|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-542 |
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: 769.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIG-KEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMKAN- 78
Cdd:TIGR00955 53 LLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDaKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRv 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 -KHTRRERVDEIIEMLRLQNCRDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:TIGR00955 133 tKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 158 ANSGRT---LIHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWIQSKLSVIPNNETKSRET 234
Cdd:TIGR00955 213 AQKGKTiicTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRER 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 235 IGKIIEFYEKSIIHQKSIVEIRV--------IATTELPPYIE-NPGFFAETGALLKRACLDVIRSPAQMRMKLIQKVVMG 305
Cdd:TIGR00955 293 IEKICDSFAVSDIGRDMLVNTNLwsgkagglVKDSENMEGIGyNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 306 LFIGSLYWQQPLDPRGVRNTNSALYFLIAELTFSTMFGIMTFMEHELPLIAREYHDGLFYVISYYISRFLSYLPLFTIDG 385
Cdd:TIGR00955 373 ILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILP 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 386 ALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSGLYGNTNNFPVYIR 465
Cdd:TIGR00955 453 ALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFK 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 466 WMQWTSWCRYGFEGLVVNQWSQVDNPKWD--------PFYRELILKQFSFNKDNYQLDVIGLCSIVIFFYLAGYIALFIR 537
Cdd:TIGR00955 533 WLSYLSWFRYGNEGLLINQWSDVDNIECTsanttgpcPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIR 612
|
....*
gi 1017384763 538 IRLSR 542
Cdd:TIGR00955 613 IRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-191 |
3.21e-68 |
|
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: 218.19 E-value: 3.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNmKGLEKNGTVKVNGTKIGK-EISLISGFAQQQEIFIPTLTVDEYLMIQARLRmkank 79
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGRPLDKrSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 htrrervdeiiemlrlqncrdlkigtpglvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAN 159
Cdd:cd03213 111 -------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 160 SGRTL---IHQPTAELFFQFDKIIFLSMGKTAFMG 191
Cdd:cd03213 160 TGRTIicsIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-489 |
1.67e-61 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 219.59 E-value: 1.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRM--KAN 78
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQpkSVS 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 KHTRRERVDEIIEMLRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNP-SLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:TIGR00956 871 KSEKMEYVEEVIKLLEMESYADAVVGVPG--EGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKL 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 158 ANSGRTL---IHQPTAELFFQFDKIIFLSMG-KTAFMG----TPHESVKFFADCG-HPIPKLFNPPEWIQSKLSVIPNNE 228
Cdd:TIGR00956 949 ADHGQAIlctIHQPSAILFEEFDRLLLLQKGgQTVYFGdlgeNSHTIINYFEKHGaPKCPEDANPAEWMLEVIGAAPGAH 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 229 TKsretigkiIEFYEK---SIIHQKSIVEI-RVIATTELPPYIENPG--------FFAETGALLKRACLDVIRSPAQMRM 296
Cdd:TIGR00956 1029 AN--------QDYHEVwrnSSEYQAVKNELdRLEAELSKAEDDNDPDalskyaasLWYQFKLVLWRTFQQYWRTPDYLYS 1100
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 297 KLIQKVVMGLFIGSLYWQQPLDPRGVRNTNSALY--FLIAELTFSTMFGimTFMEHELPLIAREYHDGLFYVISYYISRF 374
Cdd:TIGR00956 1101 KFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFmaTVLFNPLIQQYLP--PFVAQRDLYEVRERPSRTFSWLAFIAAQI 1178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 375 LSYLPLFTIDGALMIVISYWMIGL-------NSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLF 447
Cdd:TIGR00956 1179 TVEIPYNLVAGTIFFFIWYYPVGFywnasktGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMC 1258
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1017384763 448 ALLSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVNQWSQVD 489
Cdd:TIGR00956 1259 LSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVP 1300
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-191 |
9.87e-54 |
|
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: 181.32 E-value: 9.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISL-ISGFAQQQEIFIPTLTVDEYLMIQARLRMKanK 79
Cdd:cd03234 35 VMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQkCVAYVRQDDILLPGLTVRETLTYTAILRLP--R 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 HTRRERVDEIIEMLRLQNCRDLKIGTPgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAN 159
Cdd:cd03234 113 KSSDAIRKKRVEDVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 160 SGRTL---IHQPTAELFFQFDKIIFLSMGKTAFMG 191
Cdd:cd03234 192 RNRIViltIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-526 |
1.24e-53 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 196.61 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKnGTVKVNG-TKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRM--KA 77
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKTGGYIE-GDIRISGfPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLpkEV 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKHTRRERVDEIIEMLRLQNCRDLKIGTPGlVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PLN03140 987 SKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 158 ANSGRTL---IHQPTAELFFQFDKIIFLSMGKTAFMGTP-----HESVKFF-ADCGHP-IPKLFNPPEWIQSKLSVipnn 227
Cdd:PLN03140 1066 VDTGRTVvctIHQPSIDIFEAFDELLLMKRGGQVIYSGPlgrnsHKIIEYFeAIPGVPkIKEKYNPATWMLEVSSL---- 1141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 228 ETKSRETIgKIIEFYEKSIIHQKSIVEIRVIATTelPPYIENPGF---FAETGALLKRACL-----DVIRSPAQMRMKLI 299
Cdd:PLN03140 1142 AAEVKLGI-DFAEHYKSSSLYQRNKALVKELSTP--PPGASDLYFatqYSQSTWGQFKSCLwkqwwTYWRSPDYNLVRFF 1218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 300 QKVVMGLFIGSLYWQQPldprGVRNTNSALYFLIAELTFSTMFGIMTFMEHELPLIA-------REYHDGLFYVISYYIS 372
Cdd:PLN03140 1219 FTLAAALMVGTIFWKVG----TKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAvertvfyRERAAGMYSALPYAIA 1294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 373 RFLSYLPLFTIDGALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSG 452
Cdd:PLN03140 1295 QVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSG 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 453 LYGNTNNFPVYIRWMQW---TSWCRYgfeGLVVNQWSQVDNP------KWDPFYRELILKQFSFNKDnYQLDVIG-LCSI 522
Cdd:PLN03140 1375 FFIPRPKIPKWWVWYYWicpVAWTVY---GLIVSQYGDVEDTikvpggAPDPTIKWYIQDHYGYDPD-FMGPVAAvLVGF 1450
|
....
gi 1017384763 523 VIFF 526
Cdd:PLN03140 1451 TVFF 1454
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-191 |
4.05e-48 |
|
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: 165.49 E-value: 4.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKnGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRmkankh 80
Cdd:cd03232 35 LTALMGESGAGKTTLLDVLAGRKTAGVIT-GEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 trrervdeiiemlrlqncrdlkigtpglvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANS 160
Cdd:cd03232 108 ------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 161 GRTL---IHQPTAELFFQFDKIIFL-SMGKTAFMG 191
Cdd:cd03232 158 GQAIlctIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-485 |
3.77e-46 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 171.60 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRnMKGLEKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMkANKH 80
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGR-IQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRL-PKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 TRRERV---DEIIEMLRLQNCRDLKIGTpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PLN03211 174 TKQEKIlvaESVISELGLTKCENTIIGN-SFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 158 ANSGRTL---IHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWI----------------- 217
Cdd:PLN03211 253 AQKGKTIvtsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLldlangvcqtdgvsere 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 218 --QSKLSVIPNNET------KSRETIGKIIEFYEKSIIHQKSIVEIRVIattelppYIENPGFFAETGALLKRAcLDVIR 289
Cdd:PLN03211 333 kpNVKQSLVASYNTllapkvKAAIEMSHFPQANARFVGSASTKEHRSSD-------RISISTWFNQFSILLQRS-LKERK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 290 SPAQMRMKLIQKVVMGLFIGSLYWQQplDPRGVRNTNSALYFL-IAELTFSTMFGIMTFMEhELPLIAREYHDGLFYVIS 368
Cdd:PLN03211 405 HESFNTLRVFQVIAAALLAGLMWWHS--DFRDVQDRLGLLFFIsIFWGVFPSFNSVFVFPQ-ERAIFVKERASGMYTLSS 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 369 YYISRFLSYLPLFTIDGALMIVISYWMIGLNStwQQVAKSILISVLVEQSATSCGLFLAclfetTSLAIAFAVPASGL-- 446
Cdd:PLN03211 482 YFMARIVGDLPMELILPTIFLTVTYWMAGLKP--ELGAFLLTLLVLLGYVLVSQGLGLA-----LGAAIMDAKKASTIvt 554
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1017384763 447 -----FALLSGLYgnTNNFPVYIRWMQWTSWCRYGFEGLVVNQW 485
Cdd:PLN03211 555 vtmlaFVLTGGFY--VHKLPSCMAWIKYISTTFYSYRLLINVQY 596
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-195 |
1.56e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.67 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRm 75
Cdd:COG1131 28 IFGLLGPNGAGKTTTIRMLL-----GLLRptSGEVRVLGEDVARDPAEVRrriGYVPQEPALYPDLTVRENLRFFARLY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILK 155
Cdd:COG1131 102 GLPRKEARERIDELLELFGLTDAADRKVGT------LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1017384763 156 NLANSGRTLI---HQpTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG1131 176 ELAAEGKTVLlstHY-LEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-494 |
2.86e-39 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 153.73 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGL-EKNGTVKVNG---TKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMK 76
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIASNTDGFHiGVEGVITYDGitpEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 AN------KHTRRERV-DEIIEMLRLQNCRDLKIGTPgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:TIGR00956 169 QNrpdgvsREEYAKHIaDVYMATYGLSHTRNTKVGND-FVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 150 VVQILKNLANSGRTL----IHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWIQSKLS--- 222
Cdd:TIGR00956 248 FIRALKTSANILDTTplvaIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSpae 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 223 --VIPNNETKSRETIGKIIEFYEKSIIHQKSIVEI-----RVIATTELPPYIENP----------------GFFAETGAL 279
Cdd:TIGR00956 328 rqIKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIdeyldRCSESDTKEAYRESHvakqskrtrpsspytvSFSMQVKYC 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 280 LKRACLDVIRSPAQMRMKLIQKVVMGLFIGSLYWQQPLDPRGVRNTNSALYFLIAELTFSTMFGIMTFMEHeLPLIAREY 359
Cdd:TIGR00956 408 LARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIASMYEA-RPIVEKHR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 360 HDGLFYVISYYISRFLSYLPLFTIDGALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATscGLFLACLFETTSLAIAF 439
Cdd:TIGR00956 487 KYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMS--HLFRSIGAVTKTLSEAM 564
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 440 AVPASGLFAL--LSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVNQWSqvdNPKWD 494
Cdd:TIGR00956 565 TPAAILLLALsiYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFH---GRRFE 618
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
279-483 |
1.17e-35 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 132.40 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 279 LLKRACLDVIRSPAQMRMKLIQKVVMGLFIGSLYWQQPlDPRGVRNTNSALYFLIAELTFSTMFGIMTFMEHELPLIARE 358
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 359 YHDGLFYVISYYISRFLSYLPLFTIDGALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIA 438
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1017384763 439 FAVPASGLFALLSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVN 483
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-195 |
3.35e-31 |
|
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: 121.12 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRmK 76
Cdd:COG4555 30 TGLLGPNGAGKTTLLRMLA-----GLLKpdSGSILIDGEDVRKEPREARrqiGVLPDERGLYDRLTVRENIRYFAELY-G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ANKHTRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKN 156
Cdd:COG4555 104 LFDEELKKRIEELIELLGLEEFLDRR------VGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1017384763 157 LANSGRTLI---HQPtAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG4555 178 LKKEGKTVLfssHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-186 |
3.91e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.53 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIG----KEISLI----SGFaqqqeIF-----IPTLTVDE 65
Cdd:COG1136 36 FVAIVGPSGSGKSTLLNIL-----GGLDRptSGEVLIDGQDISslseRELARLrrrhIGF-----VFqffnlLPELTALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 66 YLMIQARLRmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:COG1136 106 NVALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQ------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1017384763 146 MAASVVQILKNLA-NSGRTLI---HQPtaELFFQFDKIIFLSMGK 186
Cdd:COG1136 179 TGEEVLELLRELNrELGTTIVmvtHDP--ELAARADRVIRLRDGR 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-193 |
3.37e-30 |
|
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: 117.61 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRMK 76
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLT-----GELRptSGTAYINGYSIRTDRKAARqslGYCPQFDALFDELTVREHLRFYARLKGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 aNKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKN 156
Cdd:cd03263 106 -PKSEIKEEVELLLRVLGLTDKANKRART------LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1017384763 157 LAnSGRTLI---HQPT-AELFfqFDKIIFLSMGKTAFMGTP 193
Cdd:cd03263 179 VR-KGRSIIlttHSMDeAEAL--CDRIAIMSDGKLRCIGSP 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-186 |
1.39e-29 |
|
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: 115.64 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIG----KEISLISGFAQQ---QEIFipTLTVDEYLMIqA 71
Cdd:cd03225 29 FVLIVGPNGSGKSTLLRLLN-----GLLGptSGEVLVDGKDLTklslKELRRKVGLVFQnpdDQFF--GPTVEEEVAF-G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03225 101 LENLGLPEEEIEERVEEALELVGLEGLRDRSPFT------LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 152 QILKNLANSGRTLI---HQPtAELFFQFDKIIFLSMGK 186
Cdd:cd03225 175 ELLKKLKAEGKTIIivtHDL-DLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-186 |
1.41e-29 |
|
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: 115.66 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIGK----EISLIS----GFAQQQEIFIPTLTVDEYLMIQ 70
Cdd:cd03255 32 FVAIVGPSGSGKSTLLNIL-----GGLDRptSGEVRVDGTDISKlsekELAAFRrrhiGFVFQSFNLLPDLTALENVELP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:cd03255 107 LLLA-GVPKKERRERAEELLERVGLGDRLNHYPSE------LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1017384763 151 VQILKNLA-NSGRTLI---HQPtaELFFQFDKIIFLSMGK 186
Cdd:cd03255 180 MELLRELNkEAGTTIVvvtHDP--ELAEYADRIIELRDGK 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-493 |
1.65e-26 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 114.56 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISL-ISGFAQQQEIFIPTLTVDEYLMIQARLRMKANK 79
Cdd:PLN03140 193 MTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRkTSAYISQNDVHVGVMTVKETLDFSARCQGVGTR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 H------TRRER---------------------------VDEIIEMLRLQNCRDLKIGTPgLVKGISGGEARRLTFAcEL 126
Cdd:PLN03140 273 YdllselARREKdagifpeaevdlfmkatamegvkssliTDYTLKILGLDICKDTIVGDE-MIRGISGGQKKRVTTG-EM 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 127 LSNPS-LLFADEPTSGLDSFMAASVVQILKNLA--NSGRTLIH--QPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFA 201
Cdd:PLN03140 351 IVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSllQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 202 DCGHPIPKLFNPPEWIQSKLS----------------VIPNNETKSRET---IGKIIEF-----YEKSIIHQKSIVEIRV 257
Cdd:PLN03140 431 SCGFKCPERKGTADFLQEVTSkkdqeqywadrnkpyrYISVSEFAERFKsfhVGMQLENelsvpFDKSQSHKAALVFSKY 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 258 -IATTElppyienpgffaetgalLKRACLD-----VIRSPAQMRMKLIQKVVMGLFIGSLYWQQPLDPRGvrNTNSALYf 331
Cdd:PLN03140 511 sVPKME-----------------LLKACWDkewllMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRN--EEDGALY- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 332 lIAELTFSTM------FGIMTFMEHELPLIAREyHDGLFY-VISYYISRFLSYLPLFTIDGALMIVISYWMIGLNSTWQQ 404
Cdd:PLN03140 571 -IGALLFSMIinmfngFAELALMIQRLPVFYKQ-RDLLFHpPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASR 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 405 VAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVNQ 484
Cdd:PLN03140 649 FFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNE 728
|
....*....
gi 1017384763 485 WSQvdnPKW 493
Cdd:PLN03140 729 MFA---PRW 734
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-191 |
9.69e-25 |
|
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: 101.57 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISLISG---FAQQQEIFIPTLTVDEylMIQARLRMKA 77
Cdd:cd03233 35 MVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGeiiYVSEEDVHFPTLTVRE--TLDFALRCKG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NkhtrrervdeiiEMLRlqncrdlkigtpglvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:cd03233 113 N------------EFVR----------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 158 ANSGRTL----IHQPTAELFFQFDKIIFLSMGKTAFMG 191
Cdd:cd03233 165 ADVLKTTtfvsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-202 |
1.67e-24 |
|
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: 102.03 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnvlmCRNMKGLEK--NGTVKVNGTKIGKE-ISLIS---GFAQQ----QeIFIPTltVDE----YL 67
Cdd:COG1122 30 VAIIGPNGSGKSTL-----LRLLNGLLKptSGEVLVDGKDITKKnLRELRrkvGLVFQnpddQ-LFAPT--VEEdvafGP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 68 MiqarlRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:COG1122 102 E-----NLGLPREEIRERVEEALELVGLEHLADRPPHE------LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1017384763 148 ASVVQILKNLANSGRTLI---HQPtAELFFQFDKIIFLSMGKTAFMGTPHEsvkFFAD 202
Cdd:COG1122 171 RELLELLKRLNKEGKTVIivtHDL-DLVAELADRVIVLDDGRIVADGTPRE---VFSD 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-140 |
1.83e-24 |
|
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: 99.26 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKI--------GKEISLISgfaqQQEIFIPTLTVDEYLMIQ 70
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIA-----GLLSptEGTILLDGQDLtdderkslRKEIGYVF----QDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANKHtRRERVDEIIEMLRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:pfam00005 84 LLLKGLSKRE-KDARAEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-195 |
2.06e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.09 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIsGFAQQQEIFIPT--LTVDEYLM--IQARLR 74
Cdd:COG1121 34 FVAIVGPNGAGKSTLLKAIL-----GLLPptSGTVRLFGKPPRRARRRI-GYVPQRAEVDWDfpITVRDVVLmgRYGRRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 M-KANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:COG1121 108 LfRRPSRADREAVDEALERVGLEDLADRPIGE------LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1017384763 154 LKNLANSGRTLI---H--QPTAELffqFDKIIFLSMGKTAFmGTPHE 195
Cdd:COG1121 182 LRELRREGKTILvvtHdlGAVREY---FDRVLLLNRGLVAH-GPPEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-189 |
2.37e-24 |
|
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: 101.07 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKIGKEISLIsGFAQQQEIFIPT--LTVDEYLMIQARLRM-- 75
Cdd:cd03235 28 LAIVGPNGAGKSTLLKAIL-----GLLKPtsGSIRVFGKPLEKERKRI-GYVPQRRSIDRDfpISVRDVVLMGLYGHKgl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 -KANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:cd03235 102 fRRLSKADKAKVDEALERVGLSELADRQIGE------LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 155 KNLANSGRTLI---HQPTAELFFqFDKIIFLSMGKTAF 189
Cdd:cd03235 176 RELRREGMTILvvtHDLGLVLEY-FDRVLLLNRTVVAS 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-187 |
3.29e-24 |
|
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: 100.37 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEI-------SLISGfaqqqEIFIPTLTVDEYLMIQAR 72
Cdd:cd03268 29 YGFLGPNGAGKTTTMKIIL-----GLIKpdSGEITFDGKSYQKNIealrrigALIEA-----PGFYPNLTARENLRLLAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKankhtRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03268 99 LLGI-----RKKRIDEVLDVVGLKDSAKKK------VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 153 ILKNLANSGRTLI---HQpTAELFFQFDKIIFLSMGKT 187
Cdd:cd03268 168 LILSLRDQGITVLissHL-LSEIQKVADRIGIINKGKL 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-186 |
2.02e-23 |
|
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: 97.08 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVdeylmiqarlrm 75
Cdd:cd03230 28 IYGLLGPNGAGKTTLIKIIL-----GLLKPdsGEIKVLGKDIKKEPEEVKrriGYLPEEPSLYENLTV------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 kankhtrrervdeiIEMLRLqncrdlkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILK 155
Cdd:cd03230 91 --------------RENLKL-----------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR 139
|
170 180 190
....*....|....*....|....*....|....
gi 1017384763 156 NLANSGRTLI---HQpTAELFFQFDKIIFLSMGK 186
Cdd:cd03230 140 ELKKEGKTILlssHI-LEEAERLCDRVAILNNGR 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-186 |
6.06e-23 |
|
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: 95.39 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISlisgfaqqqeifiptltvdeylmiqarlrmkan 78
Cdd:cd00267 27 IVALVGPNGSGKSTLLRAIA-----GLLKptSGEILIDGKDIAKLPL--------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 kHTRRERVdeiiemlrlqncrdlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLA 158
Cdd:cd00267 69 -EELRRRI--------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180 190
....*....|....*....|....*....|.
gi 1017384763 159 NSGRTLI---HQPtAELFFQFDKIIFLSMGK 186
Cdd:cd00267 128 EEGRTVIivtHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1-143 |
3.29e-22 |
|
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: 94.95 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGK---EISLISGFAQQQEIFIPTLTVDEYLMIQARLRM 75
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILA-----TLTPpsSGTIRIDGQDVLKqpqKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKG 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017384763 76 KANKHtRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:cd03264 102 IPSKE-VKARVDEVLELVNLGDRAKKKIGS------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-211 |
4.46e-22 |
|
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: 95.26 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGK--EISLIS-----GFAQQQEIFIPTLTVDEYLMIQAR 72
Cdd:cd03261 29 LAIIGPSGSGKSTLL-----RLIVGLLRpdSGEVLIDGEDISGlsEAELYRlrrrmGMLFQSGALFDSLTVFENVAFPLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEMLRLQNCRDLKigtPGlvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03261 104 EHTRLSEEEIREIVLEKLEAVGLRGAEDLY---PA---ELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017384763 153 ILKNLANS-GRTLI---HQpTAELFFQFDKIIFLSMGKTAFMGTPHEsvkfFADCGHPIPKLF 211
Cdd:cd03261 178 LIRSLKKElGLTSImvtHD-LDTAFAIADRIAVLYDGKIVAEGTPEE----LRASDDPLVRQF 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-183 |
9.27e-22 |
|
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: 93.31 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEI----SLISGFAQQQEIFiPTLTVDEYLMIQARLR 74
Cdd:COG4133 30 ALALTGPNGSGKTTLLRILA-----GLLPpsAGEVLWNGEPIRDARedyrRRLAYLGHADGLK-PELTVRENLRFWAALY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 mkaNKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:COG4133 104 ---GLRADREAIDEALEAVGLAGLADLPVRQ------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170 180 190
....*....|....*....|....*....|..
gi 1017384763 155 KNLANSGRTLI---HQPtaeLFFQFDKIIFLS 183
Cdd:COG4133 175 AAHLARGGAVLlttHQP---LELAAARVLDLG 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-195 |
1.62e-21 |
|
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: 93.66 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKI-GKEISLIS--GFA---QQQEIFiPTLTVDEYLMIQARL 73
Cdd:cd03219 29 HGLIGPNGAGKTTLFNLIS-----GFLRptSGSVLFDGEDItGLPPHEIArlGIGrtfQIPRLF-PELTVLENVMVAAQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMK---------ANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:cd03219 103 RTGsglllararREEREARERAEELLERVGLADLADRPAGE------LSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 145 FMAASVVQILKNLANSGRTLI---HQptAELFFQF-DKIIFLSMGKTAFMGTPHE 195
Cdd:cd03219 177 EETEELAELIRELRERGITVLlveHD--MDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-165 |
4.41e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 91.73 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKE---------ISLIsgfAQQQEIFiPTLTVDEYLMIQ 70
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIM-----GLLPprSGSIRFDGRDITGLppheraragIGYV---PEGRRIF-PELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANkhtRRERVDEIIEML-RLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:cd03224 100 AYARRRAK---RKARLERVYELFpRLKERRKQLAGT------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170
....*....|....*.
gi 1017384763 150 VVQILKNLANSGRTLI 165
Cdd:cd03224 171 IFEAIRELRDEGVTIL 186
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-195 |
2.98e-20 |
|
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: 94.05 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKIG--------KEISLISgfaQQQEIFIPTltvdeylmIQ 70
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLL-----GFLPPysGSILINGVDLSdldpaswrRQIAWVP---QNPYLFAGT--------IR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANKHTRRE--------RVDEIIEmlRLQNCRDLKIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGL 142
Cdd:COG4988 429 ENLRLGRPDASDEEleaaleaaGLDEFVA--ALPDGLDTPLGEGGR--GLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 143 DSFMAASVVQILKNLANsGRTLI---HQPtaELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG4988 505 DAETEAEILQALRRLAK-GRTVIlitHRL--ALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
3-195 |
6.01e-20 |
|
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: 90.53 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLMCrnmkgLEK--NGTVKVNGTKIGKE-------ISLISGFAQQQEIfiptLTVDEYLMIQARL 73
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTT-----LLRptSGTARVAGYDVVREprkvrrsIGIVPQYASVDED----LTGRENLEMMGRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 rMKANKHTRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:TIGR01188 94 -YGLPKDEAEERAEELLELFELGEAADRP------VGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1017384763 154 LKNLANSGRTLI----HQPTAELFfqFDKIIFLSMGKTAFMGTPHE 195
Cdd:TIGR01188 167 IRALKEEGVTILltthYMEEADKL--CDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-165 |
7.32e-20 |
|
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: 88.23 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNvLMCRnmKGLEKNGTVKVNGTKI----GKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARL 73
Cdd:cd03292 29 FVFLVGPSGAGKSTLLK-LIYK--EELPTSGTIRVNGQDVsdlrGRAIPYLRrkiGVVFQDFRLLPDRNVYENVAFALEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTRReRVDEIIEMLRLQNcrdlKIGTpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:cd03292 106 TGVPPREIRK-RVPAALELVGLSH----KHRA--LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170
....*....|..
gi 1017384763 154 LKNLANSGRTLI 165
Cdd:cd03292 179 LKKINKAGTTVV 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-206 |
1.21e-19 |
|
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: 91.89 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKeISLISGFAQQQEI----------FIPTLTVDEYLM 68
Cdd:COG1123 293 TLGLVGESGSGKSTLARLLL-----GLLRptSGSILFDGKDLTK-LSRRSLRELRRRVqmvfqdpyssLNPRMTVGDIIA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVDEIIEMLRLQ-NCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:COG1123 367 EPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHE------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 148 ASVVQILKNLANS-GRTLIhqptaelffqF------------DKIIFLSMGKTAFMGTPHEsvkFFADCGHP 206
Cdd:COG1123 441 AQILNLLRDLQRElGLTYL----------FishdlavvryiaDRVAVMYDGRIVEDGPTEE---VFANPQHP 499
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-186 |
1.50e-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: 87.19 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGK------EISLIsgFaqQQEIFIPTLTVDEYLMIQAR 72
Cdd:cd03259 28 FLALLGPSGCGKTTLLRLIA-----GLERpdSGEILIDGRDVTGvpperrNIGMV--F--QDYALFPHLTVAENIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03259 99 LR-GVPKAEIRARVRELLELVGLEGLLNRYPHE------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 153 ILKNL-ANSGRTLI---HQPtAELFFQFDKIIFLSMGK 186
Cdd:cd03259 172 ELKELqRELGITTIyvtHDQ-EEALALADRIAVMNEGR 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2-191 |
1.51e-19 |
|
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: 87.35 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKI---GKEISLIS-----GFAQQQEIFIPTLTVDEYLMIQa 71
Cdd:cd03297 26 TGIFGASGAGKSTLL-----RCIAGLEKpdGGTIVLNGTVLfdsRKKINLPPqqrkiGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 rLRMKANKhTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03297 100 -LKRKRNR-EDRISVDELLDLLGLDHLLNRYPAQ------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1017384763 152 QILKNL-ANSGRTLI---HQPTaELFFQFDKIIFLSMGKTAFMG 191
Cdd:cd03297 172 PELKQIkKNLNIPVIfvtHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-186 |
1.82e-19 |
|
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: 86.09 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLI------SGFAQQQEIFIPTLTVdeylmiqar 72
Cdd:cd03229 28 IVALLGPSGSGKSTLLRCIA-----GLEEpdSGSILIDGEDLTDLEDELpplrrrIGMVFQDFALFPHLTV--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 lrmkankhtrrervdeiiemlrLQNcrdlkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03229 94 ----------------------LEN----------IALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 1017384763 153 ILKNL-ANSGRTLIHQpTAELFFQF---DKIIFLSMGK 186
Cdd:cd03229 142 LLKSLqAQLGITVVLV-THDLDEAArlaDRVVVLRDGK 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-195 |
2.55e-19 |
|
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: 86.65 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRMKA 77
Cdd:cd03265 30 GLLGPNGAGKTTTIKML-----TTLLKptSGRATVAGHDVVREPREVRrriGIVFQDLSVDDELTGWENLYIHARLYGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKhTRRERVDEIIEMLRLQNCRDlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:cd03265 105 GA-ERRERIDELLDFVGLLEAAD------RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1017384763 158 ANSGRTLIHQPT-----AELFfqFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03265 178 KEEFGMTILLTThymeeAEQL--CDRVAIIDHGRIIAEGTPEE 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-195 |
5.65e-19 |
|
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: 90.21 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIgKEIS------LISGFAQQQEIFIPTLtvdeylmiqaR- 72
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLL-----RFLDpqSGSITLGGVDL-RDLDeddlrrRIAVVPQRPHLFDTTL----------Re 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 -LRMKANKHTRrervDEIIEMLR-------LQNCR---DLKIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:COG4987 428 nLRLARPDATD----EELWAALErvglgdwLAALPdglDTWLGEGGR--RLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 142 LDSFMAASVVQILKNLANsGRTLI---HQPTAelFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLlitHRLAG--LERMDRILVLEDGRIVEQGTHEE 555
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-211 |
8.03e-19 |
|
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: 85.80 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGKeisliSGFAQQQEI-------F-----IPTLTVDEYL 67
Cdd:COG1127 34 LAIIGGSGSGKSVLL-----KLIIGLLRpdSGEILVDGQDITG-----LSEKELYELrrrigmlFqggalFDSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 68 MIqaRLRMkankHTR------RERVDEIIEMLRLQNCRDLKigtPGlvkGISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:COG1127 104 AF--PLRE----HTDlseaeiRELVLEKLELVGLPGAADKM---PS---ELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 142 LDSFMAASVVQILKNLANS-GRTLI---HQpTAELFFQFDKIIFLSMGKTAFMGTPHEsvkfFADCGHPIPKLF 211
Cdd:COG1127 172 LDPITSAVIDELIRELRDElGLTSVvvtHD-LDSAFAIADRVAVLADGKIIAEGTPEE----LLASDDPWVRQF 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-195 |
1.14e-18 |
|
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: 85.48 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIG----KEISLISGFAQQQEIFIPTLTVDEYLMIqARL- 73
Cdd:COG1120 29 VTALLGPNGSGKSTLLRALA-----GLLKpsSGEVLLDGRDLAslsrRELARRIAYVPQEPPAPFGLTVRELVAL-GRYp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 ---RMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDsfMA--A 148
Cdd:COG1120 103 hlgLFGRPSAEDREAVEEALERTGLEHLADRPVDE------LSGGERQRVLIARALAQEPPLLLLDEPTSHLD--LAhqL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 149 SVVQILKNLA-NSGRTLI---HQPTaeLFFQF-DKIIFLSMGKTAFMGTPHE 195
Cdd:COG1120 175 EVLELLRRLArERGRTVVmvlHDLN--LAARYaDRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-186 |
1.32e-18 |
|
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: 84.50 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnvlmCRNMKGLEK--NGTVKVNGTKI---GKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARL 73
Cdd:cd03262 29 VVIIGPSGSGKSTL-----LRCINLLEEpdSGTIIIDGLKLtddKKNINELRqkvGMVFQQFNLFPHLTVLENITLAPIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:cd03262 104 VKGMSKAEAEERALELLEKVGLADKADAYPAQ------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1017384763 154 LKNLANSGRTLI---HQptaelfFQF-----DKIIFLSMGK 186
Cdd:cd03262 178 MKDLAEEGMTMVvvtHE------MGFarevaDRVIFMDDGR 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-187 |
3.46e-18 |
|
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: 83.08 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGL--EKNGTVKVNGTKIG-KEISLISGFAQQQ---EIFipTLTVDEYLmiqaRLRM 75
Cdd:cd03226 29 IALTGKNGAGKTTLAKILA-----GLikESSGSILLNGKPIKaKERRKSIGYVMQDvdyQLF--TDSVREEL----LLGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KaNKHTRRERVDEIIEMLRL-----QNCRDLkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:cd03226 98 K-ELDAGNEQAETVLKDLDLyalkeRHPLSL-----------SGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1017384763 151 VQILKNLANSGRTLI---HQPtaELFFQF-DKIIFLSMGKT 187
Cdd:cd03226 166 GELIRELAAQGKAVIvitHDY--EFLAKVcDRVLLLANGAI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-195 |
4.68e-18 |
|
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: 87.58 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIgKEISLISgFAQQ-----QEIFI-------------PT 60
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLL-----GLYEptSGRILIDGIDL-RQIDPAS-LRRQigvvlQDVFLfsgtirenitlgdPD 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 61 LTVDEylMIQArLRMkANkhtrrerVDEIIEmlRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:COG2274 576 ATDEE--IIEA-ARL-AG-------LHDFIE--ALPMGYDTVVGEGG--SNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 141 GLDSFMAASVVQILKNLANsGRTLI---HQP-TAELffqFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG2274 641 ALDAETEAIILENLRRLLK-GRTVIiiaHRLsTIRL---ADRIIVLDKGRIVEDGTHEE 695
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-165 |
4.85e-18 |
|
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: 83.49 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKE---------ISLISgfaQQQEIFiPTLTVDEYLMIQ 70
Cdd:COG0410 32 VALLGRNGAGKTTLLKAIS-----GLLPprSGSIRFDGEDITGLpphriarlgIGYVP---EGRRIF-PSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRmkANKHTRRERVDEIIEML-RLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:COG0410 103 AYAR--RDRAEVRADLERVYELFpRLKERRRQRAGT------LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEE 174
|
170
....*....|....*.
gi 1017384763 150 VVQILKNLANSGRTLI 165
Cdd:COG0410 175 IFEIIRRLNREGVTIL 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-195 |
6.57e-18 |
|
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: 86.50 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKI--------GKEISLISGFAQQQeiFIPtLTVDEYLMIQARL 73
Cdd:COG1123 35 VALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLlelsealrGRRIGMVFQDPMTQ--LNP-VTVGDQIAEALEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:COG1123 112 L-GLSRAEARARVLELLEAVGLERRLDRYPHQ------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1017384763 154 LKNL-ANSGRT--LIHQPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG1123 185 LRELqRERGTTvlLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-165 |
1.97e-17 |
|
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: 81.40 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKI-----------GKEISLIsgFAQQQEIFIPTLTVDEYLM 68
Cdd:cd03257 34 LGLVGESGSGKSTLARAIL-----GLLKPtsGSIIFDGKDLlklsrrlrkirRKEIQMV--FQDPMSSLNPRMTIGEQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVdeIIEMLRlqncrdlKIGTPGLVKG-----ISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:cd03257 107 EPLRIHGKLSKKEARKEA--VLLLLV-------GVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
170 180
....*....|....*....|...
gi 1017384763 144 SFMAASVVQILKNLANS-GRTLI 165
Cdd:cd03257 178 VSVQAQILDLLKKLQEElGLTLL 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-165 |
2.48e-17 |
|
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: 81.33 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVlmcrnMKGLEK--NGTVKVNGTKI------------GKEIslisGFAQQQEIFIPTLTVDEYL 67
Cdd:COG4181 41 VAIVGASGSGKSTLLGL-----LAGLDRptSGTVRLAGQDLfaldedararlrARHV----GFVFQSFQLLPTLTALENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 68 MIQARLRMKANKHTRRErvdeiiEML-------RLQNcrdlkigTPglvKGISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:COG4181 112 MLPLELAGRRDARARAR------ALLervglghRLDH-------YP---AQLSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180
....*....|....*....|....*.
gi 1017384763 141 GLDSFMAASVVQILKNL-ANSGRTLI 165
Cdd:COG4181 176 NLDAATGEQIIDLLFELnRERGTTLV 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-186 |
3.96e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.48 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGK----EISLIsgfaqQQEI--------FIPTLTVDEY 66
Cdd:COG2884 30 FVFLTGPSGAGKSTLLKLLY-----GEERptSGQVLVNGQDLSRlkrrEIPYL-----RRRIgvvfqdfrLLPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 LMIQARLrMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:COG2884 100 VALPLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHE------LSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1017384763 147 AASVVQILKNLANSGRTLI---HQPtaELFFQFDK-IIFLSMGK 186
Cdd:COG2884 173 SWEIMELLEEINRRGTTVLiatHDL--ELVDRMPKrVLELEDGR 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-161 |
4.88e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.28 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNvLMCrnmkgleknGTVKVNGTKI---GKEISL----------ISGFAQQQEIFIpTLTVDEYLM 68
Cdd:cd03218 29 VGLLGPNGAGKTTTFY-MIV---------GLVKPDSGKIlldGQDITKlpmhkrarlgIGYLPQEASIFR-KLTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:cd03218 98 AVLEIR-GLSKKEREEKLEELLEEFHITHLRKSKASS------LSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170
....*....|...
gi 1017384763 149 SVVQILKNLANSG 161
Cdd:cd03218 171 DIQKIIKILKDRG 183
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-186 |
1.24e-16 |
|
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: 77.42 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIgKEISLISGFAQ----QQEIFIPTLTVdeylmiqarlr 74
Cdd:cd03228 30 KVAIVGPSGSGKSTLLKLLL-----RLYDptSGEILIDGVDL-RDLDLESLRKNiayvPQDPFLFSGTI----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 mkankhtrRERVdeiiemlrlqncrdlkigtpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:cd03228 93 --------RENI-------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 155 KNLANsGRTLI---HQPTAELffQFDKIIFLSMGK 186
Cdd:cd03228 140 RALAK-GKTVIviaHRLSTIR--DADRIIVLDDGR 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-197 |
1.82e-16 |
|
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: 78.86 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTkigkEISL----------ISGFAQQQEIFiPTLTVDEYLMI 69
Cdd:TIGR04406 30 VGLLGPNGAGKTTSFYMIV-----GLVRpdAGKILIDGQ----DITHlpmherarlgIGYLPQEASIF-RKLTVEENIMA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:TIGR04406 100 VLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS------LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 150 VVQILKNLANSG-RTLI--HQpTAELFFQFDKIIFLSMGKTAFMGTPHESV 197
Cdd:TIGR04406 174 IKKIIKHLKERGiGVLItdHN-VRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-195 |
2.63e-16 |
|
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: 78.93 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKI-GKEISLIS--GFA---QQQEIFiPTLTVDEYLMIQARL 73
Cdd:COG0411 33 VGLIGPNGAGKTTLFNLIT-----GFYRptSGRILFDGRDItGLPPHRIArlGIArtfQNPRLF-PELTVLENVLVAAHA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKAN--------------KHTRRERVDEIIEMLRLQNCRDLkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:COG0411 107 RLGRGllaallrlprarreEREARERAEELLERVGLADRADE------PAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 140 SGLDSFMAASVVQILKNL-ANSGRTLI---HQptAELFFQF-DKIIFLSMGKTAFMGTPHE 195
Cdd:COG0411 181 AGLNPEETEELAELIRRLrDERGITILlieHD--MDLVMGLaDRIVVLDFGRVIAEGTPAE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-180 |
3.46e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCrnmkgLEK--NGTVKVNGTKI----GKEISLIS----GFAQQQEIFIPTLTVDEYLMIQ 70
Cdd:PRK10535 36 MVAIVGASGSGKSTLMNILGC-----LDKptSGTYRVAGQDVatldADALAQLRrehfGFIFQRYHLLSHLTAAQNVEVP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ArLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK10535 111 A-VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ------LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190
....*....|....*....|....*....|...
gi 1017384763 151 VQILKNLANSGRTLI---HQPTAELffQFDKII 180
Cdd:PRK10535 184 MAILHQLRDRGHTVIivtHDPQVAA--QAERVI 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-167 |
3.65e-16 |
|
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: 77.32 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGL--EKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRmKAN 78
Cdd:cd03269 28 IFGLLGPNGAGKTTTIRMIL-----GIilPDSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLK-GLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 KHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLA 158
Cdd:cd03269 102 KEEARRRIDEWLERLELSEYANKRVEE------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA 175
|
170
....*....|..
gi 1017384763 159 NSGRTLI---HQ 167
Cdd:cd03269 176 RAGKTVIlstHQ 187
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-165 |
4.86e-16 |
|
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: 77.92 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKIGKEISLiSGFAQQQEIFI-PTLTVDEYLMIQARLRMKAN 78
Cdd:COG1124 34 FGLVGESGSGKSTLLRALA-----GLERPwsGEVTFDGRPVTRRRRK-AFRRRVQMVFQdPYASLHPRHTVDRILAEPLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 KHTRRERVDEIIEMLRL----QNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:COG1124 108 IHGLPDREERIAELLEQvglpPSFLDRYPHQ------LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLL 181
|
170
....*....|..
gi 1017384763 155 KNL-ANSGRTLI 165
Cdd:COG1124 182 KDLrEERGLTYL 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-155 |
5.28e-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: 77.37 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGL--EKNGTVKVNG-------TKIGKEISLIsgFAQQQEIFIPTLTVDEYLMIQA 71
Cdd:cd03267 49 IVGFIGPNGAGKTTTLKIL-----SGLlqPTSGEVRVAGlvpwkrrKKFLRRIGVV--FGQKTQLWWDLPVIDSFYLLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRMKANKHtrRERVDEIIEMLRLQNCRDlkigTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03267 122 IYDLPPARF--KKRLDELSELLDLEELLD----TP--VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
....
gi 1017384763 152 QILK 155
Cdd:cd03267 194 NFLK 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-161 |
6.46e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.38 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKI-----------GkeislISGFAQQQEIFiPTLTVDEYLM 68
Cdd:COG1137 32 VGLLGPNGAGKTTTFYMIV-----GLVKpdSGRIFLDGEDIthlpmhkrarlG-----IGYLPQEASIF-RKLTVEDNIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKaNKHTRRERVDEIIEMLRLQNCRDlkigTPGLVkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:COG1137 101 AVLELRKL-SKKEREERLEELLEEFGITHLRK----SKAYS--LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVA 173
|
170
....*....|...
gi 1017384763 149 SVVQILKNLANSG 161
Cdd:COG1137 174 DIQKIIRHLKERG 186
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-186 |
6.94e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 76.39 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIG--------KEISLISgfaqqQEifiPTL---TVDEYLM 68
Cdd:COG4619 29 VAITGPSGSGKSTLLRALA-----DLDPptSGEIYLDGKPLSampppewrRQVAYVP-----QE---PALwggTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRmkaNKHTRRERVDEIIEMLRL------QNCRDLkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGL 142
Cdd:COG4619 96 FPFQLR---ERKFDRERALELLERLGLppdildKPVERL-----------SGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1017384763 143 DSFMAASVVQILKNL-ANSGRTLI---HQPtAELFFQFDKIIFLSMGK 186
Cdd:COG4619 162 DPENTRRVEELLREYlAEEGRAVLwvsHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-195 |
1.39e-15 |
|
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: 76.45 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIGKEISLI-------SGFAQQQEIFIPTLTVDEYLMIqA 71
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCL-----NGLVEptSGSVLIDGTDINKLKGKAlrqlrrqIGMIFQQFNLIERLSVLENVLS-G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLrmkANKHTRR------------------ERVDeiieMLRLQNCRdlkigtpglVKGISGGEARRLTFACELLSNPSLL 133
Cdd:cd03256 103 RL---GRRSTWRslfglfpkeekqralaalERVG----LLDKAYQR---------ADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 134 FADEPTSGLDSFMAASVVQILKNLANS-GRTLI---HQPTAELFFqFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIvslHQVDLAREY-ADRIVGLKDGRIVFDGPPAE 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-182 |
2.08e-15 |
|
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: 78.87 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGL--EKNGTVKVNGTKI--------GKEISLISgfaQQQEIFIPTLT-------- 62
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLL-----GFvdPTEGSIAVNGVPLadadadswRDQIAWVP---QHPFLFAGTIAenirlarp 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 63 -VDEYLMIQARLRMKANkhtrrERVDEIIEMLrlqncrDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:TIGR02857 422 dASDAEIREALERAGLD-----EFVAALPQGL------DTPIGEGG--AGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1017384763 142 LDSFMAASVVQILKNLANsGRTLI---HQPtaELFFQFDKIIFL 182
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ-GRTVLlvtHRL--ALAALADRIVVL 529
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-163 |
4.77e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrNMKGLEKNGTVKVNGTKIG-------KEISLIS---GFAQQQEIFIPTLTVDEYLmIQA 71
Cdd:COG4161 31 LVLLGPSGAGKSSLLRVL---NLLETPDSGQLNIAGHQFDfsqkpseKAIRLLRqkvGMVFQQYNLWPHLTVMENL-IEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLR-MKANKHTRRERVDEIIEMLRLQNCRD---LKIgtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:COG4161 107 PCKvLGLSKEQAREKAMKLLARLRLTDKADrfpLHL---------SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170
....*....|....*.
gi 1017384763 148 ASVVQILKNLANSGRT 163
Cdd:COG4161 178 AQVVEIIRELSQTGIT 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-149 |
5.90e-15 |
|
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: 74.05 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKI---GKEIslisGFAQQQEIFIPTLTVDEYLMIQARLRMK 76
Cdd:cd03293 33 VALVGPSGCGKSTLLRII-----AGLERptSGEVLVDGEPVtgpGPDR----GYVFQQDALLPWLTVLDNVALGLELQGV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017384763 77 ANKHtRRERVDEIIEMLRLQNCRDLkigTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:cd03293 104 PKAE-ARERAEELLELVGLSGFENA---YP---HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-163 |
6.82e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.28 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrNMKGLEKNGTVKVNGTKIG-------KEISLIS---GFAQQQEIFIPTLTVDEYLmIQA 71
Cdd:PRK11124 31 LVLLGPSGAGKSSLLRVL---NLLEMPRSGTLNIAGNHFDfsktpsdKAIRELRrnvGMVFQQYNLWPHLTVQQNL-IEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLR-MKANKHTRRERVDEIIEMLRLQNCRD---LKIgtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK11124 107 PCRvLGLSKDQALARAEKLLERLRLKPYADrfpLHL---------SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170
....*....|....*.
gi 1017384763 148 ASVVQILKNLANSGRT 163
Cdd:PRK11124 178 AQIVSIIRELAETGIT 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-195 |
7.78e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.15 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGKEIslISGFAqqqeiFIP-------TLTVDE---YLm 68
Cdd:COG4152 29 IFGLLGPNGAGKTTTI-----RIILGILApdSGEVLWDGEPLDPED--RRRIG-----YLPeerglypKMKVGEqlvYL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 iqARLR-MKanKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:COG4152 96 --ARLKgLS--KAEAKRRADEWLERLGLGDRANKKVEE------LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 148 ASVVQILKNLANSGRTLI---HQ-PTAELFfqFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG4152 166 ELLKDVIRELAAKGTTVIfssHQmELVEEL--CDRIVIINKGRKVLSGSVDE 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-198 |
8.05e-15 |
|
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: 73.91 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkgleknGTVKVNGTKI---GKEISLIS------GFAQQQEIFIPTLTVDEYLMIQAR 72
Cdd:cd03299 28 FVILGPTGSGKSVLLETIA----------GFIKPDSGKIllnGKDITNLPpekrdiSYVPQNYALFPHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03299 98 KR-KVDKKEIERKVLEIAEMLGIDHLLNRKPET------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1017384763 153 ILKNL-ANSGRTLIH--QPTAELFFQFDKIIFLSMGKTAFMGTPHESVK 198
Cdd:cd03299 171 ELKKIrKEFGVTVLHvtHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-186 |
1.06e-14 |
|
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: 72.47 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNvLMCRNMKGleKNGTVKVNGTKIG----KEISLISGFAQQqeifiptltvdeyLMiqarlrmk 76
Cdd:cd03214 27 IVGILGPNGAGKSTLLK-TLAGLLKP--SSGEILLDGKDLAslspKELARKIAYVPQ-------------AL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ankhtrrERVDeiIEMLRLQNCRDLkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKN 156
Cdd:cd03214 83 -------ELLG--LAHLADRPFNEL-----------SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 157 LANS-GRTLI---HQPtaELFFQF-DKIIFLSMGK 186
Cdd:cd03214 143 LARErGKTVVmvlHDL--NLAARYaDRVILLKDGR 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-195 |
1.55e-14 |
|
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: 73.58 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMCRNMKGleKNGTVKVNGTKIGKE--------ISLISGFAQQQeiFIPTLTV---------- 63
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLPPT--YGNDVRLFGERRGGEdvwelrkrIGLVSPALQLR--FPRDETVldvvlsgffd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 64 -----DEYLMIQarlrmkankhtrRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEP 138
Cdd:COG1119 108 siglyREPTDEQ------------RERARELLELLGLAHLADRPFGT------LSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 139 TSGLDSFMAASVVQILKNLANSG-RTLI---HQPtAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGaPTLVlvtHHV-EEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-157 |
1.96e-14 |
|
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: 74.32 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN-----GTVKVNGTKI------------GKEISLIsgFaqqQEIFI---PTL 61
Cdd:COG0444 34 LGLVGESGSGKSTLARAIL-----GLLPPpgitsGEILFDGEDLlklsekelrkirGREIQMI--F---QDPMTslnPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 62 TVDEYLMIQARLRMKANKHTRRERVdeiIEMLRLqncrdLKIGTPGLVKG-----ISGGEARRLTFACELLSNPSLLFAD 136
Cdd:COG0444 104 TVGDQIAEPLRIHGGLSKAEARERA---IELLER-----VGLPDPERRLDrypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180
....*....|....*....|.
gi 1017384763 137 EPTSGLDSFMAASVVQILKNL 157
Cdd:COG0444 176 EPTTALDVTIQAQILNLLKDL 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-157 |
2.45e-14 |
|
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: 72.61 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTkigkEISLISGFAQQQE------IF-----IPTLTVDEYLMIQAR 72
Cdd:cd03258 38 GRSGAGKSTLI-----RCINGLERptSGSVLVDGT----DLTLLSGKELRKArrrigmIFqhfnlLSSRTVFENVALPLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LrMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03258 109 I-AGVPKAEIEERVLELLELVGLEDKADAYPAQ------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILA 181
|
....*
gi 1017384763 153 ILKNL 157
Cdd:cd03258 182 LLRDI 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-193 |
3.19e-14 |
|
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: 76.21 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVlmcrnMKGL--EKNGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRM 75
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSI-----LTGLlpPTSGTVLVGGKDIETNLDAVRqslGMCPQHNILFHHLTVAEHILFYAQLKG 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRErVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILK 155
Cdd:TIGR01257 1033 RSWEEAQLE-MEAMLEDTGLHHKRNEE------AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1017384763 156 NLaNSGRTLI----HQPTAELFfqFDKIIFLSMGKTAFMGTP 193
Cdd:TIGR01257 1106 KY-RSGRTIImsthHMDEADLL--GDRIAIISQGRLYCSGTP 1144
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-195 |
3.20e-14 |
|
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: 73.99 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVlmcrnMKGLEK--NGTVKVNGTKI---GKEISLIS-----GFAQQQEIFIPTLTVDEYLMIQA 71
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRL-----IAGLTRpdEGEIVLNGRTLfdsRKGIFLPPekrriGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RlrmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:TIGR02142 101 K---RARPSERRISFERVIELLGIGHLLGRLPGR------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1017384763 152 QILKNLANSGRTLI----HQPTaELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:TIGR02142 172 PYLERLHAEFGIPIlyvsHSLQ-EVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-165 |
4.80e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIgKEISLISGFAQQQeifiPTL----TVDEYLMIQARLRm 75
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIA-----GLEKptSGEVLVDGKPV-TGPGPDRGVVFQE----PALlpwlTVLDNVALGLELR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV-VQIL 154
Cdd:COG1116 109 GVPKAERRERARELLELVGLAGFEDAYPHQ------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLqDELL 182
|
170
....*....|.
gi 1017384763 155 KNLANSGRTLI 165
Cdd:COG1116 183 RLWQETGKTVL 193
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-195 |
5.10e-14 |
|
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: 71.49 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcRNMKGLEknGTVKVNGTKIgKEISLIS-----GFAQQQEIFI------------PTLTVD 64
Cdd:cd03253 30 VAIVGPSGSGKSTILRLLF-RFYDVSS--GSILIDGQDI-REVTLDSlrraiGVVPQDTVLFndtigynirygrPDATDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 65 EylMIQARlrmkankhtRRERVDEIIemLRLQNCRDLKIGTPGLVkgISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:cd03253 106 E--VIEAA---------KAAQIHDKI--MRFPDGYDTIVGERGLK--LSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 145 FMAASVVQILKNLANsGRTLI---HQPTAelFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIviaHRLST--IVNADKIIVLKDGRIVERGTHEE 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-165 |
9.09e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNVLMCRNMKgleKNGTVKVNGTKI---GKEISLISGFAQQQEIFIPTLTVDEYLMIQAR-LRMKAnk 79
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHP---DAGSISLCGEPVpsrARHARQRVGVVPQFDNLDPDFTVRENLLVFGRyFGLSA-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 HTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAN 159
Cdd:PRK13537 113 AAARALVPPLLEFAKLENKADAKVGE------LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA 186
|
....*.
gi 1017384763 160 SGRTLI 165
Cdd:PRK13537 187 RGKTIL 192
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
2-165 |
2.15e-13 |
|
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: 68.99 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGL--EKNGTVKVNGTKIG----------KEISLISGFAQQQeIFIPTltVDEYLMI 69
Cdd:TIGR01166 21 LALLGANGAGKSTLL-----LHLNGLlrPQSGAVLIDGEPLDysrkgllerrQRVGLVFQDPDDQ-LFAAD--VDQDVAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARlRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:TIGR01166 93 GPL-NLGLSEAEVERRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170
....*....|....*.
gi 1017384763 150 VVQILKNLANSGRTLI 165
Cdd:TIGR01166 166 MLAILRRLRAEGMTVV 181
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-195 |
2.49e-13 |
|
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: 69.56 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGTKIG--KEISLISGFAQ-QQEIFIPTLTVDEylmiqaRLRMK 76
Cdd:cd03254 32 VAIVGPTGAGKTTLINLLM-----RFYDPqkGQILIDGIDIRdiSRKSLRSMIGVvLQDTFLFSGTIME------NIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ANKHTRRE--------RVDEIIEmlRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:cd03254 101 RPNATDEEvieaakeaGAHDFIM--KLPNGYDTVLGENG--GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1017384763 149 SVVQILKNLANsGRTLI---HQPTAELFfqFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03254 177 LIQEALEKLMK-GRTSIiiaHRLSTIKN--ADKILVLDDGKIIEEGTHDE 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-168 |
4.42e-13 |
|
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: 71.62 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGL--EKNGTVKVNGTKI----GKEIS-LISGFAQQQEIFipTLTVDEYLMIqarlr 74
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLA-----GLldPLQGEVTLDGVPVssldQDEVRrRVSVCAQDAHLF--DTTVRENLRL----- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 mkANKHTRRERVDEIIEMLRLQN-CRDLKIGTPGLVKG----ISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:TIGR02868 432 --ARPDATDEELWAALERVGLADwLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 1017384763 150 VVQILkNLANSGRTLI---HQP 168
Cdd:TIGR02868 510 LLEDL-LAALSGRTVVlitHHL 530
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-143 |
4.67e-13 |
|
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: 70.51 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIgkeislisgFAQQQEIFIPT-----------------LTV 63
Cdd:COG4148 29 ALFGPSGSGKTTLLRAI-----AGLERpdSGRIRLGGEVL---------QDSARGIFLPPhrrrigyvfqearlfphLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 64 deylmiQARLR--MK-ANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:COG4148 95 ------RGNLLygRKrAPRAERRISFDEVVELLGIGHLLDRRPAT------LSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
...
gi 1017384763 141 GLD 143
Cdd:COG4148 163 ALD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-161 |
6.67e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkgleknGTVKVNGTKI---GKEISLIS---------GFAQQQEIFIPTLTVDEYLM 68
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVV----------GIVPRDAGNIiidDEDISLLPlhararrgiGYLPQEASIFRRLSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVDEIIEMLRLQNCRDlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:PRK10895 101 AVLQIRDDLSAEQREDRANELMEEFHIEHLRD------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170
....*....|...
gi 1017384763 149 SVVQILKNLANSG 161
Cdd:PRK10895 175 DIKRIIEHLRDSG 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-196 |
1.05e-12 |
|
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: 67.64 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcRNMKGLEknGTVKVNGTKIgKEISLISGFAQ----QQEIFIPTLTVDEYLMIQarlrmk 76
Cdd:cd03251 30 TVALVGPSGSGKSTLVNLIP-RFYDVDS--GRILIDGHDV-RDYTLASLRRQiglvSQDVFLFNDTVAENIAYG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ankhTRRERVDEIIEMLRLQNCRDL----------KIGTPGlVKgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:cd03251 100 ----RPGATREEVEEAARAANAHEFimelpegydtVIGERG-VK-LSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 147 AASVVQILKNLAnSGRTLI---HQ-PTAElffQFDKIIFLSMGKTAFMGTpHES 196
Cdd:cd03251 174 ERLVQAALERLM-KNRTTFviaHRlSTIE---NADRIVVLEDGKIVERGT-HEE 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-191 |
1.50e-12 |
|
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: 67.01 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGK---EISLISGFAQQQEIFIPTLTVDEYLMIQARLRmK 76
Cdd:cd03266 34 TGLLGPNGAGKTTTL-----RMLAGLLEpdAGFATVDGFDVVKepaEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-G 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ANKHTRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKN 156
Cdd:cd03266 108 LKGDELTARLEELADRLGMEELLDRR------VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1017384763 157 LANSGRTLI---H--QPTAELffqFDKIIFLSMGKTAFMG 191
Cdd:cd03266 182 LRALGKCILfstHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-165 |
1.59e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQAR-LRMKA 77
Cdd:PRK13536 72 LLGPNGAGKSTIARMIL-----GMTSpdAGKITVLGVPVPARARLARariGVVPQFDNLDLEFTVRENLLVFGRyFGMST 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKhtRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK13536 147 RE--IEAVIPSLLEFARLESKADAR------VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
....*...
gi 1017384763 158 ANSGRTLI 165
Cdd:PRK13536 219 LARGKTIL 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-143 |
2.22e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVN-GTKIGKeislisgFAQQQEIFIPTLTVDEYlmIQARLRMKAN 78
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLA-----GELEpdSGTVKLGeTVKIGY-------FDQHQEELDPDKTVLDE--LRDGAPGGTE 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 79 KHTR---------RERVDEIIEMLrlqncrdlkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:COG0488 410 QEVRgylgrflfsGDDAFKPVGVL-------------------SGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-195 |
2.70e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnvLMCRNMkgLEK--NGT-----VKVNGTKIG-KEISLISGFAQQQEIFIPTLTVDEYLMIQARL 73
Cdd:PRK09493 30 VVIIGPSGSGKSTL---LRCINK--LEEitSGDlivdgLKVNDPKVDeRLIRQEAGMVFQQFYLFPHLTALENVMFGPLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTRRERVDEIIEmlrlqncrdlKIGT-------PGlvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:PRK09493 105 VRGASKEEAEKQARELLA----------KVGLaerahhyPS---ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 147 AASVVQILKNLANSGRTLIhQPTAELFFQFD---KIIFLSMGKTAFMGTPHE 195
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTMV-IVTHEIGFAEKvasRLIFIDKGRIAEDGDPQV 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-191 |
2.96e-12 |
|
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: 66.40 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGtKIGKEISLISGFAqqqeifiPTLTVDEYLMIQARLrMKANK 79
Cdd:cd03220 51 IGLIGRNGAGKSTLLRLL-----AGIYPpdSGTVTVRG-RVSSLLGLGGGFN-------PELTGRENIYLNGRL-LGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 HTRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAN 159
Cdd:cd03220 117 KEIDEKIDEIIEFSELGDFIDLP------VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 1017384763 160 SGRTLI---HQPtaELFFQF-DKIIFLSMGKTAFMG 191
Cdd:cd03220 191 QGKTVIlvsHDP--SSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-195 |
3.44e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLmnvLMCRNMkgLEK--NGTVKVNGtkigKEISLISGFAQQQEIFiptlTVDEYLMIQARLRMkAN 78
Cdd:PRK10619 33 VISIIGSSGSGKSTF---LRCINF--LEKpsEGSIVVNG----QTINLVRDKDGQLKVA----DKNQLRLLRTRLTM-VF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 KH-------TRRERVDEI-IEMLRL--QNCRDL------KIGTPGLVKG-----ISGGEARRLTFACELLSNPSLLFADE 137
Cdd:PRK10619 99 QHfnlwshmTVLENVMEApIQVLGLskQEARERavkylaKVGIDERAQGkypvhLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 138 PTSGLDSFMAASVVQILKNLANSGRTLIhQPTAELFFQ---FDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMV-VVTHEMGFArhvSSHVIFLHQGKIEEEGAPEQ 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-165 |
4.51e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEKNGTVKVNgtKIGKEISLIS------------GFAQQQEIFIPTLTVDEYLMI 69
Cdd:PRK10584 39 IALIGESGSGKSTLLAIL-----AGLDDGSSGEVS--LVGQPLHQMDeearaklrakhvGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLRMKANKHTRrERVDEIIEML----RLQNcrdlkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:PRK10584 112 PALLRGESSRQSR-NGAKALLEQLglgkRLDH----------LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|.
gi 1017384763 146 MAASVVQILKNL-ANSGRTLI 165
Cdd:PRK10584 181 TGDKIADLLFSLnREHGTTLI 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
2-191 |
5.23e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.56 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKI---GKEISLISgfaqQQEIFIPTLTVDE--YLMIQARLR 74
Cdd:TIGR01184 14 ISLIGHSGCGKSTLLNLI-----SGLAQptSGGVILEGKQItepGPDRMVVF----QNYSLLPWLTVREniALAVDRVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 mKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:TIGR01184 85 -DLSKSERRAIVEEHIALVGLTEAADKRPGQ------LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1017384763 155 KNLANSGRT---LIHQPTAELFFQFDKIIFLSMGKTAFMG 191
Cdd:TIGR01184 158 MQIWEEHRVtvlMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-186 |
8.28e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkG-LEKNGTVKVNGTKIgKEISL------ISGFAQQQEIFIPTLtVDEYLMIQARLR 74
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALL-----GfLPYQGSLKINGIEL-RELDPeswrkhLSWVGQNPQLPHGTL-RDNVLLGNPDAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 MKANKHT-RRERVDEIIEmlRLQNCRDLKIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:PRK11174 452 DEQLQQAlENAWVSEFLP--LLPQGLDTPIGDQAA--GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 154 LKNLANSGRTLI--HQptAELFFQFDKIIFLSMGK 186
Cdd:PRK11174 528 LNAASRRQTTLMvtHQ--LEDLAQWDQIWVMQDGQ 560
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-205 |
8.75e-12 |
|
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: 65.01 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNvlMCRNMkgLE-KNGTVKVNGTKIgKEISLIS-----GFAQQQEIFIPTLTVDEYLMIQARLrM 75
Cdd:cd03295 30 LVLIGPSGSGKTTTMK--MINRL--IEpTSGEIFIDGEDI-REQDPVElrrkiGYVIQQIGLFPHMTVEENIALVPKL-L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQncrdlkigtPGLVKG-----ISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:cd03295 104 KWPKEKIRERADELLALVGLD---------PAEFADrypheLSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 151 VQILKNLAN-SGRTLI---HQpTAELFFQFDKIIFLSMGKTAFMGTP--------HESVKFFADCGH 205
Cdd:cd03295 175 QEEFKRLQQeLGKTIVfvtHD-IDEAFRLADRIAIMKNGEIVQVGTPdeilrspaNDFVAEFVGADR 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-186 |
9.64e-12 |
|
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: 64.89 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVL--MCRNMKGLEKNGTVKVNGTKI-GKEISLIS-----GFAQQQeifiPTL---TVDEYLMIQ 70
Cdd:cd03260 29 TALIGPSGCGKSTLLRLLnrLNDLIPGAPDEGEVLLDGKDIyDLDVDVLElrrrvGMVFQK----PNPfpgSIYDNVAYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANKHTRRERVDEIIEmlrlqncrdlKIGTPGLVK------GISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:cd03260 105 LRLHGIKLKEELDERVEEALR----------KAALWDEVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1017384763 145 FMAASVVQILKNLANSGRTLI--H--QPTAELffqFDKIIFLSMGK 186
Cdd:cd03260 175 ISTAKIEELIAELKKEYTIVIvtHnmQQAARV---ADRTAFLLNGR 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-143 |
1.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.32 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVL--MCRNMKGLEKNGTVKVNGTKIGKeISLISGFAQQQEIF-----IPTLTVDEYLMIQARL 73
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRVFnrLIELYPEARVSGEVYLDGQDIFK-MDVIELRRRVQMVFqipnpIPNLSIFENVALGLKL 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 74 -RMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK14247 110 nRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-166 |
1.79e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGtkiGKEISLIsgfAQQQEIfIPTL--TVDEYLMIQA-RLRM 75
Cdd:NF040873 20 LTAVVGPNGSGKSTLLKVLA-----GVLRptSGTVRRAG---GARVAYV---PQRSEV-PDSLplTVRDLVAMGRwARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRER--VDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:NF040873 88 LWRRLTRDDRaaVDDALERVGLADLAGRQLGE------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170
....*....|...
gi 1017384763 154 LKNLANSGRTLIH 166
Cdd:NF040873 162 LAEEHARGATVVV 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-202 |
1.91e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcrnmkgLEKNGTVKVNGTKI---GKEI-----SLIS-----GFAQQQ---EIFIPTltVD 64
Cdd:PRK13639 30 MVALLGPNGAGKSTLF----------LHFNGILKPTSGEVlikGEPIkydkkSLLEvrktvGIVFQNpddQLFAPT--VE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 65 EYLMIqARLRMKANKHTRRERVDEIIEmlrlqncrdlKIGTPGLVKG----ISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:PRK13639 98 EDVAF-GPLNLGLSKEEVEKRVKEALK----------AVGMEGFENKpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 141 GLDSFMAASVVQILKNLANSGRTLI---HQ----PTAElffqfDKIIFLSMGKTAFMGTPHEsvkFFAD 202
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIistHDvdlvPVYA-----DKVYVMSDGKIIKEGTPKE---VFSD 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-211 |
2.42e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.00 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLmnvLMCRNMKGLEKNGTVKV-----NGTK-IGKEISLIS------GFAQQQEIFIPTLTVDEYLm 68
Cdd:PRK11264 31 VVAIIGPSGSGKTTL---LRCINLLEQPEAGTIRVgditiDTARsLSQQKGLIRqlrqhvGFVFQNFNLFPHRTVLENI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKanKHTRRERVDEIIEMLRlqncrdlKIGTPG----LVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:PRK11264 107 IEGPVIVK--GEPKEEATARARELLA-------KVGLAGketsYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 145 FMAASVVQILKNLANSGRTLIhQPTAELFFQFD---KIIFLSMGKTAFMGtphESVKFFADCGHPIPKLF 211
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDvadRAIFMDQGRIVEQG---PAKALFADPQQPRTRQF 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-195 |
2.52e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGKeiSLIsgfaQQQEIFI--------PTLTVDEYlmIQ 70
Cdd:PRK11432 34 MVTLLGPSGCGKTTVL-----RLVAGLEKptEGQIFIDGEDVTH--RSI----QQRDICMvfqsyalfPHMSLGEN--VG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRM-KANKHTRRERVDEIIEMLRLQNCRDLkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:PRK11432 101 YGLKMlGVPKEERKQRVKEALELVDLAGFEDR------YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1017384763 150 VVQILKNLANS-GRT---LIHQPTaELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK11432 175 MREKIRELQQQfNITslyVTHDQS-EAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-165 |
2.80e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.72 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTL---MNVLMC----------RNMKGLEKNGTVKVNGTK----------------IGKEISLISGFA 51
Cdd:PRK13651 35 FIAIIGQTGSGKTTFiehLNALLLpdtgtiewifKDEKNKKKTKEKEKVLEKlviqktrfkkikkikeIRRRVGVVFQFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 52 QQQeIFIPTLTVDeylMIQARLRMKANKHTRRERVDEIIEMlrlqncrdlkIGTPG--LVK---GISGGEARRLTFACEL 126
Cdd:PRK13651 115 EYQ-LFEQTIEKD---IIFGPVSMGVSKEEAKKRAAKYIEL----------VGLDEsyLQRspfELSGGQKRRVALAGIL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1017384763 127 LSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTII 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-168 |
2.92e-11 |
|
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: 63.38 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGK----EISLISGFAQQQeifiPTL---TVDEYLMIqar 72
Cdd:cd03245 33 VAIIGRVGSGKSTLLKLLA-----GLYKptSGSVLLDGTDIRQldpaDLRRNIGYVPQD----VTLfygTLRDNITL--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 lrmkANKHTRRERVDEIIEML-------RLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:cd03245 101 ----GAPLADDERILRAAELAgvtdfvnKHPNGLDLQIGERG--RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180
....*....|....*....|....*.
gi 1017384763 146 MAASVVQILKNLAnSGRTLI---HQP 168
Cdd:cd03245 175 SEERLKERLRQLL-GDKTLIiitHRP 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-191 |
3.11e-11 |
|
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: 62.90 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLE--KNGTVKVNGTKIG------KEISLIsgFaQQQEIFiPTLTVDEY--LMIQA 71
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLI-----AGFEtpQSGRVLINGVDVTaappadRPVSML--F-QENNLF-AHLTVEQNvgLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRMKANKhtrRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03298 98 GLKLTAED---RQAIEVALARVGLAGLEKRLPGE------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1017384763 152 QILKNL-ANSGRTLI---HQPTAELFFqFDKIIFLSMGKTAFMG 191
Cdd:cd03298 169 DLVLDLhAETKMTVLmvtHQPEDAKRL-AQRVVFLDNGRIAAQG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-165 |
3.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNG-------TKIGKEISLIsgFAQQQEIF--IPTLtvDEYLMI 69
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKML-----TGILVptSGEVRVLGyvpfkrrKEFARRIGVV--FGQRSQLWwdLPAI--DSFRLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLRMKANKHtrRERVDEIIEMLRLQNcrdlKIGTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:COG4586 121 KAIYRIPDAEY--KKRLDELVELLDLGE----LLDTP--VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170
....*....|....*..
gi 1017384763 150 VVQILKNL-ANSGRTLI 165
Cdd:COG4586 193 IREFLKEYnRERGTTIL 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-195 |
4.11e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.57 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNvLMCRNMKGLEknGTVKVNGTKIgKEISLIS-----GFAQQqEIFIPTLTVDEylmiqaRLRM 75
Cdd:COG1132 368 TVALVGPSGSGKSTLVN-LLLRFYDPTS--GRILIDGVDI-RDLTLESlrrqiGVVPQ-DTFLFSGTIRE------NIRY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRrervDEIIEMLRLQNCRDL----------KIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:COG1132 437 GRPDATD----EEVEEAAKAAQAHEFiealpdgydtVVGERGV--NLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 146 MAASVVQILKNLAnSGRTLI---HQP-TAElffQFDKIIFLSMGKTAFMGTPHE 195
Cdd:COG1132 511 TEALIQEALERLM-KGRTTIviaHRLsTIR---NADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-195 |
4.53e-11 |
|
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: 63.02 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIG------KEISLIsgFaQQQEIFiPTLTVDEYLMIQARL 73
Cdd:cd03300 29 FTLLGPSGCGKTTLLRLI-----AGFETptSGEILLDGKDITnlpphkRPVNTV--F-QNYALF-PHLTVFENIAFGLRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RmKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:cd03300 100 K-KLPKAEIKERVAEALDLVQLEGYANRKPSQ------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1017384763 154 LKNLANS-GRTLIH--QPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03300 173 LKRLQKElGITFVFvtHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-143 |
6.55e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKV-NGTKIGKeislisgFAQQQEIFiPTLTVDEYLM------IQAR 72
Cdd:COG0488 27 IGLVGRNGAGKSTLLKILA-----GELEpdSGEVSIpKGLRIGY-------LPQEPPLD-DDLTVLDTVLdgdaelRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEMLRLQNCRD-----------------LKIGTPGL---VKGISGGEARRLTFACELLSNPSL 132
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAELQEEFEalggweaearaeeilsgLGFPEEDLdrpVSELSGGWRRRVALARALLSEPDL 173
|
170
....*....|.
gi 1017384763 133 LFADEPTSGLD 143
Cdd:COG0488 174 LLLDEPTNHLD 184
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-195 |
8.38e-11 |
|
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: 62.36 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNgtkiGKEISLIS------GFAQQQEIFIPTLTVDEYLMIQAR 72
Cdd:cd03296 30 LVALLGPSGSGKTTLL-----RLIAGLERpdSGTILFG----GEDATDVPvqernvGFVFQHYALFRHMTVFDNVAFGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKA---NKHTRRERVDEIIEMLRLQNCRDlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSfmaas 149
Cdd:cd03296 101 VKPRSerpPEAEIRAKVHELLKLVQLDWLAD------RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA----- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 150 vvQILKNLANSGRTL---IHQPT-------AELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03296 170 --KVRKELRRWLRRLhdeLHVTTvfvthdqEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-191 |
2.83e-10 |
|
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: 59.63 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNvLMCRNMKGLEknGTVKVNGTKI---GKEIS-LISGFAQQQEIFIPTLtvdeylmiqarlrmka 77
Cdd:cd03247 31 IALLGRSGSGKSTLLQ-LLTGDLKPQQ--GEITLDGVPVsdlEKALSsLISVLNQRPYLFDTTL---------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 nkhtrrervdeiiemlrLQNcrdlkIGTPglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:cd03247 92 -----------------RNN-----LGRR-----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1017384763 158 ANsGRTLI---HQPTAelFFQFDKIIFLSMGKTAFMG 191
Cdd:cd03247 145 LK-DKTLIwitHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-165 |
3.00e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnvLMCrnMKG-LEKNGTVKVNGTKI----GKEISLISG-FAQQQEifiPTLTVDEYLMIQARLRM 75
Cdd:PRK03695 25 LHLVGPNGAGKSTL---LAR--MAGlLPGSGSIQFAGQPLeawsAAELARHRAyLSQQQT---PPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNcrdlKIGTPglVKGISGGEARRLTFACELL-----SNPS--LLFADEPTSGLDSFMAA 148
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDD----KLGRS--VNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQA 170
|
170
....*....|....*..
gi 1017384763 149 SVVQILKNLANSGRTLI 165
Cdd:PRK03695 171 ALDRLLSELCQQGIAVV 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-157 |
3.57e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGK-----------EISLIsgFAQQQEIFIPTLTVDEYLM 68
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLV-----GLESpsQGNVSWRGEPLAKlnraqrkafrrDIQMV--FQDSISAVNPRKTVREIIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVDEIIEMLRLqncrDLKIGT--PGLVkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:PRK10419 114 EPLRHLLSLDKAERLARASEMLRAVDL----DDSVLDkrPPQL---SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170
....*....|.
gi 1017384763 147 AASVVQILKNL 157
Cdd:PRK10419 187 QAGVIRLLKKL 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-157 |
5.32e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIGKEISLIS--------GFAQQQEIFIPTLTVDEY---- 66
Cdd:PRK11629 37 MMAIVGSSGSGKSTLLHLL-----GGLDTptSGDVIFNGQPMSKLSSAAKaelrnqklGFIYQFHHLLPDFTALENvamp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 LMIQARLRMKANKHTRrervdeiiEMLRlqncrdlkigTPGLVK-------GISGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:PRK11629 112 LLIGKKKPAEINSRAL--------EMLA----------AVGLEHranhrpsELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170
....*....|....*...
gi 1017384763 140 SGLDSFMAASVVQILKNL 157
Cdd:PRK11629 174 GNLDARNADSIFQLLGEL 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-164 |
1.03e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmCRNMKGLEknGTVKVNG--------TKIGKEIslISGFAQQQEIFiPTLTVDEYLMIQAR 72
Cdd:PRK11614 33 IVTLIGANGAGKTTLLGTL-CGDPRATS--GRIVFDGkditdwqtAKIMREA--VAIVPEGRRVF-SRMTVEENLAMGGF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEmlRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:PRK11614 107 FAERDQFQERIKWVYELFP--RLHERRIQRAGT------MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD 178
|
170
....*....|..
gi 1017384763 153 ILKNLANSGRTL 164
Cdd:PRK11614 179 TIEQLREQGMTI 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
1.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGK----EISLISGFAQQQ---EIFIPTLTVDeylMIQAR 72
Cdd:PRK13652 33 IAVIGPNGAGKSTLF-----RHFNGILKptSGSVLIRGEPITKenirEVRKFVGLVFQNpddQIFSPTVEQD---IAFGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEMLRLQNCRDLkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:PRK13652 105 INLGLDEETVAHRVSSALHMLGLEELRDR------VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1017384763 153 ILKNLANS-GRTLI---HQPT--AELffqFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13652 179 FLNDLPETyGMTVIfstHQLDlvPEM---ADYIYVMDKGRIVAYGTVEE 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-185 |
1.28e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcRNMKGLEKNGTVKVNGTKIGKEISLISGFAqqqeifiptltvdeylmiqarlrmkankht 81
Cdd:COG2401 59 VLIVGASGSGKSTLLRLLA-GALKGTPVAGCVDVPDNQFGREASLIDAIG------------------------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 82 RRERVDEIIEmlRLQNCrdlKIGTPGL----VKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:COG2401 108 RKGDFKDAVE--LLNAV---GLSDAVLwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170 180 190
....*....|....*....|....*....|..
gi 1017384763 158 A-NSGRTLI---HQPTAELFFQFDKIIFLSMG 185
Cdd:COG2401 183 ArRAGITLVvatHHYDVIDDLQPDLLIFVGYG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-145 |
1.50e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 58.72 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVlmcrnMKGLEK--NGTVKVNGTKI---GKEisliSGFAQQQEIFIPTLTVDEYLMIQARLRmK 76
Cdd:COG4525 36 VVALGASGCGKTTLLNL-----IAGFLApsSGEITLDGVPVtgpGAD----RGVVFQKDALLPWLNVLDNVAFGLRLR-G 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 77 ANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:COG4525 106 VPKAERRARAEELLALVGLADFARRRIWQ------LSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1-186 |
1.88e-09 |
|
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: 56.84 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLISG-----FAQQQEIFIPTLTvdeylmiqarl 73
Cdd:cd03246 30 SLAIIGPSGSGKSTLARLIL-----GLLRptSGRVRLDGADISQWDPNELGdhvgyLPQDDELFSGSIA----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 rmkankhtrrervdEIIemlrlqncrdlkigtpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:cd03246 94 --------------ENI---------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1017384763 154 LKNLANSGRTLI---HQPtaELFFQFDKIIFLSMGK 186
Cdd:cd03246 139 IAALKAAGATRIviaHRP--ETLASADRILVLEDGR 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-165 |
1.92e-09 |
|
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: 57.65 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNG---TKIG---KEISLIsgFaqQQEIFIPTLTVDEYLMIQARL 73
Cdd:cd03301 29 VVLLGPSGCGKTTTL-----RMIAGLEEptSGRIYIGGrdvTDLPpkdRDIAMV--F--QNYALYPHMTVYDNIAFGLKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RmKANKHTRRERVDEIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSF----MAAS 149
Cdd:cd03301 100 R-KVPKDEIDERVREVAELLQIEHLLDRK------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKlrvqMRAE 172
|
170
....*....|....*.
gi 1017384763 150 VVQILKNLansGRTLI 165
Cdd:cd03301 173 LKRLQQRL---GTTTI 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-210 |
2.43e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.84 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLE--KNGTVKVNGTKIGKE------ISLISgfaQQQEIFiPTLTVDE--YLMIQA 71
Cdd:COG3840 28 VAILGPSGAGKSTLLNLI-----AGFLppDSGRILWNGQDLTALppaerpVSMLF---QENNLF-PHLTVAQniGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRMKAnkhTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:COG3840 99 GLKLTA---EQRAQVEQALERVGLAGLLDRLPGQ------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 152 QILKNLANS-GRTLI---HQPT-AELFfqFDKIIFLSMGKTAFMGTPHEsvkFFAdcGHPIPKL 210
Cdd:COG3840 170 DLVDELCRErGLTVLmvtHDPEdAARI--ADRVLLVADGRIAADGPTAA---LLD--GEPPPAL 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-200 |
5.56e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.01 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGtKIGkeiSLI---SGfaqqqeiFIPTLTVDEYLMIQARLrMK 76
Cdd:COG1134 55 VGIIGRNGAGKSTLLKLIA-----GILEptSGRVEVNG-RVS---ALLelgAG-------FHPELTGRENIYLNGRL-LG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ANKHTRRERVDEIIEMLRLQNcrdlKIGTPglVKGISGGEARRLTFACELLSNPSLLFADEPTS-GLDSFMAASvVQILK 155
Cdd:COG1134 118 LSRKEIDEKFDEIVEFAELGD----FIDQP--VKTYSSGMRARLAFAVATAVDPDILLVDEVLAvGDAAFQKKC-LARIR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1017384763 156 NLANSGRTLI---HQPTA--ELffqFDKIIFLSMGKTAFMGTPHESVKFF 200
Cdd:COG1134 191 ELRESGRTVIfvsHSMGAvrRL---CDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-157 |
5.99e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.78 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLmnvLMCRNmkGLEK--NGTVKVNGTKIG-----------KEISLIsgFaqQQeiF--IPTLTVDE---YL 67
Cdd:COG1135 38 GYSGAGKSTL---IRCIN--LLERptSGSVLVDGVDLTalserelraarRKIGMI--F--QH--FnlLSSRTVAEnvaLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 68 MIQArlrmKANKHTRRERVDEIIEMLRLQNCRD-----LkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGL 142
Cdd:COG1135 107 LEIA----GVPKAEIRKRVAELLELVGLSDKADaypsqL-----------SGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170
....*....|....*
gi 1017384763 143 DSFMAASVVQILKNL 157
Cdd:COG1135 172 DPETTRSILDLLKDI 186
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-150 |
6.81e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.95 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIG------KEISLIsgfaQQQEIFIPTLTVDEYLMIQarLRM 75
Cdd:COG4136 30 LTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTalpaeqRRIGIL----FQDDLLFPHLSVGENLAFA--LPP 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:COG4136 104 TIGRAQRRARVEQALEEAGLAGFADRDPAT------LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-195 |
8.26e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIG----KEISLisGFAQQQEIFIPTLTVDEYLMIQARLrM 75
Cdd:PRK11000 32 VVFVGPSGCGKSTLL-----RMIAGLEDitSGDLFIGEKRMNdvppAERGV--GMVFQSYALYPHLSVAENMSFGLKL-A 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNCRDLKigtPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSF----MAASVV 151
Cdd:PRK11000 104 GAKKEEINQRVNQVAEVLQLAHLLDRK---P---KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqMRIEIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1017384763 152 QILKNLansGRTLIH--QPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK11000 178 RLHKRL---GRTMIYvtHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-186 |
8.66e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNvLMCRNMkgLEKNGTVKVNGTKIGK--EISL---ISGFAQQQEIFIPTLtvdeylmiqaR--LR 74
Cdd:PRK11160 369 VALLGRTGCGKSTLLQ-LLTRAW--DPQQGEILLNGQPIADysEAALrqaISVVSQRVHLFSATL----------RdnLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 MKANKHTRrervDEIIEMLR-------LQNCR--DLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDsf 145
Cdd:PRK11160 436 LAAPNASD----EALIEVLQqvgleklLEDDKglNAWLGEGG--RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD-- 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1017384763 146 mAASVVQILKNLAN--SGRTLI---HQPTAelFFQFDKIIFLSMGK 186
Cdd:PRK11160 508 -AETERQILELLAEhaQNKTVLmitHRLTG--LEQFDRICVMDNGQ 550
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-165 |
9.23e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKI-----------GkeISLIsgfaqQQEI-FIPTLTVDEYLM 68
Cdd:COG1129 34 ALLGENGAGKSTLMKILS-----GVYQpdSGEILLDGEPVrfrsprdaqaaG--IAII-----HQELnLVPNLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IqARLRMKA---NKHTRRERVDEIIEMLRLqncrDLKIGTPglVKGISGGE------ARrltfacELLSNPSLLFADEPT 139
Cdd:COG1129 102 L-GREPRRGgliDWRAMRRRARELLARLGL----DIDPDTP--VGDLSVAQqqlveiAR------ALSRDARVLILDEPT 168
|
170 180
....*....|....*....|....*.
gi 1017384763 140 SGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-200 |
9.23e-09 |
|
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: 57.89 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcRNMKGL--------------EKNGTVKVNgTKIGKEISLISGFAQQQEIFIPTLTVDEY- 66
Cdd:TIGR03269 29 LGILGRSGAGKSVLMHVL--RGMDQYeptsgriiyhvalcEKCGYVERP-SKVGEPCPVCGGTLEPEEVDFWNLSDKLRr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 -------LMIQARLRMKANK--------------HTRRERVD---EIIEMLRLQN-----CRDLkigtpglvkgiSGGEA 117
Cdd:TIGR03269 106 rirkriaIMLQRTFALYGDDtvldnvlealeeigYEGKEAVGravDLIEMVQLSHrithiARDL-----------SGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 118 RRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLA-NSGRTLI---HQP--TAELffqFDKIIFLSMGKTAFMG 191
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVltsHWPevIEDL---SDKAIWLENGEIKEEG 251
|
....*....
gi 1017384763 192 TPHESVKFF 200
Cdd:TIGR03269 252 TPDEVVAVF 260
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-165 |
9.43e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEI--SLISGFAQQQEI--FIPTLTVDEYLMIQ---- 70
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALM-----GFVRlaSGKISILGQPTRQALqkNLVAYVPQSEEVdwSFPVLVEDVVMMGRyghm 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRmKANKHTRrERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK15056 110 GWLR-RAKKRDR-QIVTAALARVDMVEFRHRQIGE------LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170
....*....|....*
gi 1017384763 151 VQILKNLANSGRTLI 165
Cdd:PRK15056 182 ISLLRELRDEGKTML 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-165 |
9.61e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGtkigKEISlISGFAQ---------QQEiF--IPTLTVDEYLMI 69
Cdd:COG3845 35 ALLGENGAGKSTLMKILY-----GLYQpdSGEILIDG----KPVR-IRSPRDaialgigmvHQH-FmlVPNLTVAENIVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QA--RLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLtfacE----LLSNPSLLFADEPTSGL- 142
Cdd:COG3845 104 GLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVED------LSVGEQQRV----EilkaLYRGARILILDEPTAVLt 173
|
170 180
....*....|....*....|....*..
gi 1017384763 143 ----DSFMAasvvqILKNLANSGRTLI 165
Cdd:COG3845 174 pqeaDELFE-----ILRRLAAEGKSII 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-195 |
1.01e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNvlmcrNMKGL--EKNGTVKVNGTKIG------------------------KEISLISGFAQQQeIF 57
Cdd:PRK13631 57 IIGNSGSGKSTLVT-----HFNGLikSKYGTIQVGDIYIGdkknnhelitnpyskkiknfkelrRRVSMVFQFPEYQ-LF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 58 IPTLTVDeyLMIqARLRMKANKHTRRERVDEIIEMLRLqncrdlkiGTPGLVK---GISGGEARRLTFACELLSNPSLLF 134
Cdd:PRK13631 131 KDTIEKD--IMF-GPVALGVKKSEAKKLAKFYLNKMGL--------DDSYLERspfGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 135 ADEPTSGLDSFMAASVVQILKNLANSGRTLI---HQPTAELFFQfDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFvitHTMEHVLEVA-DEVIVMDKGKILKTGTPYE 262
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-195 |
1.49e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.77 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGtkigKEISLISGFAQ------QQEIFIPTLTVDEYLMiqar 72
Cdd:PRK11607 47 IFALLGASGCGKSTLL-----RMLAGFEQptAGQIMLDG----VDLSHVPPYQRpinmmfQSYALFPHMTVEQNIA---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDS----FMAA 148
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKP---HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1017384763 149 SVVQILKNLANSGRTLIHQpTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK11607 191 EVVDILERVGVTCVMVTHD-QEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-195 |
1.57e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNgtkiGKEISLIS------GFAQQQEIFIPTLTVDEYLMIQAR 72
Cdd:PRK10851 30 MVALLGPSGSGKTTLL-----RIIAGLEHqtSGHIRFH----GTDVSRLHardrkvGFVFQHYALFRHMTVFDNIAFGLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 L---RMKANKHTRRERVDEIIEMLRLQNcrdLKIGTPGlvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSfmaas 149
Cdd:PRK10851 101 VlprRERPNAAAIKAKVTQLLEMVQLAH---LADRYPA---QLSGGQKQRVALARALAVEPQILLLDEPFGALDA----- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 150 vvQILKNLansgRTLIHQPTAELFFQ--F------------DKIIFLSMGKTAFMGTPHE 195
Cdd:PRK10851 170 --QVRKEL----RRWLRQLHEELKFTsvFvthdqeeamevaDRVVVMSQGNIEQAGTPDQ 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-145 |
1.98e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 56.31 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIgkEISLIS-----GF-AQQQEIFiPTLTVDEYlmIQAR 72
Cdd:COG1118 30 LVALLGPSGSGKTTLLRII-----AGLETpdSGRIVLNGRDL--FTNLPPrerrvGFvFQHYALF-PHMTVAEN--IAFG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017384763 73 LRMK-ANKHTRRERVDEIIEMLRLqncrdlkigtPGLVK----GISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:COG1118 100 LRVRpPSKAEIRARVEELLELVQL----------EGLADrypsQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-195 |
2.57e-08 |
|
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: 54.85 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmkglEK-----NGTVKVNGTKIG--------KEISLISgfaqqQEifiPTLtvdeYLM 68
Cdd:cd03249 32 VALVGSSGCGKSTVVSLL--------ERfydptSGEILLDGVDIRdlnlrwlrSQIGLVS-----QE---PVL----FDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 -IQARLRMKANKHTrrerVDEIIEMLRLQNCRDLKIGTPG----LV--KG--ISGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:cd03249 92 tIAENIRYGKPDAT----DEEVEEAAKKANIHDFIMSLPDgydtLVgeRGsqLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 140 SGLDsfmAAS--VVQILKNLANSGRTLI---HQPT----AelffqfDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03249 168 SALD---AESekLVQEALDRAMKGRTTIviaHRLStirnA------DLIAVLQNGQVVEQGTHDE 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-143 |
3.96e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIgkeislisgFAQQQEIFIPTltvdE-----YLMIQARL-- 73
Cdd:PRK11144 28 AIFGRSGAGKTSLINAI-----SGLTRpqKGRIVLNGRVL---------FDAEKGICLPP----EkrrigYVFQDARLfp 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 74 --RMKAN-----KHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK11144 90 hyKVRGNlrygmAKSMVAQFDKIVALLGIEPLLDRYPGS------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1-165 |
4.76e-08 |
|
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: 53.30 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcRNMKGLEKNGTVKVNGTKIGK----EISLISGF-AQQQEIFIPTLTVDEYLmiqarlrm 75
Cdd:cd03217 28 VHALMGPNGSGKSTLAKTIM-GHPKYEVTEGEILFKGEDITDlppeERARLGIFlAFQYPPEIPGVKNADFL-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 kankhtrRErVDEiiemlrlqncrdlkigtpglvkGISGGEARRltfaCELLS----NPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03217 99 -------RY-VNE----------------------GFSGGEKKR----NEILQllllEPDLAILDEPDSGLDIDALRLVA 144
|
170
....*....|....
gi 1017384763 152 QILKNLANSGRTLI 165
Cdd:cd03217 145 EVINKLREEGKSVL 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-198 |
5.03e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.67 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNG----------TKIGKEISLISGFAQQQeIFIPTLTVDeylMI 69
Cdd:PRK13637 36 VGLIGHTGSGKSTLI-----QHLNGLLKptSGKIIIDGvditdkkvklSDIRKKVGLVFQYPEYQ-LFEETIEKD---IA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLRMKANKHTRRERVDEIIEMLRLqNCRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:PRK13637 107 FGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSP---FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 150 VVQILKNL-ANSGRTLI---H--QPTAELffqFDKIIFLSMGKTAFMGTPHESVK 198
Cdd:PRK13637 183 ILNKIKELhKEYNMTIIlvsHsmEDVAKL---ADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-165 |
7.49e-08 |
|
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: 52.05 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIgkeislisgfaqqqeifiptltvdeylmiqarlrmkaNK 79
Cdd:cd03216 29 HALLGENGAGKSTLMKILS-----GLYKpdSGEILVDGKEV-------------------------------------SF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 HTRRERvdeiiemlrlqncRDLKIGTpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAN 159
Cdd:cd03216 67 ASPRDA-------------RRAGIAM---VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA 130
|
....*.
gi 1017384763 160 SGRTLI 165
Cdd:cd03216 131 QGVAVI 136
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
7.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnvLMCRNMKGLEKNGTVKVNGTKIG----KEISLISGFAQQQ---EIFIPTLTVDeylMIQARLR 74
Cdd:PRK13647 34 TALLGPNGAGKSTL---LLHLNGIYLPQRGRVKVMGREVNaeneKWVRSKVGLVFQDpddQVFSSTVWDD---VAFGPVN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 MKANKHTRRERVDEIIEMLRLQNCRDlkiGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQIL 154
Cdd:PRK13647 108 MGLDKDEVERRVEEALKAVRMWDFRD---KPP---YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 155 KNLANSGRTLI---HQptAELFFQF-DKIIFLSMGKTAFMGTP----HESVKFFADCGHP-IPKLFNP-PEWIQSKlsvI 224
Cdd:PRK13647 182 DRLHNQGKTVIvatHD--VDLAAEWaDQVIVLKEGRVLAEGDKslltDEDIVEQAGLRLPlVAQIFEDlPELGQSK---L 256
|
250
....*....|....*
gi 1017384763 225 PNNETKSRETIGKII 239
Cdd:PRK13647 257 PLTVKEAVQIIRKLL 271
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-195 |
9.90e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGL--EKNGTVKVNGTKIGKEISLISGFAQQ---------QEIFIPTLTVDeylmI 69
Cdd:PRK13638 29 VTGLVGANGCGKSTLF-----MNLSGLlrPQKGAVLWQGKPLDYSKRGLLALRQQvatvfqdpeQQIFYTDIDSD----I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLR-MKANKHTRRERVDEIIEMLRLQNCRDLKIgtpglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:PRK13638 100 AFSLRnLGVPEAEITRRVDEALTLVDAQHFRHQPI------QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1017384763 149 SVVQILKNLANSG-RTLIHQPTAELFFQF-DKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13638 174 QMIAIIRRIVAQGnHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGE 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1-168 |
1.02e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.15 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK----NGTVKVNGTKI---------GKEISLisgfAQQQEIFIPTLTVDEYL 67
Cdd:COG0396 28 VHAIMGPNGSGKSTLAKVLM-----GHPKyevtSGSILLDGEDIlelspderaRAGIFL----AFQYPVEIPGVSVSNFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 68 miqarlRMKANKHtRRERVD--EIIEMLRlQNCRDLKIgTPGLVK-----GISGGEARRLtfacELLS----NPSLLFAD 136
Cdd:COG0396 99 ------RTALNAR-RGEELSarEFLKLLK-EKMKELGL-DEDFLDryvneGFSGGEKKRN----EILQmlllEPKLAILD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1017384763 137 EPTSGLDSFMAASVVQILKNLANSGRTLI---HQP 168
Cdd:COG0396 166 ETDSGLDIDALRIVAEGVNKLRSPDRGILiitHYQ 200
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-227 |
1.03e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNVLMcrnmkGL-EKNG----TVKVNGTKI------------GKEISLIsgFAQQQEIFIPTLTVDEY 66
Cdd:PRK09473 47 IVGESGSGKSQTAFALM-----GLlAANGriggSATFNGREIlnlpekelnklrAEQISMI--FQDPMTSLNPYMRVGEQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 LMIQARLRMKANKHtrrERVDEIIEMLRLqncrdLKIgtPGLVKGI-------SGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:PRK09473 120 LMEVLMLHKGMSKA---EAFEESVRMLDA-----VKM--PEARKRMkmyphefSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 140 SGLDSFMAASVVQILKNLANSGRTLIHQPTAELFFQF---DKIIFLSMGKTAFMGTPHEsvkFFADCGHP--------IP 208
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgicDKVLVMYAGRTMEYGNARD---VFYQPSHPysigllnaVP 266
|
250
....*....|....*....
gi 1017384763 209 KLFNPPEwiqsKLSVIPNN 227
Cdd:PRK09473 267 RLDAEGE----SLLTIPGN 281
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-165 |
1.34e-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: 54.63 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLMCRNMKgleKNGTVKVNGTKIGKEISLIS---GFAQQQEIFIPTLTVDEYLMIQARLRMKANK 79
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTV---TSGDATVAGKSILTNISDVHqnmGYCPQFDAIDDLLTGREHLYLYARLRGVPAE 2045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 80 HTrrERV-DEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLA 158
Cdd:TIGR01257 2046 EI--EKVaNWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
....*..
gi 1017384763 159 NSGRTLI 165
Cdd:TIGR01257 2118 REGRAVV 2124
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-186 |
1.43e-07 |
|
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: 52.09 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkG-LEK-NGTVKVNGTkigkeISLISgfaqqQEIFIPTLTVDEYLMIQARLRMkan 78
Cdd:cd03250 33 LVAIVGPVGSGKSSLLSALL-----GeLEKlSGSVSVPGS-----IAYVS-----QEPWIQNGTIRENILFGKPFDE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 khtrrERVDEIIEMLRLQncRDLKIGTPGL-----VKGI--SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:cd03250 95 -----ERYEKVIKACALE--PDLEILPDGDlteigEKGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1017384763 152 Q--ILKNLANsGRTLI---HQPtaELFFQFDKIIFLSMGK 186
Cdd:cd03250 168 EncILGLLLN-NKTRIlvtHQL--QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-165 |
1.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcrNMKGLEKNGTVKVNGTKIG------------KEISLISGFAQQQeIFIPTLTVDEYLMIQ 70
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLL---NGLHVPTQGSVRVDDTLITstsknkdikqirKKVGLVFQFPESQ-LFEETVLKDVAFGPQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 --ARLRMKANKHTRRE-RVDEIIEMLRLQNCRDLkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK13649 113 nfGVSQEEAEALAREKlALVGISESLFEKNPFEL-----------SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170
....*....|....*...
gi 1017384763 148 ASVVQILKNLANSGRTLI 165
Cdd:PRK13649 182 KELMTLFKKLHQSGMTIV 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-195 |
1.69e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVL--MCRNMKGLEKNGTVKVNGTKIGKEIS-------LISGFAQQQeIFIPTLTVDEYLMIQarl 73
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLngLLQPTEGKVTVGDIVVSSTSKQKEIKpvrkkvgVVFQFPESQ-LFEETVLKDVAFGPQ--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTRRERVDEIIEMLRLQncRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:PRK13643 112 NFGIPKEKAEKIAAEKLEMVGLA--DEFWEKSP---FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1017384763 154 LKNLANSGRT--LIHQPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13643 187 FESIHQSGQTvvLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-195 |
2.59e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGL-----EKNGTVKVNGTKIGKEISLI---------SGFAQQQEIFIPTLTVDEY 66
Cdd:PRK09984 32 MVALLGPSGSGKSTLL-----RHLSGLitgdkSAGSHIELLGRTVQREGRLArdirksranTGYIFQQFNLVNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 LMIQA-------RLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:PRK09984 107 VLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVST------LSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 140 SGLDSFMAASVVQILKNL-ANSGRTLI---HQPTAELFFqFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK09984 181 ASLDPESARIVMDTLRDInQNDGITVVvtlHQVDYALRY-CERIVALRQGHVFYDGSSQQ 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-195 |
2.95e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.64 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNG---TKIGKEISLISGFAQQQEIFiPTLTVDEYlmIQARLRM-KA 77
Cdd:PRK09452 45 LLGPSGCGKTTVL-----RLIAGFETpdSGRIMLDGqdiTHVPAENRHVNTVFQSYALF-PHMTVFEN--VAFGLRMqKT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKHTRRERVDEIIEMLRLQNCRDLKIgtpglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK09452 117 PAAEITPRVMEALRMVQLEEFAQRKP------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1017384763 158 ANS-GRTLI---HQpTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK09452 191 QRKlGITFVfvtHD-QEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
83-165 |
3.15e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 83 RERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGR 162
Cdd:COG1245 190 RGKLDELAEKLGLENILDRDISE------LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK 263
|
...
gi 1017384763 163 TLI 165
Cdd:COG1245 264 YVL 266
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-195 |
3.60e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrNMKGLEKNGTVKVNGTKI--GKEISLIS--------GFAQQQEIFIPTLTVDEYLMIQ 70
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVL---NRLIEIYDSKIKVDGKVLyfGKDIFQIDaiklrkevGMVFQQPNPFPHLSIYDNIAYP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK14246 115 LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1017384763 151 VQILKNLANSGRTLI--HQPTaELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK14246 193 EKLITELKNEIAIVIvsHNPQ-QVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-159 |
4.91e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.31 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcRNMKGLEKN----GTVKVNGTKI----------GKEISLIsgfAQQQEIFIPTLtvdeYLM 68
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSI--NRMNDLNPEvtitGSIVYNGHNIysprtdtvdlRKEIGMV---FQQPNPFPMSI----YEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHtrRERVDEIIEM-LRLQNCRD-LKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:PRK14239 106 VVYGLRLKGIKD--KQVLDEAVEKsLKGASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPIS 183
|
170
....*....|...
gi 1017384763 147 AASVVQILKNLAN 159
Cdd:PRK14239 184 AGKIEETLLGLKD 196
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-203 |
6.74e-07 |
|
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: 50.72 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKI------------GKEISLI-SGFAqqqeiFIPTLTVDEY-- 66
Cdd:cd03294 55 IMGLSGSGKSTLL-----RCINRLIEptSGKVLIDGQDIaamsrkelrelrRKKISMVfQSFA-----LLPHRTVLENva 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 --LMIQARlrmkaNKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:cd03294 125 fgLEVQGV-----PRAEREERAAEALELVGLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 145 FMAASVVQILKNL-ANSGRTLI---HQPtAELFFQFDKIIFLSMGKTAFMGTPHESV---------KFFADC 203
Cdd:cd03294 194 LIRREMQDELLRLqAELQKTIVfitHDL-DEALRLGDRIAIMKDGRLVQVGTPEEILtnpandyvrEFFRGV 264
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
7.16e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKE--------ISLIsgFAQQQEIFIpTLTVDEYlmIQA 71
Cdd:PRK13632 38 VAILGHNGSGKSTISKILT-----GLLKpqSGEIKIDGITISKEnlkeirkkIGII--FQNPDNQFI-GATVEDD--IAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRmkaNKHTRRERVDEIIEMLRLqncrdlKIGTPGLVK----GISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK13632 108 GLE---NKKVPPKKMKDIIDDLAK------KVGMEDYLDkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 148 ASVVQILKNLANSG-RTLI---HQptAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13632 179 REIKKIMVDLRKTRkKTLIsitHD--MDEAILADKVIVFSEGKLIAQGKPKE 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-165 |
8.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNG------------TKIGKEISLISGFAQQQeIFIPTLTVD--- 64
Cdd:PRK13641 36 VALVGHTGSGKSTLM-----QHFNALLKpsSGTITIAGyhitpetgnknlKKLRKKVSLVFQFPEAQ-LFENTVLKDvef 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 65 ---EYLMIQARLRMKANKHTRRERVDEiiemlrlqncrDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:PRK13641 110 gpkNFGFSEDEAKEKALKWLKKVGLSE-----------DLISKSP---FELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180
....*....|....*....|....
gi 1017384763 142 LDSFMAASVVQILKNLANSGRTLI 165
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVI 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-150 |
9.44e-07 |
|
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: 51.47 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVN-GTKIGkeislisgFAQQQEIFIPTLTVDEYLM--------IQAR 72
Cdd:TIGR03719 36 VLGLNGAGKSTLL-----RIMAGVDKdfNGEARPQpGIKVG--------YLPQEPQLDPTKTVRENVEegvaeikdALDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKH-----------TRRERVDEIIEMLRLQNC-RDLKIGTPGL--------VKGISGGEARRLTFACELLSNPSL 132
Cdd:TIGR03719 103 FNEISAKYaepdadfdklaAEQAELQEIIDAADAWDLdSQLEIAMDALrcppwdadVTKLSGGERRRVALCRLLLSKPDM 182
|
170
....*....|....*...
gi 1017384763 133 LFADEPTSGLDsfmAASV 150
Cdd:TIGR03719 183 LLLDEPTNHLD---AESV 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-143 |
1.06e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNVLMcrnmkgleknGTVKVNGTKIGKEISLISGFAQQQEIFIPT--LTVDEYLmiqaRLRMKANKht 81
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVL----------GLVAPDEGVIKRNGKLRIGYVPQKLYLDTTlpLTVNRFL----RLRPGTKK-- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 82 rrervDEIIEMLRLQNCRDLkIGTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK09544 99 -----EDILPALKRVQAGHL-IDAP--MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
112-157 |
1.14e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1017384763 112 ISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-144 |
1.31e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGtkigKEISLISGFAQ-----QQEIFIPTLTVDEYLMIQARLR 74
Cdd:PRK13539 31 LVLTGPNGSGKTTLL-----RLIAGLLPpaAGTIKLDG----GDIDDPDVAEAchylgHRNAMKPALTVAENLEFWAAFL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 mkankHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:PRK13539 102 -----GGEELDIAAALEAVGLAPLAHLPFGY------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
1.43e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLM---NVLMCRNMKGlEKNGTVKVNGTKIGK------EISLISGFAQQQEIFIPTLTVDEYLMIQARL 73
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEA-RVEGEVRLFGRNIYSpdvdpiEVRREVGMVFQYPNPFPHLTIYDNVAIGVKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 rmkaNKHTR-RERVDEIIE-MLR----LQNCRDLKIGTPGlvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK14267 113 ----NGLVKsKKELDERVEwALKkaalWDEVKDRLNDYPS---NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 148 ASVVQILKNLANSGRTLI--HQPtAELFFQFDKIIFLSMGKTAFMGtphesvkffadcghPIPKLFNPPE 215
Cdd:PRK14267 186 AKIEELLFELKKEYTIVLvtHSP-AQAARVSDYVAFLYLGKLIEVG--------------PTRKVFENPE 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
40-157 |
2.19e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.74 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 40 IGKEISLIsgFAQQQEIFIPTLTVDEYLMIQARLRMKANKHTRRERVdeiIEMLRLqncrdlkIGTPGLVKGI------- 112
Cdd:PRK11022 87 VGAEVAMI--FQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRA---IDLLNQ-------VGIPDPASRLdvyphql 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1017384763 113 SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-165 |
2.25e-06 |
|
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: 48.20 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTK---------IGKEISLISGFAQQQEIFiPTLTVDEYLMI 69
Cdd:cd03215 28 IVGIAGLVGNGQTELAEALF-----GLRPpaSGEITLDGKPvtrrsprdaIRAGIAYVPEDRKREGLV-LDLSVAENIAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 70 QARLrmkankhtrrervdeiiemlrlqncrdlkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:cd03215 102 SSLL---------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170
....*....|....*.
gi 1017384763 150 VVQILKNLANSGRTLI 165
Cdd:cd03215 143 IYRLIRELADAGKAVL 158
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-165 |
2.33e-06 |
|
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: 48.97 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMnvlmcrnmKGLekNGTVKVNGTKI-----GKEISLISgfAQQQEI-------------F------ 57
Cdd:COG4778 40 VALTGPSGAGKSTLL--------KCI--YGNYLPDSGSIlvrhdGGWVDLAQ--ASPREIlalrrrtigyvsqFlrvipr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 58 IPTLTVdeylMIQARLRMKANKHTRRERVDEIIEMLRL-QNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFAD 136
Cdd:COG4778 108 VSALDV----VAEPLLERGVDREEARARARELLARLNLpERLWDLPPAT------FSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180
....*....|....*....|....*....
gi 1017384763 137 EPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-143 |
2.44e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNvLMCRNMKGleKNGTVKVnGTKIgkEISLisgFAQQQEIFIPTLTVDEYL-------MIQARLR 74
Cdd:PRK11147 348 IALIGPNGCGKTTLLK-LMLGQLQA--DSGRIHC-GTKL--EVAY---FDQHRAELDPEKTVMDNLaegkqevMVNGRPR 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 75 MKANK------HTRRERvdeiiemlrlqncrdlkigTPglVKGISGGEARRLTFAcELLSNPS-LLFADEPTSGLD 143
Cdd:PRK11147 419 HVLGYlqdflfHPKRAM-------------------TP--VKALSGGERNRLLLA-RLFLKPSnLLILDEPTNDLD 472
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-198 |
2.53e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVlMCRNMKGLEkNGTVKVNGTkigkeislISGFAQQQEIFipTLTVDEYLMIQARLRmkankh 80
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISA-MLGELSHAE-TSSVVIRGS--------VAYVPQVSWIF--NATVRENILFGSDFE------ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 trRERVDEIIEMLRLQNCRDL-------KIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ- 152
Cdd:PLN03232 707 --SERYWRAIDVTALQHDLDLlpgrdltEIGERGV--NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDs 782
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1017384763 153 -ILKNLANSGRTLIhqpTAELFF--QFDKIIFLSMGKTAFMGTPHESVK 198
Cdd:PLN03232 783 cMKDELKGKTRVLV---TNQLHFlpLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-195 |
2.83e-06 |
|
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: 48.64 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGL--EKNGTVKVNGTKIGkeislisgfaqqqeifiptlTVD-EYLMIQARLRMKA 77
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLI-----QRFyvPENGRVLVDGHDLA--------------------LADpAWLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 N---KHTRRERV---------DEIIEMLRLQNCRD----LKIGTPGLV----KGISGGEARRLTFACELLSNPSLLFADE 137
Cdd:cd03252 85 NvlfNRSIRDNIaladpgmsmERVIEAAKLAGAHDfiseLPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 138 PTSGLDSFMAASVVQILKNLAnSGRTLI---HQPTAelFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIiiaHRLST--VKNADRIIVMEKGRIVEQGSHDE 222
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
93-165 |
3.21e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 93 LRLQNcrdLKIGTPglVKGISGGEARRLTFACELLS---NPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:PRK00635 796 LGLDY---LPLGRP--LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVV 866
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-157 |
4.05e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.93 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLmnvlmCRNMKGLEK--NGTVKVNG---TKIG--------KEISLIsgFAQQQEIFIPTLTVDEylMIQAR 72
Cdd:PRK15079 54 GESGCGKSTF-----ARAIIGLVKatDGEVAWLGkdlLGMKddewravrSDIQMI--FQDPLASLNPRMTIGE--IIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKANKHTRRERVDEIIEMLrlqncrdLKIGT-PGLVK----GISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK15079 125 LRTYHPKLSRQEVKDRVKAMM-------LKVGLlPNLINryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170
....*....|
gi 1017384763 148 ASVVQILKNL 157
Cdd:PRK15079 198 AQVVNLLQQL 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
5.92e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.31 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGT----------KIGKEISLISGFAQQQeIFIPTLTVDeylMIQ 70
Cdd:PRK13636 36 AILGGNGAGKSTLF-----QNLNGILKpsSGRILFDGKpidysrkglmKLRESVGMVFQDPDNQ-LFSASVYQD---VSF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKANKHTRRERVDEIIEMLRLQNCRDlkigTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK13636 107 GAVNLKLPEDEVRKRVDNALKRTGIEHLKD----KP--THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 151 VQILKNLANS-GRTLI---HQ-PTAELFfqFDKIIFLSMGKTAFMGTPHEsvkFFAD 202
Cdd:PRK13636 181 MKLLVEMQKElGLTIIiatHDiDIVPLY--CDNVFVMKEGRVILQGNPKE---VFAE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-145 |
7.20e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.77 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALmGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKI---GKEisliSGFAQQQEIFIPTLTVDEYLMIQARLRM 75
Cdd:PRK11248 30 LVVL-GPSGCGKTTLLNLI-----AGFVPyqHGSITLDGKPVegpGAE----RGVVFQNEGLLPWRNVQDNVAFGLQLAG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 76 KAnkhtRRERVDEIIEMLRlqncrdlKIGTPGLVK----GISGGEARRLTFACELLSNPSLLFADEPTSGLDSF 145
Cdd:PRK11248 100 VE----KMQRLEIAHQMLK-------KVGLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-192 |
8.48e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.57 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLmnVLMCRNMkgLEKN-GTVKVNGTKI---------------GKEISLISGFAQQQEIFIPTLTVDE 65
Cdd:TIGR00958 510 VALVGPSGSGKSTV--AALLQNL--YQPTgGQVLLDGVPLvqydhhylhrqvalvGQEPVLFSGSVRENIAYGLTDTPDE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 66 YLMIQArlrMKANKHtrrervDEIIEMlrlQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDsf 145
Cdd:TIGR00958 586 EIMAAA---KAANAH------DFIMEF---PNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRVLILDEATSALD-- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 146 maASVVQILKNLANS-GRTLI---HQ-PTAElffQFDKIIFLSMGKTAFMGT 192
Cdd:TIGR00958 650 --AECEQLLQESRSRaSRTVLliaHRlSTVE---RADQILVLKKGSVVEMGT 696
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-193 |
8.71e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 47.10 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcRNMKGLEknGTVKVNG---TKIGKE-----ISLISgfaqqQEIFIPTLTV---------- 63
Cdd:cd03244 33 VGIVGRTGSGKSSLLLALF-RLVELSS--GSILIDGvdiSKIGLHdlrsrISIIP-----QDPVLFSGTIrsnldpfgey 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 64 -DEYLmIQARLRMKAnkhtrRERVDEIIEMLrlqncrDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGL 142
Cdd:cd03244 105 sDEEL-WQALERVGL-----KEFVESLPGGL------DTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1017384763 143 DSFMAASVVQILKNlANSGRTLI---HQPTAELffQFDKIIFLSMGKTAFMGTP 193
Cdd:cd03244 171 DPETDALIQKTIRE-AFKDCTVLtiaHRLDTII--DSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-186 |
8.87e-06 |
|
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: 47.08 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcRNMKGLEKnGTVKVNGTKIG--------KEISLISgfaQQQEIFIPTLTVD-EYLMIQARL 73
Cdd:cd03248 44 ALVGPSGSGKSTVVALL--ENFYQPQG-GQVLLDGKPISqyehkylhSKVSLVG---QEPVLFARSLQDNiAYGLQSCSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RM------KANKHtrrervDEIIEMlrlQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:cd03248 118 ECvkeaaqKAHAH------SFISEL---ASGYDTEVGEKG--SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1017384763 148 ASVVQILKNlANSGRTLI----HQPTAElffQFDKIIFLSMGK 186
Cdd:cd03248 187 QQVQQALYD-WPERRTVLviahRLSTVE---RADQILVLDGGR 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
113-156 |
8.99e-06 |
|
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: 45.52 E-value: 8.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1017384763 113 SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKN 156
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-158 |
9.48e-06 |
|
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: 46.72 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNGTKIGKEISLISG---FAQQQEIFIPTLTVDEYLMIQARLRm 75
Cdd:cd03231 28 ALQVTGPNGSGKTTLL-----RILAGLSPplAGRVLLNGGPLDFQRDSIARgllYLGHAPGIKTTLSVLENLRFWHADH- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 kankhtRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDsfmAASVVQILK 155
Cdd:cd03231 102 ------SDEQVEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGVARFAE 166
|
...
gi 1017384763 156 NLA 158
Cdd:cd03231 167 AMA 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-166 |
1.16e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTK----------------IGKEISLISGFAQQQEIFIPTLTVD 64
Cdd:PRK09700 35 ALLGENGAGKSTLMKVL-----SGIHEptKGTITINNINynkldhklaaqlgigiIYQELSVIDELTVLENLYIGRHLTK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 65 EYLMIQ----ARLRMKANkhtrrervdeiIEMLRLqncrDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTS 140
Cdd:PRK09700 110 KVCGVNiidwREMRVRAA-----------MMLLRV----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180
....*....|....*....|....*.
gi 1017384763 141 GLDSFMAASVVQILKNLANSGRTLIH 166
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVY 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-195 |
1.52e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 46.69 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmCRNMKGleKNGTVKVNGTKI----GKEISLISGFAQQQeifiPTL----TVDEYLmiqar 72
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRAL-SGELSP--DSGEVRLNGRPLadwsPAELARRRAVLPQH----SSLsfpfTVEEVV----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 lRMKANKHTRRE-RVDEII-EMLRLQNC-----RDLkigtPGLvkgiSGGEARRLTFA---CELLSN---PSLLFADEPT 139
Cdd:PRK13548 98 -AMGRAPHGLSRaEDDALVaAALAQVDLahlagRDY----PQL----SGGEQQRVQLArvlAQLWEPdgpPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 140 SGLDSFMAASVVQILKNLANsgrtliHQPTA--------ELFFQF-DKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAH------ERGLAvivvlhdlNLAARYaDRIVLLHQGRLVADGTPAE 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-195 |
1.64e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 46.55 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmCRNMKglEKNGTVKVNGTKIG----KEISLISGFAQQQEIFIPTLTVDE--------YLMIQ 70
Cdd:PRK11231 32 ALIGPNGCGKSTLLKCF-ARLLT--PQSGTVFLGDKPISmlssRQLARRLALLPQHHLTPEGITVRElvaygrspWLSLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKankhtRRERVDEIIEMLRLQNCRDlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK11231 109 GRLSAE-----DNARVNQAMEQTRINHLAD------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 151 VQILKNLANSGRTLI------HQPTAELffqfDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK11231 178 MRLMRELNTQGKTVVtvlhdlNQASRYC----DHLVVLANGHVMAQGTPEE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-165 |
1.64e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmCRNMKGLEknGTVKVNGTKIGKEISliSGFAQQQEiFIPT-------LTVDEYLMIQ----- 70
Cdd:PRK10575 41 GLIGHNGSGKSTLLKML-GRHQPPSE--GEILLDAQPLESWSS--KAFARKVA-YLPQqlpaaegMTVRELVAIGrypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 -ARLRMKANKhtrRERVDEIIEMLrlqncrDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:PRK10575 115 gALGRFGAAD---REKVEEAISLV------GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170
....*....|....*..
gi 1017384763 150 VVQILKNLANS-GRTLI 165
Cdd:PRK10575 186 VLALVHRLSQErGLTVI 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-168 |
1.65e-05 |
|
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: 45.81 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKIGKEisliSGFAQQQEIFI-------PTLTVDEYLMIQA 71
Cdd:TIGR01189 28 ALQVTGPNGIGKTTLLRIL-----AGLLRpdSGEVRWNGTPLAEQ----RDEPHENILYLghlpglkPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLRMKAnkhtrRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV 151
Cdd:TIGR01189 99 AIHGGA-----QRTIEDALAAVGLTGFEDLPAAQ------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170 180
....*....|....*....|
gi 1017384763 152 QILK-NLANSGRTLI--HQP 168
Cdd:TIGR01189 168 GLLRaHLARGGIVLLttHQD 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-159 |
1.71e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVL---MCRNMKGLEKNGT---V--KVNGTKIG--------KEISLISgfaQQQEI-FIPTL--- 61
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILsgeLIPNLGDYEEEPSwdeVlkRFRGTELQnyfkklynGEIKVVH---KPQYVdLIPKVfkg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 62 TVDEYLMiqarlrmKANKhtrRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:PRK13409 179 KVRELLK-------KVDE---RGKLDEVVERLGLENILDRDISE------LSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170
....*....|....*...
gi 1017384763 142 LDSFMAASVVQILKNLAN 159
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-195 |
1.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTT---LMNVLMCRNM-----------KGLEKNGTVKvngtKIGKEISLISGFAQQQeIFIPTLTVDey 66
Cdd:PRK13645 39 VTCVIGTTGSGKSTmiqLTNGLIISETgqtivgdyaipANLKKIKEVK----RLRKEIGLVFQFPEYQ-LFQETIEKD-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 67 lMIQARLRMKANKHTRRERVDEIIEMLRLQncRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFM 146
Cdd:PRK13645 112 -IAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSP---FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1017384763 147 AASVVQILKNL-ANSGRTLIH--QPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMvtHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-159 |
1.76e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVL--MCRNMKGLEKNGTVKVNGTKIGK-----EISLISGFAQQQEIFIPTLTVDEYLMIQARL 73
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSIFNyrdvlEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGLvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQI 153
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR---LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
....*.
gi 1017384763 154 LKNLAN 159
Cdd:PRK14271 206 IRSLAD 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-195 |
2.38e-05 |
|
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: 47.25 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLMCRnMKGLEknGTVKVNGTkigkeisliSGFAQQQEiFIPTLTVDEYLMIQARLRMKANKH 80
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAE-MDKVE--GHVHMKGS---------VAYVPQQA-WIQNDSLRENILFGKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 TRrERVDEIIEMLRLQNCRDLKIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA----SVVQILKN 156
Cdd:TIGR00957 733 VL-EACALLPDLEILPSGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhifeHVIGPEGV 809
|
170 180 190
....*....|....*....|....*....|....*....
gi 1017384763 157 LANSGRTLIHQPTAELfFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:TIGR00957 810 LKNKTRILVTHGISYL-PQVDVIIVMSGGKISEMGSYQE 847
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-165 |
2.43e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNGtkigKEISLIS-------GFA------QQQEIFiPTLTVDE- 65
Cdd:COG1129 281 LGIAGLVGAGRTELARALF-----GADPAdsGEIRLDG----KPVRIRSprdairaGIAyvpedrKGEGLV-LDLSIREn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 66 -YLMIQARLRMKA--NKHTRRERVDEIIemlrlqncRDLKIGTPGL---VKGISGGEARRLTFACELLSNPSLLFADEPT 139
Cdd:COG1129 351 iTLASLDRLSRGGllDRRRERALAEEYI--------KRLRIKTPSPeqpVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190
....*....|....*....|....*....|...
gi 1017384763 140 SGLDsfmaasvV-------QILKNLANSGRTLI 165
Cdd:COG1129 423 RGID-------VgakaeiyRLIRELAAEGKAVI 448
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-157 |
2.72e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.33 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLmnvLMCRNMkgLEK--NGTVKVNGTKI----GKEISLisgfAQQQ--EIF-----IPTLTVDEYLMIQAR 72
Cdd:PRK11153 38 GASGAGKSTL---IRCINL--LERptSGRVLVDGQDLtalsEKELRK----ARRQigMIFqhfnlLSSRTVFDNVALPLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LrmkAN--KHTRRERVDEIIEMLRLQNCRDlkiGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASV 150
Cdd:PRK11153 109 L---AGtpKAEIKARVTELLELVGLSDKAD---RYP---AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
|
....*..
gi 1017384763 151 VQILKNL 157
Cdd:PRK11153 180 LELLKDI 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-165 |
2.95e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.25 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNvLMCrnmkGLEK--NGTVKVNGTKIGKEISLISGFAQQQeifIPTLTVDEYLMIQARLR---- 74
Cdd:PRK10908 30 MAFLTGHSGAGKSTLLK-LIC----GIERpsAGKIWFSGHDITRLKNREVPFLRRQ---IGMIFQDHHLLMDRTVYdnva 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 75 -----MKANKHTRRERVDEIIEML-RLQNCRDLKIGtpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:PRK10908 102 ipliiAGASGDDIRRRVSAALDKVgLLDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170
....*....|....*..
gi 1017384763 149 SVVQILKNLANSGRTLI 165
Cdd:PRK10908 175 GILRLFEEFNRVGVTVL 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-150 |
3.17e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLMnvlmcRNMKGLEK--NGTVKV-NGTKIGkeislisgFAQQQEIFIPTLTVDEylMIQARLRMKANKHTR 82
Cdd:PRK11819 40 GLNGAGKSTLL-----RIMAGVDKefEGEARPaPGIKVG--------YLPQEPQLDPEKTVRE--NVEEGVAEVKAALDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 83 RERV-----------DEII-EMLRLQNCRD----------LKIGTPGL--------VKGISGGEARRLTFACELLSNPSL 132
Cdd:PRK11819 105 FNEIyaayaepdadfDALAaEQGELQEIIDaadawdldsqLEIAMDALrcppwdakVTKLSGGERRRVALCRLLLEKPDM 184
|
170
....*....|....*...
gi 1017384763 133 LFADEPTSGLDsfmAASV 150
Cdd:PRK11819 185 LLLDEPTNHLD---AESV 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-143 |
4.05e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.96 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVlmcrnMKGL--EKNGTVKVNG---TKIGKEISLISGFAQQQEIFiPTLTVDEY--LMIQARL 73
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNL-----IAGFltPASGSLTLNGqdhTTTPPSRRPVSMLFQENNLF-SHLTVAQNigLGLNPGL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMkanKHTRRERVDEIIEMLRLQNCRDLkigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK10771 101 KL---NAAQREKLHAIARQMGIEDLLAR------LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-143 |
4.84e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmKGLEK--NGTVKVNGTKI----GKEIS---LISGFaQQQEIFiPTLTVDEYLMIQAR 72
Cdd:PRK11300 34 VSLIGPNGAGKTTVFNCL-----TGFYKptGGTILLRGQHIeglpGHQIArmgVVRTF-QHVRLF-REMTVIENLLVAQH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKAN-----------KHTRRERVDEIIEMLRLQNCRDLKIGTPGlvkGISGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:PRK11300 107 QQLKTGlfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
..
gi 1017384763 142 LD 143
Cdd:PRK11300 184 LN 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2-156 |
4.97e-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: 45.09 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkgleknGTVKVNGTKIGKEISLISGFAQQQEIFIPTlTVDEYLMiqarlRMKANKHT 81
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLA----------GVLKPDEGDIEIELDTVSYKPQYIKADYEG-TVRDLLS-----SITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 82 RRERVDEIIEMLRLQNCRDlkigtpGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDS---FMAASVVQ--ILKN 156
Cdd:cd03237 92 HPYFKTEIAKPLQIEQILD------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVIRrfAENN 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-197 |
5.00e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLmCRNMKGLEknGTVKVNGTKI----GKEISLISGFAQQQEIFIPTLTVDEYLmiqARLRMKAN 78
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTL-SRLMTPAH--GHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDITVQELV---ARGRYPHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 79 ---KHTRRERVDEIIEMLRLQNCRDLKIGTpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILK 155
Cdd:PRK10253 111 plfTRWRKEDEEAVTKAMQATGITHLADQS---VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1017384763 156 NLANS-GRTL---IHQPTAELFFQfDKIIFLSMGKTAFMGTPHESV 197
Cdd:PRK10253 188 ELNREkGYTLaavLHDLNQACRYA-SHLIALREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-195 |
5.32e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMnvlmcRNMKGLEK--NGTVKVNG------TK------IGKEISLISGFAQQQeIFIPTLtvdEYLM 68
Cdd:PRK13646 37 AIVGQTGSGKSTLI-----QNINALLKptTGTVTVDDitithkTKdkyirpVRKRIGMVFQFPESQ-LFEDTV---EREI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVDEIieMLRLQNCRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:PRK13646 108 IFGPKNFKMNLDEVKNYAHRL--LMDLGFSRDVMSQSP---FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1017384763 149 SVVQILKNLA---NSGRTLIHQPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13646 183 QVMRLLKSLQtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-195 |
5.74e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.41 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 4 LMGASGAGKTTLMNVLmcrNMKGLEKNGTVKVNGTKIGK----EISLIS----GFAQQQEIFIPTLTVdeylMIQARLRM 75
Cdd:PRK10070 59 IMGLSGSGKSTMVRLL---NRLIEPTRGQVLIDGVDIAKisdaELREVRrkkiAMVFQSFALMPHMTV----LDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KANKHTRRERVDEIIEMLRLQNCRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV-QIL 154
Cdd:PRK10070 132 ELAGINAEERREKALDALRQVGLENYAHSYP---DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1017384763 155 KNLANSGRTL--IHQPTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK10070 209 KLQAKHQRTIvfISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
86-144 |
5.82e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 5.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 86 VDEIIEmlRLQNCRDLKIGTPGlvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:PTZ00265 1337 IDEFIE--SLPNKYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-165 |
6.45e-05 |
|
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: 44.66 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKHTRRERVDEIIEMLRLQNCRDLKIgtpglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:cd03236 112 KKKDERGKLDELVDQLELRHVLDRNI------DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL 185
|
....*...
gi 1017384763 158 ANSGRTLI 165
Cdd:cd03236 186 AEDDNYVL 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-157 |
8.31e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLM-----------CRNMKGLEKNGTVKVNGTKIGKEISLISG------FAQQQEIFIPTLTVD 64
Cdd:PRK10261 45 LAIVGESGSGKSVTALALMrlleqagglvqCDKMLLRRRSRQVIELSEQSAAQMRHVRGadmamiFQEPMTSLNPVFTVG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 65 EYLMIQARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPglvKGISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:PRK10261 125 EQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP---HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV 201
|
170
....*....|...
gi 1017384763 145 FMAASVVQILKNL 157
Cdd:PRK10261 202 TIQAQILQLIKVL 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-165 |
8.81e-05 |
|
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: 43.86 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMnVLMCRNMKGLE-----KNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRm 75
Cdd:cd03290 29 LTMIVGQVGCGKSSLL-LAILGEMQTLEgkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 kankhtrRERVDEIIEMLRLQNCRDL-------KIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:cd03290 107 -------KQRYKAVTDACSLQPDIDLlpfgdqtEIGERGI--NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170
....*....|....*....
gi 1017384763 149 SVVQ--ILKNLANSGRTLI 165
Cdd:cd03290 178 HLMQegILKFLQDDKRTLV 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
83-165 |
8.85e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 83 RERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGR 162
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAK------YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
...
gi 1017384763 163 TLI 165
Cdd:NF000106 196 TVL 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-193 |
8.87e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 43.94 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmKGLE-KNGTVKVNGTKIGKeISL------ISGFAQQQEIFIPTL--TVDEYlmiqar 72
Cdd:cd03369 37 IGIVGRTGAGKSTLILALF----RFLEaEEGKIEIDGIDIST-IPLedlrssLTIIPQDPTLFSGTIrsNLDPF------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 lrmkaNKHTRrervDEIIEMLRlqncrdlkIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ 152
Cdd:cd03369 106 -----DEYSD----EEIYGALR--------VSEGGL--NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1017384763 153 ILKNLANSGRTLIHQPTAELFFQFDKIIFLSMGKTAFMGTP 193
Cdd:cd03369 167 TIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-186 |
9.11e-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: 45.20 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLMNVLMCRNMKGLEknGTVKVNGTK---------IGKEISLISGFAQQQEIfIPTLTVDEYLMIQArlrmk 76
Cdd:TIGR02633 293 GLVGAGRTELVQALFGAYPGKFE--GNVFINGKPvdirnpaqaIRAGIAMVPEDRKRHGI-VPILGVGKNITLSV----- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 77 ANKHTRRERVDEIIE-------MLRLQncrdLKIGTPGL-VKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:TIGR02633 365 LKSFCFKMRIDAAAElqiigsaIQRLK----VKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1017384763 149 SVVQILKNLANSGRTLI--HQPTAELFFQFDKIIFLSMGK 186
Cdd:TIGR02633 441 EIYKLINQLAQEGVAIIvvSSELAEVLGLSDRVLVIGEGK 480
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-158 |
9.13e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTtlmnvLMCRNMKGL------EKNGTVKVNGTKI------GKEISLIsgFAQQQEIFIPTLTVDEYlmiq 70
Cdd:PRK10418 33 ALVGGSGSGKS-----LTCAAALGIlpagvrQTAGRVLLDGKPVapcalrGRKIATI--MQNPRSAFNPLHTMHTH---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 71 ARLRMKA-NKHTRRERVDEIIEMLRLQNcrdlkigtPGLVKG-----ISGGEARRLTFACELLSNPSLLFADEPTSGLDS 144
Cdd:PRK10418 102 ARETCLAlGKPADDATLTAALEAVGLEN--------AARVLKlypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170
....*....|....
gi 1017384763 145 FMAASVVQILKNLA 158
Cdd:PRK10418 174 VAQARILDLLESIV 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
83-195 |
1.04e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.31 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 83 RERVDEIIEMLRLQNCRDLkigTPGLvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL-ANSG 161
Cdd:PRK13633 122 RERVDESLKKVGMYEYRRH---APHL---LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYG 195
|
90 100 110
....*....|....*....|....*....|....*..
gi 1017384763 162 RTLI---HqpTAELFFQFDKIIFLSMGKTAFMGTPHE 195
Cdd:PRK13633 196 ITIIlitH--YMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-166 |
1.17e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLMCRNmkgLEKNGTVKVNGTK---------IGKEISLIsgfaqQQEI-FIPTLTVDEYLMIqAR 72
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNY---QPDAGSILIDGQEmrfasttaaLAAGVAII-----YQELhLVPEMTVAENLYL-GQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 73 LRMKA---NKHTRRERVDEIIEMLRLqncrDLKIGTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAAS 149
Cdd:PRK11288 105 LPHKGgivNRRLLNYEAREQLEHLGV----DIDPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170
....*....|....*..
gi 1017384763 150 VVQILKNLANSGRTLIH 166
Cdd:PRK11288 179 LFRVIRELRAEGRVILY 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
113-157 |
1.64e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.38 E-value: 1.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1017384763 113 SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGL 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-143 |
1.74e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmKGLEKN-GTVKVNgtkigkEISLISGFAQQQEI-FIPTLTVDEYlMIQarlrmkank 79
Cdd:PRK15064 348 LAIIGENGVGKTTLLRTLV----GELEPDsGTVKWS------ENANIGYYAQDHAYdFENDLTLFDW-MSQ--------- 407
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 80 hTRRERVDE--IIEML-RLQNCRDlKIGTPglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK15064 408 -WRQEGDDEqaVRGTLgRLLFSQD-DIKKS--VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-192 |
2.32e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVlMCRNMKGLEkNGTVKVNGTkigkeislISGFAQQQEIFipTLTVDEYLMIQARLrmKANKH 80
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISA-MLGELPPRS-DASVVIRGT--------VAYVPQVSWIF--NATVRDNILFGSPF--DPERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 TRRERVDEIIEMLRLQNCRDL-KIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQ--ILKNL 157
Cdd:PLN03130 711 ERAIDVTALQHDLDLLPGGDLtEIGERGV--NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDEL 788
|
170 180 190
....*....|....*....|....*....|....*..
gi 1017384763 158 ANSGRTLIhqpTAELFF--QFDKIIFLSMGKTAFMGT 192
Cdd:PLN03130 789 RGKTRVLV---TNQLHFlsQVDRIILVHEGMIKEEGT 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
110-165 |
2.48e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1017384763 110 KGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-165 |
3.09e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEKN--GTVKVNG--TKIGKEISLI-SGFA-----QQQEIFIPTLTVDEYLMIQA 71
Cdd:PRK11288 282 VGLFGLVGAGRSELMKLLY-----GATRRtaGQVYLDGkpIDIRSPRDAIrAGIMlcpedRKAEGIIPVHSVADNINISA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 R-----LRMKANKHTRRERVDEIIemlrlqncRDLKIGTPG---LVKGISGGEARRLTFACELLSNPSLLFADEPTSGLD 143
Cdd:PRK11288 357 RrhhlrAGCLINNRWEAENADRFI--------RSLNIKTPSreqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180
....*....|....*....|..
gi 1017384763 144 SFMAASVVQILKNLANSGRTLI 165
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVL 450
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-188 |
3.12e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 6 GASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIGKEISLIS---GFA-----QQQEIFIPTLTVDEYLMIQARLRM 75
Cdd:PRK09700 296 GLVGSGRTELMNCLF-----GVDKraGGEIRLNGKDISPRSPLDAvkkGMAyitesRRDNGFFPNFSIAQNMAISRSLKD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 76 KA--------NKHTRRERVDEIIEMLRL------QNCRDLkigtpglvkgiSGGEARRLTFACELLSNPSLLFADEPTSG 141
Cdd:PRK09700 371 GGykgamglfHEVDEQRTAENQRELLALkchsvnQNITEL-----------SGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1017384763 142 LDSFMAASVVQILKNLANSGRTLI--HQPTAELFFQFDKIIFLSMGKTA 188
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGKVILmvSSELPEIITVCDRIAVFCEGRLT 488
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
327-534 |
4.24e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 41.72 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 327 SALYFLIAELTFSTMFGIMTFMeheLPLIAREYHDGLFY--------VISYYISRFLSYLPLFTIDGALMIVISYWMIGL 398
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLT---ALSIAREREQGTLErllvtpvsRLEILLGKVLAYLLRGLLQALLVLLVALLFFGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 399 NSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSGLYGNTNNFPVyirWMQWTSWC---RY 475
Cdd:COG0842 78 PLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPG---WLQAIAYLnplTY 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 476 GFEGLvvnqwsqvdnpkwdpfyRELILKQFSFnkDNYQLDVIGLCSIVIFFYLAGYIAL 534
Cdd:COG0842 155 FVEAL-----------------RALFLGGAGL--ADVWPSLLVLLAFAVVLLALALRLF 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
113-157 |
4.62e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 4.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1017384763 113 SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-142 |
4.63e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVlmcrnMKGLE--KNGTVKVNGTKIGKeisLISGFAQQ-------QEIFI-PTLTVDEYLMiqar 72
Cdd:PRK15439 41 ALLGGNGAGKSTLMKI-----IAGIVppDSGTLEIGGNPCAR---LTPAKAHQlgiylvpQEPLLfPNLSVKENIL---- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017384763 73 LRMkANKHTRRERVDEIIEMLRLQNCRDLKIGT-----PGLVKGISGgearrltfaceLLSNPSLLFADEPTSGL 142
Cdd:PRK15439 109 FGL-PKRQASMQKMKQLLAALGCQLDLDSSAGSlevadRQIVEILRG-----------LMRDSRILILDEPTASL 171
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
108-180 |
6.41e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 108 LVKGISGGEARRLT----FACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLI---HQPtaELFFQFDKII 180
Cdd:cd03227 74 TRLQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIvitHLP--ELAELADKLI 151
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-166 |
7.04e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVL--------------------MCRNMKGLEKNGtvkvngtkigkeISLIsgfaqQQEI-FIPT 60
Cdd:PRK13549 34 VSLCGENGAGKSTLMKVLsgvyphgtyegeiifegeelQASNIRDTERAG------------IAII-----HQELaLVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 61 LTVDEYLMIQARL----RMKANKHTRRerVDEIIEMLRLqncrDLKIGTPglVKGISGGEARRLTFACELLSNPSLLFAD 136
Cdd:PRK13549 97 LSVLENIFLGNEItpggIMDYDAMYLR--AQKLLAQLKL----DINPATP--VGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|
gi 1017384763 137 EPTSGLDSFMAASVVQILKNLANSGRTLIH 166
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIY 198
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
101-165 |
8.20e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017384763 101 LKIGTPGLVkgISGGEARRLTFACElLSNPS----LLFADEPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:cd03271 161 IKLGQPATT--LSGGEAQRIKLAKE-LSKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVV 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
112-195 |
8.63e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 41.28 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 112 ISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL-ANSGRTLI---HQPTAELffQFDKIIFLSMGKT 187
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIIsitHDLSEAM--EADHVIVMNKGTV 220
|
....*...
gi 1017384763 188 AFMGTPHE 195
Cdd:PRK13648 221 YKEGTPTE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
109-183 |
9.50e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 9.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017384763 109 VKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANsgrtlihQPTAELFFQ--FDKIIFLS 183
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-------QNVAVLFISsdLEEIEQMA 470
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1-192 |
9.74e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.38 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNvlmcrnmKGLEKNGTVKVngtkigkeISLISGFAQQQEIFIPTLtvdeylmiqarlrmkankh 80
Cdd:cd03238 23 LVVVTGVSGSGKSTLVN-------EGLYASGKARL--------ISFLPKFSRNKLIFIDQL------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 81 trRERVDEIIEMLRLqncrDLKIGTpglvkgISGGEARRLTFACELLSNP--SLLFADEPTSGLDSFMAASVVQILKNLA 158
Cdd:cd03238 69 --QFLIDVGLGYLTL----GQKLST------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 1017384763 159 NSGRTLI---HQPTaeLFFQFDKIIFLSMGKTAFMGT 192
Cdd:cd03238 137 DLGNTVIlieHNLD--VLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-157 |
1.07e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.18 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcRNMKGLEKN----GTVKVNGTKIGKEISLISGFAQQQEIFIPT-----LTVDEYLMIQA 71
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCL--NRMNELESEvrveGRVEFFNQNIYERRVNLNRLRRQVSMVHPKpnlfpMSVYDNVAYGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 72 RLrmkANKHTRRErVDEIIE-MLRLQNCRDL---KIGTPGLvkGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMA 147
Cdd:PRK14258 113 KI---VGWRPKLE-IDDIVEsALKDADLWDEikhKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170
....*....|
gi 1017384763 148 ASVVQILKNL 157
Cdd:PRK14258 187 MKVESLIQSL 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-161 |
1.07e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcrnmkGLEK--NGTVKVNGTKIG----KEIsLISGFAqqqeiFIP----------TLTVDE 65
Cdd:COG3845 287 LGIAGVAGNGQSELAEALA-----GLRPpaSGSIRLDGEDITglspRER-RRLGVA-----YIPedrlgrglvpDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 66 YLMIQARLRMKA------NKHTRRERVDEIIEmlrlqncrDLKIGTPGL---VKGISGGEARRLTFACELLSNPSLLFAD 136
Cdd:COG3845 356 NLILGRYRRPPFsrggflDRKAIRAFAEELIE--------EFDVRTPGPdtpARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180
....*....|....*....|....*.
gi 1017384763 137 EPTSGLDsFMAASVV-QILKNLANSG 161
Cdd:COG3845 428 QPTRGLD-VGAIEFIhQRLLELRDAG 452
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-167 |
1.12e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 1 MVALMGASGAGKTTLMNVLmcrnmKGL--EKNGTVKVNGTKIGKEISLIsgfaQQQEIFIPTLT-VDEYLMIQARLRMKA 77
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLI-----AGLlnPEKGEILFERQSIKKDLCTY----QKQLCFVGHRSgINPYLTLRENCLYDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 78 NKHTRRERVDEIIEMLRLQNCRDLKIGTpglvkgISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVV-QILKN 156
Cdd:PRK13540 100 HFSPGAVGITELCRLFSLEHLIDYPCGL------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIItKIQEH 173
|
170
....*....|...
gi 1017384763 157 LANSGRTLI--HQ 167
Cdd:PRK13540 174 RAKGGAVLLtsHQ 186
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
2-25 |
1.14e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 39.40 E-value: 1.14e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
61-143 |
1.35e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 61 LTVDEYLMIQARL-RMKANKhtRRERVDEIIEMLRLQNCRDlkiGTPG-LVKGIsggeaR-RLTFACELLSNPSLLFADE 137
Cdd:NF033858 354 LTVRQNLELHARLfHLPAAE--IAARVAEMLERFDLADVAD---ALPDsLPLGI-----RqRLSLAVAVIHKPELLILDE 423
|
....*.
gi 1017384763 138 PTSGLD 143
Cdd:NF033858 424 PTSGVD 429
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
40-225 |
1.72e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 40 IGKEISLIsgFAQQQEIFIPTLTVDEYLmIQA------RLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPglvKGIS 113
Cdd:PRK15093 87 VGHNVSMI--FQEPQSCLDPSERVGRQL-MQNipgwtyKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFP---YELT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 114 GGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNL-ANSGRT--LIHQPTAELFFQFDKIIFLSMGKT--- 187
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTilLISHDLQMLSQWADKINVLYCGQTvet 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1017384763 188 ----AFMGTPHES-----VKFFADCGHPIPKlfnppewiQSKLSVIP 225
Cdd:PRK15093 241 apskELVTTPHHPytqalIRAIPDFGSAMPH--------KSRLNTLP 279
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
101-188 |
1.83e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 101 LKIGTPG---LVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGR--TLIHQPTAELFFQ 175
Cdd:PRK10982 378 MRVKTPGhrtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgiIIISSEMPELLGI 457
|
90
....*....|...
gi 1017384763 176 FDKIIFLSMGKTA 188
Cdd:PRK10982 458 TDRILVMSNGLVA 470
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-157 |
1.93e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLMcRNMKglEKNGTVKVNGtkigKEISLISGFAQQ------QEIFI-------PTLTVDEYLM 68
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALL-RLVE--SQGGEIIFNG----QRIDTLSPGKLQalrrdiQFIFQdpyasldPRQTVGDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 69 IQARLRMKANKHTRRERVDEIIEMLRLQNCRDLKigtpgLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAA 148
Cdd:PRK10261 426 EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWR-----YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
....*....
gi 1017384763 149 SVVQILKNL 157
Cdd:PRK10261 501 QIINLLLDL 509
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
113-163 |
2.91e-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: 40.19 E-value: 2.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 113 SGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLAnSGRT 163
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRT 545
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
62-157 |
3.99e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.56 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 62 TVDEYLMIQARLrmkaNKHTRRERVdeiIEMLRlqncrdlKIGT--------PGLvkgISGGEARRLTFACELLSNPSLL 133
Cdd:PRK11308 114 ILEEPLLINTSL----SAAERREKA---LAMMA-------KVGLrpehydryPHM---FSGGQRQRIAIARALMLDPDVV 176
|
90 100
....*....|....*....|....
gi 1017384763 134 FADEPTSGLDSFMAASVVQILKNL 157
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDL 200
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
101-165 |
4.61e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017384763 101 LKIGTPGLVkgISGGEARRLTFACELL---SNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLI 165
Cdd:TIGR00630 821 IRLGQPATT--LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-165 |
5.15e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.38 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 2 VALMGASGAGKTTLMNVLmcrnmkglekNGTVKVNGTKIGKEISlISGFAQQQEIFIPtLTVDEYLMiqarlrmKANKht 81
Cdd:COG1245 369 LGIVGPNGIGKTTFAKIL----------AGVLKPDEGEVDEDLK-ISYKPQYISPDYD-GTVEEFLR-------SANT-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 82 rrERVD------EIIEMLRLQNCRDLKigtpglVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILK 155
Cdd:COG1245 428 --DDFGssyyktEIIKPLGLEKLLDKN------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|.
gi 1017384763 156 NLA-NSGRTLI 165
Cdd:COG1245 500 RFAeNRGKTAM 510
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-162 |
6.10e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 3 ALMGASGAGKTTLMNVLM---CRNMKGLEKNG-TVKVNGTKIGKE--ISLIsgfaqQQEI-FIPTLTVDE--YLMIQARL 73
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTgiyTRDAGSILYLGkEVTFNGPKSSQEagIGII-----HQELnLIPQLTIAEniFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017384763 74 RMKANKHTR-RERVDEIIEMLRL-----QNCRDLKIGTPGLVKgIsggeARRLTFacellsNPSLLFADEPTSGLDSFMA 147
Cdd:PRK10762 109 RFGRIDWKKmYAEADKLLARLNLrfssdKLVGELSIGEQQMVE-I----AKVLSF------ESKVIIMDEPTDALTDTET 177
|
170
....*....|....*
gi 1017384763 148 ASVVQILKNLANSGR 162
Cdd:PRK10762 178 ESLFRVIRELKSQGR 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
112-162 |
8.60e-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: 37.55 E-value: 8.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1017384763 112 ISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGR 162
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
|
| |
