
170
....*....|..
gi 2492600 184 FLFCDEPTTGLD 195
Cdd:PRK10762 416 VLILDEPTRGVD 427
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
46-209 |
2.19e-05 |
|
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: 45.39 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsqrlrgnltgdvvlngmaMERDQMTRISSFLREFEinvktftaYDDLYF 125
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG------------------LYASGKARLISFLPKFS--------RNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKmhrrttksekrqavsdLLLAVGLRDAAHTRI-QQLSGGERKRLSLAEELITDP---IFLFcDEPTTGLDSFSAYT 201
Cdd:cd03238 65 IDQLQ----------------FLIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPpgtLFIL-DEPSTGLHQQDINQ 127
|
....*...
gi 2492600 202 VIKTLRHL 209
Cdd:cd03238 128 LLEVIKGL 135
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-209 |
2.85e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 46.25 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 51 GHLKTGDLIAILGGSGAGKTTLLAAISQRLR------GNLTGDVVLNGMAMERDQMTRISSFLREfeinvKTftayDDLY 124
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKpdegdiEIELDTVSYKPQYIKADYEGTVRDLLSS-----IT----KDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFKmhrrttksekrqavSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIK 204
Cdd:cd03237 91 THPYFK--------------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
....*
gi 2492600 205 TLRHL 209
Cdd:cd03237 157 VIRRF 161
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
55-209 |
2.99e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 55 TGDLIAILGGSGAGKTTLLAAI------SQRLRGNLTGDVVLNGmamerDQMTRISsflREFEINVKTFTAyddLYFMSH 128
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIryalygKARSRSKLRSDLINVG-----SEEASVE---LEFEHGGKRYRI---ERRQGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 129 FKMHRRTTKSEKRQAVSDLL----------LAVGLRDAAHTRIQQ-----------------------LSGGERKRLSLA 175
Cdd:COG0419 91 FAEFLEAKPSERKEALKRLLgleiyeelkeRLKELEEALESALEElaelqklkqeilaqlsgldpietLSGGERLRLALA 170
|
170 180 190
....*....|....*....|....*....|....
gi 2492600 176 EELitdpiFLFCDepTTGLDSFSAYTVIKTLRHL 209
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALEEL 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-222 |
3.98e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.60 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 60 AILGGSGAGKTTLLAAISQRLRGN----LTGDVVLNGMAMERDQMTRIS-----SFLREFEINVKTFTAYDDLYFmsHFK 130
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLELNeearVEGEVRLFGRNIYSPDVDPIEvrrevGMVFQYPNPFPHLTIYDNVAI--GVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 131 MHRRT-TKSEKRQAVSDLLLAVGLRDAAHTRIQ----QLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKT 205
Cdd:PRK14267 112 LNGLVkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170
....*....|....*....
gi 2492600 206 LRHLCTRRRI--AKHSLTQ 222
Cdd:PRK14267 192 LFELKKEYTIvlVTHSPAQ 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
45-189 |
5.38e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.07 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqrlrGNL---TGDVVLNGmamerdqmtRISSFLrefEINV---KTFT 118
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA----GILeptSGRVEVNG---------RVSALL---ELGAgfhPELT 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 119 AYDDLYFMSHF-KMHRRTTKsEKRQAVSDllLAvGLRDAAHTRIQQLSGGERKRLSLAEELITDP-IFLFcDE 189
Cdd:COG1134 105 GRENIYLNGRLlGLSRKEID-EKFDEIVE--FA-ELGDFIDQPVKTYSSGMRARLAFAVATAVDPdILLV-DE 172
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-209 |
6.34e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 118 TAYD-DLYFMSHFKMHrrttksEKRQAvsdlLLAVGLRDAAHTR-IQQLSGGERKRLSLAEELIT---DPIFLFCDEPTT 192
Cdd:PRK00635 772 TAYEaEKFFLDEPSIH------EKIHA----LCSLGLDYLPLGRpLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTT 841
|
90
....*....|....*..
gi 2492600 193 GLDSFSAYTVIKTLRHL 209
Cdd:PRK00635 842 GLHTHDIKALIYVLQSL 858
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
42-195 |
6.46e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.38 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 42 ELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAaISQRLRGNLTGDVVLNGMAMERD--QMTRISSFLREFEInVKTFTA 119
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTNGLIISETGQTIVGDYAIPANlkKIKEVKRLRKEIGL-VFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YD--------DLYFMShfkMHRRTTKSEKRQAVSDLLLAVGL-RDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEP 190
Cdd:PRK13645 101 YQlfqetiekDIAFGP---VNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
....*
gi 2492600 191 TTGLD 195
Cdd:PRK13645 178 TGGLD 182
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
49-208 |
7.07e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 49 VSGHLKTGDLIAILGGSGAGKTTLLAAISQRL--RGNLT-GDVVLNGMAME--RDQMTRIS-------SFLREfeiNVkt 116
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLpyQGSLKiNGIELRELDPEswRKHLSWVGqnpqlphGTLRD---NV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 117 ftayddlyFMSHFKMHRRTTKSEKRQA-VSDLL--LAVGLrdaaHTRIQQ----LSGGERKRLSLAEELITDPIFLFCDE 189
Cdd:PRK11174 444 --------LLGNPDASDEQLQQALENAwVSEFLplLPQGL----DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDE 511
|
170
....*....|....*....
gi 2492600 190 PTTGLDSFSAYTVIKTLRH 208
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNA 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
48-209 |
7.28e-05 |
|
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: 45.70 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 48 DVSGHLKTGDLIAILGGSGAGKTTLLAAIS---QRLRGNLT-GD-VVLNGMAMERDQMT-------RISSFLREFEINVK 115
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITgqeQPDSGTIEiGEtVKLAYVDQSRDALDpnktvweEISGGLDIIKLGKR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 116 TFT--AYddlyfMSHFKMhrRTTKSEKRqavsdlllaVGlrdaahtriqQLSGGERKRLSLAEELITDPIFLFCDEPTTG 193
Cdd:TIGR03719 420 EIPsrAY-----VGRFNF--KGSDQQKK---------VG----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
170
....*....|....*.
gi 2492600 194 LDsfsaytvIKTLRHL 209
Cdd:TIGR03719 474 LD-------VETLRAL 482
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-221 |
8.04e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.86 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAIsQRLRGNLTGDVVLNGMAMERdqmTRISSFLREFEINVKTFTAYDDLy 124
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLI-QRHFDVSEGDIRFHDIPLTK---LQLDSWRSRLAVVSQTPFLFSDT- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 125 FMSHFKMHRRTTKSEKRQAVS-------DLL-LAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDS 196
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVArlasvhdDILrLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180
....*....|....*....|....*..
gi 2492600 197 FSAYTVIKTLRHLCTRRR--IAKHSLT 221
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTviISAHRLS 511
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-195 |
1.03e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.74 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRLRGNLT---GDVVLNGMAMERDQMTRISSFLR-------EF-EINV 114
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIM----QLLNGLHVptqGSVRVDDTLITSTSKNKDIKQIRkkvglvfQFpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYF-MSHFKMhrrtTKSEKRQAVSDLLLAVGLRDAAHTRIQ-QLSGGERKRLSLAEELITDPIFLFCDEPTT 192
Cdd:PRK13649 99 FEETVLKDVAFgPQNFGV----SQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
...
gi 2492600 193 GLD 195
Cdd:PRK13649 175 GLD 177
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-195 |
1.04e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 1 MPMDEGDAQGSLLLEWKQLNYYVPAQEqsnysfwnecrkqrelgILHDVSGHLKTGDLIAILGGSGAGKTTLLaaisQRL 80
Cdd:PRK11147 307 MQVEEASRSGKIVFEMENVNYQIDGKQ-----------------LVKDFSAQVQRGDKIALIGPNGCGKTTLL----KLM 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 81 RGNLTGDvvlNGmamerdqmtrissflrEFEINVKTFTAYddlyfmshFKMHRRTTKSEKrqAVSDLLlAVG-------- 152
Cdd:PRK11147 366 LGQLQAD---SG----------------RIHCGTKLEVAY--------FDQHRAELDPEK--TVMDNL-AEGkqevmvng 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2492600 153 --------LRD------AAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK11147 416 rprhvlgyLQDflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
46-206 |
1.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQrLRGNLTGDVVLNGMAM-----------------ERDQMTRISSFLr 108
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG-IREKSAGTITLHGKKInnhnaneainhgfalvtEERRSTGIYAYL- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 109 efEINVKTFTAYDDLYfMSHFKMHRRTTKSEKRQAVSDlllAVGLRDAAH-TRIQQLSGGERKRLSLAEELITDPIFLFC 187
Cdd:PRK10982 342 --DIGFNSLISNIRNY-KNKVGLLDNSRMKSDTQWVID---SMRVKTPGHrTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180
....*....|....*....|..
gi 2492600 188 DEPTTGLD---SFSAYTVIKTL 206
Cdd:PRK10982 416 DEPTRGIDvgaKFEIYQLIAEL 437
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-223 |
1.88e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAMERDQMTRIssflreFEINVKtftayDDLYF 125
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQVSWI------FNATVR-----DNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 126 MSHFKMHRRTTKSEKRQAVSDLLLAVGlRDaaHTRIQQ----LSGGERKRLSLAEELITDP-IFLFcDEPTTGLDSFSAY 200
Cdd:PLN03130 702 GSPFDPERYERAIDVTALQHDLDLLPG-GD--LTEIGErgvnISGGQKQRVSMARAVYSNSdVYIF-DDPLSALDAHVGR 777
|
170 180 190
....*....|....*....|....*....|...
gi 2492600 201 TVIKTlrhlCTRRRIAK----------HSLTQV 223
Cdd:PLN03130 778 QVFDK----CIKDELRGktrvlvtnqlHFLSQV 806
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-76 |
2.95e-04 |
|
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: 42.46 E-value: 2.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2492600 34 WNEcRKQRELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI 76
Cdd:cd03250 10 WDS-GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL 51
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-209 |
3.46e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 41 RELGILHDVSGHLKTGDLIAILGGSGAGKTTLLAAI--SQRLRGnltGDVVLNGMAME--------RDQMTRISSFLRE- 109
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgVDKRAG---GEIRLNGKDISprspldavKKGMAYITESRRDn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 110 -----FEI--------NVKTfTAYDDLYFMSHFKMHRRTTKSEKRqavsdlLLAVGLRdAAHTRIQQLSGGERKRLSLAE 176
Cdd:PRK09700 351 gffpnFSIaqnmaisrSLKD-GGYKGAMGLFHEVDEQRTAENQRE------LLALKCH-SVNQNITELSGGNQQKVLISK 422
|
170 180 190
....*....|....*....|....*....|...
gi 2492600 177 ELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
52-195 |
8.37e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 52 HLKTGDLIAILGGSGAGKTTLLAAISqrlrgnltGDVVLNGMAMERDQMTRISSFL----REFEINVKTFTA-------- 119
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILN--------GEVLLDDGRIIYEQDLIVARLQqdppRNVEGTVYDFVAegieeqae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 ----YDDLyfmSHFKMHRRTTKSEKRQA-----------------VSDLLLAVGLrdAAHTRIQQLSGGERKRLSLAEEL 178
Cdd:PRK11147 97 ylkrYHDI---SHLVETDPSEKNLNELAklqeqldhhnlwqlenrINEVLAQLGL--DPDAALSSLSGGWLRKAALGRAL 171
|
170
....*....|....*..
gi 2492600 179 ITDPIFLFCDEPTTGLD 195
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD 188
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
164-194 |
9.20e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 9.20e-04
10 20 30
....*....|....*....|....*....|....*
gi 2492600 164 LSGGERKRLSLAEELI---TDP-IFLFcDEPTTGL 194
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKtLYIL-DEPTTGL 860
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
55-92 |
9.36e-04 |
|
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: 40.05 E-value: 9.36e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2492600 55 TGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNG 92
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG 38
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
58-83 |
9.81e-04 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 40.98 E-value: 9.81e-04
10 20
....*....|....*....|....*.
gi 2492600 58 LIAILGGSGAGKTTLLAAISQRLRGN 83
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGAD 34
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
46-194 |
1.10e-03 |
|
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: 41.45 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTLL-----AAISQRLRGNLT----GDVVLNGMAMER----DQ------------- 99
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEqpgnHDRIEGLEHIDKviviDQspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 100 MTRISSFLREF---------------EINVKTFTAYDDL---------YFMSHFKMHRRTtksekrqavsDLLLAVGLrd 155
Cdd:cd03271 91 YTGVFDEIRELfcevckgkrynretlEVRYKGKSIADVLdmtveealeFFENIPKIARKL----------QTLCDVGL-- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2492600 156 aAHTRIQQ----LSGGERKRLSLAEELI---TDPIFLFCDEPTTGL 194
Cdd:cd03271 159 -GYIKLGQpattLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-206 |
1.40e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2492600 162 QQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTL 206
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
160-209 |
1.51e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2492600 160 RIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDsfsaytvIKTLRHL 209
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRAL 484
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-194 |
1.99e-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: 41.54 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2492600 146 DLLLAVGLrdaAHTRIQQ----LSGGERKRLSLAEEL---ITDPIFLFCDEPTTGL 194
Cdd:TIGR00630 811 QTLCDVGL---GYIRLGQpattLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL 863
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
137-195 |
2.04e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2492600 137 KSEKRQAVSDLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
53-214 |
2.07e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.94 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 53 LKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDvvlngmameRDQMTRISSFLREFEinvktfTAYDDLYFMSHFKMH 132
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAITYALYGKTPRY---------GRQENLRSVFAPGED------TAEVSFTFQLGGKKY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 133 R--RTTKSEKRQAVSDLLLAVGLRDAAHTR-IQQLSGGER------KRLSLAEELITD---PI-FLFCDEPTTGLDSFSA 199
Cdd:cd03279 90 RveRSRGLDYDQFTRIVLLPQGEFDRFLARpVSTLSGGETflaslsLALALSEVLQNRggaRLeALFIDEGFGTLDPEAL 169
|
170
....*....|....*
gi 2492600 200 YTVIKTLRHLCTRRR 214
Cdd:cd03279 170 EAVATALELIRTENR 184
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
46-209 |
2.44e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.46 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 46 LHDVSGHLKTGDLIAILGGSGAGKTTllaaISQRLRGNLT---GDVVLNGMAMERDQMTrissflreFEINVKT---FTA 119
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALLIpseGKVYVDGLDTSDEENL--------WDIRNKAgmvFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 120 YD----------DLYFMSHfkmHRRTTKSEKRQAVSDLLLAVGL----RDAAHTriqqLSGGERKRLSLAEELITDPIFL 185
Cdd:PRK13633 94 PDnqivativeeDVAFGPE---NLGIPPEEIRERVDESLKKVGMyeyrRHAPHL----LSGGQKQRVAIAGILAMRPECI 166
|
170 180
....*....|....*....|....
gi 2492600 186 FCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKEL 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-223 |
3.48e-03 |
|
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: 40.70 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 33 FWNECRKQRE-LG-ILHDVSGHLKTGDLIAILGGSGAGKTTLLAAISqRLRGNLTGDVVLNGMAME-------RDQMTRI 103
Cdd:TIGR00957 1287 FRNYCLRYREdLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESAEGEIIIDGLNIAkiglhdlRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 104 SS----FLREFEINVKTFTAY-DDLYFMSHFKMHRRTTKSEkrqavsdllLAVGLRDAAHTRIQQLSGGERKRLSLAEEL 178
Cdd:TIGR00957 1366 PQdpvlFSGSLRMNLDPFSQYsDEEVWWALELAHLKTFVSA---------LPDKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2492600 179 ITDPIFLFCDEPTTGLDSFSAYTVIKTLR---HLCTRRRIAkHSLTQV 223
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRtqfEDCTVLTIA-HRLNTI 1483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
164-209 |
3.67e-03 |
|
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: 39.09 E-value: 3.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2492600 164 LSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYTVIKTLRHL 209
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
58-116 |
4.18e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 36.16 E-value: 4.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492600 58 LIAILGGSGAGKTTLLAAISQRLRGN----LTGDVVLNGMAMERDQMTRISSFLREFEINVKT 116
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGGRsvvvLDEIVILEGLYASYKSRDARIRDLADLKIYLDA 63
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
58-90 |
4.23e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 39.17 E-value: 4.23e-03
10 20 30
....*....|....*....|....*....|...
gi 2492600 58 LIAILGGSGAGKTTLLAAISQRLRGNLTgDVVL 90
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLAERLEARGY-EVVL 33
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-223 |
4.87e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTLLAA---ISQRLRGNLT---GDVVLNGMAMERDQMTRISS----FLREFEINV 114
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAlfrIVELEKGRIMiddCDVAKFGLTDLRRVLSIIPQspvlFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492600 115 KTFTAYDDLYFMShfKMHRRTTKSEKRQAvsdlllAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGL 194
Cdd:PLN03232 1331 DPFSEHNDADLWE--ALERAHIKDVIDRN------PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190
....*....|....*....|....*....|..
gi 2492600 195 DSFSAYTVIKTLRH---LCTRRRIAkHSLTQV 223
Cdd:PLN03232 1403 DVRTDSLIQRTIREefkSCTMLVIA-HRLNTI 1433
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
159-195 |
8.60e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 8.60e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2492600 159 TRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| DO-GTPase2 |
pfam19993 |
Double-GTPase 2; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs ... |
58-86 |
9.58e-03 |
|
Double-GTPase 2; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs to a previously unrecognized family of the TRAFAC clade with a conserved glutamate in its Walker B motif.
Pssm-ID: 466247 Cd Length: 227 Bit Score: 38.06 E-value: 9.58e-03
10 20 30
....*....|....*....|....*....|
gi 2492600 58 LIAILGGSGAGKTTLLAAI-SQRLRGNLTG 86
Cdd:pfam19993 2 VIGIVGPPDAGKTTLLASLyLLLLRGALAG 31
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-195 |
9.64e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 9.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2492600 155 DAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLD 195
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-72 |
9.71e-03 |
|
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: 39.03 E-value: 9.71e-03
10 20
....*....|....*....|....*...
gi 2492600 45 ILHDVSGHLKTGDLIAILGGSGAGKTTL 72
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTL 400
|
|
| |
