|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-326 |
0e+00 |
|
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: 507.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVgTADRMTFDGVELLGLPEKK 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGI-TSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRV 163
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 244 ASPRHPYTRGLLDCIPVRGKtlPGSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLNTAGGDktHHVRCHKV 323
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDP--DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPG--HRVACHLY 315
|
...
gi 515278464 324 TAA 326
Cdd:COG0444 316 EEE 318
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-263 |
3.24e-152 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 437.96 E-value: 3.24e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGLP 80
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLR 160
Cdd:COG4172 83 ERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 161 QRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVG 240
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250 260
....*....|....*....|...
gi 515278464 241 QLFASPRHPYTRGLLDCIPVRGK 263
Cdd:COG4172 243 ELFAAPQHPYTRKLLAAEPRGDP 265
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-322 |
3.17e-123 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 357.11 E-value: 3.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAV--GTAdrmTFDGVELLG 78
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRigGSA---TFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEA-MLEKpGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSG 157
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVlMLHK-GMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 238 DVGQLFASPRHPYTRGLLDCIPvRGKTlPGSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLNTAGGdkthH 317
Cdd:PRK09473 245 NARDVFYQPSHPYSIGLLNAVP-RLDA-EGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPG----R 318
|
....*.
gi 515278464 318 VR-CHK 322
Cdd:PRK09473 319 LRaCFK 324
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-321 |
1.92e-115 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 337.09 E-value: 1.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDLPTENGML-------HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVE 75
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP----TSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 76 LLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQL 155
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 236 TADVGQLFASPRHPYTRGLLDCIPVRGktlPGSKLQAIP--GVVPSLVGNIGGCVFRNRCSLADATC-EQDPPMLNTAGG 312
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAVPVPD---PERRRERIVleGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLREVGPG 315
|
....*....
gi 515278464 313 dktHHVRCH 321
Cdd:COG4608 316 ---HQVACH 321
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-321 |
2.12e-112 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 329.39 E-value: 2.12e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRV 163
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 244 ASPRHPYTRGLLDCIP--VRGKtlpgSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLNTAGGdktHHVRCH 321
Cdd:PRK11022 243 RAPRHPYTQALLRALPefAQDK----ARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAG---RQSKCH 315
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-237 |
9.00e-112 |
|
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: 324.07 E-value: 9.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKK 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP----TSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNqLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLhRTGISNAEDRLRQYPHQLSGGLRQRV 163
Cdd:cd03257 77 RK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-321 |
1.26e-106 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 314.92 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMlekPGVT-------RAEAR-DRAIYLLHRTGISNAEDRLRQYPHQL 155
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAI---PSWTfkgkwwqRFKWRkKRAIELLHRVGIKDHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 236 TADVGQLFASPRHPYTRGLLDCIPVRGKTLP-GSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLNtaggDK 314
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPDFRQPLPhKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRK----IK 315
|
....*..
gi 515278464 315 THHVRCH 321
Cdd:COG4170 316 GHEFACH 322
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-247 |
7.13e-104 |
|
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: 314.15 E-value: 7.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPteNGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVgTADRMTFDGVELLGLP 80
Cdd:COG1123 1 MTPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGR-ISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EkklnQLRGQRMSMIFQEPMTSLNPSyTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLR 160
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEA-LENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 161 QRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVG 240
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
....*..
gi 515278464 241 QLFASPR 247
Cdd:COG1123 229 EILAAPQ 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-260 |
3.65e-103 |
|
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: 312.22 E-value: 3.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLPT-ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLP 80
Cdd:COG1123 258 EPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----TSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLR 160
Cdd:COG1123 334 RRSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 161 QRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVG 240
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|
gi 515278464 241 QLFASPRHPYTRGLLDCIPV 260
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPS 510
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-266 |
1.13e-95 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 293.53 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRK-AVGTADRMTFDGVELLGLPEK 82
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQR 162
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 163 VMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260
....*....|....*....|....
gi 515278464 243 FASPRHPYTRGLLDCIPvRGKTLP 266
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEP-SGDPVP 267
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-324 |
1.45e-92 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 278.90 E-value: 1.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDLPTENG---------MLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDG 73
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 74 VELLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAMLE-KPGVTRAEARDRAIYLLHRTGI-SNAEDRlrqY 151
Cdd:PRK15079 83 KDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINR---Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 152 PHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAG 231
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 232 QVVETADVGQLFASPRHPYTRGLLDCIPV------RGKTlpgskLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPP 305
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVPIpdpdleRNKT-----IQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRP 313
|
330
....*....|....*....
gi 515278464 306 MLNtagGDKTHHVRCHKVT 324
Cdd:PRK15079 314 VLE---GSFRHAVSCLKVD 329
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-259 |
7.31e-90 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 278.49 E-value: 7.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDLPTENGML-------HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavgTADRMTFDGVE 75
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLFrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 76 LLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAM-LEKPGVTRAEARDRAIYLLHRTGISnAEDRLRqYPHQ 154
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLrVHGPGLSAAERRARVAEALEEVGLD-PAARHR-YPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*
gi 515278464 235 ETADVGQLFASPRHPYTRGLLDCIP 259
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-323 |
1.17e-87 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 266.45 E-value: 1.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGM------LHAVRGIDFQVKRGEMLCLVGESGCGKSmtSLALMGLLPRKAvgTADRMTFDGV 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLfkperlVKALDGVSFTLERGKTLAVVGESGCGKS--TLARLLTMIETP--TGGELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 75 ELLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsNAE--DRlrqYP 152
Cdd:PRK11308 78 DLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEhyDR---YP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 153 HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 233 VVETADVGQLFASPRHPYTRGLLDCIPVRGKTLPGSKLQaIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLNTAGG 312
Cdd:PRK11308 233 CVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIK-LTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDG 311
|
330
....*....|.
gi 515278464 313 dktHHVRCHKV 323
Cdd:PRK11308 312 ---RLVACFAV 319
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-266 |
1.76e-86 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 272.50 E-value: 1.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGTAD-------RMTFDGVEL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL-EQAGGLVQcdkmllrRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 LGLPEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLS 156
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260 270
....*....|....*....|....*....|....
gi 515278464 237 ADVGQLFASPRHPYTRGLLDCIP----VRGKTLP 266
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVPqlgaMKGLDYP 284
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-321 |
4.82e-85 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 259.73 E-value: 4.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMlekPGVT-------RAEARD-RAIYLLHRTGISNAEDRLRQYPHQL 155
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNI---PGWTykgrwwqRFGWRKrRAIELLHRVGIKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 236 TADVGQLFASPRHPYTRGLLDCIPVRGKTLP-GSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPMLntagGDK 314
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPDFGSAMPhKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLT----GAK 315
|
....*..
gi 515278464 315 THHVRCH 321
Cdd:PRK15093 316 NHLYACH 322
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-255 |
6.09e-85 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 255.76 E-value: 6.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGLpekklnQLRGQRMSMIFQEPMTS 102
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQLCEAMLEKpGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLL 255
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-259 |
1.60e-84 |
|
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: 255.50 E-value: 1.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELlglPEKK 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER----PWSGEVTFDGRPV---TRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGqRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKpgvTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRV 163
Cdd:COG1124 74 RKAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 515278464 244 ASPRHPYTRGLLDCIP 259
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-256 |
8.41e-68 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 213.02 E-value: 8.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPtenGMLhaVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELLGlpekkl 84
Cdd:PRK10418 5 IELRNIALQAA---QPL--VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKpGVTRAEARDRAIylLHRTGISNAEDRLRQYPHQLSGGLRQRVM 164
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETCLAL-GKPADDATLTAA--LEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|..
gi 515278464 245 SPRHPYTRGLLD 256
Cdd:PRK10418 231 APKHAVTRSLVS 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-235 |
1.11e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 201.43 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLL--PrkavgTADRMTFDGVELLG 78
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrP-----TSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRGQRMSMIFQEPmtSLNPSYT-LGNqlCEAMLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSG 157
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF--NLLPELTaLEN--VALPLLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-273 |
1.70e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 204.54 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 7 VKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLPEKKLNQ 86
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLERP---TSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 87 LRgQRMSMIFQEPmtSLNPSYT-LGNQlceAM-LEKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVM 164
Cdd:COG1135 80 AR-RKIGMIFQHF--NLLSSRTvAENV---ALpLEIAGVPKAEIRKRVAELLELVGLS---DKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250 260
....*....|....*....|....*....
gi 515278464 245 SPRHPYTRGLLDciPVRGKTLPGSKLQAI 273
Cdd:COG1135 231 NPQSELTRRFLP--TVLNDELPEELLARL 257
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-233 |
1.57e-62 |
|
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: 198.10 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLPEKKL 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRP---TSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRGQRMSMIFQEPmtSLNPSYT-LGNQLCEAMLekPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRV 163
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTaLENVELPLLL--AGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQV 233
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-260 |
6.39e-62 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 207.79 E-value: 6.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGML-------HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtaDRMTFDGVEL 76
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 LGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISnAEDRLRqYPHQLS 156
Cdd:PRK10261 389 DTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLL-PEHAWR-YPHEFS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
250 260
....*....|....*....|....
gi 515278464 237 ADVGQLFASPRHPYTRGLLDCIPV 260
Cdd:PRK10261 546 GPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-255 |
1.08e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 199.93 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLPTENGML-------HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtadRMTFDGV 74
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-----EIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 75 ELLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLCEAM-LEKPGVTRAEARDRAIYLLHRTGIsNAEDRLRqYPH 153
Cdd:PRK15134 348 PLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGL-DPETRHR-YPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250 260
....*....|....*....|..
gi 515278464 234 VETADVGQLFASPRHPYTRGLL 255
Cdd:PRK15134 505 VEQGDCERVFAAPQQEYTRQLL 526
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-255 |
2.25e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 191.59 E-value: 2.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLH-----AVRGIDFQVKRGEMLCLVGESGCGKSmtSLALM--GLLPRkavgTADRMTFDG 73
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKS--TLAKMlaGIIEP----TSGEILING 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 74 VELlglpEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLcEAMLEKPGVTRAEARDRAIYL-LHRTGISnaEDRLRQYP 152
Cdd:COG4167 75 HKL----EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQIL-EEPLRLNTDLTAEEREERIFAtLRLVGLL--PEHANFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 153 HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|...
gi 515278464 233 VVETADVGQLFASPRHPYTRGLL 255
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLI 250
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-251 |
3.75e-59 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 191.18 E-value: 3.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDG-----VELLG 78
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPTSGSVYYRDrdggpRDLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnAEDRLRQYPHQLSGG 158
Cdd:COG4107 84 LSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEI--PLERIDDLPRTFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETAD 238
Cdd:COG4107 162 MQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGL 241
|
250
....*....|...
gi 515278464 239 VGQLFASPRHPYT 251
Cdd:COG4107 242 TDQVLEDPQHPYT 254
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-247 |
5.83e-59 |
|
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: 189.71 E-value: 5.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 7 VKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLPEKKLNQ 86
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERP---TSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 87 LRgQRMSMIFQEpmTSLNPSYT-LGNqlCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMI 165
Cdd:cd03258 80 AR-RRIGMIFQH--FNLLSSRTvFEN--VALPLEIAGVPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 166 AMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 515278464 246 PR 247
Cdd:cd03258 232 PQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
25-252 |
9.88e-54 |
|
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: 176.32 E-value: 9.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPRkavgTADRMTFDGVELLGLPEKKLNQLRgQRMSMIFQEP--MT 101
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKS-VLLkLIIGLLRP----DSGEILVDGQDITGLSEKELYELR-RRIGMLFQGGalFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLnpsyTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:COG1127 96 SL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 182 TTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPrHPYTR 252
Cdd:COG1127 169 TAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVR 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-252 |
1.42e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 175.95 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLL--PrkavgTADRMTFDGVELlGLPEKKLNQLRgQRMSMIF 96
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLeeP-----DSGTITVDGEDL-TDSKKDINKLR-RKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QepmtSLN--PSYT-LGNqLCEAMLEKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:COG1126 84 Q----QFNlfPHLTvLEN-VTLAPIKVKKMSKAEAEERAMELLERVGLA---DKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTR 252
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-256 |
2.75e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 178.46 E-value: 2.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 21 LHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLPEKKLNQLRgQRMSMIFQEpm 100
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERP---TSGRVLVDGQDLTALSEKELRKAR-RQIGMIFQH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTL-GNQlceAM-LEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:PRK11153 91 FNLLSSRTVfDNV---ALpLELAGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLLD 256
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-253 |
1.44e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 171.43 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrkavGTADRMTFDGVELLGL 79
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLrLIAGLEK----PTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 pekklnqlrGQRMSMIFQEPmtSLNPSYT-LGNqlCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGG 158
Cdd:COG1116 79 ---------GPDRGVVFQEP--ALLPWLTvLDN--VALGLELRGVPKAERRERARELLELVGLAGFEDA---YPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDV----TIQAQILRmireLQREFGTAVVFITHDLG--VvsRIADRVAVMYA-- 230
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLR----LWQETGKTVLFVTHDVDeaV--FLADRVVVLSArp 216
|
250 260
....*....|....*....|...
gi 515278464 231 GQVVETADVGqlFASPRHPYTRG 253
Cdd:COG1116 217 GRIVEEIDVD--LPRPRDRELRT 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-252 |
2.46e-51 |
|
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: 169.99 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLPEKKL 84
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKS-TLLRLIVGLLRPDSGE---VLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRgQRMSMIFQEPmtSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDrlrQYPHQLSGGLRQRVM 164
Cdd:cd03261 73 YRLR-RRMGMLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED---LYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*...
gi 515278464 245 SPrHPYTR 252
Cdd:cd03261 227 SD-DPLVR 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-244 |
6.07e-51 |
|
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: 168.66 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLglpEKKL 84
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK----PTSGEVLVDGKDIT---KKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRgQRMSMIFQepmtslNPSytlgNQLCEAMLEK-----P---GVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLS 156
Cdd:COG1122 71 RELR-RKVGLVFQ------NPD----DQLFAPTVEEdvafgPenlGLPREEIRERVEEALELVGLEHLADR---PPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
....*...
gi 515278464 237 ADVGQLFA 244
Cdd:COG1122 216 GTPREVFS 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-261 |
1.58e-49 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 166.52 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSMTSLALMGlLPRKAVGTadrMTFDGVELLGLPEKKLNQLRgQRMSMIFQEPMTSLNP 105
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEKPAQGT---VSFRGQDLYQLDRKQRRAFR-RDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTAL 185
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 186 DVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASpRHPYTRGLLDCI----PVR 261
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVlpehPVR 260
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-240 |
1.15e-48 |
|
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: 162.64 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRkavgTADRMTFDGVELLGlpekk 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIaGLERP----TSGEVLVDGEPVTG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 lnqlRGQRMSMIFQEPmtSLNPSYT-LGNqlCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQR 162
Cdd:cd03293 71 ----PGPDRGYVFQQD--ALLPWLTvLDN--VALGLELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 163 VMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYA--GQVVETADVG 240
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEVD 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-237 |
2.81e-48 |
|
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: 161.83 E-value: 2.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLprkaVGTADRMTFDGVELLGLPEK 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLD----RPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRGQRMSMIFQEPMtsLNPSYT-LGNqlceAMLEKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQ 161
Cdd:COG4181 83 ARARLRARHVGFVFQSFQ--LLPTLTaLEN----VMLPLELAGRRDARARARALLERVGLG---HRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 162 RVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVETA 237
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-252 |
8.86e-48 |
|
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: 162.04 E-value: 8.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:cd03294 20 LLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLIEPTSGKVLIDGQDIAAMSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQRMSMIFQE----PMTSLNPSYTLGnqlceamLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGL 159
Cdd:cd03294 96 LRELRRKKISMVFQSfallPHRTVLENVAFG-------LEVQGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADV 239
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
250
....*....|...
gi 515278464 240 GQLFASPRHPYTR 252
Cdd:cd03294 246 EEILTNPANDYVR 258
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-242 |
2.60e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrmtfdgVELLGL-PEKKLNQLRgQRMSMIFQEPm 100
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS-GE--------VRVLGEdVARDPAEVR-RRIGYVPQEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 tSLNPSYTLGNQL---CEAMlekpGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLII 177
Cdd:COG1131 83 -ALYPDLTVRENLrffARLY----GLPRKEARERIDELLELFGL---TDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 178 ADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-250 |
5.56e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 159.49 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPRkavgTADRMTFDGVELLGL 79
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKT-TLLrMIAGFETP----DSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 -PEKklnqlRGqrMSMIFQepmtslnpSYTL------------GnqlceamLEKPGVTRAEARDRAIYLLHRTGISNAED 146
Cdd:COG3842 73 pPEK-----RN--VGMVFQ--------DYALfphltvaenvafG-------LRMRGVPKAEIRARVAELLELVGLEGLAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 147 RlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVA 226
Cdd:COG3842 131 R---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA 207
|
250 260
....*....|....*....|....
gi 515278464 227 VMYAGQVVETADVGQLFASPRHPY 250
Cdd:COG3842 208 VMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-237 |
2.15e-45 |
|
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: 153.83 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKKl 84
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 nqlrgQRMSMIFQEPmtSLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVM 164
Cdd:cd03259 72 -----RNIGMVFQDY--ALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-261 |
2.94e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 155.23 E-value: 2.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlprkavgtaDRMTFDGVELLGLPEKKLN--QLRGQR--MSMIFQEP 99
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL---------ESPSQGNVSWRGEPLAKLNraQRKAFRrdIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 MTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIAD 179
Cdd:PRK10419 99 ISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 180 EPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASpRHPYTRGLLDCI- 258
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNAVl 255
|
....*.
gi 515278464 259 ---PVR 261
Cdd:PRK10419 256 pafPVR 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-232 |
6.38e-45 |
|
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: 152.62 E-value: 6.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 7 VKNLRVDLPTENGmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKKLnq 86
Cdd:cd03225 2 LKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEVLVDGKDLTKLSLKEL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 87 lrGQRMSMIFQepmtslNPSytlgNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGG 158
Cdd:cd03225 74 --RRKVGLVFQ------NPD----DQFFGPTveeevafgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-233 |
9.47e-44 |
|
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: 149.60 E-value: 9.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGlPEKKLNQLRgQRMSMIFQE 98
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPDSGT---IIIDGLKLTD-DKKNINELR-QKVGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 pmTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:cd03262 85 --FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-234 |
6.14e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 6.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrkavGTADRMTFDGVELLGLPEK 82
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVE----PTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRgQRMSMIFQEPmtSLNPSYT-LGNQLCEAMLEKPGVT------RAEARDRAIYLLHRTGISnaeDRLRQYPHQL 155
Cdd:COG3638 74 ALRRLR-RRIGMIFQQF--NLVPRLSvLTNVLAGRLGRTSTWRsllglfPPEDRERALEALERVGLA---DKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-251 |
6.70e-43 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 148.92 E-value: 6.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDG-----VE 75
Cdd:PRK11701 3 DQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMrdgqlRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 76 LLGLPEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnAEDRLRQYPHQL 155
Cdd:PRK11701 75 LYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI--DAARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
250
....*....|....*.
gi 515278464 236 TADVGQLFASPRHPYT 251
Cdd:PRK11701 233 SGLTDQVLDDPQHPYT 248
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-234 |
8.14e-43 |
|
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: 148.27 E-value: 8.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTEngmlHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPRKAvGTadrMTFDGVELLGLPEK 82
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSS-GE---VLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KlnqlRGQRMSMIFQEPmtSLNPSYTlgnqlCEAMLE------KPGVTRAEARDRAI--YLLHRTGISNAEDRlrqYPHQ 154
Cdd:COG1120 72 E----LARRIAYVPQEP--PAPFGLT-----VRELVAlgryphLGLFGRPSAEDREAveEALERTGLEHLADR---PVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-258 |
1.70e-42 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 147.67 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTADRMTFDG--VELLGLPE 81
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDH-GTATYIMRSGaeLELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 82 KKLNQLRGQRMSMIFQEPMTSLNPSYTLGNQLCEAML----EKPGVTRAEARDraiyLLHRTGISnaEDRLRQYPHQLSG 157
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMaigaRHYGNIRATAQD----WLEEVEID--PTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 515278464 238 DVGQLFASPRHPYTRGLLDCI 258
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-255 |
4.73e-42 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 146.86 E-value: 4.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLH-----AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVE 75
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP----TSGELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 76 LlglpEKKLNQLRGQRMSMIFQEPMTSLNPSYTLGnQLCEAMLEKPGVTRAEARDRAIYL-LHRTGISNaeDRLRQYPHQ 154
Cdd:PRK15112 77 L----HFGDYSYRSQRIRMIFQDPSTSLNPRQRIS-QILDFPLRLNTDLEPEQREKQIIEtLRQVGLLP--DHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|.
gi 515278464 235 ETADVGQLFASPRHPYTRGLL 255
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLI 250
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
26-235 |
9.98e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 144.80 E-value: 9.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPrkaVGTADRMTFDGVELLGLPEKKLNQLRGQRMSMIFQepMTSLNP 105
Cdd:TIGR02211 23 GVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLD---NPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQ--FHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYT-LGNQLCEAMLEKPGVTraEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTA 184
Cdd:TIGR02211 97 DFTaLENVAMPLLIGKKSVK--EAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515278464 185 LDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIaDRVAVMYAGQVVE 235
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-257 |
1.57e-41 |
|
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: 144.75 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTslalMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQlrgqRMSMIFQEpmTS 102
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINRLIEPTSGEIFIDGEDIREQDPVELRR----KIGYVIQQ--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLgNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:cd03295 86 LFPHMTV-EENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLLDC 257
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-234 |
1.87e-41 |
|
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: 144.63 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVdlpTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKL 84
Cdd:cd03256 1 IEVENLSK---TYPNGKKALKDVSLSINPGEFVALIGPSGAGKS----TLLRCLNGLVEPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRgQRMSMIFQEPmTSLNPSYTLGNQLCEAMLEKP-------GVTRAEaRDRAIYLLHRTGISnaeDRLRQYPHQLSG 157
Cdd:cd03256 74 RQLR-RQIGMIFQQF-NLIERLSVLENVLSGRLGRRStwrslfgLFPKEE-KQRALAALERVGLL---DKAYQRADQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-241 |
3.40e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.57 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmTslaLMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRgQRMSMIFQE---- 98
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS-T---LLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQDfrll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 -----------PMtslnpsytlgnqlcEAMlekpGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAM 167
Cdd:COG2884 92 pdrtvyenvalPL--------------RVT----GKSRKEIRRRVREVLDLVGLS---DKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 168 ALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQ 241
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-246 |
7.16e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.53 E-value: 7.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLL--PRKAVGTADRMTFDGVEllGLPEKKLNQLRgQRMSMIF 96
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGQLNIAGHQFDFSQ--KPSEKAIRLLR-QKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEpmTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQrEFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVgQLFASP 246
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQP 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
1.58e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENgmlhAVRGIDFQVKRGEMLCLVGESGCGKSmtSL--ALMGLLPRKAvGTadrmtfdgVELLG 78
Cdd:COG1121 3 MMPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKS--TLlkAILGLLPPTS-GT--------VRLFG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRG---QRMSMIFQEPMT-----SLNPSYTLGnqlceaMLEKPgvtRAEARDRAIYLLHRTGISNAEDRlrQ 150
Cdd:COG1121 68 KPPRRARRRIGyvpQRAEVDWDFPITvrdvvLMGRYGRRG------LFRRP---SRADREAVDEALERVGLEDLADR--P 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 151 YpHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:COG1121 137 I-GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-234 |
1.82e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 139.36 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKS----TLLRCINRLVEPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRgQRMSMIFQEpMTSLNPSYTLGNQLCEAMLEKPGV-------TRAEaRDRAIYLLHRTGISnaeDRLRQYPHQLS 156
Cdd:TIGR02315 74 LRKLR-RRIGMIFQH-YNLIERLTVLENVLHGRLGYKPTWrsllgrfSEED-KERALSALERVGLA---DKAYQRADQLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-238 |
3.78e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.61 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGT---ADRmTFDgveLLGLP-EKKLNQLRgQRMSMIFQEpmTS 102
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPRSGTlniAGN-HFD---FSKTPsDKAIRELR-RNVGMVFQQ--YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 183 TALDVTIQAQILRMIRELQrEFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETAD 238
Cdd:PRK11124 170 AALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-256 |
6.01e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.34 E-value: 6.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSvLLDVKNLRVDLpTENGMLHavrGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGT--ADRMTFDGVELLG 78
Cdd:PRK11264 1 MS-AIEVKNLVKKF-HGQTVLH---GIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAGTirVGDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRgQRMSMIFQEpmTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGG 158
Cdd:PRK11264 75 QQKGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVfITHDLGVVSRIADRVAVMYAGQVVETAD 238
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....*...
gi 515278464 239 VGQLFASPRHPYTRGLLD 256
Cdd:PRK11264 228 AKALFADPQQPRTRQFLE 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-234 |
3.92e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 136.79 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELLGlpEKKLNQLRgQRMSMIFQepmts 102
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL----LPTSGKVTVDGLDTLD--EENLWEIR-KKVGMVFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lNPSytlgNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIA--MALMcg 172
Cdd:TIGR04520 85 -NPD----NQFVGATveddvafgLENLGVPREEMRKRVDEALKLVGM---EDFRDREPHLLSGGQKQRVAIAgvLAMR-- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVV 234
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIV 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-234 |
5.75e-38 |
|
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: 133.33 E-value: 5.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 6 DVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPRKAvGTadrMTFDGVELLGLPEKKL 84
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSS-GE---ILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRGqrmsmifqepmtslnpsytlgnqlceamlekpgvtraeardraiYL---LHRTGISNAEDRlrqYPHQLSGGLRQ 161
Cdd:cd03214 72 ARKIA--------------------------------------------YVpqaLELLGLAHLADR---PFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 162 RVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-228 |
9.01e-38 |
|
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: 134.20 E-value: 9.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrKAVGTadrmtfdgVELLGLPEKKLNQLRG---QRMSMIFQ 97
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLK-PTSGS--------IRVFGKPLEKERKRIGyvpQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 98 EPMTSLNpSYTLGnqlCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLII 177
Cdd:cd03235 83 FPISVRD-VVLMG---LYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIG---ELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515278464 178 ADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-234 |
1.38e-37 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 133.99 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLPEKKLNQLRgQRMSMIFQEpmTSLNP 105
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKT-TLLTLIGGLRSVQEGS---LKVLGQELHGASKKQLVQLR-RRIGYIFQA--HNLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTAL 185
Cdd:TIGR02982 96 FLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 186 DVTIQAQILRMIRELQREFGTAVVFITHDlgvvSRI---ADRVAVMYAGQVV 234
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKEQGCTILMVTHD----NRIldvADRILQMEDGKLL 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-232 |
5.01e-37 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.16 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLpEKKL 84
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKS-TLLRCIAGLEEPDSGS---ILIDGEDLTDL-EDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRgQRMSMIFQEPmtSLNPsytlgnqlceamlekpgvtraeardraiyllHRTGISNaedrlRQYPhqLSGGLRQRVM 164
Cdd:cd03229 72 PPLR-RRIGMVFQDF--ALFP-------------------------------HLTVLEN-----IALG--LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-250 |
2.52e-36 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 134.01 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlprkAVGTADRMTFDGVELLGLP 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGRDITRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNqlrgqrMSMIFQepmtslnpSYTLGNQLCEAM-----LEKPGVTRAEARDRAIYLLHRTGISNAEdrlRQYPHQL 155
Cdd:TIGR03265 73 PQKRD------YGIVFQ--------SYALFPNLTVADniaygLKNRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:TIGR03265 136 SGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQ 215
|
250
....*....|....*
gi 515278464 236 TADVGQLFASPRHPY 250
Cdd:TIGR03265 216 VGTPQEIYRHPATPF 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-242 |
2.92e-36 |
|
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: 130.38 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVdlptENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTAD--RMTFDGVELLGLPEK 82
Cdd:cd03260 1 IELRDLNV----YYGDKHALKDISLDIPKGEITALIGPSGCGKS-TLLRLLNRLNDLIPGAPDegEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNqLRgQRMSMIFQEPM---TSL--NPSYTLgnqlcEAMLEKPgvtRAEARDRAIYLLHRTGISNAEDRlRQYPHQLSG 157
Cdd:cd03260 76 VLE-LR-RRVGMVFQKPNpfpGSIydNVAYGL-----RLHGIKL---KEELDERVEEALRKAALWDEVKD-RLHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfgTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 515278464 238 DVGQL 242
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-233 |
8.33e-36 |
|
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: 127.51 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrmtfdgVELLGLPEKKL 84
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS-GE--------IKVLGKDIKKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRGQRMSMIFQEPmtSLNPSYTlgnqlceamlekpgvtraeARDraiYLlhrtgisnaedrlrqyphQLSGGLRQRVM 164
Cdd:cd03230 68 PEEVKRRIGYLPEEP--SLYENLT-------------------VRE---NL------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-247 |
1.01e-35 |
|
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: 129.48 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVdlptENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTslaLMGLLPRKAVGTADRMTFDGVELLGLPEKKL 84
Cdd:cd03219 1 LEVRGLTK----RFGGLVALDDVSFSVRPGEIHGLIGPNGAGKT-T---LFNLISGFLRPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRgqrMSMIFQepMTSLNPSYT------LGNQL---CEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLrqyPHQL 155
Cdd:cd03219 73 ARLG---IGRTFQ--IPRLFPELTvlenvmVAAQArtgSGLLLARARREEREARERAEELLERVGLADLADRP---AGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 515278464 236 TADVGQLFASPR 247
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-257 |
1.38e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.81 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSvlLDVKNLRVDLPTEngmlHAVRGIDFQVKRGEMLCLVGESGCGKSMT--SLAlmGLLprkavgTAD--RMTFDGVEL 76
Cdd:COG1118 1 MS--IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLlrIIA--GLE------TPDsgRIVLNGRDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 L-GLPEKKlnqlRgqRMSMIFQEP-----MTSL-NPSYTLGNQlceamlekpGVTRAEARDRAIYLLHRTGISNAEDRlr 149
Cdd:COG1118 67 FtNLPPRE----R--RVGFVFQHYalfphMTVAeNIAFGLRVR---------PPSKAEIRARVEELLELVQLEGLADR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 150 qYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:COG1118 130 -YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
250 260
....*....|....*....|....*...
gi 515278464 230 AGQVVETADVGQLFASPRHPYTRGLLDC 257
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-183 |
1.58e-35 |
|
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: 126.22 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKKLnqlrGQRMSMIFQEPmtSL 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS----PTEGTILLDGQDLTDDERKSL----RKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLCEAMLEKpGVTRAEARDRAIYLLHRTGISNAEDR-LRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:pfam00005 71 FPRLTVRENLRLGLLLK-GLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 515278464 183 T 183
Cdd:pfam00005 150 A 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-233 |
4.75e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGmlhaVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrkavGTADRMTFDGVELLGLPekk 83
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKS-TLLrALADLDP----PTSGEIYLDGKPLSAMP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRgQRMSMIFQEPmtslnpsyTLGNQLCEAMLEKPGVTRAEA--RDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQ 161
Cdd:COG4619 69 PPEWR-RQVAYVPQEP--------ALWGGTVRDNLPFPFQLRERKfdRERALELLERLGLP--PDILDKPVERLSGGERQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 162 RVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:COG4619 138 RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-249 |
5.98e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.16 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 12 VDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTAD------RMTFDGVELLGLPEKKLN 85
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPSEGSIVvngqtiNLVRDKDGQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 86 QLRGQRMSMIFQEpmTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQ-YPHQLSGGLRQRVM 164
Cdd:PRK10619 88 RLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI---DERAQGkYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
....*
gi 515278464 245 SPRHP 249
Cdd:PRK10619 242 NPQSP 246
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-235 |
7.48e-35 |
|
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: 126.97 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlprkAVGTADRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmT 101
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLPPHK------RPVNTVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:cd03300 82 ALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 182 TTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-236 |
2.20e-34 |
|
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: 123.69 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGvellglpekklnqlrgqrmsmifqE 98
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP----DSGEILVDG------------------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 PMTSLNPsytlgnqlceamlekpgvtrAEARDRAIYLLHrtgisnaedrlrqyphQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:cd03216 63 EVSFASP--------------------RDARRAGIAMVY----------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-250 |
4.01e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPrkavGTADRMTFDGVELLGLPEKKlnqlRGqrMSMIFQEP- 99
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKS-TLLRMIaGLED----PTSGEILIGGRDVTDLPPKD----RN--IAMVFQSYa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 ----MTSL-NPSYTLGNQlceamlekpGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:COG3839 86 lyphMTVYeNIAFPLKLR---------KVPKAEIDRRVREAAELLGLEDLLDR---KPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPY 250
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-232 |
7.08e-34 |
|
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: 121.97 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPekklnqlrgqrmsmifqepmt 101
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKDIAKLP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlgnqlceamlekpgvtRAEARDRAIYLlhrtgisnaedrlrqypHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:cd00267 68 -----------------------LEELRRRIGYV-----------------PQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-242 |
7.88e-34 |
|
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: 124.02 E-value: 7.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTADRMTFDGVellglpeKKLNQLRgQRMSMIFQEPmtS 102
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS-GRATVAGHDVV-------REPREVR-RRIGIVFQDL--S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTlGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYphqLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:cd03265 84 VDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-255 |
1.12e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.71 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRkavgTADRMTFDGVELLGLPEkklnqlrGQR-MSMIFQEpmTSLN 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKS-TLLNLIaGFLPP----DSGRILWNGQDLTALPP-------AERpVSMLFQE--NNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 105 PSYTLGNQLCEAMleKPGVT-RAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:COG3840 84 PHLTVAQNIGLGL--RPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 184 ALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLL 255
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-246 |
1.86e-33 |
|
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: 123.60 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHaVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKAvgtadRMTFDGVELLGLPEKK 83
Cdd:cd03299 1 LKVENLSKDW----KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSG-----KILLNGKDITNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 lnqlrgQRMSMIFQEpmTSLNPSYTLGNQLcEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRV 163
Cdd:cd03299 71 ------RDISYVPQN--YALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
...
gi 515278464 244 ASP 246
Cdd:cd03299 219 KKP 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-246 |
2.68e-33 |
|
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: 125.98 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLpRKAVGtadRMTFDGvELLGLPEKKLNQLRGQR-MSMIFQEPmtSL 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGK--TTLlrAIAGLE-RPDSG---RIRLGG-EVLQDSARGIFLPPHRRrIGYVFQEA--RL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYT-LGNqLCEAMLEKPGVTRAEARDRAIYLLhrtGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:COG4148 89 FPHLSvRGN-LLYGRKRAPRAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-245 |
4.10e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 4.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPteNGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrMTFDGVELlglP 80
Cdd:PRK13635 2 KEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA-GT---ITVGGMVL---S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNQLRgQRMSMIFQEPmtslnpsytlGNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYP 152
Cdd:PRK13635 73 EETVWDVR-RQVGMVFQNP----------DNQFVGATvqddvafgLENIGVPREEMVERVDQALRQVGM---EDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 153 HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQ 232
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|...
gi 515278464 233 VVETADVGQLFAS 245
Cdd:PRK13635 218 ILEEGTPEEIFKS 230
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-255 |
1.87e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 122.51 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLL--PrkavgTADRMTFDGVELLGLPekkLNQLRgQRMSMIFQEpm 100
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRMINRLieP-----TSGRILIDGEDIRDLD---PVELR-RRIGYVIQQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTLG-N-----QLCeamlekpGVTRAEARDRAIYLLHRTGIsNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:COG1125 85 IGLFPHMTVAeNiatvpRLL-------GWDKERIRARVDELLELVGL-DPEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 175 LIIADEPTTALD-VT---IQAQILRmireLQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPY 250
Cdd:COG1125 157 ILLMDEPFGALDpITreqLQDELLR----LQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 515278464 251 TRGLL 255
Cdd:COG1125 233 VADFV 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-244 |
3.90e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNL--RVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELlg 78
Cdd:PRK13650 1 MSNIIEVKNLtfKYKEDQEK---YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDLL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 lPEKKLNQLRgQRMSMIFQEPmtslnpsytlGNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGISNAEDRlrq 150
Cdd:PRK13650 72 -TEENVWDIR-HKIGMVFQNP----------DNQFVGATveddvafgLENKGIPHEEMKERVNEALELVGMQDFKER--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 151 YPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSrIADRVAVMYA 230
Cdd:PRK13650 137 EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKN 215
|
250
....*....|....
gi 515278464 231 GQVVETADVGQLFA 244
Cdd:PRK13650 216 GQVESTSTPRELFS 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-252 |
9.68e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.83 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRGQRMSMIF 96
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEpmTSLNPSYTLGNQLCEAMlEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:PRK10070 113 QS--FALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTR 252
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-242 |
1.50e-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: 118.42 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLpRKAVGTAdrmTFDGVEllglPEKKLNQLRgQRMSMIFQEPM 100
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKT-TLLrMLAGLL-KPDSGSI---LIDGED----VRKEPREAR-RQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 tsLNPSYTL-GNQLCEAMLEkpGVTRAEARDRAIYLLHRTGISNAEDRLRqypHQLSGGLRQRVMIAMALMCGPDLIIAD 179
Cdd:COG4555 85 --LYDRLTVrENIRYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 180 EPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-233 |
3.19e-31 |
|
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: 116.74 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRgQRMSMIFQE 98
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 pmTSLNPSYTLGNQLCEAMlEKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:cd03292 87 --FRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLS---HKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-255 |
5.49e-31 |
|
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: 117.05 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLldVKNLRvdlpTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLP 80
Cdd:cd03296 1 MSIE--VRNVS----KRFGDFVALDDVSLDIPSGELVALLGPSGSGKT-TLLRLIAGLERP---DSGTILFGGEDATDVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNqlrgqrMSMIFQEpmTSLNPSYTLGNQLCEAMLEKPGVTR---AEARDRAIYLLHRTGISNAEDRlrqYPHQLSG 157
Cdd:cd03296 71 VQERN------VGFVFQH--YALFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADR---YPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
250
....*....|....*...
gi 515278464 238 DVGQLFASPRHPYTRGLL 255
Cdd:cd03296 220 TPDEVYDHPASPFVYSFL 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-242 |
5.92e-31 |
|
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: 116.38 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGtadRMTFDGVELLGLPEKKL 84
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS-G---SIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQlRGqrMSMIFQEPMtsLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTgisnaEDRLRQYPHQLSGGLRQRVM 164
Cdd:cd03224 73 AR-AG--IGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRL-----KERRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
6.99e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 6.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKS--MTSLALMG-LLPR-KAVGtadRMTFDGVEL 76
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKStlLRCLNRMNdLIPGaRVEG---EILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 LGlPEKKLNQLRgQRMSMIFQEPmtslNP---S-Y---TLGnqlceamLEKPGVT-RAEARDRAIYLLHRTGISNaE--D 146
Cdd:COG1117 81 YD-PDVDVVELR-RRVGMVFQKP----NPfpkSiYdnvAYG-------LRLHGIKsKSELDEIVEESLRKAALWD-EvkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 147 RLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFgtAVVFITHDLGVVSRIADRVA 226
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTA 224
|
250 260
....*....|....*....|....*.
gi 515278464 227 VMYAGQVVETADVGQLFASPRHPYTR 252
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-245 |
1.08e-30 |
|
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: 121.79 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKkl 84
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILINGVDLSDLDPA-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 nQLRgQRMSMIFQEPMTslnPSYTLGNQLCEAmleKPGVTRAEARDraiyLLHRTGisnAEDRLRQYPH----------- 153
Cdd:COG4988 408 -SWR-RQIAWVPQNPYL---FAGTIRENLRLG---RPDASDEELEA----ALEAAG---LDEFVAALPDgldtplgeggr 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQV 233
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRI 549
|
250
....*....|..
gi 515278464 234 VETADVGQLFAS 245
Cdd:COG4988 550 VEQGTHEELLAK 561
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-242 |
1.20e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTslaLM----GLLPRkavgTADRMTFDGVELlglpeKKLNQLRGQRM--SMI 95
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKS-T---LMkilsGVYQP----DSGEILLDGEPV-----RFRSPRDAQAAgiAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 96 FQEPmtSLNPSYT------LGNQLCEAMLekpgVTRAEARDRAIYLLHRTGIS-NAEDRLRQyphqLSGGLRQRVMIAMA 168
Cdd:COG1129 85 HQEL--NLVPNLSvaenifLGREPRRGGL----IDWRAMRRRARELLARLGLDiDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-228 |
1.51e-30 |
|
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: 115.61 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVD--LPTENGM-LHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFD----G 73
Cdd:COG4778 1 MTTLLEVENLSKTftLHLQGGKrLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNYLPDSGSILVRhdggW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 74 VELLGLPEKKLNQLRGQRMSMIFQ----EPMTSlnpsyTLgNQLCEAMLEKpGVTRAEARDRAIYLLHRTGIsnaEDRLR 149
Cdd:COG4778 77 VDLAQASPREILALRRRTIGYVSQflrvIPRVS-----AL-DVVAEPLLER-GVDREEARARARELLARLNL---PERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 150 Q-YPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:COG4778 147 DlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-225 |
1.69e-30 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 114.63 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLPEKKLNQLRGQRMSMIFQEpmT 101
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDSG---QVYLNGQETPPLNSKKASKFRREKLGYLFQN--F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAMLEKPGvTRAEARDRAIYLLHRTGISNaedRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:TIGR03608 86 ALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNL---KLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHDLgVVSRIADRV 225
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-238 |
2.26e-30 |
|
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: 120.68 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVELlglpEKKLNQLRG---QRMS 93
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDM----TKPGPDGRGrakRYIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 94 MIFQEpmTSLNPSYTLGNQLCEAM-LEKPgvtRAEARDRAIYLLHRTGISN--AEDRLRQYPHQLSGGLRQRVMIAMALM 170
Cdd:TIGR03269 369 ILHQE--YDLYPHRTVLDNLTEAIgLELP---DELARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 171 CGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETAD 238
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
22-232 |
2.39e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 114.65 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRgQRMSMIFQEpmT 101
Cdd:TIGR02673 16 AALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:TIGR02673 89 RLLPDRTVYENVALP-LEVRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:TIGR02673 165 TGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-234 |
2.42e-30 |
|
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: 114.70 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKrGEMLCLVGESGCGKSMTSLALMGLLpRKAVGTA---DRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmTSL 103
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLE-KPDGGTIvlnGTVLFDSRKKINLPPQQ------RKIGLVFQQ--YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLCEAMlekPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:cd03297 87 FPHLNVRENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515278464 184 ALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-250 |
2.67e-30 |
|
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: 117.91 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVG---TADRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmTSL 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKT-TLIRLIAGLTRPDEGeivLNGRTLFDSRKGIFLPPEK------RRIGYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLceamleKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:TIGR02142 87 FPHLSVRGNL------RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 184 ALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPY 250
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-233 |
3.26e-30 |
|
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: 113.30 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDlptengmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGvellglpek 82
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP----ASGEITLDG--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 klnqlrgqrmsmifqEPMTSLNPsytlgnqlceamlekpgvtrAEARDRAIYLLhrtgisnAEDRLRQ------------ 150
Cdd:cd03215 62 ---------------KPVTRRSP--------------------RDAIRAGIAYV-------PEDRKREglvldlsvaeni 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 151 -YPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:cd03215 100 aLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMY 178
|
....
gi 515278464 230 AGQV 233
Cdd:cd03215 179 EGRI 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
26-255 |
3.79e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGlPEKKLNQLRgQRMSMIFQEpmTSLNP 105
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEEITSGD---LIVDGLKVND-PKVDERLIR-QEAGMVFQQ--FYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTAL 185
Cdd:PRK09493 91 HLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLA---ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 186 DVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLL 255
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-247 |
5.92e-30 |
|
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: 113.92 E-value: 5.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGtadRMTFDGVELLGLPE 81
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS-G---SIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 82 KKLNQL--------RGqrmsmIFqepmtslnPSYT------LGnqlceAMLEKPGVTRAEARDRaIY-----Llhrtgis 142
Cdd:COG0410 73 HRIARLgigyvpegRR-----IF--------PSLTveenllLG-----AYARRDRAEVRADLER-VYelfprL------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 143 naEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIA 222
Cdd:COG0410 127 --KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIA 203
|
250 260
....*....|....*....|....*
gi 515278464 223 DRVAVMYAGQVVETADVGQLFASPR 247
Cdd:COG0410 204 DRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-234 |
6.23e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 6.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLP 80
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPTSGT---YRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNQLRGQRMSMIFQEpmtslnpsYTLGNQLCEAM-LEKP----GVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQL 155
Cdd:PRK10535 77 ADALAQLRREHFGFIFQR--------YHLLSHLTAAQnVEVPavyaGLERKQRLLRAQELLQRLGL---EDRVEYQPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRiADRVAVMYAGQVV 234
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-251 |
9.83e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.85 E-value: 9.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLA----LMGLLPRKAVgtADRMTFDGVELLGLP 80
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKS-TLLRvfnrLIELYPEARV--SGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 ekkLNQLRgQRMSMIFQEPmtslNPSYTLG---NQLCEAMLEKPGVTRAEARDRAIYLLHRTGI-SNAEDRLRQYPHQLS 156
Cdd:PRK14247 77 ---VIELR-RRVQMVFQIP----NPIPNLSifeNVALGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFgtAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
250
....*....|....*
gi 515278464 237 ADVGQLFASPRHPYT 251
Cdd:PRK14247 227 GPTREVFTNPRHELT 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-234 |
2.68e-29 |
|
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: 111.60 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPR---KAVGTADRMTFDGVELLG-LPEKklnqlRGqrmsmifqe 98
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdsgEVLFDGKPLDIAARNRIGyLPEE-----RG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 pmtsLNPSYTLGNQLCE-AMLEkpGVTRAEARDRAIYLLHRTGISN-AEDRLRQyphqLSGGLRQRVMIAMALMCGPDLI 176
Cdd:cd03269 81 ----LYPKMKVIDQLVYlAQLK--GLKKEEARRRIDEWLERLELSEyANKRVEE----LSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-237 |
4.75e-29 |
|
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: 111.19 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlprkAVGTADRMTFDGVELLGLPEKKLNqlrgqrMSMIFQEpmT 101
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDRD------IAMVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:cd03301 82 ALYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 182 TTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-247 |
8.41e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLlDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRkavgTADRMTFDGVELLGl 79
Cdd:COG4525 1 MSML-TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIaGFLAP----SSGEITLDGVPVTG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 PekklnqlrGQRMSMIFQE----PMTSLNPSYTLGNQLceamlekPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQL 155
Cdd:COG4525 74 P--------GADRGVVFQKdallPWLNVLDNVAFGLRL-------RGVPKAERRARAEELLALVGLADFARR---RIWQL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDV----TIQAQILRmireLQREFGTAVVFITHD----------LGVVS-- 219
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDAltreQMQELLLD----VWQRTGKGVFLITHSveealflatrLVVMSpg 211
|
250 260 270
....*....|....*....|....*....|
gi 515278464 220 --RIADRVAVMYAGQVVETADVGQLFASPR 247
Cdd:COG4525 212 pgRIVERLELDFSRRFLAGEDARAIKSDPA 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-277 |
1.04e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkavgTAD--RMTFDGVEL-------LG-LPEKklnqlRGqr 91
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL------APDsgEVLWDGEPLdpedrrrIGyLPEE-----RG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 92 msmifqepmtsLNPSYTLGNQLCE-AMLEkpGVTRAEARDRAIYLLHRTGIS-NAEDRLRQyphqLSGGLRQRVMIAMAL 169
Cdd:COG4152 82 -----------LYPKMKVGEQLVYlARLK--GLSKAEAKRRADEWLERLGLGdRANKKVEE----LSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 170 MCGPDLIIADEPTTALDVtIQAQILR-MIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFAspRH 248
Cdd:COG4152 145 LHDPELLILDEPFSGLDP-VNVELLKdVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QF 220
|
250 260
....*....|....*....|....*....
gi 515278464 249 PYTRGLLDCipvrgkTLPGSKLQAIPGVV 277
Cdd:COG4152 221 GRNTLRLEA------DGDAGWLRALPGVT 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-232 |
1.13e-28 |
|
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: 108.62 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPekkLNQLRgQRMSMIFQEPmts 102
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLD---LESLR-KNIAYVPQDP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsytlgnqlceamlekpgvtraeardraiYLLHRTGISNAedrlrqyphqLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:cd03228 86 -------------------------------FLFSGTIRENI----------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515278464 183 TALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQ 232
Cdd:cd03228 125 SALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-235 |
1.13e-28 |
|
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: 116.47 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtSLA--LMGLLPrkavGTADRMTFDGVELLGLPekkLNQLRGQrMSMIFQEPM 100
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKS--TLLklLLGLYE----PTSGRILIDGIDLRQID---PASLRRQ-IGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 ---TSL--NpsYTLGNqlceamlekPGVTRAEARDRAIyllhrtgISNAEDRLRQYPH-----------QLSGGLRQRVM 164
Cdd:COG2274 560 lfsGTIreN--ITLGD---------PDATDEEIIEAAR-------LAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQVVE 235
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-246 |
1.16e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLP--TEngmlhAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PrkavgTADRMTFDGvELLGLP 80
Cdd:PRK13639 1 ILETRDLKYSYPdgTE-----ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkP-----TSGEVLIKG-EPIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLNQLRgQRMSMIFQEPmtslnpsytlGNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISNAEDRLrqyP 152
Cdd:PRK13639 70 KKSLLEVR-KTVGIVFQNP----------DDQLFAPTVEEDvafgplnlGLSKEEVEKRVKEALKAVGMEGFENKP---P 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 153 HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGK 214
|
250
....*....|....
gi 515278464 233 VVETADVGQLFASP 246
Cdd:PRK13639 215 IIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-245 |
1.38e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.80 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PrkavgTADRMTFDGVELLG-LPEKKLNQLRgQRMSMIFQEPM 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkP-----TTGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TslnpsytlgnQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCG 172
Cdd:PRK13646 96 S----------QLFEDTVEREiifgpknfKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-256 |
4.22e-28 |
|
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: 114.48 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLPteNGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPE 81
Cdd:COG4987 331 GPSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP----QSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 82 KklnQLRgQRMSMIFQEPmtslnpsY----TLGNQLceaMLEKPGVTRAEARDraiyLLHRTGIsnaEDRLRQYPH---- 153
Cdd:COG4987 405 D---DLR-RRIAVVPQRP-------HlfdtTLRENL---RLARPDATDEELWA----ALERVGL---GDWLAALPDgldt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 -------QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVA 226
Cdd:COG4987 464 wlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRIL 540
|
250 260 270
....*....|....*....|....*....|
gi 515278464 227 VMYAGQVVETADVGQLFAspRHPYTRGLLD 256
Cdd:COG4987 541 VLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-234 |
4.41e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 4.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELLGlpEKKLNQLRgQRMSMIFQEPmts 102
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL----IPSEGKVYVDGLDTSD--EENLWDIR-NKAGMVFQNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsytlGNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISnaEDRlRQYPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:PRK13633 95 -------DNQIVATIVEEDvafgpenlGIPPEEIRERVDESLKKVGMY--EYR-RHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVV 234
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-241 |
7.63e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.95 E-value: 7.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptENGMLhaVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkAVGTADRMTFDGVELLGLP-EKK 83
Cdd:COG4136 2 LSLENLTITL--GGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSP-AFSASGEVLLNGRRLTALPaEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 lnqlrgqRMSMIFQEPMtsLNPSYTLGNQLCEAMleKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRV 163
Cdd:COG4136 77 -------RIGILFQDDL--LFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDlgvvsrIADRVAvmyAGQVVETADVGQ 241
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD------EEDAPA---AGRVLDLGNWQH 211
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-255 |
9.02e-28 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 108.35 E-value: 9.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLPekklnqLRGQRMSMIFQE 98
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKS-TLLRIIAGLEQPDSG---RIRLNGQDATRVH------ARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 pmTSLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:TIGR00968 81 --YALFKHLTVRDNIAFG-LEIRKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLL 255
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-233 |
1.08e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.98 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGVELLGLPEKKLNQLRGQRMSMIFQepMTSL 103
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTP---TSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYT-LGNQlceAM-LEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:PRK11629 99 LPDFTaLENV---AMpLLIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 182 TTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIaDRVAVMYAGQV 233
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-234 |
1.12e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.34 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGtadRMTFDGvellglpeKKLNQLRGQRMS-MIFQEPMTS 102
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI-KESSG---SILLNG--------KPIKAKERRKSIgYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNpSYTLGNQLCEAMLEKP-GVTRAEArdraiyLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:cd03226 84 LF-TDSVREELLLGLKELDaGNEQAET------VLKDLDLYALKER---HPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-246 |
1.44e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRK-AVGTADRMTFDGVEllglpEKKLNQLRgQRMSMIFQEPM 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSgTVTIGERVITAGKK-----NKKLKPLR-KKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 tslnpsytlgNQLCEAMLEK-----P---GVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCG 172
Cdd:PRK13634 96 ----------HQLFEETVEKdicfgPmnfGVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-251 |
1.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVdlptENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADrmtfDGVELLG-- 78
Cdd:PRK14267 1 MKFAIETVNLRV----YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVE----GEVRLFGrn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPEKKLNQLRGQR-MSMIFQEPmtslNPSYTLG---NQLCEAMLEKPGVTRAEARDRAIYLLHRTGI-SNAEDRLRQYPH 153
Cdd:PRK14267 73 IYSPDVDPIEVRReVGMVFQYP----NPFPHLTiydNVAIGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRLNDYPS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFgtAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
250
....*....|....*...
gi 515278464 234 VETADVGQLFASPRHPYT 251
Cdd:PRK14267 227 IEVGPTRKVFENPEHELT 244
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
232-322 |
2.95e-27 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 102.44 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 232 QVVETADVGQLFASPRHPYTRGLLDCIPVRGKtlPGSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATCEQDPPML-NTA 310
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKK--RDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALvEIA 78
|
90
....*....|..
gi 515278464 311 GGdktHHVRCHK 322
Cdd:TIGR01727 79 EG---HRVACHL 87
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-234 |
3.05e-27 |
|
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: 106.44 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGTAdrmTFDGVELLglpeKKLNQLRgQRMSMIF 96
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPTSGTA---YINGYSIR----TDRKAAR-QSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEPM--TSLNPSYTLgnQLCeAMLEkpGVTRAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:cd03263 82 QFDAlfDELTVREHL--RFY-ARLK--GLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-241 |
3.85e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 21 LHAVRGIDFQVKRGEMLCLVGESGCGKSmTslaLM----GLLprkavgTAD--RMTFDGVELlglpekklnQLRGQRMS- 93
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKS-T---LMkilyGLY------QPDsgEILIDGKPV---------RIRSPRDAi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 94 -----MIFQEPMtsLNPSYT------LGnqlceamLEKPG---VTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGL 159
Cdd:COG3845 79 algigMVHQHFM--LVPNLTvaenivLG-------LEPTKggrLDRKAARARIRELSERYGL---DVDPDAKVEDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALdvTIQ--AQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTV 223
|
....
gi 515278464 238 DVGQ 241
Cdd:COG3845 224 DTAE 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
3.89e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.78 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRV--DLPTENgMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKA------VGTADRMTFDG 73
Cdd:PRK13631 20 IILRVKNLYCvfDEKQEN-ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGtiqvgdIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 74 VELLGLPEKKLN--QLRgQRMSMIFQepmtslNPSYtlgnQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISn 143
Cdd:PRK13631 99 LITNPYSKKIKNfkELR-RRVSMVFQ------FPEY----QLFKDTIEKDimfgpvalGVKKSEAKKLAKFYLNKMGLD- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 144 aEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIAD 223
Cdd:PRK13631 167 -DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVAD 244
|
250 260
....*....|....*....|...
gi 515278464 224 RVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-237 |
4.74e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRGQRMSMIFQEPM--TSL 103
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NpsyTLGNQLCEAMLEkpGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:PRK10584 104 N---ALENVELPALLR--GESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 184 ALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVETA 237
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-244 |
9.72e-27 |
|
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: 105.39 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLpekKLNQLRGQrMSMIFQEPMTS 102
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ-IGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpSYTLGNQLceaMLEKPGVTRAEARDRAiyllhrtGISNAEDRLRQYPH-----------QLSGGLRQRVMIAMALMC 171
Cdd:cd03251 89 ---NDTVAENI---AYGRPGATREEVEEAA-------RAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVfITHDLGVVsRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTI-ENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-246 |
1.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMG-LLPRKAVGTadRMTFDGVELlglPEKKLNQLRgQRMSMIFQEPmt 101
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNS--KITVDGITL---TAKTVWDIR-EKVGIVFQNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlGNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGISNAEDrlrQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:PRK13640 94 --------DNQFVGATvgddvafgLENRAVPRPEMIKIVRDVLADVGMLDYID---SEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSrIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-266 |
1.68e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENGmLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgtadrmtFDG-VELLG- 78
Cdd:PRK13642 1 MNKILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE----------FEGkVKIDGe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 -LPEKKLNQLRgQRMSMIFQEPMTSLNPSyTLGNQLCEAMlEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSG 157
Cdd:PRK13642 70 lLTAENVWNLR-RKIGMVFQNPDNQFVGA-TVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVETA 237
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 515278464 238 DVGQLFASPRH--------PYTRGLLDCIPVRGKTLP 266
Cdd:PRK13642 223 APSELFATSEDmveigldvPFSSNLMKDLRKNGFDLP 259
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-235 |
2.01e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.48 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmTslaLMGLLPRKAVGTADRMTFDGVELLGLPekkLNQLRgQRMSMIFQEPM-- 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS-T---LVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 -TSL--NpsYTLGnqlceamleKPGVTRAEARdRAIyllhrtGISNAEDRLRQYPH-----------QLSGGLRQRVMIA 166
Cdd:COG1132 427 sGTIreN--IRYG---------RPDATDEEVE-EAA------KAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 167 MALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQVVE 235
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDDGRIVE 554
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-244 |
2.33e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGvELLGLPEKKLNQLRgQRMSMIFQEPmt 101
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP----SSGRILFDG-KPIDYSRKGLMKLR-ESVGMVFQDP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlGNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISNaedrLRQYP-HQLSGGLRQRVMIAMALMCG 172
Cdd:PRK13636 92 --------DNQLFSASVYQDvsfgavnlKLPEDEVRKRVDNALKRTGIEH----LKDKPtHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-242 |
3.66e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVdlPTENGmLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEK 82
Cdd:COG3845 256 VVLEVENLSV--RDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP----ASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 klnQLRGQRMSMIFQEPM-TSLNPSYT------LGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGI--SNAEDRLRQyph 153
Cdd:COG3845 329 ---ERRRLGVAYIPEDRLgRGLVPDMSvaenliLGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVrtPGPDTPARS--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 qLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:COG3845 403 -LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
....*....
gi 515278464 234 VETADVGQL 242
Cdd:COG3845 481 VGEVPAAEA 489
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-246 |
3.68e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 106.04 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 39 LVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLPEkklnQLRGqrMSMIFQEpmTSLNPSYTLGNQLCEAmL 118
Cdd:TIGR01187 1 LLGPSGCGKT-TLLRLLAGFEQPDSG---SIMLDGEDVTNVPP----HLRH--INMVFQS--YALFPHMTVEENVAFG-L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 119 EKPGVTRAEARDRAIYLLhrtGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIR 198
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEAL---RLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515278464 199 ELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-238 |
1.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.53 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprKAvgTADRMTFDGVELlglPEKKLNQLRGqRMSMIFQEPmts 102
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--KP--QSGEIKIDGITI---SKENLKEIRK-KIGIIFQNP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsytlGNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:PRK13632 93 -------DNQFIGATveddiafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSrIADRVAVMYAGQVVETAD 238
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-234 |
1.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprKAvgTADRMTFDGVELLGlPEKKLNQLRgQRMSMIFQEPmts 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL--KP--TSGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQYP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpSYtlgnQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISnAEDRLRQYPHQLSGGLRQRVMIAMALMCGPD 174
Cdd:PRK13637 93 ---EY----QLFEETIEKDiafgpinlGLSEEEIENRVKRAMNIVGLD-YEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-234 |
2.32e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.46 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEK 82
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS----PDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRG---QRMSMIFqePMTSLnpsytlgnqlcE--AMLEKPGVTRAEARDRAI-YLLHRTGISNAEDRLrqYPhQLS 156
Cdd:PRK13548 73 ELARRRAvlpQHSSLSF--PFTVE-----------EvvAMGRAPHGLSRAEDDALVaAALAQVDLAHLAGRD--YP-QLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALM------CGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYA 230
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
....
gi 515278464 231 GQVV 234
Cdd:PRK13548 217 GRLV 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-244 |
3.23e-24 |
|
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: 98.77 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSMTslalMGLLPRKAVGTADRMTFDGVELlglpeKKLN--QLRGQrMSMIFQEPM-- 100
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTV----VSLLERFYDPTSGEILLDGVDI-----RDLNlrWLRSQ-IGLVSQEPVlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 -TSLNPSYTLGnqlceamleKPGVTRAEArDRAIYLlhrtgiSNAEDRLRQYPH-----------QLSGGLRQRVMIAMA 168
Cdd:cd03249 90 dGTIAENIRYG---------KPDATDEEV-EEAAKK------ANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVAVMYAGQVVETADVGQLFA 244
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-234 |
9.19e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 97.25 E-value: 9.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLPEKKLNQLRGQrMSMIFQE 98
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERPSAG---KIWFSGHDITRLKNREVPFLRRQ-IGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 PMTSLNpsYTLGNQLCEAMLeKPGVTRAEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:PRK10908 88 HHLLMD--RTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLL---DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQReFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
27-246 |
9.39e-24 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 100.07 E-value: 9.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprKAVGTADRMTFDGVELLGLPEKKLNqlrgqrMSMIFQEpmTSLNPS 106
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFV--KAAGLTGRIAIADRDLTHAPPHKRG------LALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 107 YTLGNQLCEAmLEKPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALD 186
Cdd:TIGR03258 94 LKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 187 VTIQAQILRMIRELQREF-GTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:TIGR03258 170 ANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
1.72e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.11 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTslaLMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLLTGELTPSSGEVRLNGRPLAAWSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRG---QRmsmifqepmTSLNPSYT------LGnqlceamLEKPGVTRAEARDRAIYLLHRTGISNAEDRLrqYPhQ 154
Cdd:COG4559 73 LARRRAvlpQH---------SSLAFPFTveevvaLG-------RAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-T 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMAL-------MCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAV 227
Cdd:COG4559 134 LSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILL 212
|
....*..
gi 515278464 228 MYAGQVV 234
Cdd:COG4559 213 LHQGRLV 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-252 |
1.72e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKavgTADRMTFDGvellglpEKKLNQLRGQR-MSMIFQE----PMT 101
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKT-TVLRLVAGLEKP---TEGQIFIDG-------EDVTHRSIQQRdICMVFQSyalfPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SL--NPSYTLgnqlceAMLekpGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIAD 179
Cdd:PRK11432 94 SLgeNVGYGL------KML---GVPKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 180 EPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFaspRHPYTR 252
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQPASR 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-234 |
1.96e-23 |
|
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: 96.28 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELLGLPekklnqlRGQRMSMIF 96
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGFDVVKEP-------AEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEPMTSLNPSYTLGNQLcEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:cd03266 83 VSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-251 |
3.03e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.09 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 39 LVGESGCGKSmTSLALMGLLPRKAVGtadrMTFDGVELLG----LPEKKLNQLRgQRMSMIFQEPmtSLNPSYTLGNQLC 114
Cdd:PRK14271 52 LMGPTGSGKT-TFLRTLNRMNDKVSG----YRYSGDVLLGgrsiFNYRDVLEFR-RRVGMLFQRP--NPFPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 115 EAMLEKPgVTRAEARDRAIYLLHRTGISNA-EDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQI 193
Cdd:PRK14271 124 GVRAHKL-VPRKEFRGVAQARLTEVGLWDAvKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 194 LRMIRELQREFgtAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYT 251
Cdd:PRK14271 203 EEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-252 |
3.17e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTEngmlHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKK 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 lnqlrgQRMSMIFQEpmTSLNPSYTLGNQLCEAmLEKPGVTRAEARDRAIYLLhrtGISNAEDRLRQYPHQLSGGLRQRV 163
Cdd:PRK11607 91 ------RPINMMFQS--YALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEML---GLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
....*....
gi 515278464 244 aspRHPYTR 252
Cdd:PRK11607 239 ---EHPTTR 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-248 |
5.54e-23 |
|
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: 95.23 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLprkavgtaDRMTFDGVELLGlpeKKLNQLRGQRMsMIFQEpmTSL 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS-TLLNLISGL--------AQPTSGGVILEG---KQITEPGPDRM-VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLCEAMLE-KPGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:TIGR01184 66 LPWLTVRENIALAVDRvLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGqvvETADVGQL----FASPRH 248
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG---PAANIGQIlevpFPRPRD 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-234 |
9.16e-23 |
|
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: 94.71 E-value: 9.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkavgtadRMTFDGVELLGL-PEKKLNQLRgQRMSMIF-QEPM 100
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---------QPTSGEVRVAGLvPWKRRKKFL-RRIGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLhrtgisNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 181 PTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-234 |
1.16e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrMTFDGVELLGLPEKKLnqlrGQRMSMIFQEPMTsl 103
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS-GT---VFLGDKPISMLSSRQL----ARRLALLPQHHLT-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 nPSytlGNQLCE--AMLEKPGVT---RAEARDRAI--YLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:PRK11231 88 -PE---GITVRElvAYGRSPWLSlwgRLSAEDNARvnQAMEQTRINHLADRRLT---DLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-234 |
2.03e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDlptengmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrMTFDGVEL------ 76
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS-GE---IRLDGKPVrirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 ------LGL-PEKKLNQlrGqrmsmIFQEpMtSLNPSYTLGNQlceAMLEKPG-VTRAEARDRAIYLLHRTGI--SNAED 146
Cdd:COG1129 323 dairagIAYvPEDRKGE--G-----LVLD-L-SIRENITLASL---DRLSRGGlLDRRRERALAEEYIKRLRIktPSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 147 RLRQyphqLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVA 226
Cdd:COG1129 391 PVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRIL 465
|
....*...
gi 515278464 227 VMYAGQVV 234
Cdd:COG1129 466 VMREGRIV 473
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-214 |
2.46e-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: 92.93 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPRKAvGTadrmtfdgVELLGLPEKKLNQLRGQRMSMIFQEPMts 102
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGK--TTLlrILAGLLPPSA-GE--------VLWNGEPIRDAREDYRRRLAYLGHADG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQL-CEAMLEKPGVTRAEARDraiyLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:COG4133 86 LKPELTVRENLrFWAALYGLRADREAIDE----ALEAVGLAGLADLP---VRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHD 214
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-251 |
3.43e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKS--MTSLALMG-LLPRkaVGTADRMTFDGVELL 77
Cdd:PRK14239 2 TEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKStlLRSINRMNdLNPE--VTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 78 GlPEKKLNQLRgQRMSMIFQEPmtslNP-SYTLGNQLCEAmLEKPGVTRAEARDRAI-YLLHRTGISN-AEDRLRQYPHQ 154
Cdd:PRK14239 76 S-PRTDTVDLR-KEIGMVFQQP----NPfPMSIYENVVYG-LRLKGIKDKQVLDEAVeKSLKGASIWDeVKDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVfiTHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLI 226
|
250
....*....|....*..
gi 515278464 235 ETADVGQLFASPRHPYT 251
Cdd:PRK14239 227 EYNDTKQMFMNPKHKET 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-237 |
4.05e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 92.28 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEPmt 101
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKP----DSGEITFDGKSYQKNIEAL------RRIGALIEAP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYT----LGNQLCEAMLEKPGVTRaeardraiyLLHRTGISNAEDR-LRQYphqlSGGLRQRVMIAMALMCGPDLI 176
Cdd:cd03268 82 GFYPNLTarenLRLLARLLGIRKKRIDE---------VLDVVGLKDSAKKkVKGF----SLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETA 237
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-256 |
8.22e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLpekklnQLRGQRMSMIFQ-----EPMT 101
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEHQTSG---HIRFHGTDVSRL------HARDRKVGFVFQhyalfRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SL-NPSYTLgnqlceAML---EKPgvTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLII 177
Cdd:PRK10851 91 VFdNIAFGL------TVLprrERP--NAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 178 ADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFaspRHPYTRGLLD 256
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW---REPATRFVLE 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-246 |
8.90e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.84 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKKlnqlRGQR-MSMIFQEPm 100
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGKILLDGQDITKLPMHK----RARLgIGYLPQEA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 tSLNPSYTLGNQLcEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:cd03218 85 -SIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKAS---SLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 181 PTTALDVTIQAQILRMIREL-QREFGtavVFIT-HDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-234 |
9.22e-22 |
|
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: 91.40 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 28 DFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmTSLNPSY 107
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 108 TLGNQLceAMLEKPGVT-RAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALD 186
Cdd:cd03298 86 TVEQNV--GLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515278464 187 VTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-284 |
1.81e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKAVgtadrMTFDGVEL-LGLPEKKLNQLRgQRMSMIFQEPMTSLn 104
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGT-----ITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 105 psytLGNQLCEAMLEKP---GVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:PRK13641 99 ----FENTVLKDVEFGPknfGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 182 TTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYTRGLLDciPVR 261
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDE--PAT 249
|
250 260
....*....|....*....|....*...
gi 515278464 262 GK-----TLPGSKLQAIPGVVPSLVGNI 284
Cdd:PRK13641 250 SRfasklEKGGFKFSEMPLTIDELVDGI 277
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-251 |
2.25e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDG-VELLGLPEKKLNQLRGQR-MSMIFQEPmt 101
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKS----TLLKVLNRLIEIYDSKIKVDGkVLYFGKDIFQIDAIKLRKeVGMVFQQP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGI-SNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 181 PTTALDVTIQAQILRMIRELQREFgtAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPRHPYT 251
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-245 |
2.37e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.30 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLPTENgmlhAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRKAvgtaDRMTFDGVELLGlpek 82
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKT-TLLNLIaGFVPYQH----GSITLDGKPVEG---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 klnqlRGQRMSMIFQE----PMTSLNPSYTLGNQLCeamlekpGVTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGG 158
Cdd:PRK11248 68 -----PGAERGVVFQNegllPWRNVQDNVAFGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMY--AGQVVET 236
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
250
....*....|.
gi 515278464 237 --ADVGQLFAS 245
Cdd:PRK11248 213 lpLNFARRFVA 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-234 |
3.17e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.46 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLprkaVGTADRmtfdgVELLGL-PEKKLNQLR-------GQRM 92
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLtGIL----VPTSGE-----VRVLGYvPFKRRKEFArrigvvfGQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 93 SMIFQEPmtsLNPSYTLgNQlceAMLEkpgVTRAEARDRAIYLlhrTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCG 172
Cdd:COG4586 106 QLWWDLP---AIDSFRL-LK---AIYR---IPDAEYKKRLDEL---VELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-238 |
8.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 14 LPTEngmLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL---------------PRKAVGTADRMTFDGVelLG 78
Cdd:PRK13651 16 LPTE---LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdtgtiewifkdekNKKKTKEKEKVLEKLV--IQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 LPE----KKLNQLRgQRMSMIFQepmtslNPSYtlgnQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISnaED 146
Cdd:PRK13651 91 KTRfkkiKKIKEIR-RRVGVVFQ------FAEY----QLFEQTIEKDiifgpvsmGVSKEEAKKRAAKYIELVGLD--ES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 147 RLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVA 226
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|..
gi 515278464 227 VMYAGQVVETAD 238
Cdd:PRK13651 237 FFKDGKIIKDGD 248
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
1.30e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRV----DLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrkavGTADRMTFDGVELLGL 79
Cdd:COG1101 2 LELKNLSKtfnpGTVNEK---RALDGLNLTIEEGDFVTVIGSNGAGKS-TLLnAIAGSLP----PDSGSILIDGKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 PEKKlnqlRGQRMSMIFQEPMTSLNPSYTLGNQLCEAMLE------KPGVTRAEaRDRAIYLLHRTGIsNAEDRLRQYPH 153
Cdd:COG1101 74 PEYK----RAKYIGRVFQDPMMGTAPSMTIEENLALAYRRgkrrglRRGLTKKR-RELFRELLATLGL-GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
.
gi 515278464 234 V 234
Cdd:COG1101 228 I 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-234 |
1.34e-20 |
|
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: 88.40 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGeMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKklnqLRgQRMSMIFQEPMT 101
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP----PSSGTIRIDGQDVLKQPQK----LR-RRIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SlnPSYTLGNQLCEAMLEKpGVTRAEARDRAIYLLHRTgisNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:cd03264 84 Y--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELV---NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 182 TTALDVtiqAQILRmIRELQREFGTAVVFI--THDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03264 158 TAGLDP---EERIR-FRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-239 |
1.57e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.15 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQLRgqrMSMIFQE 98
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG---IGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 -----PMTSLNPSYtLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAedrLRQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:PRK09700 89 lsvidELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD---LDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADV 239
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-244 |
1.88e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKAVgtadrMTFDGvELLGLPEKKLNQLRgQRMSMIFQEPMTS 102
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGA-----VLWQG-KPLDYSKRGLLALR-QQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LnpSYTLGNQLCEAMLEKPGVTRAE-AR--DRAIYLLhrtgisNAEdRLRQYPHQ-LSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:PRK13638 90 I--FYTDIDSDIAFSLRNLGVPEAEiTRrvDEALTLV------DAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFA 244
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-213 |
2.81e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPteNGMLhAVRGIDFQVKRGEMLCLVGESGCGKSmtSL--ALMGLLPRkAVGTADRMtfDGVELLGLPek 82
Cdd:COG4178 363 LALEDLTLRTP--DGRP-LLEDLSLSLKPGERLLITGPSGSGKS--TLlrAIAGLWPY-GSGRIARP--AGARVLFLP-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 klnqlrgQRMSMifqepmtslnPSYTLGNQLCeamleKPGVTRAEARDRAIYLLHRTGISNAEDRL---RQYPHQLSGGL 159
Cdd:COG4178 433 -------QRPYL----------PLGTLREALL-----YPATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElqREFGTAVVFITH 213
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-233 |
3.12e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.22 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 28 DFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmTSLNPSY 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPASGS---IKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 108 TLGNQLceAMLEKPGVT-RAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALD 186
Cdd:TIGR01277 86 TVRQNI--GLGLHPGLKlNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515278464 187 VTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-228 |
4.62e-20 |
|
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: 90.81 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLPEKKLnqlrGQRMSMIFQepmts 102
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNGVPLADADADSW----RDQIAWVPQ----- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lNPSYTLGNQLCEAMLEKPGVTRAEARdRAiylLHRTGISNAEDRLRQY--------PHQLSGGLRQRVMIAMALMCGPD 174
Cdd:TIGR02857 404 -HPFLFAGTIAENIRLARPDASDAEIR-EA---LERAGLDEFVAALPQGldtpigegGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 175 LIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVAVM 228
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
5.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkavgtadRMTFDGVELLGLPEKKLNqLRGQR--MSMIF 96
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL---------KPTSGSVLIRGEPITKEN-IREVRkfVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEPmtslnpsytlGNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMA 168
Cdd:PRK13652 85 QNP----------DDQIFSPTVEQDiafgpinlGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-239 |
1.10e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPrkAVGtadRMTFDGVELLGLPEKKLNQLRGqrmsmifqepmtsln 104
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLP--GQG---EILLNGRPLSDWSAAELARHRA--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 105 psYTLGNQLCEAM--------LEKPGVTRAEARDRAI-YLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALM----- 170
Cdd:COG4138 73 --YLSQQQSPPFAmpvfqylaLHQPAGASSEAVEQLLaQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLLqvwpt 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 171 CGPD--LIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV---ETADV 239
Cdd:COG4138 148 INPEgqLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVasgETAEV 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-245 |
1.19e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLpekKLNQLRgQRMSMIFQEPMts 102
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQRVFDPQSGRILIDGTDIRTV---TRASLR-RNIAVVFQDAG-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsytLGNQLCEAMLE--KPGVTRAEARDRAiyllhrtGISNAEDRLRQYPH-----------QLSGGLRQRVMIAMAL 169
Cdd:PRK13657 420 ------LFNRSIEDNIRvgRPDATDEEMRAAA-------ERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 170 MCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVvfITHDLGVVsRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTV-RNADRILVFDNGRVVESGSFDELVAR 559
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-246 |
1.61e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 41 GESGCGKsmTSL--ALMGLL-PRKA-VGTADRMTFDGVELLGLPEKKlnqlrgQRMSMIFQEpmTSLNPSYTLGNQLCEA 116
Cdd:PRK11144 31 GRSGAGK--TSLinAISGLTrPQKGrIVLNGRVLFDAEKGICLPPEK------RRIGYVFQD--ARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 117 MLEKpgvtRAEARDRAIYLLhrtGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRM 196
Cdd:PRK11144 101 MAKS----MVAQFDKIVALL---GI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515278464 197 IRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-239 |
1.67e-19 |
|
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: 84.89 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVdlptENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlPRKAVgTADRMTFDGVELLGLPEkkl 84
Cdd:cd03217 1 LEIKDLHV----SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEV-TEGEILFKGEDITDLPP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 nQLRGQR-MSMIFQEPMtslnpsytlgnqlceamlEKPGVTRAeardraiyllhrtgisnaeDRLRQYPHQLSGGLRQRV 163
Cdd:cd03217 72 -EERARLgIFLAFQYPP------------------EIPGVKNA-------------------DFLRYVNEGFSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 164 MIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRI-ADRVAVMYAGQVVETADV 239
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-233 |
1.82e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 10 LRVDLPTENGMLHavrgIDFQVKRGEMLCLVGESGCGKsmTSLA--LMGLLPRKAvgtaDRMTFDGVE------------ 75
Cdd:PRK15439 269 LTVEDLTGEGFRN----ISLEVRAGEILGLAGVVGAGR--TELAetLYGLRPARG----GRIMLNGKEinalstaqrlar 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 76 -LLGLPEKKlnqlrgQRMSMIFQEPMTSLNPSYTLGNqlceamlekPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQ 154
Cdd:PRK15439 339 gLVYLPEDR------QSSGLYLDAPLAWNVCALTHNR---------RGFWIKPARENAVLERYRRALNIKFNHAEQAART 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-231 |
1.98e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PrkavgTADRMTFDGVELLGLPEK 82
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkP-----TGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLnqlrgQRMSMI--FQ-----EPMTSLN-----PSYTLGNQLCEAMLEKPGVTRAE--ARDRAIYLLHRTGISNAEDRl 148
Cdd:PRK11300 76 QI-----ARMGVVrtFQhvrlfREMTVIEnllvaQHQQLKTGLFSGLLKTPAFRRAEseALDRAATWLERVGLLEHANR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 149 rqYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:PRK11300 150 --QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
...
gi 515278464 229 YAG 231
Cdd:PRK11300 228 NQG 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
23-233 |
2.20e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELLGLPEKKlnqlrgQRMSMIFQE---- 98
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFETPDSG---RIMLDGQDITHVPAEN------RHVNTVFQSyalf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 P-MTSL-NPSYTLGNQlceamlekpGVTRAEARDR---AIYLLHrtgisnAEDRLRQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:PRK09452 99 PhMTVFeNVAFGLRMQ---------KTPAAEITPRvmeALRMVQ------LEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-235 |
2.43e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.90 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGmlHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLglpekKL 84
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVS-----DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLRGQRMSMIFQEPmtslnpsytlgnqlceamlekpgvtraeardraiYLLHRTGISNAEDRLrqyphqlSGGLRQRVM 164
Cdd:cd03247 70 EKALSSLISVLNQRP----------------------------------YLFDTTLRNNLGRRF-------SGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfgTAVVFITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-244 |
2.67e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 88.62 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELlglPEKKLNQLRGQrMSMIFQEPMTS 102
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLRRQ-VALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNpsyTLGNQLceAMLEKPGVTRAEARDRAIyllhrtgISNAEDRLRQYP---HQ--------LSGGLRQRVMIAMALMC 171
Cdd:TIGR02203 419 ND---TIANNI--AYGRTEQADRAEIERALA-------AAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVvfITHDLGVVSRiADRVAVMYAGQVVETADVGQLFA 244
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLV--IAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-235 |
3.10e-19 |
|
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: 84.97 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLpekKLNQLRgQRMSMIFQEpmTSL- 103
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIREV---TLDSLR-RAIGVVPQD--TVLf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPsyTLGNQLCEAmleKPGVTRAEARDRAIyllhrtgISNAEDRLRQYPHQ-----------LSGGLRQRVMIAMALMCG 172
Cdd:cd03253 88 ND--TIGYNIRYG---RPDATDEEVIEAAK-------AAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-233 |
5.12e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKKL 84
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 nqlrGQRMSMIFQEpmTSLNPSYTlGNQLCEaMLEKPGVTR----AEARDRAI-YLLHRTGISNAEDRLRQyphQLSGGL 159
Cdd:PRK09536 76 ----SRRVASVPQD--TSLSFEFD-VRQVVE-MGRTPHRSRfdtwTETDRAAVeRAMERTGVAQFADRPVT---SLSGGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFItHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRV 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-252 |
8.14e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENgmlhAVRGIDFQVKRGEMLCLVGESGCGKS--MTSLALMGLLpRKAVGTADRMTFDGVELLglpEK 82
Cdd:PRK14258 8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNEL-ESEVRVEGRVEFFNQNIY---ER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 K--LNQLRGQrMSMIFQEPM---TSLNPSYTLGNQLC--EAMLEKPGVTRAEARDRAIYllhrtgiSNAEDRLRQYPHQL 155
Cdd:PRK14258 80 RvnLNRLRRQ-VSMVHPKPNlfpMSVYDNVAYGVKIVgwRPKLEIDDIVESALKDADLW-------DEIKHKIHKSALDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYA----- 230
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenri 231
|
250 260
....*....|....*....|..
gi 515278464 231 GQVVETADVGQLFASPRHPYTR 252
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTR 253
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-243 |
9.46e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELLGLPEKK-LNQLRgQRMSMIFQEPMt 101
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH----VPTQGSVRVDDTLITSTSKNKdIKQIR-KKVGLVFQFPE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlgNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:PRK13649 96 ---------SQLFEETVLKDvafgpqnfGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-233 |
9.66e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVrgiDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkavgTADRMTFDGVELLGLPEKKLNQL-RGQRMS-- 93
Cdd:PRK09984 16 QHQALHAV---DLNIHHGEMVALLGPSGSGKSTLLRHLSGLI------TGDKSAGSHIELLGRTVQREGRLaRDIRKSra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 94 ---MIFQEpMTSLNPSYTLGNQLCEAMLEKP-------GVTRAEaRDRAIYLLHRTGISNaedrlrqYPHQ----LSGGL 159
Cdd:PRK09984 87 ntgYIFQQ-FNLVNRLSVLENVLIGALGSTPfwrtcfsWFTREQ-KQRALQALTRVGMVH-------FAHQrvstLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-246 |
1.22e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKAvgtadrmtfdGVELLGLPEKKLNQLRGQR--MSMIFQEP 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKG----------KVLVSGIDTGDFSKLQGIRklVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 MTSLnpsytLGNQLCEAMLEKPG---VTRAEARDRAIYLLHRTGISNAEDRlrqYPHQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:PRK13644 87 ETQF-----VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVsRIADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-239 |
1.30e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmTSLALMG-LLPRKAvGtadRMTFDGVELLGLPEKKLnqlrGQRMSMIFQEPMTS 102
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPDS-G---EVLVDGLDVATTPSREL----AKRLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LN------------PsYTLGnqlceamleKPGVTRAEARDRAIYLLHRTGIsnaEDRlrqYPHQLSGGLRQRVMIAMALM 170
Cdd:COG4604 88 SRltvrelvafgrfP-YSKG---------RLTAEDREIIDEAIAYLDLEDL---ADR---YLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 171 CGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE---TADV 239
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAqgtPEEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-234 |
2.18e-18 |
|
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: 83.21 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPrKAVGtadrmtfDGVELLGlpEKK----LNQLRGQ------RM 92
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKS-TLLSLItGDLP-PTYG-------NDVRLFG--ERRggedVWELRKRiglvspAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 93 SMIFQEPMTSLN-------PSYTLGNQLCEAMlekpgvtraeaRDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMI 165
Cdd:COG1119 88 QLRFPRDETVLDvvlsgffDSIGLYREPTDEQ-----------RERARELLELLGLAHLADRP---FGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 166 AMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-233 |
2.64e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.51 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtSLALM--GLlprKAVgTADRMTFDGvellglpeKKLNQL----RGqrMSMIF 96
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS--TLLRMvaGL---ERI-TSGEIWIGG--------RVVNELepadRD--IAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QE----PMTSL--NPSYTLGNQlceamlekpGVTRAEARDRaiyLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALM 170
Cdd:PRK11650 83 QNyalyPHMSVreNMAYGLKIR---------GMPKAEIEER---VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 171 CGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-245 |
2.96e-18 |
|
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: 82.53 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELlGLPEKklNQLRGQrMSMIFQEPMT- 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKS----TLTKLIQRFYVPENGRVLVDGHDL-ALADP--AWLRRQ-VGVVLQENVLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 --SLNPSYTLGNqlcEAMlekpgvtraeARDRAIYLLHRTGisnAEDRLRQYPH-----------QLSGGLRQRVMIAMA 168
Cdd:cd03252 89 nrSIRDNIALAD---PGM----------SMERVIEAAKLAG---AHDFISELPEgydtivgeqgaGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-300 |
3.30e-18 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 77.44 E-value: 3.30e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 234 VETADVGQLFASPRHPYTRGLLDCIPVRGKtlPGSKLQAIPGVVPSLVGNIGGCVFRNRCSLADATC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP--PKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-215 |
6.64e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 84.33 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtaDRMTFDGVELLGLPEKKLNQlrgqRMSMIFQEPMTS 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpSYTLGNQLceaMLEKPGVTRAEARDraiyLLHRTGIsnaEDRLRQYPH-----------QLSGGLRQRVMIAMALMC 171
Cdd:TIGR02868 422 ---DTTVRENL---RLARPDATDEELWA----ALERVGL---ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIreLQREFGTAVVFITHDL 215
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-245 |
7.32e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKavgTADRMTFDGVELLGLPE-KKLNQLRgQRMSMIFQepmt 101
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISE---TGQTIVGDYAIPANLKKiKEVKRLR-KEIGLVFQ---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slNPSYtlgnQLCEAMLEKP--------GVTRAEARDRAIYLLHRtgISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGP 173
Cdd:PRK13645 98 --FPEY----QLFQETIEKDiafgpvnlGENKQEAYKKVPELLKL--VQLPEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-228 |
8.97e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTADRMTFDGVELLGlpekklnqlrgQRMSMIFQEPMTS 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS-GTVRRAGGARVAYVP-----------QRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNpSYTLGNQLCEAMLEKPgvtRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:NF040873 75 RD-LVAMGRWARRGLWRRL---TRDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515278464 183 TALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRiADRVAVM 228
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-234 |
1.09e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 28 DFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPrkavGTADRMTFDGVELLGLPEkklnqlrGQR-MSMIFQEpmTSLNP 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLT----PASGSLTLNGQDHTTTPP-------SRRpVSMLFQE--NNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMleKPGVT-RAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTA 184
Cdd:PRK10771 85 HLTVAQNIGLGL--NPGLKlNAAQREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515278464 185 LDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-233 |
1.11e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadrmtfdgvELLGlPEKKLNQLRgQRMSMIFQE----PM 100
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPSAG----------ELLA-GTAPLAEAR-EDTRLMFQDarllPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTLGnqlceamlekpgvTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:PRK11247 96 KKVIDNVGLG-------------LKGQWRDAALQALAAVGL---ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515278464 181 PTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-235 |
2.37e-17 |
|
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: 79.38 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRV----DLPTengmlhAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavGTADRMTFDGVELLGLP 80
Cdd:cd03369 7 IEVENLSVryapDLPP------VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE----AEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 ekkLNQLRgQRMSMIFQEPM-------TSLNP--SYTlgnqlceamlekpgvtraearDRAIY--LLHRTGISNaedrlr 149
Cdd:cd03369 77 ---LEDLR-SSLTIIPQDPTlfsgtirSNLDPfdEYS---------------------DEEIYgaLRVSEGGLN------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 150 qyphqLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElqrEF-GTAVVFITHDLGVVSRIaDRVAVM 228
Cdd:cd03369 126 -----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE---EFtNSTILTIAHRLRTIIDY-DKILVM 196
|
....*..
gi 515278464 229 YAGQVVE 235
Cdd:cd03369 197 DAGEVKE 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-243 |
2.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.93 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGTAdrMTFDGVELLGLPEKKLNQLRgQRMSMIFQEPMTS 102
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-QPTEGKV--TVGDIVVSSTSKQKEIKPVR-KKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQLCEAmlEKPGVTRAEARDRAIYLLHRTGISnaEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:PRK13643 97 LFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 183 TALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLF 243
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-244 |
2.79e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNlrVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPE 81
Cdd:PRK11160 336 QVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 82 KklnQLRgQRMSMIFQEPMTSlnpSYTLGNQLceaMLEKPGVTRAEARDraiyLLHRTGISN---AEDRLRQY----PHQ 154
Cdd:PRK11160 410 A---ALR-QAISVVSQRVHLF---SATLRDNL---LLAAPNASDEALIE----VLQQVGLEKlleDDKGLNAWlgegGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRIaDRVAVMYAGQVV 234
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
250
....*....|
gi 515278464 235 ETADVGQLFA 244
Cdd:PRK11160 553 EQGTHQELLA 562
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
2.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.55 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTENgmlHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGL-LPRKAvgtadRMTFDGVELLGL 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRG-----RVKVMGREVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 PEKklnQLRGqRMSMIFQEPmtslnpsytlGNQLCEAMLEKP--------GVTRAEARDRAIYLLHRTGISNAEDRLrqy 151
Cdd:PRK13647 73 NEK---WVRS-KVGLVFQDP----------DDQVFSSTVWDDvafgpvnmGLDKDEVERRVEEALKAVRMWDFRDKP--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 152 PHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAG 231
Cdd:PRK13647 136 PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
....*...
gi 515278464 232 QVVETADV 239
Cdd:PRK13647 215 RVLAEGDK 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-242 |
3.02e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 79.51 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 29 FQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKA--VGTADRMTFDGVELLG-LPekklnqlrgQRMSMIFQEPMtSLNP 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKgtVKVAGASPGKGWRHIGyVP---------QRHEFAWDFPI-SVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMLEKPGVTRAEARDRAiylLHRTGISNAEDRlrqyP-HQLSGGLRQRVMIAMALMCGPDLIIADEPTTA 184
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRPCVADFAAVRDA---LRRVGLTELADR----PvGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 185 LDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVaVMYAGQVVETADVGQL 242
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-239 |
4.44e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.76 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavGTAD-RMTFDGvellglpekKLNQLRGQRMS------MI 95
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH---GSYEgEILFDG---------EVCRFKDIRDSealgivII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 96 FQE----PMTSLNPSYTLGNQLceamlEKPGV-TRAEARDRAIYLLHRTGisnaedrLRQYPHQLSG----GLRQRVMIA 166
Cdd:NF040905 84 HQElaliPYLSIAENIFLGNER-----AKRGViDWNETNRRARELLAKVG-------LDESPDTLVTdigvGKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 167 MALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADV 239
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDC 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-252 |
4.53e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 9 NLRVDLPTEN-----GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLA----LMGLLPR-KAVGtadRMTFDGVELLG 78
Cdd:PRK14243 6 GTETVLRTENlnvyyGSFLAVKNVWLDIPKNQITAFIGPSGCGKS-TILRcfnrLNDLIPGfRVEG---KVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 79 lPEKKLNQLRgQRMSMIFQEPM---TSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYllhrtgiSNAEDRLRQYPHQL 155
Cdd:PRK14243 82 -PDVDPVEVR-RRIGMVFQKPNpfpKSIYDNIAYGARINGYKGDMDELVERSLRQAALW-------DEVKDKLKQSGLSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFgtAVVFITHDLGVVSRIADRVAVMYA----- 230
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVelteg 230
|
250 260
....*....|....*....|....*.
gi 515278464 231 ----GQVVETADVGQLFASPRHPYTR 252
Cdd:PRK14243 231 ggryGYLVEFDRTEKIFNSPQQQATR 256
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-235 |
5.05e-17 |
|
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: 78.69 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPekkLNQLRgQRMSMIFQEPMT- 101
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL----SSGSILIDGVDISKIG---LHDLR-SRISIIPQDPVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 ------SLNP--SYTLGnQLCEAmLEKPGVTRA-EARDRAIYLLHRTGISNaedrlrqyphqLSGGLRQRVMIAMALMCG 172
Cdd:cd03244 91 sgtirsNLDPfgEYSDE-ELWQA-LERVGLKEFvESLPGGLDTVVEEGGEN-----------LSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRElqrEF-GTAVVFITHdlgvvsRI-----ADRVAVMYAGQVVE 235
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAH------RLdtiidSDRILVLDKGRVVE 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-245 |
6.48e-17 |
|
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: 78.42 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLL-PRKAvgtadRMTFDGVELLGLPEKklnQLRgQRMSMIFQEPM 100
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKG-----QILIDGIDIRDISRK---SLR-SMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 ---TSLNPSYTLGNQlcEAMLEKpgVTRAEARDRAIYLlhrtgISNAEDRLRQYP----HQLSGGLRQRVMIAMALMCGP 173
Cdd:cd03254 88 lfsGTIMENIRLGRP--NATDEE--VIEAAKEAGAHDF-----IMKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVsRIADRVAVMYAGQVVETADVGQLFAS 245
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-233 |
1.05e-16 |
|
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: 76.49 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGMLhaVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLpekKL 84
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP----TSGRVRLDGADISQW---DP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 85 NQLrGQRMSMIFQEpmtslnpsytlgnqlceamlekpgvtraeardraIYLLHRTGISNAedrlrqyphqLSGGLRQRVM 164
Cdd:cd03246 72 NEL-GDHVGYLPQD----------------------------------DELFSGSIAENI----------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 165 IAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVsRIADRVAVMYAGQV 233
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-234 |
1.07e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkavgtadRMTFDGVELLGLPEKKlnqlrGQRMSMIFQEPMTS 102
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---------RLASGKISILGQPTRQ-----ALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 -LNPSYTLgnqLCE--AMLEKPG----VTRAEARDRAIYLLHRTGISNAEDRLRQYpHQLSGGLRQRVMIAMALMCGPDL 175
Cdd:PRK15056 88 eVDWSFPV---LVEdvVMMGRYGhmgwLRRAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 176 IIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADrVAVMYAGQVV 234
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVL 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-246 |
1.09e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmtSLALmgLLPRKAVGTADRMTFDGVELLGLPEKKLNqlrgQRMSMIFQEPMT--- 101
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKS--TVAA--LLQNLYQPTGGQVLLDGVPLVQYDHHYLH----RQVALVGQEPVLfsg 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEaMLEKPGVTRAeardraiyllhrtgiSNAEDRLRQYPH-----------QLSGGLRQRVMIAMALM 170
Cdd:TIGR00958 570 SVRENIAYGLTDTP-DEEIMAAAKA---------------ANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 171 CGPDLIIADEPTTALDvtiqAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVETADVGQLFASP 246
Cdd:TIGR00958 634 RKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-242 |
1.91e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTengmLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkaVGTAD-RMTFDGVELlgl 79
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP---HGTYEgEIIFEGEEL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 pekklnQLRGQR------MSMIFQEPMtsLNPSYT------LGNQLCEAmlekpGVTR-AEARDRAIYLLHRTGIS-NAE 145
Cdd:PRK13549 72 ------QASNIRdteragIAIIHQELA--LVKELSvlenifLGNEITPG-----GIMDyDAMYLRAQKLLAQLKLDiNPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 146 DRLRQYphqlSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRV 225
Cdd:PRK13549 139 TPVGNL----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTI 213
|
250
....*....|....*..
gi 515278464 226 AVMYAGQVVETADVGQL 242
Cdd:PRK13549 214 CVIRDGRHIGTRPAAGM 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-239 |
2.49e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMG--LLPrkavgTADRMTFDGvellglpekklnqlrgqRMSMIFqEP 99
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIAgiLEP-----TSGRVEVNG-----------------RVSALL-EL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 MTSLNPSYTlGNQLCE---AMLekpGVTRAEARDRAIYLLHRTGISNAEDR-LRQYphqlSGGLRQRVMIAMALMCGPDL 175
Cdd:COG1134 96 GAGFHPELT-GRENIYlngRLL---GLSRKEIDEKFDEIVEFAELGDFIDQpVKTY----SSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 176 IIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADV 239
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-239 |
2.70e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 29 FQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRKAvgtadRMTFDGVELLGLPEKKLNQLRG---QRMSMIFQEPMTSln 104
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKS-TLLARMaGLLPGSG-----SIQFAGQPLEAWSAAELARHRAylsQQQTPPFAMPVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 105 psYTlgnqlceAMLEKPGVTRAEARDRAIYLLHRTGIsnaEDRLRQYPHQLSGGLRQRVMIAMA-LMCGPD------LII 177
Cdd:PRK03695 89 --YL-------TLHQPDKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 178 ADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV---ETADV 239
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLasgRRDEV 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-241 |
3.02e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSMtslalmglLPRKAVGTADRMTFDgvelLGLPEKKLNQL----RGqrMSM 94
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKST--------LLRMIAGLEDITSGD----LFIGEKRMNDVppaeRG--VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 95 IFQepmtslnpSYTLGNQL--CEAM---LEKPGVTRAEARDRaiyLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMAL 169
Cdd:PRK11000 80 VFQ--------SYALYPHLsvAENMsfgLKLAGAKKEEINQR---VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 170 MCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVvetADVGQ 241
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV---AQVGK 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-258 |
3.69e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.11 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmTSLALMG--LLPRKAvgtadRMTFDGVELLGLPEKKLNQLRgQRMSMIFQEP--MTS 102
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKT-TLLRLIGgqIAPDHG-----EILFDGENIPAMSRSRLYTVR-KRMSMLFQSGalFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 L----NPSYTL--GNQLCEAMLEKPGVTRAEArdraiyllhrTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:PRK11831 99 MnvfdNVAYPLreHTQLPAPLLHSTVMMKLEA----------VGLRGAAKLM---PSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQLFASPrHPYTRGLLD 256
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLD 244
|
..
gi 515278464 257 CI 258
Cdd:PRK11831 245 GI 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-235 |
3.90e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 15 PTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPRKAvGTADRmtfdgvellglpekklnqlRGQRMS 93
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLaGIYPPDS-GTVTV-------------------RGRVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 94 MIfqEPMTSLNPSYTlGNQ----LCEAMlekpGVTRAEARDRAIYLLHRTGISNAEDR-LRQYphqlSGGLRQRVMIAMA 168
Cdd:cd03220 88 LL--GLGGGFNPELT-GREniylNGRLL----GLSRKEIDEKIDEIIEFSELGDFIDLpVKTY----SSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-234 |
4.43e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.09 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLprkaVGTADRMTFDGVELLGLPekkLNQLRgQRMSMIFQEPMT 101
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 ---SLNPSYTLGNQlceamlekpgvtraEARDRAIylLHRTGISNAEDRLRQYPH-----------QLSGGLRQRVMIAM 167
Cdd:cd03245 90 fygTLRDNITLGAP--------------LADDERI--LRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 168 ALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSrIADRVAVMYAGQVV 234
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-238 |
1.10e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGL----------LPRKAV----GTADRMT 70
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHVALcekcGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 71 FDG--------------VELLGLPEKKLNQLRgQRMSMIFQEPMTSLNPSYTLGNQLcEAmLEKPGVTRAEARDRAIYLL 136
Cdd:TIGR03269 77 KVGepcpvcggtlepeeVDFWNLSDKLRRRIR-KRIAIMLQRTFALYGDDTVLDNVL-EA-LEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 137 HRTgisNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLG 216
Cdd:TIGR03269 154 EMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|..
gi 515278464 217 VVSRIADRVAVMYAGQVVETAD 238
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGT 252
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-234 |
1.33e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtaDRMTFD--GVELLGLPEKKLnqlRGqrMSMIFQEPmt 101
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDdeDISLLPLHARAR---RG--IGYLPQEA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515278464 182 TTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-247 |
1.63e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPrkavgtAD--RMTFDGVELLGLPekkLNQlRGQR-MSMIFQEP- 99
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PDsgRIFLDGEDITHLP---MHK-RARLgIGYLPQEAs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 ----MTSLNpsytlgNQLceAMLEKPGVTRAEARDRAIYLLHRTGISnaedRLRQYP-HQLSGGLRQRVMIAMALMCGPD 174
Cdd:COG1137 89 ifrkLTVED------NIL--AVLELRKLSKKEREERLEELLEEFGIT----HLRKSKaYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 175 LIIADEPTTALD-VTIqAQILRMIREL-QREFGtavVFIT-HD----LGVVsriaDRVAVMYAGQVVETADVGQLFASPR 247
Cdd:COG1137 157 FILLDEPFAGVDpIAV-ADIQKIIRHLkERGIG---VLITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-243 |
2.04e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSMTSLALMGLlprkAVGTADRMTFDGvelLGLPEKKLNQLRgQRMSMIFQEPmtslnps 106
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----EKVKSGEIFYNN---QAITDDNFEKLR-KHIGIVFQNP------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 107 ytlGNQLCEAM--------LEKPGVTRAEARDRAIYLLHRTGISNAEDrlrQYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:PRK13648 93 ---DNQFVGSIvkydvafgLENHAVPYDEMHRRVSEALKQVDMLERAD---YEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVETADVGQLF 243
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-238 |
3.73e-15 |
|
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: 76.02 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavGTAD-RMTFDGVELLGlpeK 82
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH---GTWDgEIYWSGSPLKA---S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRGQRMSMIFQE----PMTSLNPSYTLGNQLCE--AMLEKPGVTRaeardRAIYLLHRTGISNAEDRLRQypHQLS 156
Cdd:TIGR02633 71 NIRDTERAGIVIIHQEltlvPELSVAENIFLGNEITLpgGRMAYNAMYL-----RAKNLLRELQLDADNVTRPV--GDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 157 GGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
..
gi 515278464 237 AD 238
Cdd:TIGR02633 223 KD 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-235 |
4.48e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDgvellgLPEKKLnqlrGQRMSMIfqepmt 101
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLLAGALKGTPVAGCVD------VPDNQF----GREASLI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlgnqlcEAmlekpgVTRAEARDRAIYLLHRTGISNAEDRLRQYPHqLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:COG2401 104 -------------DA------IGRKGDFKDAVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 182 TTALDVTiQAQIL-RMIRELQREFGTAVVFITHDLGVVSRIADRVAVM--YAGQVVE 235
Cdd:COG2401 164 CSHLDRQ-TAKRVaRNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-234 |
7.25e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDgVELLGLPEKKLNQLRGQRMSMIFQEpmtSL 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGD-VTLNGEPLAAIDAPRLARLRAVLPQ---AA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLCEAMLEKPGVTRAEA---RDRAIyLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMAL---------MC 171
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGAlthRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-246 |
9.30e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPRKavGTadrMTFDGVELLGLPekkLNQLRgQRMSMIFQEPM---T 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGK--TSLlnALLGFLPYQ--GS---LKINGIELRELD---PESWR-KHLSWVGQNPQlphG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQlceamlekpgvtraEARDRAIY-LLHRTGISNAEDRLRQ---YPHQ-----LSGGLRQRVMIAMALMCG 172
Cdd:PRK11174 438 TLRDNVLLGNP--------------DASDEQLQqALENAWVSEFLPLLPQgldTPIGdqaagLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRIaDRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
151-228 |
1.02e-14 |
|
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: 70.17 E-value: 1.02e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 151 YPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDV-TIQAqilrMIRELQrEFGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-242 |
1.15e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLPTengmLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGT----ADRMTFDGvel 76
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA-GSilylGKEVTFNG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 lglpeKKLNQLRGqrMSMIFQEpmtsLN--PSYT------LGNQLCEAMlekPGVTRAEARDRAIYLLHRTGISNAEDRL 148
Cdd:PRK10762 73 -----PKSSQEAG--IGIIHQE----LNliPQLTiaenifLGREFVNRF---GRIDWKKMYAEADKLLARLNLRFSSDKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 149 RQyphQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVM 228
Cdd:PRK10762 139 VG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
250
....*....|....
gi 515278464 229 YAGQVVETADVGQL 242
Cdd:PRK10762 215 RDGQFIAEREVADL 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-223 |
1.78e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmTslaLMGLLprkavgtADRMTFDGVELLgLPekklnqlRGQRMSMIFQEP----- 99
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKS-T---LLKIL-------AGELEPDSGEVS-IP-------KGLRIGYLPQEPplddd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 100 -------MTSLNPSYTLGNQLcEAMLEKPGVTRA------------------EARDRAIYLLHRTGISnaEDRLRQYPHQ 154
Cdd:COG0488 76 ltvldtvLDGDAELRALEAEL-EELEAKLAEPDEdlerlaelqeefealggwEAEARAEEILSGLGFP--EEDLDRPVSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDvtiqaqiLRMIRELQ---REFGTAVVFITHD---L-GVVSRIAD 223
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEeflKNYPGTVLVVSHDryfLdRVATRILE 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-232 |
2.51e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrmtfdgVELLGLPEKKLNQLRGQRMSMIFQepMTSL 103
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA-GS--------ISLCGEPVPSRARHARQRVGVVPQ--FDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLcEAMLEKPGVTRAEARDRAIYLLHRTGISN-AEDRLRQyphqLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:PRK13537 92 DPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENkADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515278464 183 TALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-234 |
4.12e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLnqlrGQRMSMIFQEPMTSlnps 106
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV----ARRIGLLAQNATTP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 107 ytlGNQLCEAMLEK------PGVTR--AEARDRAIYLLHRTGISnaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIA 178
Cdd:PRK10253 94 ---GDITVQELVARgryphqPLFTRwrKEDEEAVTKAMQATGIT---HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-225 |
7.56e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSVLLDVKNLRVDLptenGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTADRMtfDGVELLGLP 80
Cdd:PRK09544 1 MTSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-GVIKRN--GKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKklnqlrgqrmsmifqepmtsLNPSYTLGNQLCEAMLEKPGVTRAE-----ARDRAIYLLhrtgisnaedrlrQYPHQ- 154
Cdd:PRK09544 74 QK--------------------LYLDTTLPLTVNRFLRLRPGTKKEDilpalKRVQAGHLI-------------DAPMQk 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRV 225
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-235 |
7.70e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmTSL-ALMGLLPrkavgtADRMTFDgvellglpekklnqlRGQRMSMIF--QEpM 100
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKS-TLLkLLAGELE------PDSGTVK---------------LGETVKIGYfdQH-Q 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTLGNQLCEAMlekPGVTRAEARDraiyLLHRTGISNaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:COG0488 388 EELDPDKTVLDELRDGA---PGGTEQEVRG----YLGRFLFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 181 PTTALDV-TIQAqilrmIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:COG0488 459 PTNHLDIeTLEA-----LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-242 |
1.19e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMtfdgveLLGLP- 80
Cdd:TIGR00955 19 SWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL------LNGMPi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKlnQLRgQRMSMIFQEPMtsLNPSYTLGNQLC-EAMLEKP-GVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQ---L 155
Cdd:TIGR00955 93 DAK--EMR-AISAYVQQDDL--FIPTLTVREHLMfQAHLRMPrRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
....*..
gi 515278464 236 TADVGQL 242
Cdd:TIGR00955 248 LGSPDQA 254
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-233 |
1.23e-13 |
|
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: 69.04 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQlrgqRMSMIFQEPMTSl 103
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 npSYTLGNQLCEAMLEKPGVTRAEARDRAiyllhrtgisNAEDRLRQYPH-----------QLSGGLRQRVMIAMALMCG 172
Cdd:cd03248 101 --ARSLQDNIAYGLQSCSFECVKEAAQKA----------HAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELQREfgTAVVFITHDLGVVSRiADRVAVMYAGQV 233
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-238 |
1.81e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDlPTENGMLhavRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlPRKAVgTADRMTFDGVELLGL-PEKk 83
Cdd:COG0396 1 LEIKNLHVS-VEGKEIL---KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEV-TSGSILLDGEDILELsPDE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 lnqlRGQR-MSMIFQEPM------------TSLNpsytlgnqlceAMLEKPgVTRAEARDRAIYLLHRTGISnaEDRLRQ 150
Cdd:COG0396 74 ----RARAgIFLAFQYPVeipgvsvsnflrTALN-----------ARRGEE-LSAREFLKLLKEKMKELGLD--EDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 151 YPHQ-LSGGLRQRVMIAMALMCGPDLIIADEPTTALDV-TIQAqILRMIRELQREfGTAVVFITHdlgvVSRI-----AD 223
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITH----YQRIldyikPD 209
|
250
....*....|....*
gi 515278464 224 RVAVMYAGQVVETAD 238
Cdd:COG0396 210 FVHVLVDGRIVKSGG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-234 |
2.05e-13 |
|
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: 68.45 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVgTADRMTFDGVELlglpEKKLNQlrgQRMSMIFQEpmTSLNP 105
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT-TSGQILFNGQPR----KPDQFQ---KCVAYVRQD--DILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQLCEAMLEKPGVTRAEARDR---AIYLLHRTGISNAEDRLRQYphqLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKkrvEDVLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-234 |
2.28e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.55 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGMLhaVRGIDFQVKRGEMLCLVGESGCGKSmtSLA--LMGLLPRkavgTADRMTFDGVEL------ 76
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKS--TLArlLVGVWPP----TAGSVRLDGADLsqwdre 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 77 -LG-----LPekklnqlrgqrmsmifQEP-------------MTSLNPsytlgnqlceamlEKpgVTRAeARdraiyllh 137
Cdd:COG4618 403 eLGrhigyLP----------------QDVelfdgtiaeniarFGDADP-------------EK--VVAA-AK-------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 138 RTGISNAEDRLRQ-Y-------PHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVV 209
Cdd:COG4618 443 LAGVHEMILRLPDgYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVV 521
|
250 260
....*....|....*....|....*
gi 515278464 210 FITHDLGVVSrIADRVAVMYAGQVV 234
Cdd:COG4618 522 VITHRPSLLA-AVDKLLVLRDGRVQ 545
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-213 |
3.88e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.41 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPrkaVGTADrmtfdgvelLGLPEkklnqlrGQRMSMIFQEPMT 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGK--SSLfrALAGLWP---WGSGR---------IGMPE-------GEDLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnPSYTLGNQLCeamlekpgvtraeardraiyllhrtgisnaedrlrqYP--HQLSGGLRQRVMIAMALMCGPDLIIAD 179
Cdd:cd03223 76 ---PLGTLREQLI------------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 515278464 180 EPTTALDVTIQAQILRMIRELqrefGTAVVFITH 213
Cdd:cd03223 117 EATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-234 |
5.82e-13 |
|
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: 66.42 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 5 LDVKNLRVDLPTENGMLHA--VRGIDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPRKAV-GTadrmtfdgVELLGL 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGK--STLlnALAGRRTGLGVsGE--------VLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 PEKKlNQLRGqRMSMIFQEPMtsLNPSYTLGnqlcEAMLekpgvtraeardraiYLLHrtgisnaedrLRQyphqLSGGL 159
Cdd:cd03213 74 PLDK-RSFRK-IIGYVPQDDI--LHPTLTVR----ETLM---------------FAAK----------LRG----LSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDL-GVVSRIADRVAVMYAGQVV 234
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-235 |
6.63e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtaDRMTFDGVELLglPEKKLNQLRgQRMSMIFQE----- 98
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG----GEIRLNGKDIS--PRSPLDAVK-KGMAYITESrrdng 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 --PMTSLNPSYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLI 176
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 177 IADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-234 |
1.28e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 28 DFQVKRGEMLCLVGESGCGKSmtslALMGLL--------------------------PRKAVGTadrmTFD----GVELL 77
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKS----TLMKILngevllddgriiyeqdlivarlqqdpPRNVEGT----VYDfvaeGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 78 GLPEKKLNQLRGQRMSmifqepmtslNPSYTLGNQLCE--AMLEKPGVTRAEARDRAIylLHRTGIsNAEDRLRQyphqL 155
Cdd:PRK11147 95 AEYLKRYHDISHLVET----------DPSEKNLNELAKlqEQLDHHNLWQLENRINEV--LAQLGL-DPDAALSS----L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDV-TIQaqilrMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIeTIE-----WLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
1.56e-12 |
|
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: 66.62 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 31 VKRGEMLCLVGESGCGKSmTSLALMG--LLPRkaVGTADR--------MTFDGVELlglpEKKLNQLRGQRMSMIFQEPM 100
Cdd:cd03236 23 PREGQVLGLVGPNGIGKS-TALKILAgkLKPN--LGKFDDppdwdeilDEFRGSEL----QNYFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 101 TSLNPSYTLGNqlCEAMLEKpgvtrAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:cd03236 96 VDLIPKAVKGK--VGELLKK-----KDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515278464 181 PTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-231 |
4.12e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrmtfdgVELLGLPEKKLNQLRGQRMSMIFQepMTSL 103
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA-GK--------ITVLGVPVPARARLARARIGVVPQ--FDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGnqlcEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:PRK13536 126 DLEFTVR----ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515278464 184 ALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAG 231
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-233 |
4.24e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.77 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLRVDLPTeNGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGtadRMTFDGVELlglPEK 82
Cdd:TIGR02633 256 VILEARNLTCWDVI-NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEG---NVFINGKPV---DIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KLNQLRGQRMSMIFQE-PMTSLNPSYTLGNQLCEAMLEK---PGVTRAEARDRAIyllhRTGISNAEDRlRQYPH----Q 154
Cdd:TIGR02633 329 NPAQAIRAGIAMVPEDrKRHGIVPILGVGKNITLSVLKSfcfKMRIDAAAELQII----GSAIQRLKVK-TASPFlpigR 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
125-229 |
4.30e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 125 RAEARDRAIYLLHRTGISNAEDR-LRQyphqLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQRE 203
Cdd:COG1245 186 KVDERGKLDELAEKLGLENILDRdISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE 261
|
90 100
....*....|....*....|....*.
gi 515278464 204 fGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:COG1245 262 -GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
155-246 |
6.52e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
90
....*....|..
gi 515278464 235 ETADVGQLFASP 246
Cdd:PRK10575 228 AQGTPAELMRGE 239
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-246 |
6.98e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGvelLGLPEKKLNQLRGqRMSMIFQEPMTS 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHD---IPLTKLQLDSWRS-RLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpSYTLGNQLCeamLEKPGVTRAEARDRAiyllhrtGISNAED---RLRQ-YPHQ-------LSGGLRQRVMIAMALMC 171
Cdd:PRK10789 402 ---SDTVANNIA---LGRPDATQQEIEHVA-------RLASVHDdilRLPQgYDTEvgergvmLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVAVMYAGQVVETADVGQLFASP 246
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-214 |
8.17e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 16 TENGMLHAVRGIDFQV-------------KRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELLGLPEK 82
Cdd:PRK10247 2 QENSPLLQLQNVGYLAgdakilnnisfslRAGEFKLITGPSGCGKS-TLLKIVASLISPTSGT---LLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 klnQLRgQRMSMIFQEPMTSLNPSYTlgnqlceaMLEKPGVTRAEARDRAIYL--LHRTGIsnAEDRLRQYPHQLSGGLR 160
Cdd:PRK10247 78 ---IYR-QQVSYCAQTPTLFGDTVYD--------NLIFPWQIRNQQPDPAIFLddLERFAL--PDTILTKNIAELSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515278464 161 QRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHD 214
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-238 |
9.14e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTadrmtfdgVELLGLPEKKLNQLRGQRMS--MIFQEPMts 102
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS-GT--------LEIGGNPCARLTPAKAHQLGiyLVPQEPL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQLCEAMlekPGVTRAEARDRAiyLLHRTGISNAedrlrqyPHQLSGGL----RQRVMIAMALMCGPDLIIA 178
Cdd:PRK15439 97 LFPNLSVKENILFGL---PKRQASMQKMKQ--LLAALGCQLD-------LDSSAGSLevadRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 179 DEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV---ETAD 238
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIAlsgKTAD 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-238 |
9.68e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGTadrMTFDGVELlglpekklnQLRGQRMSM------IF 96
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPDAGS---ILIDGQEM---------RFASTTAALaagvaiIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 97 QEpmTSLNPSYTLGNQLCEAML-EKPG-VTRAEARDRAIYLLHRTGIS-NAEDRLRQyphqLSGGLRQRVMIAMALMCGP 173
Cdd:PRK11288 86 QE--LHLVPEMTVAENLYLGQLpHKGGiVNRRLLNYEAREQLEHLGVDiDPDTPLKY----LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 174 DLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETAD 238
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFD 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
123-229 |
1.42e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 123 VTRAEARDRAIYLLHRTGISNAEDR-LRQyphqLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQ 201
Cdd:PRK13409 184 LKKVDERGKLDEVVERLGLENILDRdISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
90 100
....*....|....*....|....*...
gi 515278464 202 RefGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:PRK13409 260 E--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-235 |
1.54e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELlglPEKKLNQLRGQrMSMIFQEpMTS 102
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ-VALVSQN-VHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPsyTLGNQLCEAMLEKpgVTRAEArDRAIYLLHrtgisnAEDRLRQYPH-----------QLSGGLRQRVMIAMALMC 171
Cdd:PRK11176 429 FND--TIANNIAYARTEQ--YSREQI-EEAARMAY------AMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVfITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN-RTSLV-IAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
154-233 |
4.29e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
155-227 |
6.46e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 6.46e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAV 227
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-233 |
9.71e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 9.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvGTAdrmtfdgvELLGlpeKKLN----QLRgQR---MSMI 95
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE-GEA--------WLFG---QPVDagdiATR-RRvgyMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 96 FqepmtSLnpsYT----LGNQLCEAMLEkpGVTRAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMC 171
Cdd:NF033858 348 F-----SL---YGeltvRQNLELHARLF--HLPAAEIAARVAEMLERFDLADVADAL---PDSLPLGIRQRLSLAVAVIH 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREFG-TavVFI-THDLGVVSRiADRVAVMYAGQV 233
Cdd:NF033858 415 KPELLILDEPTSGVDPVARDMFWRLLIELSREDGvT--IFIsTHFMNEAER-CDRISLMHAGRV 475
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-235 |
1.03e-10 |
|
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: 62.53 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELlglpeKKLNQ--LRGQrMSMIFQEpmTS 102
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKS----TLARLLFRFYDVTSGRILIDGQDI-----RDVTQasLRAA-IGIVPQD--TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 L-NPsyTLGNQLCEAmleKPGVTRAEARdRAIYLLHrtgIsnaEDRLRQYPHQ-----------LSGGLRQRVMIAMALM 170
Cdd:COG5265 443 LfND--TIAYNIAYG---RPDASEEEVE-AAARAAQ---I---HDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 171 CGPDLIIADEPTTALDVTIQAQILRMIRELQRefGTAVVFITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
155-227 |
1.09e-10 |
|
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: 62.49 E-value: 1.09e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAV 227
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-232 |
1.39e-10 |
|
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: 59.79 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGvellglpekklnqlrgqRMSMIFQEPM---T 101
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK----LSGSVSVPG-----------------SIAYVSQEPWiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 SLNPSYTLGNQLCEAMLEKpgVTRAEARDRAIYLLH---RT-----GISnaedrlrqyphqLSGGLRQRVMIAMALMCGP 173
Cdd:cd03250 81 TIRENILFGKPFDEERYEK--VIKACALEPDLEILPdgdLTeigekGIN------------LSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 174 DLIIADEPTTALDVTIQAQILRM-IRELQREFGTaVVFITHDLGVVSRiADRVAVMYAGQ 232
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-238 |
1.61e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLpTENGMLhavRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgTADRMTFDGVELLGL-PEK 82
Cdd:PRK09580 1 MLSIKDLHVSV-EDKAIL---RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV--TGGTVEFKGKDLLELsPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 83 KlnqlRGQRMSMIFQEPmtslnpsytlgnqlceamLEKPGVTRAEARDRAIYLLHRTGISNAEDR------------LRQ 150
Cdd:PRK09580 75 R----AGEGIFMAFQYP------------------VEIPGVSNQFFLQTALNAVRSYRGQEPLDRfdfqdlmeekiaLLK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 151 YPHQL---------SGGLRQRVMIAMALMCGPDLIIADEPTTALDV---TIQAQILRMIRELQREFgtavVFITHDLGVV 218
Cdd:PRK09580 133 MPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKRSF----IIVTHYQRIL 208
|
250 260
....*....|....*....|.
gi 515278464 219 SRIA-DRVAVMYAGQVVETAD 238
Cdd:PRK09580 209 DYIKpDYVHVLYQGRIVKSGD 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-233 |
1.65e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 61.98 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 11 RVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKKLnqlrGQ 90
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP----TSGSVRLDGADLKQWDRETF----GK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 91 RMSMIFQEpmTSLNPSyTLGNQLCEamlekpgvTRAEARDRAIYLLHRtgISNAEDRLRQYPH-----------QLSGGL 159
Cdd:TIGR01842 393 HIGYLPQD--VELFPG-TVAENIAR--------FGENADPEKIIEAAK--LAGVHELILRLPDgydtvigpggaTLSGGQ 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 160 RQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTaVVFITHDLGVVSrIADRVAVMYAGQV 233
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGIT-VVVITHRPSLLG-CVDKILVLQDGRI 531
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-242 |
2.40e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLP-------RKAVGTADRMTFDGVELLGLPEKKlnqlrGQR 91
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagrrpwRF*TWCANRRALRRTIG*HRPVR*-----GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 92 MSMIFQEPMtslnpsYTLGNQLceamlekpGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMC 171
Cdd:NF000106 99 ESFSGRENL------YMIGR*L--------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 172 GPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-234 |
3.03e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 3 VLLDVKNLrvdlptengMLHAVRG-IDFQVKRGEMLCLVGESGCGKSmtslALMgllprKAVGTADRMTFDGVELlglpe 81
Cdd:PRK11288 256 VRLRLDGL---------KGPGLREpISFSVRAGEIVGLFGLVGAGRS----ELM-----KLLYGATRRTAGQVYL----- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 82 kklnqlRGQRMSmiFQEPMTSLNPsytlGNQLCEAMLEKPG-VTRAEARD-----------RAIYLLH-RTGISNAEDRL 148
Cdd:PRK11288 313 ------DGKPID--IRSPRDAIRA----GIMLCPEDRKAEGiIPVHSVADninisarrhhlRAGCLINnRWEAENADRFI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 149 RQY------PHQ----LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQrEFGTAVVFITHDLGVV 218
Cdd:PRK11288 381 RSLniktpsREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEV 459
|
250
....*....|....*.
gi 515278464 219 SRIADRVAVMYAGQVV 234
Cdd:PRK11288 460 LGVADRIVVMREGRIA 475
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-234 |
5.47e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 19 GMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLPEKKLNQL------RGQRm 92
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpEGRR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 93 smIFQEpMTsLNPSYTLGNQLCEAmlekpgvTRAEARDRAIYLLhrtgISNAEDRLRQYPHQLSGGLRQRVMIAMALMCG 172
Cdd:PRK11614 91 --VFSR-MT-VEENLAMGGFFAER-------DQFQERIKWVYEL----FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-218 |
5.68e-10 |
|
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: 58.14 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 12 VDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPRKAvGTADrmtfdgvellgLPEKKLNQLRG 89
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGK--TTLlrILAGLLRPDS-GEVR-----------WNGTPLAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 90 QRMSMIfqepmtslnpsYTLGNQlcEAMleKPGVTRAE----------ARDRAIY-LLHRTGISNAEDRLrqyPHQLSGG 158
Cdd:TIGR01189 70 EPHENI-----------LYLGHL--PGL--KPELSALEnlhfwaaihgGAQRTIEdALAAVGLTGFEDLP---AAQLSAG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 159 LRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRE-LQRefGTAVVFITH-DLGVV 218
Cdd:TIGR01189 132 QQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-244 |
6.62e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLrvdlpTENGmlhaVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGL-P 80
Cdd:PRK10762 255 EVRLKVDNL-----SGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPR----TSGYVTLDGHEVVTRsP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKKLN----------QLRGQRMSMIFQEPM--TSLNPSYTLGNQLCEAMlEKPGVT--------RAEARDRAIYLLhrtg 140
Cdd:PRK10762 322 QDGLAngivyisedrKRDGLVLGMSVKENMslTALRYFSRAGGSLKHAD-EQQAVSdfirlfniKTPSMEQAIGLL---- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 141 isnaedrlrqyphqlSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSR 220
Cdd:PRK10762 397 ---------------SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLG 460
|
250 260
....*....|....*....|....*....
gi 515278464 221 IADRVAVMYAGQV-----VETADVGQLFA 244
Cdd:PRK10762 461 MSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
27-245 |
1.20e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.35 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 27 IDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELLGLPEKKLNqlrgQRMSMIFQEPMT---SL 103
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----TEGEIRLDGRPLSSLSHSVLR----QGVAMVQQDPVVladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGNQLCEA----MLEKpgVTRAEardraiylLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIAD 179
Cdd:PRK10790 432 LANVTLGRDISEEqvwqALET--VQLAE--------LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 180 EPTTALDV-TIQA--QILRMIRElqrefGTAVVFITHDLGVVSRiADRVAVMYAGQVVETADVGQLFAS 245
Cdd:PRK10790 502 EATANIDSgTEQAiqQALAAVRE-----HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
155-234 |
1.60e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-244 |
2.04e-09 |
|
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: 59.19 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 11 RVDLPTENGmlhavrgIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGvELLGLPEKKLNQLRGQ 90
Cdd:TIGR00957 648 RDLPPTLNG-------ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK----VEGHVHMKG-SVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 91 RMSMIFQEPmtsLNPSYTLGNQLCEAMLEK----PGVTRAEARDRAIyllhrtgisnaedrlrqyphQLSGGLRQRVMIA 166
Cdd:TIGR00957 716 RENILFGKA---LNEKYYQQVLEACALLPDleilPSGDRTEIGEKGV--------------------NLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 167 MALMCGPDLIIADEPTTALDVTIQAQIL-RMIRELQREFGTAVVFITHDLGVVSRIaDRVAVMYAGQVVETADVGQLFA 244
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-229 |
5.17e-09 |
|
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: 54.89 E-value: 5.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMY 229
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-225 |
7.98e-09 |
|
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: 54.81 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 12 VDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadrmtfdgvELLgLPEKKLNQLRGqr 91
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKT-TLLRILAGLSPPLAG----------RVL-LNGGPLDFQRD-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 92 msmIFQEPMTSLNPSYTLGNQLceAMLEKPGVTRAEARDRAIY-LLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALM 170
Cdd:cd03231 70 ---SIARGLLYLGHAPGIKTTL--SVLENLRFWHADHSDEQVEeALARVGLNGFEDRP---VAQLSAGQQRRVALARLLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515278464 171 CGPDLIIADEPTTALDVTIQAQIL-RMIRELQRefGTAVVFITH-DLGVVSRIADRV 225
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAeAMAGHCAR--GGMVVLTTHqDLGLSEAGAREL 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
155-241 |
9.02e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQV- 233
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
90
....*....|
gi 515278464 234 --VETADVGQ 241
Cdd:PRK10982 471 giVDTKTTTQ 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-234 |
1.03e-08 |
|
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: 54.58 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKaVGTADRMTFDGVELLGLPEKKLNQLrgqrmsmIFQEPMTSL 103
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEFAEKYPGEI-------IYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 NPSYTLGnQLCEAMLEKPGvtraeardraiyllhrtgisnaedrlRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTT 183
Cdd:cd03233 95 FPTLTVR-ETLDFALRCKG--------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 184 ALDVTIQAQILRMIRELQREFGTAVVFITHDLGV-VSRIADRVAVMYAGQVV 234
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-225 |
1.05e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 34 GEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGV--------ELLGLPEKKLNQ-LRGQRMSMIFQEPMTSLN 104
Cdd:PRK10636 27 GQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPGNwqlawvnqETPALPQPALEYvIDGDREYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 105 PSYTlGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNaeDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTA 184
Cdd:PRK10636 103 ERND-GHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSN--EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515278464 185 LDVTiqaQILRMIRELQREFGTaVVFITHDLGVVSRIADRV 225
Cdd:PRK10636 180 LDLD---AVIWLEKWLKSYQGT-LILISHDRDFLDPIVDKI 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-231 |
2.14e-08 |
|
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: 53.87 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 21 LHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGllprkAVGTADRMTFDGVELLGLPEKKLNQLRgQRMSMIF--QE 98
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG-----EMQTLEGKVHWSNKNESEPSFEATRSR-NRYSVAYaaQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 99 PM---TSLNPSYTLGNQLCEAMLEkpGVTRAEARDRAIYLLHRTGISNAEDRlrqyPHQLSGGLRQRVMIAMALMCGPDL 175
Cdd:cd03290 88 PWllnATVEENITFGSPFNKQRYK--AVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 176 IIADEPTTALDV-----TIQAQILRMIRELQRefgtAVVFITHDLGVVSRiADRVAVMYAG 231
Cdd:cd03290 162 VFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-236 |
4.79e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 28 DFQVKRGEMLCLVGESGCGKSMTSLALMGllprkavgtadrmtfdgvellglpekKLNQLRGQRMSMiFQEPmTSLnpSY 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG--------------------------ELPLLSGERQSQ-FSHI-TRL--SF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 108 TLGNQLCEA--------ML----EKPGVTRAE-------ARDRAIYLLHRTGISNAEDRLRQYphqLSGGLRQRVMIAMA 168
Cdd:PRK10938 73 EQLQKLVSDewqrnntdMLspgeDDTGRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 169 LMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAGQVVET 236
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAET 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
154-222 |
5.31e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 5.31e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVtiqaQILRMIRELQREFGTAVVFITHDLGVVSRIA 222
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDRWFLDRIA 507
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-265 |
6.08e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 11 RVDLPTengMLHavrGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLpekKLNQLRgQ 90
Cdd:PLN03232 1245 RPGLPP---VLH---GLSFFVSPSEKVGVVGRTGAGKS----SMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLR-R 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 91 RMSMIFQEPMTSlnpsytlgnqlceamlekPGVTR------AEARDRAIY-LLHRTGISNAEDR--------LRQYPHQL 155
Cdd:PLN03232 1311 VLSIIPQSPVLF------------------SGTVRfnidpfSEHNDADLWeALERAHIKDVIDRnpfgldaeVSEGGENF 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElqrEFGT-AVVFITHDLGVVSRiADRVAVMYAGQVV 234
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE---EFKScTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
250 260 270
....*....|....*....|....*....|.
gi 515278464 235 ETADVGQLFASPRHPYTRGLLDCIPVRGKTL 265
Cdd:PLN03232 1449 EYDSPQELLSRDTSAFFRMVHSTGPANAQYL 1479
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-248 |
6.44e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 31 VKRGEMLCLVGESGCGKSMTSLALMGLLPRKAVGTADRMTFDGVEllglPEKKLNQLRGQrmsMIFQEPMTSLNPSYTLG 110
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGIT----PEEIKKHYRGD---VVYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 111 NQLCEAMLEKPGVTRAEARDRAIYLLHRT-------GISN------AEDRLRQyphqLSGGLRQRVMIAMALMCGPDLII 177
Cdd:TIGR00956 157 ETLDFAARCKTPQNRPDGVSREEYAKHIAdvymatyGLSHtrntkvGNDFVRG----VSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 178 ADEPTTALDVTIQAQILRMIRELQREF-GTAVVFI------THDLgvvsriADRVAVMYAGQvvetadvgQLFASPRH 248
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILdTTPLVAIyqcsqdAYEL------FDKVIVLYEGY--------QIYFGPAD 296
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-224 |
7.40e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 33 RGEMLCLVGESGCGKSMTSLALMGLLPRKAVgtadrmtfdGVELLGLPEkklnqlrgqrmsmifqepmtslnpsytlgnq 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG---------GVIYIDGED------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 113 lceamlekpgvtraeardraiyLLHRTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQ 192
Cdd:smart00382 41 ----------------------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*..
gi 515278464 193 ILRMIR-----ELQREFGTAVVFITHDLGVVSRIADR 224
Cdd:smart00382 99 LLLLEElrlllLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-213 |
1.34e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 12 VDLPTENGMLhAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLP-RKAVGTADRmtfDGvELLGLPEKKLNQLRGQ 90
Cdd:TIGR00954 457 IPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTKPA---KG-KLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 91 RMSMIFqePMTSLN-PSYTLGNQLCEAMLEKPGVTraeardraiYLLHRTGisnAEDRLRQYPHQLSGGLRQRvmIAMAL 169
Cdd:TIGR00954 532 RDQIIY--PDSSEDmKRRGLSDKDLEQILDNVQLT---------HILEREG---GWSAVQDWMDVLSGGEKQR--IAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515278464 170 MC--GPDLIIADEPTTALDVTIQAQILRmireLQREFGTAVVFITH 213
Cdd:TIGR00954 596 LFyhKPQFAILDECTSAVSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-225 |
1.48e-07 |
|
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: 50.78 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 22 HAVRGIDFQVKRGEMLCLVGESGCGKSmtSLALMGLlprKAVGTADRmtfdgVELLGLPEKKLNQLRGQRMSMIfqepmt 101
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKS--TLVNEGL---YASGKARL-----ISFLPKFSRNKLIFIDQLQFLI------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 102 slnpsytlgnqlceamleKPGVTraeardraiYLlhrtgisnaedRLRQYPHQLSGGLRQRVMIA--MALMCGPDLIIAD 179
Cdd:cd03238 73 ------------------DVGLG---------YL-----------TLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILD 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515278464 180 EPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRiADRV 225
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-233 |
2.02e-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: 52.71 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRkavgTADRMTFDGVELlglpEKKLNQLRgQRMSMIFQEPMts 102
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNI-- 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 LNPSYTLGNQ-LCEAMLEkpGVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADEP 181
Cdd:TIGR01257 1014 LFHHLTVAEHiLFYAQLK--GRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 182 TTALDVTIQAQILRMIreLQREFGTAVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-232 |
2.87e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 26 GIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLPRKAvgtadrmtFDGVELLGlpEKKLNQLRGQRMSMIFQEPMtsLNP 105
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN--------FTGTILAN--NRKPTKQILKRTGFVTQDDI--LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 106 SYTLGNQL--CeAMLEKP-GVTRAEARDRAIYLLHRTGISNAEDRL--RQYPHQLSGGLRQRVMIAMALMCGPDLIIADE 180
Cdd:PLN03211 154 HLTVRETLvfC-SLLRLPkSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515278464 181 PTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRIADRVAVMYAGQ 232
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-231 |
2.96e-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: 52.32 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 31 VKRGEMLCLVGESGCGKSMTSLALMGllpRKAVGTADrMTFDGVELLglpekklNQLRGQRMSMIFQEPMTSLNPSYTlG 110
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGD-ATVAGKSIL-------TNISDVHQNMGYCPQFDAIDDLLT-G 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 111 NQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQ 190
Cdd:TIGR01257 2030 REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515278464 191 AQILRMIRELQREfGTAVVFITHDLGVVSRIADRVAVMYAG 231
Cdd:TIGR01257 2107 RMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
149-227 |
3.81e-07 |
|
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: 50.48 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 149 RQYPhQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIREL-QREFGTAVVfITHDLGVVSRIADRVAV 227
Cdd:cd03237 111 REVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFV-VEHDIIMIDYLADRLIV 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
68-227 |
6.80e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 68 RMTFDGVELLGLPEKKLNQLrgqrMSMIFQEPM---TSLNPSYTLGNQlcEAMLEKpgVTRA---EARDRAIYLLHRTGI 141
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNL----FSIVSQEPMlfnMSIYENIKFGKE--DATRED--VKRAckfAAIDEFIESLPNKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 142 SNaedrLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRi 221
Cdd:PTZ00265 1350 TN----VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1424
|
....*.
gi 515278464 222 ADRVAV 227
Cdd:PTZ00265 1425 SDKIVV 1430
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-229 |
7.01e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.51 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 153 HQLSGGLRQRVMIAMAL---MCGPD-LIIADEPTTALDVTIQAQILRMIRElQREFGTAVVFITHDLGVVSRiADRVAVM 228
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAEL-ADKLIHI 153
|
.
gi 515278464 229 Y 229
Cdd:cd03227 154 K 154
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-219 |
7.73e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKsmTSL--ALMGLLPRKAvGTadrmtfdgVELLGLPekkLNQLRGQRMSMIFqepmts 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGK--TSLlrILAGLARPDA-GE--------VLWQGEP---IRRQRDEYHQDLL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsYtLGNQlceamlekPGV----TRAE------------ARDRAIYLLHRTGISNAEDRLrqyPHQLSGGLRQRVMIA 166
Cdd:PRK13538 78 ----Y-LGHQ--------PGIktelTALEnlrfyqrlhgpgDDEALWEALAQVGLAGFEDVP---VRQLSAGQQRRVALA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 167 MALMCGPDLIIADEPTTALDVTIQAQILRMIRE-LQRefGTAVVFITH-DLGVVS 219
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVAS 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-235 |
1.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 11 RVDLPTengMLHavrGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLPRKAVGTADRMTFDGVELLGLpekKLNQLRgQ 90
Cdd:PLN03130 1248 RPELPP---VLH---GLSFEISPSEKVGIVGRTGAGKS----SMLNALFRIVELERGRILIDGCDISKF---GLMDLR-K 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 91 RMSMIFQEPMT-------SLNPSytlgNQLCEAMLekpgvtrAEARDRAiyllhrtgisNAEDRLRQYPHQL-------- 155
Cdd:PLN03130 1314 VLGIIPQAPVLfsgtvrfNLDPF----NEHNDADL-------WESLERA----------HLKDVIRRNSLGLdaevseag 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 ---SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElqrEFGT-AVVFITHDLGVVsrI-ADRVAVMYA 230
Cdd:PLN03130 1373 enfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE---EFKScTMLIIAHRLNTI--IdCDRILVLDA 1447
|
....*
gi 515278464 231 GQVVE 235
Cdd:PLN03130 1448 GRVVE 1452
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
154-222 |
2.09e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 2.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVtiqaQILRMIRELQREF-GTAVVfITHDLGVVSRIA 222
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEALLEFpGCAVV-ISHDRWFLDRIA 509
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-214 |
2.24e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 6 DVKNLRVDLPTENgmlhAVRGIDFQVKRGEMLCLVGESGCGKSmTSLALM--GLLP---RKAVGTA-DRMTFDgvellgl 79
Cdd:PRK11147 321 EMENVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKT-TLLKLMlgQLQAdsgRIHCGTKlEVAYFD------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 80 pekklnQLRgqrmsmifqepmTSLNPSYTLGNQLCEAmleKPGVTrAEARDRAI------YLLHrtgisnaEDRLRQYPH 153
Cdd:PRK11147 389 ------QHR------------AELDPEKTVMDNLAEG---KQEVM-VNGRPRHVlgylqdFLFH-------PKRAMTPVK 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVtiqaQILRMIRELQREFGTAVVFITHD 214
Cdd:PRK11147 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-242 |
3.31e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 16 TENGMLH-AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGL-LPRKavGTADrmTFDGVELLGLPEKKLNQLRGqrms 93
Cdd:PRK13545 31 SKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNK--GTVD--IKGSAALIAISSGLNGQLTG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 94 mifqepmtslnpsytLGN-QLCEAMLekpGVTRAEARDRAIYLLHRTGISNAedrLRQYPHQLSGGLRQRVMIAMALMCG 172
Cdd:PRK13545 103 ---------------IENiELKGLMM---GLTKEKIKEIIPEIIEFADIGKF---IYQPVKTYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVETADVGQL 242
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-246 |
5.32e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVsRIADRVAVMYAGQV 233
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRER 657
|
90
....*....|...
gi 515278464 234 VETADVGQLFASP 246
Cdd:PTZ00265 658 GSTVDVDIIGEDP 670
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-213 |
5.81e-06 |
|
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: 46.08 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 8 KNLRVDLPTENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLP-RKAVGTAD-RMTFDGVELlglpEKKLN 85
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAgRKTAGVITgEILINGRPL----DKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 86 QLRGqrmsmiFQEPMTSLNPSYTLGnqlcEAMlekpgvtRAEARDRaiyllhrtGISnaedrLRQyphqlsgglRQRVMI 165
Cdd:cd03232 79 RSTG------YVEQQDVHSPNLTVR----EAL-------RFSALLR--------GLS-----VEQ---------RKRLTI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515278464 166 AMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITH 213
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-217 |
5.90e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.41 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 25 RGIDFQVKRGEMLCLVGESGCGKSmTSLALM-GLLPrkavGTADRMTFDGVEllglpekklnqlrgqrmsMIFQEPMTSl 103
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKT-TLLRLIaGLLP----PAAGTIKLDGGD------------------IDDPDVAEA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 npSYTLGNQlcEAMleKPGVTRAE----------ARDRAIY-LLHRTGISNAEDRLRQYphqLSGGLRQRVMIAMALMCG 172
Cdd:PRK13539 75 --CHYLGHR--NAM--KPALTVAEnlefwaaflgGEELDIAaALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515278464 173 PDLIIADEPTTALDVTIQAQILRMIRElQREFGTAVVFITH-DLGV 217
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-239 |
6.72e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 2 SVLLDVKNLRVDLpTENGMLHavrGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLlPRKAVGTADrMTFDGVELLGL-P 80
Cdd:CHL00131 5 KPILEIKNLHASV-NENEILK---GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYKILEGD-ILFKGESILDLeP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 81 EKklnqlRGQR-MSMIFQEPmtslnpsytlgnqlceamLEKPGVTRAEARdRAIYLLHR--------------TGISNAE 145
Cdd:CHL00131 79 EE-----RAHLgIFLAFQYP------------------IEIPGVSNADFL-RLAYNSKRkfqglpeldpleflEIINEKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 146 DRLRQYPHQL--------SGGLRQRVMI-AMALMcGPDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLG 216
Cdd:CHL00131 135 KLVGMDPSFLsrnvnegfSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQR 212
|
250 260
....*....|....*....|....
gi 515278464 217 VVSRIA-DRVAVMYAGQVVETADV 239
Cdd:CHL00131 213 LLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
155-214 |
1.42e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.47 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDvtiqAQILRMIRELQREFGTAVVFITHD 214
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-235 |
1.87e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 23 AVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGtadRMTFDGVELlglPEKKLNQLRgQRMSMIFQEpmts 102
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-QPQSG---EILLDGKPV---TAEQPEDYR-KLFSAVFTD---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 103 lnpsYTLGNQLCEAMLEKPGVTRAEARDRAIYLLHRTGISNaeDRLRQYphQLSGGLRQRVMIAMALMCGPDLIIADEPT 182
Cdd:PRK10522 406 ----FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELED--GRISNL--KLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515278464 183 TALDVTIQAQILRMIRELQREFGTAVVFITHDLGVVSRiADRVAVMYAGQVVE 235
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-223 |
1.92e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 155 LSGGLRQRVMIAMALM---CGPDLIIADEPTTALDVtiqAQILRMIRELQR--EFGTAVVFITHDLGVVsRIAD 223
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHF---HDVKKLLEVLQRlvDKGNTVVVIEHNLDVI-KCAD 239
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-214 |
1.96e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 1.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515278464 154 QLSGG------LRQRVMIAMALMCGPDLIIADEPTTALDV-TIQAQILRMIRELQREFGTAVVFITHD 214
Cdd:cd03240 115 RCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-187 |
2.09e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 2.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515278464 126 AEARDRAIYllhrTGISNAEDRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDV 187
Cdd:PLN03073 320 AEARAASIL----AGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
122-186 |
2.44e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 2.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515278464 122 GVTRAEARDRAIYLLHRTGISNAEDRLRQyphQLSGGLRQRVMIAMALMCGPDLIIADEPTTALD 186
Cdd:NF033858 107 GQDAAERRRRIDELLRATGLAPFADRPAG---KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-245 |
3.82e-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: 45.71 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 24 VRGIDFQVKRGEMLCLVGESGCGKSMTSLALMGLLpRKAVGtadRMTFDGVELLGLpekKLNQLRGQrMSMIFQEPMtsl 103
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-ESAEG---EIIIDGLNIAKI---GLHDLRFK-ITIIPQDPV--- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 104 npsytLGNQLCEAMLEKPGVTRAEARDRAIYLLH-RTGISNAEDRLRqypHQ-------LSGGLRQRVMIAMALMCGPDL 175
Cdd:TIGR00957 1371 -----LFSGSLRMNLDPFSQYSDEEVWWALELAHlKTFVSALPDKLD---HEcaeggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 176 IIADEPTTALDVTIQAQILRMIRElqrEFGTAVVF-ITHDLGVVSRIAdRVAVMYAGQVVETADVGQLFAS 245
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRT---QFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-223 |
5.70e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 147 RLRQYPHQLSGGLRQRVMIAMALM---CGPDLIIADEPTTAL---DVtiqAQILRMIRELqREFGTAVVFITHDLGVVsR 220
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDI---KKLLEVLQRL-VDKGNTVVVIEHNLDVI-K 896
|
...
gi 515278464 221 IAD 223
Cdd:TIGR00630 897 TAD 899
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-245 |
7.72e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILR--MIRELQrefGTAVVFITHDLGVVSRIaDRVAVMYAGQ 232
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGM 816
|
90
....*....|...
gi 515278464 233 VVETADVGQLFAS 245
Cdd:PLN03232 817 IKEEGTFAELSKS 829
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
155-242 |
9.45e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVV 234
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
....*...
gi 515278464 235 ETADVGQL 242
Cdd:PRK10982 214 ATQPLAGL 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-241 |
1.06e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 1 MSvlLDVKNLRVDLPTE-------NGMLHAVRGIDFQVKRGEMLCLVGESGCGKSmtslALMGLLP-RKAVGTADrmtfD 72
Cdd:PLN03140 868 MS--FDDVNYFVDMPAEmkeqgvtEDRLQLLREVTGAFRPGVLTALMGVSGAGKT----TLMDVLAgRKTGGYIE----G 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 73 GVELLGLPEKklnQLRGQRMSMiFQEPMTSLNPSYTLGNQLC-EAMLEKPG-VTRAEARDRAIYLLHRTGISNAEDRLRQ 150
Cdd:PLN03140 938 DIRISGFPKK---QETFARISG-YCEQNDIHSPQVTVRESLIySAFLRLPKeVSKEEKMMFVDEVMELVELDNLKDAIVG 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 151 YP--HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElQREFGTAVVFITHDLGV-VSRIADRVAV 227
Cdd:PLN03140 1014 LPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLL 1092
|
250
....*....|....*
gi 515278464 228 M-YAGQVVETADVGQ 241
Cdd:PLN03140 1093 MkRGGQVIYSGPLGR 1107
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
155-235 |
1.08e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQIL-RMIR-ELQrefGTAVVFITHDLGVVSRIaDRVAVMYAGQ 232
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKdELR---GKTRVLVTNQLHFLSQV-DRIILVHEGM 816
|
...
gi 515278464 233 VVE 235
Cdd:PLN03130 817 IKE 819
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
155-214 |
2.23e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 2.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDvtiqAQ-ILRMIRELQREFGTaVVFITHD 214
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPGT-VVAVTHD 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-251 |
2.59e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.82 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 17 ENGMLHAVRGIDFQVKRGEMLCLVGESGCGKSMTSLALMgllprKAVGTAD-RMTFDGVELLGLPekkLNQLRgQRMSMI 95
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFF-----RMVDIFDgKIVIDGIDISKLP---LHTLR-SRLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 96 FQEPMT-------SLNPSYTLGNQLCEAMLEkpgvtraeardraiyllhrtgISNAEDRLRQYPHQL-----------SG 157
Cdd:cd03288 101 LQDPILfsgsirfNLDPECKCTDDRLWEALE---------------------IAQLKNMVKSLPGGLdavvteggenfSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 158 GLRQRVMIAMALMCGPDLIIADEPTTALDVTIQaqilrmiRELQREFGTA-----VVFITHdlgVVSRI--ADRVAVMYA 230
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATE-------NILQKVVMTAfadrtVVTIAH---RVSTIldADLVLVLSR 229
|
250 260
....*....|....*....|.
gi 515278464 231 GQVVETADVGQLFASPRHPYT 251
Cdd:cd03288 230 GILVECDTPENLLAQEDGVFA 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-213 |
8.25e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 4 LLDVKNLRVDLptENGMLhaVRGIDFQVKRGEMLCLVGESGCGKSmTSLALMGLLPRKAVGtadRMTFDGVELlglpEKK 83
Cdd:PRK13540 1 MLDVIELDFDY--HDQPL--LQQISFHLPAGGLLHLKGSNGAGKT-TLLKLIAGLLNPEKG---EILFERQSI----KKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 84 LNQLRGQrmsMIFQEPMTSLNPSYTLgnqlceamlekpgvtraeaRDRAIYLLHRTGISNAEDRLRQ---------YP-H 153
Cdd:PRK13540 69 LCTYQKQ---LCFVGHRSGINPYLTL-------------------RENCLYDIHFSPGAVGITELCRlfslehlidYPcG 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 154 QLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRElQREFGTAVVFITH 213
Cdd:PRK13540 127 LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
155-246 |
8.44e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAqilRMIRE--LQREFGTAVVFITHDLGVVSRiADRVAVMYAGQ 232
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE---RVVEEcfLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
90
....*....|....
gi 515278464 233 VVETADVGQLFASP 246
Cdd:PTZ00243 859 VEFSGSSADFMRTS 872
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-225 |
1.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515278464 155 LSGGLRQRVMIAMALMCG---PDLIIADEPTTALDVTIQAQILRMIRELQREfGTAVVFITHDLGVVsRIADRV 225
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV-KVADYV 881
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
136-213 |
1.18e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515278464 136 LHRTGISNaedRLRQYP-HQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELQREFGTAVVFITH 213
Cdd:PRK10938 385 LDILGIDK---RTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
146-233 |
2.73e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 146 DRLRQYPHQLSGGLRQRVMIAMALMCGPDLIIADEPTTALDVTI-QAQILRMIrelqrEFGTAVVFITHDLGVVSRIADR 224
Cdd:PRK10636 422 DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDRHLLRSTTDD 496
|
....*....
gi 515278464 225 VAVMYAGQV 233
Cdd:PRK10636 497 LYLVHDGKV 505
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
156-239 |
3.17e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 156 SGGLRQRVMIAMALMCGPDLIIADEPTTALDVTIQAQILRMIRELqREFGTAVVFITHDLGVVSRIADRVAVMYAGQVVE 235
Cdd:PRK13546 145 SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
....
gi 515278464 236 TADV 239
Cdd:PRK13546 224 YGEL 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
155-234 |
5.50e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515278464 155 LSGGLRQRVMIAMALMCGPDLIIADEPTTALDV-TIQAqiLRMIRELQRefGTaVVFITHDLGVVSRIADRVAVMYAGQV 233
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMALEKYE--GT-LIFVSHDREFVSSLATRIIEITPDGV 513
|
.
gi 515278464 234 V 234
Cdd:PRK15064 514 V 514
|
|
| |
