|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-308 |
9.98e-175 |
|
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: 487.25 E-value: 9.98e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkITADRMQFDGQDLRGISARQ 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALF 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 243 RDPHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVECDRGVvrqgPEL 308
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEE----PPL 301
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-322 |
1.76e-155 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 438.79 E-value: 1.76e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISA 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 241 LFRDPHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVECDrgvvRQGPELGLAL-----CNY 315
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCR----AEEPALNMLAgrqskCHY 316
|
....*...
gi 522061013 316 PLKD-GKP 322
Cdd:PRK11022 317 PLDDaGRP 324
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-263 |
7.56e-149 |
|
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: 429.49 E-value: 7.56e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISA 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260
....*....|....*....|...
gi 522061013 241 LFRDPHHPYTAALLAALPERAKV 263
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-297 |
5.21e-120 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 348.82 E-value: 5.21e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISA 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGE-----TLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMS 155
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEaipswTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 236 QPVRALFRDPHHPYTAALLAALPE-----RAKvgQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVEC 297
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDfrqplPHK--SRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC 305
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-235 |
4.10e-110 |
|
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: 319.84 E-value: 4.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARq 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRsIELLNLVGIPAPEDRLSNFPHQMSGGMSQRV 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE-AVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-298 |
7.36e-109 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 320.52 E-value: 7.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADrMQFDGQDLRGISA 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGS-ATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 241 LFRDPHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVECD 298
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICS 306
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-297 |
1.40e-104 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 309.74 E-value: 1.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLF-------RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQD 74
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE----PTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISARQRRRiVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQM 154
Cdd:COG4608 82 ITGLSGRELRP-LRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRP--EHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 235 EQPVRALFRDPHHPYTAALLAA--LPERAKVGQRLPsIAGVVPGQHGRPTGCLFAPRCGFATVEC 297
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAvpVPDPERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRC 302
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-259 |
4.41e-102 |
|
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: 309.53 E-value: 4.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSS-GLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISA 80
Cdd:COG1123 259 PLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIvGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQMSGGMSQ 160
Cdd:COG1123 335 RSLREL-RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*....
gi 522061013 241 LFRDPHHPYTAALLAALPE 259
Cdd:COG1123 492 VFANPQHPYTRALLAAVPS 510
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-317 |
2.25e-97 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 291.32 E-value: 2.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISA 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQL-----GETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMS 155
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLmqnipGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 236 QPVRALFRDPHHPYTAALLAALPERAKV---GQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVECDRGVVRQGPELGLAL 312
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKNHLYA 320
|
....*
gi 522061013 313 CNYPL 317
Cdd:PRK15093 321 CHFPL 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-271 |
1.14e-95 |
|
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: 292.96 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITaDRMQFDGQDLRGISAR 81
Cdd:COG1123 3 PLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRrrivGKDMAMIFQEPMSSLNPcFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQR 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|
gi 522061013 242 FRDPhhpytaALLAALPERAKVGQRLPSIA 271
Cdd:COG1123 231 LAAP------QALAAVPRLGAARGRAAPAA 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-259 |
1.50e-92 |
|
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: 285.43 E-value: 1.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFR-------AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakiTADRMQFDGQD 74
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLFRrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISARQRRRiVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVH-MGLNRKERRQRSIELLNLVGIPaPEDRlSNFPHQ 153
Cdd:COG4172 349 LDGLSRRALRP-LRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGLD-PAAR-HRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*.
gi 522061013 234 EEQPVRALFRDPHHPYTAALLAALPE 259
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-268 |
2.46e-92 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 287.52 E-value: 2.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWT-AKITADRMQFDGQ-----DLR 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAgGLVQCDKMLLRRRsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GISARQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSG 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260 270
....*....|....*....|....*....|...
gi 522061013 237 PVRALFRDPHHPYTAALLAALPER-AKVGQRLP 268
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQLgAMKGLDYP 284
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-275 |
3.65e-90 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 279.28 E-value: 3.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKI-TADRMQFDGQDLRGIS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMS 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 522061013 240 ALFRDPHHPYTAALLAALPErakvGQRLPSIAGVVP 275
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPS----GDPVPLPEPASP 274
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-258 |
3.81e-89 |
|
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: 267.44 E-value: 3.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWtakitADRMQFDGQDLRGISAR 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPW-----SGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGkdmaMIFQEPMSSLNPCFTVGFQLGETLRVHmglNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQR 161
Cdd:COG1124 76 AFRRRVQ----MVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*..
gi 522061013 242 FRDPHHPYTAALLAALP 258
Cdd:COG1124 227 LAGPKHPYTRELLAASL 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-297 |
2.76e-83 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 255.40 E-value: 2.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSG---------LFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDG 72
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 73 QDLRGISARQRRRiVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRV-HMGLNRKERRQRSIELLNLVGIpapedrLSN-- 149
Cdd:PRK15079 83 KDLLGMKDDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGL------LPNli 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 150 --FPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQ 227
Cdd:PRK15079 156 nrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 228 YAGQKVEEQPVRALFRDPHHPYTAALLAALP------ERAKVGQRLpsiAGVVPGQHGRPTGCLFAPRCGFATVEC 297
Cdd:PRK15079 236 YLGHAVELGTYDEVYHNPLHPYTKALMSAVPipdpdlERNKTIQLL---EGELPSPINPPSGCVFRTRCPIAGPEC 308
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-297 |
7.93e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 249.11 E-value: 7.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFR------AVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQD 74
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGIS--ARQRRRivgKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIpAPE--DRlsnF 150
Cdd:PRK11308 79 LLKADpeAQKLLR---QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEhyDR---Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 PHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 231 QKVEEQPVRALFRDPHHPYTAALLAALPeRAKVGQRLPSI--AGVVPGQHGRPTGCLFAPRCGFATVEC 297
Cdd:PRK11308 232 RCVEKGTKEQIFNNPRHPYTQALLSATP-RLNPDDRRERIklTGELPSPLNPPPGCAFNARCPRAFGRC 299
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-256 |
3.29e-79 |
|
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: 241.50 E-value: 3.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISARQRrrivgkDMAMIFQEPMSS 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLSIRGR------HIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 LNPCFTVGFQLGETLRVHMGLNrKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 182 TALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDPHHPYTAALLAA 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-256 |
1.32e-65 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 207.63 E-value: 1.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEfqTSSGLfraVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDLRGISARqr 83
Cdd:PRK10418 5 IELRNIALQ--AAQPL---VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rrivGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVhmgLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQRVM 163
Cdd:PRK10418 78 ----GRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFR 243
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|...
gi 522061013 244 DPHHPYTAALLAA 256
Cdd:PRK10418 231 APKHAVTRSLVSA 243
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-256 |
2.29e-62 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 199.29 E-value: 2.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFR-----AVDGVSLACDKGEILSIVGESGSGKS--VAMLALMgllpwtAKITADRMQFDGQ 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKStlAKMLAGI------IEPTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 74 DLRGISARQRrrivGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQ 153
Cdd:COG4167 76 KLEYGDYKYR----CKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLP--EHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 522061013 234 EEQPVRALFRDPHHPYTAALLAA 256
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
2-257 |
3.25e-62 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 198.88 E-value: 3.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITADRMQFDGQDLRGISA 80
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSgSVYYRDRDGGPRDLFALSE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVhMGLNRKER-RQRSIELLNLVGIPApeDRLSNFPHQMSGGMS 159
Cdd:COG4107 87 AERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMA-AGERHYGDiRARALEWLERVEIPL--ERIDDLPRTFSGGMQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:COG4107 164 QRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTD 243
|
250
....*....|....*...
gi 522061013 240 ALFRDPHHPYTAALLAAL 257
Cdd:COG4107 244 QVLEDPQHPYTQLLVSSV 261
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-258 |
5.74e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 200.69 E-value: 5.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVaMLALMGLL--PwtakiTADRMQFDGQDLRGISAR 81
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKST-LIRCINLLerP-----TSGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRiVGKDMAMIFQEP--MSSL----NpcftVGFQLgetlrVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMS 155
Cdd:COG1135 76 ELRA-ARRKIGMIFQHFnlLSSRtvaeN----VALPL-----EIAGVPKAEIRKRVAELLELVGL---SDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|...
gi 522061013 236 QPVRALFRDPHHPYTAALLAALP 258
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLPTVL 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-258 |
1.91e-61 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 206.63 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLF-------RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQD 74
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLLnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV----ESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISARQRRRiVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIpAPEDRLsNFPHQM 154
Cdd:PRK10261 388 IDTLSPGKLQA-LRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAW-RYPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260
....*....|....*....|....
gi 522061013 235 EQPVRALFRDPHHPYTAALLAALP 258
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-224 |
4.69e-60 |
|
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: 191.93 E-value: 4.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMGLLpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGL---DRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMAMIFQEPmsSLNPCFTVGfqlgETLRVHM---GLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQ 160
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTAL----ENVELPLllaGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMgVVAETAERV 224
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRI 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-245 |
3.35e-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: 190.10 E-value: 3.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMGLLpwtAKITADRMQFDGQDLRGISARQ 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGL---ERPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIvGKDMAMIFQE--PMSSLnpcfTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQ 160
Cdd:cd03258 77 LRKA-RRRIGMIFQHfnLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGL---EDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 522061013 241 LFRDP 245
Cdd:cd03258 228 VFANP 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-224 |
3.52e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.87 E-value: 3.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVaMLALMGLLpwtAKITADRMQFDGQDLRGISAR 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKST-LLNILGGL---DRPTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQEPmsSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQR 161
Cdd:COG1136 79 ELARLRRRHIGFVFQFF--NLLPELTALENVALPLLLA-GVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMgVVAETAERV 224
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRV 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-255 |
2.69e-56 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.07 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFR-------AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITadrmqFDGQD 74
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIW-----FDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISARQ----RRRIvgkdmAMIFQEPMSSLNPCFTVGFQLGETLRVHM-GLNRKERRQRSIELLNLVGIpAPEDRlSN 149
Cdd:PRK15134 349 LHNLNRRQllpvRHRI-----QVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGL-DPETR-HR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 150 FPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYA 229
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250 260
....*....|....*....|....*.
gi 522061013 230 GQKVEEQPVRALFRDPHHPYTAALLA 255
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-267 |
1.53e-55 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 182.19 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsGLFRA------VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQD 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHG-GLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL----ESPSQGNVSWRGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISaRQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPaPEDrLSNFPHQM 154
Cdd:PRK10419 76 LAKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD-DSV-LDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 522061013 235 EQPVRALFRdPHHP----YTAALLAALPERAKVGQRL 267
Cdd:PRK10419 233 TQPVGDKLT-FSSPagrvLQNAVLPAFPVRRRTTEKV 268
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-265 |
4.35e-53 |
|
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: 175.76 E-value: 4.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsGLFRA------VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLR 76
Cdd:TIGR02769 2 LLEVRDVTHTYRTG-GLFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GISARQRRRiVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQMSG 156
Cdd:TIGR02769 77 QLDRKQRRA-FRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260 270
....*....|....*....|....*....|..
gi 522061013 237 PVRALFRDPH---HPYTAALLAALPERAKVGQ 265
Cdd:TIGR02769 234 DVAQLLSFKHpagRNLQSAVLPEHPVRRSITT 265
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-256 |
1.53e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 168.83 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMGLLpwtAKITADRMQFDGQDLRGISARQ-- 82
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL---ERPTSGRVLVDGQDLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 --RRRIvgkdmAMIFQE--PMSSLNPCFTVGFQLgeTLrvhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGM 158
Cdd:PRK11153 79 kaRRQI-----GMIFQHfnLLSSRTVFDNVALPL--EL---AGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPV 238
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
250
....*....|....*...
gi 522061013 239 RALFRDPHHPYTAALLAA 256
Cdd:PRK11153 226 SEVFSHPKHPLTREFIQS 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-246 |
2.73e-49 |
|
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: 164.60 E-value: 2.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL----RPDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvGKDMAMIFQEP--MSSLNPCFTVGFqlgeTLRVHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQR 161
Cdd:cd03261 73 YRL-RRRMGMLFQSGalFDSLTVFENVAF----PLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....*
gi 522061013 242 FRDPH 246
Cdd:cd03261 225 RASDD 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-245 |
7.58e-49 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 163.27 E-value: 7.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL----KPTSGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGkdmaMIFQEPMSslnpcftvgfQL-GETLR-------VHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMS 155
Cdd:COG1122 74 RRKVG----LVFQNPDD----------QLfAPTVEedvafgpENLGLPREEIRERVEEALELVGLEHLADR---PPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
250
....*....|
gi 522061013 236 QPVRALFRDP 245
Cdd:COG1122 216 GTPREVFSDY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-241 |
1.08e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.31 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL----RPTSGEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkdmAMIFQEPmsSLNPCFTVGfqlgETLRVH---MGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQ 160
Cdd:COG1131 73 RRI-----GYVPQEP--ALYPDLTVR----ENLRFFarlYGLPRKEARERIDELLELFGLTDAADRK---VGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
.
gi 522061013 241 L 241
Cdd:COG1131 218 L 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-246 |
1.16e-48 |
|
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: 163.23 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR 81
Cdd:COG1127 4 PMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVgKDMAMIFQEP--MSSL----NpcftVGFQLgetlRVHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMS 155
Cdd:COG1127 76 ELYELR-RRIGMLFQGGalFDSLtvfeN----VAFPL----REHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|.
gi 522061013 236 QPVRALFRDPH 246
Cdd:COG1127 224 GTPEELLASDD 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-256 |
2.88e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 160.09 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQfDGQ--DLRGI 78
Cdd:PRK11701 4 QPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR-DGQlrDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLrvhMGLNRK---ERRQRSIELLNLVGIPApeDRLSNFPHQMS 155
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERL---MAVGARhygDIRATAGDWLERVEIDA--ARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|.
gi 522061013 236 QPVRALFRDPHHPYTAALLAA 256
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSS 254
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
9.67e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 9.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISA 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLE----KPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 rqrrrivgkDMAMIFQEPmsSLNPCFTVgFQ---LGetLRVhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGG 157
Cdd:COG1116 81 ---------DRGVVFQEP--ALLPWLTV-LDnvaLG--LEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-224 |
1.13e-46 |
|
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: 157.24 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRR 84
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL----GPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 85 RIVGkdmaMIFQEPMSSLnpcftvgfqLGETLR-------VHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGG 157
Cdd:cd03225 75 RKVG----LVFQNPDDQF---------FGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRS---PFTLSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERV 224
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRV 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-245 |
2.80e-46 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 158.38 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGL-FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDL---RGIS 79
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL----KPTSGTVTIDGRDItakKKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIVGkdmaMIFQEPMSSLnpcftvgFQlgETLR-------VHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPH 152
Cdd:TIGR04521 77 LKDLRKKVG----LVFQFPEHQL-------FE--ETVYkdiafgpKNLGLSEEEAEERVKEALELVGLD--EEYLERSPF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQK 232
Cdd:TIGR04521 142 ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
250
....*....|...
gi 522061013 233 VEEQPVRALFRDP 245
Cdd:TIGR04521 222 VLDGTPREVFSDV 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
3.45e-46 |
|
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: 156.09 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGisarqr 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE----RPTSGEVLVDGEPVTG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rriVGKDMAMIFQEPmsSLNPCFTVG--FQLGETLRvhmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQR 161
Cdd:cd03293 71 ---PGPDRGYVFQQD--ALLPWLTVLdnVALGLELQ---GVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-213 |
2.89e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 157.57 E-value: 2.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISA 80
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDGRDVTGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEP-----MSSL-NpcftVGFqlGetLRVHmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQM 154
Cdd:COG3842 75 EKR------NVGMVFQDYalfphLTVAeN----VAF--G--LRMR-GVPKAEIRARVAELLELVGLEGLADR---YPHQL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-257 |
2.08e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.07 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLrGISARQ 82
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVgKDMAMIFQepmsSLN--PCFTVgfqLG---ETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGG 157
Cdd:COG1126 72 INKLR-RKVGMVFQ----QFNlfPHLTV---LEnvtLAPIKVKKMSKAEAEERAMELLERVGL---ADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQKVEEQP 237
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 522061013 238 VRALFRDPHHPYTAALLAAL 257
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-240 |
3.92e-44 |
|
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: 151.43 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALM-GL-LPwtakiTADRMQFDGQDLRGIS 79
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLdRP-----TSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIVGKDMAMIFQEpmsslnpcftvgFQLGETL----RVHMGL---NRKERRQRSIELLNLVGIpapEDRLSNFPH 152
Cdd:COG4181 81 EDARARLRARHVGFVFQS------------FQLLPTLtaleNVMLPLelaGRRDARARARALLERVGL---GHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVvaetAERVQVQY---A 229
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL----AARCDRVLrlrA 221
|
250
....*....|.
gi 522061013 230 GQKVEEQPVRA 240
Cdd:COG4181 222 GRLVEDTAATA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
6.28e-44 |
|
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: 149.98 E-value: 6.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rrivgkDMAMIFQEPmsSLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVM 163
Cdd:cd03259 73 ------NIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQV 226
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-257 |
1.16e-43 |
|
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: 150.75 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFravdGVSLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTAKITADRMQFDGQDLRGISA 80
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCR----DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQMSGGMSQ 160
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDP--TRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|....*..
gi 522061013 241 LFRDPHHPYTAALLAAL 257
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSSI 252
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-231 |
1.43e-43 |
|
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: 149.42 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQ 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL----DNPTSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQepMSSLNPCFTVgfqlgeTLRVHM-----GLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGG 157
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTA------LENVAMplligKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGvVAETAERVQVQYAGQ 231
Cdd:TIGR02211 146 ERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-214 |
1.49e-43 |
|
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: 150.87 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISA 80
Cdd:cd03294 18 FKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI----EPTSGKVLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEpmSSLNPCFTV--GFQLGETLRvhmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGM 158
Cdd:cd03294 94 KELRELRRKKISMVFQS--FALLPHRTVleNVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHK---YPDELSGGM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDL 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-256 |
3.77e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 144.55 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFR-----AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADRMQFDGQDLR 76
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GISARQRrrivgkdmaMIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPApeDRLSNFPHQMSG 156
Cdd:PRK15112 84 YRSQRIR---------MIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP--DHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
250 260
....*....|....*....|
gi 522061013 237 PVRALFRDPHHPYTAALLAA 256
Cdd:PRK15112 233 STADVLASPLHELTKRLIAG 252
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-224 |
7.21e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.27 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSsglFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitaDRMQFDGQDLRGISAR 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS----GEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIvGKDMAMIFQEPmsSLNPCFTV------GfQLGE--TLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQ 153
Cdd:COG3638 74 ALRRL-RRRIGMIFQQF--NLVPRLSVltnvlaG-RLGRtsTWRSLLGLFPPEDRERALEALERVGL---ADKAYQRADQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-213 |
2.00e-40 |
|
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: 141.31 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMGLLpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIGGL---RSVQEGSLKVLGQELHGASKKQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 ---RRIVGkdmaMIFQEpmSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQ 160
Cdd:TIGR02982 78 vqlRRRIG----YIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:TIGR02982 149 RVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-224 |
3.02e-39 |
|
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: 138.05 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGisARQR 83
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPDSGTIIIDGLKLTD--DKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMAMIFQepmsSLN--PCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQR 161
Cdd:cd03262 71 INELRQKVGMVFQ----QFNlfPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERV 224
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRV 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-224 |
6.21e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQ- 82
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE----RPTSGQVLVNGQDLSRLKRREi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 ---RRRIvGkdmaMIFQEpmsslnpcftvgFQL--GET--------LRVHmGLNRKERRQRSIELLNLVGIpapEDRLSN 149
Cdd:COG2884 75 pylRRRI-G----VVFQD------------FRLlpDRTvyenvalpLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 150 FPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRV 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
1.55e-38 |
|
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: 133.93 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitaDRMQFDGQDLRGISARQRRRIVGkdmaMIFQEPmsSL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE----GTILLDGQDLTDDERKSLRKEIG----YVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIP-APEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 522061013 182 T 182
Cdd:pfam00005 150 A 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-256 |
2.07e-38 |
|
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: 136.66 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PwtakiTADRMQFDGQDLRGISARQ 82
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIeP-----TSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEpmSSLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIPaPEDRLSNFPHQMSGGMSQRV 162
Cdd:cd03295 73 LRRKIG----YVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALF 242
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|....
gi 522061013 243 RDPHHPYTAALLAA 256
Cdd:cd03295 225 RSPANDFVAEFVGA 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-246 |
2.08e-38 |
|
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: 136.41 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL----RPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRivgKDMAMIFQEPmsSLNPCFTV------GFQLGETLRVHMGLNRKER---RQRSIELLNLVGIPAPEDRLsnfPHQM 154
Cdd:cd03219 73 AR---LGIGRTFQIP--RLFPELTVlenvmvAAQARTGSGLLLARARREEreaRERAEELLERVGLADLADRP---AGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 522061013 235 EQPVRALFRDPH 246
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
3.88e-38 |
|
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: 135.77 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVefqTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQD---LRGISA 80
Cdd:cd03256 1 IEVENLSK---TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGSVLIDGTDinkLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRivgkDMAMIFQEPmsSLNPCFTV------GFqLGE--TLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPH 152
Cdd:cd03256 74 RQLRR----QIGMIFQQF--NLIERLSVlenvlsGR-LGRrsTWRSLFGLFPKEEKQRALAALERVGL---LDKAYQRAD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
7.33e-38 |
|
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: 135.56 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLRGISAR 81
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSgEVL-----LDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVgkdmAMIFQEPMSSLNpcFTVgFQLgetlrVHMGLN---------RKERRQRSIELLNLVGIPAPEDRLSNfph 152
Cdd:COG1120 72 ELARRI----AYVPQEPPAPFG--LTV-REL-----VALGRYphlglfgrpSAEDREAVEEALERTGLEHLADRPVD--- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRL 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-245 |
1.19e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 135.17 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLRGIS 79
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSgRIL-----FDGRDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ArqrRRIVGKDMAMIFQEPmsSLNPCFTV------GFQLGETLRVHMGLNR--------KERRQRSIELLNLVGIpapED 145
Cdd:COG0411 73 P---HRIARLGIARTFQNP--RLFPELTVlenvlvAAHARLGRGLLAALLRlprarreeREARERAEELLERVGL---AD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 146 RLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQ 225
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|
gi 522061013 226 VQYAGQKVEEQPVRALFRDP 245
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADP 244
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
5.22e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.91 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRgisa 80
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLFGKPPR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIvgkdmAMIFQepMSSLNPCF--TVG--FQLGetLRVHMGLNR---KERRQRSIELLNLVGIPAPEDR-LSnfph 152
Cdd:COG1121 72 RARRRI-----GYVPQ--RAEVDWDFpiTVRdvVLMG--RYGRRGLFRrpsRADREAVDEALERVGLEDLADRpIG---- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERV 224
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRV 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-244 |
6.50e-37 |
|
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: 133.32 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTveFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVamLA--LMGLL-PWTAKITADRMQF-DGQDLRGIs 79
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKST--LAklLNGLLlPTSGKVTVDGLDTlDEENLWEI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 arqrRRIVGkdmaMIFQepmsslNP-----CFTV----GFQLgETLrvhmGLNRKERRQRSIELLNLVGIpapEDRLSNF 150
Cdd:TIGR04520 76 ----RKKVG----MVFQ------NPdnqfvGATVeddvAFGL-ENL----GVPREEMRKRVDEALKLVGM---EDFRDRE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 PHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAEtAERVQVQYAG 230
Cdd:TIGR04520 134 PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKG 212
|
250
....*....|....
gi 522061013 231 QKVEEQPVRALFRD 244
Cdd:TIGR04520 213 KIVAEGTPREIFSQ 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-231 |
7.45e-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: 130.77 E-value: 7.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDL---RGIS 79
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSIL-----IDGEDLtdlEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIvgkdmAMIFQEPmsSLNPCFTVgfqlgetlrvhmglnrkerrqrsiellnlvgipapedrLSNFPHQMSGGMS 159
Cdd:cd03229 72 PPLRRRI-----GMVFQDF--ALFPHLTV--------------------------------------LENIALGLSGGQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-224 |
3.43e-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: 128.67 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL----KPDSGEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkdmAMIFQEPMsslnpcftvgfqLGETLRVHmglnrkerrqrsiELLNLvgipapedrlsnfphqmSGGMSQRVM 163
Cdd:cd03230 73 RRI-----GYLPEEPS------------LYENLTVR-------------ENLKL-----------------SGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERV 224
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRV 165
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-224 |
1.23e-35 |
|
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: 128.42 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLRGISAR-- 81
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgSIR-----VFGKPLEKERKRig 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 ---QRRrivgkdmamifqepmsSLNPCFTV-GFQLgetlrVHMGL---------NRKERRQRSIELLNLVGIPAPEDR-L 147
Cdd:cd03235 72 yvpQRR----------------SIDRDFPIsVRDV-----VLMGLyghkglfrrLSKADKAKVDEALERVGLSELADRqI 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 148 SnfphQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERV 224
Cdd:cd03235 131 G----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-254 |
4.30e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 130.65 E-value: 4.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakiTAD--RMQFDGQDLR-GISA 80
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE------TPDsgRIVLNGRDLFtNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRrivgkdMAMIFQEPMssLNPCFTVgFQ-LGETLRVhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMS 159
Cdd:COG1118 73 RERR------VGFVFQHYA--LFPHMTV-AEnIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
250
....*....|....*
gi 522061013 240 ALFRDPHHPYTAALL 254
Cdd:COG1118 220 EVYDRPATPFVARFL 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-241 |
7.54e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 127.28 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADrmqfdgqdlrGISAR 81
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPDSGSILID----------GEDVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQEPMSSLNpcFTVGfqlgETLRVH---MGLNRKERRQRSIELLNLVGIPAPEDRLSnfpHQMSGGM 158
Cdd:COG4555 67 KEPREARRQIGVLPDERGLYDR--LTVR----ENIRYFaelYGLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPV 238
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
...
gi 522061013 239 RAL 241
Cdd:COG4555 217 DEL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-230 |
7.74e-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: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RrivgkdMAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVM 163
Cdd:cd03300 73 P------VNTVFQN--YALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-224 |
1.31e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:COG4619 1 LELEGLSFRVGGKPIL----SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP----PTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVgkdmAMIFQEPmsslnpcftvgFQLGETLRVHMGL-----NRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGM 158
Cdd:COG4619 73 RRQV----AYVPQEP-----------ALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLP--PDILDKPVERLSGGE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRV 201
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-241 |
1.77e-34 |
|
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: 126.26 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQ 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV----EPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKdMAMIFQE-----PMSSLNPCFT--VGFQlgETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMS 155
Cdd:TIGR02315 74 LRKLRRR-IGMIFQHynlieRLTVLENVLHgrLGYK--PTWRSLLGRFSEEDKERALSALERVGL---ADKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*.
gi 522061013 236 QPVRAL 241
Cdd:TIGR02315 228 GAPSEL 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-224 |
2.79e-34 |
|
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: 124.08 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDLRGISARQR 83
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEIL-----LDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVgkdmAMIFQepmsslnpcftvgfqlgetlrvhmglnrkerrqrsieLLNLVGIPAPEDRLSNfphQMSGGMSQRVM 163
Cdd:cd03214 72 ARKI----AYVPQ-------------------------------------ALELLGLAHLADRPFN---ELSGGERQRVL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRV 168
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-213 |
2.92e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 129.45 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTV--------------------EFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwt 60
Cdd:COG4175 1 MPKIEVRNLYKifgkrperalklldqgkskdEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 61 akITADRMQFDGQDLRGISARQRRRIVGKDMAMIFQE----P-MSSL-NpcftVGFQLgeTLRvhmGLNRKERRQRSIEL 134
Cdd:COG4175 79 --PTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQHfallPhRTVLeN----VAFGL--EIQ---GVPKAERRERAREA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 135 LNLVGIPAPEDRlsnFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG4175 148 LELVGLAGWEDS---YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHD 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-241 |
4.60e-34 |
|
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: 124.99 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITAD-RMQFDGQDLRGISARQ 82
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 ---RRRIvgkdmAMIFQEPmsslNPcF--TVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPE-DRLSnfPHQMSG 156
Cdd:cd03260 77 lelRRRV-----GMVFQKP----NP-FpgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVkDRLH--ALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 522061013 237 PVRAL 241
Cdd:cd03260 223 PTEQI 227
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-224 |
6.47e-34 |
|
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: 123.88 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 6 IENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVaMLALMGLLpwtAKITADRMQFDGQDLRGISARQRRR 85
Cdd:TIGR03608 1 LKNISKKFGDKVIL----DDLNLTIEKGKMYAIIGESGSGKST-LLNIIGLL---EKFDSGQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 86 IVGKDMAMIFQEpmsslnpcftvgFQLGETLRV----HMGL-----NRKERRQRSIELLNLVGIpapEDRLSNFPHQMSG 156
Cdd:TIGR03608 73 FRREKLGYLFQN------------FALIENETVeenlDLGLkykklSKKEKREKKKEALEKVGL---NLKLKQKIYELSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMgVVAETAERV 224
Cdd:TIGR03608 138 GEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-235 |
8.32e-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: 8.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTSGRATVAGHDVVREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkdmAMIFQEPmsSLNPCFTvGFqlgETLRVH---MGLNRKERRQRSIELLNLVGIPAPEDRL-SNFphqmSGGMS 159
Cdd:cd03265 73 RRI-----GIVFQDL--SVDDELT-GW---ENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRLvKTY----SGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-251 |
1.21e-33 |
|
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: 127.08 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISA 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGRDITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLrVHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQ 160
Cdd:TIGR03265 74 QKR------DYGIVFQS--YALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:TIGR03265 142 RVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
250
....*....|.
gi 522061013 241 LFRDPHHPYTA 251
Cdd:TIGR03265 222 IYRHPATPFVA 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
1.63e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.20 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA----PSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 rqrrrivgkDMAMIFQEpmSSLNPCFTVG--FQLGETLRvhmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGM 158
Cdd:COG4525 77 ---------DRGVVFQK--DALLPWLNVLdnVAFGLRLR---GVPKAERRARAEELLALVGLADFARR---RIWQLSGGM 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-244 |
4.76e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 123.74 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 20 FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRRRIVGKDMAMIFQEPM 99
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 100 SSLnpcftvgFQlgETLRVHM-------GLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQRVMIAMALACNP 172
Cdd:PRK13646 96 SQL-------FE--DTVEREIifgpknfKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 173 KLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-241 |
1.44e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISA 80
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ----PDSGEILLDGEPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 R--QRRRIvgkdmAMIFQEPmsSLNPCFTVG---FqLGETLRVHMGLNRKERRQRSIELLNLVGIP-APEDRLSNfphqM 154
Cdd:COG1129 74 RdaQAAGI-----AIIHQEL--NLVPNLSVAeniF-LGREPRRGGLIDWRAMRRRARELLARLGLDiDPDTPVGD----L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
....*..
gi 522061013 235 EQPVRAL 241
Cdd:COG1129 221 TGPVAEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-245 |
2.50e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 11 VEFQTSSGLFRAV---DGVSLACDKGEILSIVGESGSGKSVaMLALMGLLpwtAKITADRMQFDGQDLRGISARQR--RR 85
Cdd:PRK09493 2 IEFKNVSKHFGPTqvlHNIDLNIDQGEVVVIIGPSGSGKST-LLRCINKL---EEITSGDLIVDGLKVNDPKVDERliRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 86 IVGkdmaMIFQE----P-MSSLNpcfTVGFQlgeTLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQ 160
Cdd:PRK09493 78 EAG----MVFQQfylfPhLTALE---NVMFG---PLRVR-GASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRA 240
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
....*
gi 522061013 241 LFRDP 245
Cdd:PRK09493 223 LIKNP 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-246 |
8.66e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 119.35 E-value: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSvAMLALMGLL--PWTAKITADRMQFDGQDLRGISA-RQRRRIVGkdmaMIFQEpmSSL 102
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTLNIAGNHFDFSKTPSDKAiRELRRNVG----MVFQQ--YNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVGFQLGET-LRVhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:PRK11124 94 WPHLTVQQNLIEApCRV-LGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 182 TALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERVQVQYAGqKVEEQPVRALFRDPH 246
Cdd:PRK11124 170 AALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENG-HIVEQGDASCFTQPQ 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-246 |
9.62e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 9.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 18 GLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMGLL--PWTAKITADRMQFD-GQDLRGISARQRRRIVGkdmaMI 94
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGQLNIAGHQFDfSQKPSEKAIRLLRQKVG----MV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 95 FQEpmSSLNPCFTVGFQLGET-LRVhMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPK 173
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEApCKV-LGLSKEQAREKAMKLLARLRL---TDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 174 LLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERVQVQYAGqKVEEQPVRALFRDPH 246
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKG-RIIEQGDASHFTQPQ 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
1.51e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVaMLALMGLL--PWTAKITADRMQFDGQdlRGI 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVL----HGIDLEVKPGEVVAIIGPSGSGKTT-LLRCINLLeqPEAGTIRVGDITIDTA--RSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQRR-RIVGKDMAMIFQEpmSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGG 157
Cdd:PRK11264 74 SQQKGLiRQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgMALVLITHDMGVVAETAERVQVQYAGQKVEEQP 237
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....*..
gi 522061013 238 VRALFRDPHHPYTAALL 254
Cdd:PRK11264 228 AKALFADPQQPRTRQFL 244
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-235 |
2.04e-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: 118.21 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL----ERPDSGTILFGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RriVGkdmaMIFQEpmSSLNPCFTVGFQLGETLRVHMGLNRK---ERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQ 160
Cdd:cd03296 75 N--VG----FVFQH--YALFRHMTVFDNVAFGLRVKPRSERPpeaEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGqKVEE 235
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG-RIEQ 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-260 |
2.61e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADRMQFDGQDLRGIsa 80
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVLSEETVWDV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 rqrRRIVGkdmaMIFQEPMSSLnpcftvgfqLGETLR--VHMGLN-----RKERRQRSIELLNLVGIpapEDRLSNFPHQ 153
Cdd:PRK13635 80 ---RRQVG----MVFQNPDNQF---------VGATVQddVAFGLEnigvpREEMVERVDQALRQVGM---EDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAEtAERVQVQYAGQKV 233
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
250 260 270
....*....|....*....|....*....|....*
gi 522061013 234 EEQPVRALFRDPHH--------PYTAALLAALPER 260
Cdd:PRK13635 220 EEGTPEEIFKSGHMlqeigldvPFSVKLKELLKRN 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
3.04e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL--LPWTAKITADRMqFDGQDLRGI 78
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVY-LDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQRRRIVgkdmAMIFQEPmsslNPCFTVgfQLGETLRVHMGLNR-----KERRQRSIELLNLVGI-PAPEDRLSNFPH 152
Cdd:PRK14247 76 DVIELRRRV----QMVFQIP----NPIPNL--SIFENVALGLKLNRlvkskKELQERVRWALEKAQLwDEVKDRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAERVQVQYAGQK 232
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*...
gi 522061013 233 VEEQPVRALFRDPHHPYT 250
Cdd:PRK14247 224 VEWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-244 |
7.24e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.84 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLlEIENLT-VEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDL--RG 77
Cdd:PRK13637 1 MSI-KIENLThIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL----KPTSGKIIIDGVDItdKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQRRRIVGkdmaMIFQEPMSSLnpcftvgFQlgETLR-------VHMGLNRKERRQRSIELLNLVGIPApEDRLSNF 150
Cdd:PRK13637 76 VKLSDIRKKVG----LVFQYPEYQL-------FE--ETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDY-EDYKDKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 PHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:PRK13637 142 PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
250
....*....|....
gi 522061013 231 QKVEEQPVRALFRD 244
Cdd:PRK13637 222 KCELQGTPREVFKE 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-224 |
7.74e-31 |
|
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: 114.26 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRR 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 85 RIVGkdmaMIFQepmsslnpcftvgfqlgetlrvhmglnrkerrqrsiellnlvgipapedrlsnfphqMSGGMSQRVMI 164
Cdd:cd00267 73 RRIG----YVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 165 AMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERV 224
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRV 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-244 |
9.47e-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: 115.99 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRivgKDMAMIFQEPMssLNPCFTVGfqlgETLRVHMGLNRKERRQRSIE-LLNLVgiPAPEDRLSNFPHQMSGGMSQRV 162
Cdd:cd03224 73 AR---AGIGYVPEGRR--IFPELTVE----ENLLLGAYARRRAKRKARLErVYELF--PRLKERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALF 242
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
..
gi 522061013 243 RD 244
Cdd:cd03224 221 AD 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-224 |
1.02e-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: 115.42 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglFRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQ 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLYGALTPSRGQVRIAGEDVNRLRGRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 ----RRRIvgkdmAMIFQEpmSSLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGM 158
Cdd:TIGR02673 74 lpllRRRI-----GVVFQD--FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:TIGR02673 143 QQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRV 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-231 |
1.96e-30 |
|
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: 114.66 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVM 163
Cdd:cd03301 73 ------DIAMVFQN--YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMgVVAET-AERVQVQYAGQ 231
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQ-VEAMTmADRIAVMNDGQ 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-273 |
2.10e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA--------KITADRMQFDGQDLRgisarqrrrivgKDMA 92
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSgtvtigerVITAGKKNKKLKPLR------------KKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 93 MIFQEPMSSLnpcftvgFQlgETLR-------VHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQRVMIA 165
Cdd:PRK13634 89 IVFQFPEHQL-------FE--ETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 166 MALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
250 260
....*....|....*....|....*...
gi 522061013 246 HhpYTAALLAALPERAKVGQRLPSIAGV 273
Cdd:PRK13634 238 D--ELEAIGLDLPETVKFKRALEEKFGI 263
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
5.28e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.10 E-value: 5.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISA 80
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE----DPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEPMssLNPCFTV----GFqlGetLRVhMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSG 156
Cdd:COG3839 73 KDR------NIAMVFQSYA--LYPHMTVyeniAF--P--LKL-RKVPKAEIDRRVREAAELLGL---EDLLDRKPKQLSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-214 |
7.44e-30 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 115.57 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQ-R 83
Cdd:COG1125 3 EFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIE----PTSGRILIDGEDIRDLDPVElR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRI------VGkdmamifqepmssLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIPaPEDRLSNFPHQMSGG 157
Cdd:COG1125 76 RRIgyviqqIG-------------LFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDI 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-245 |
1.57e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 113.64 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitaDRMQFDGQDLRGISARq 82
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH----GSITLDGKPVEGPGAE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 rRRIVGKDMAMIfqePMSSLNPCFTVGFQLGetlrvhmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRV 162
Cdd:PRK11248 72 -RGVVFQNEGLL---PWRNVQDNVAFGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM--GVVAET------------AERVQVQY 228
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIeeAVFMATelvllspgpgrvVERLPLNF 217
|
250
....*....|....*..
gi 522061013 229 AGQKVEEQPVRALFRDP 245
Cdd:PRK11248 218 ARRFVAGESSRSIKSDP 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-236 |
1.81e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.56 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 25 GVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQRRRIVGKDMAMIFQEPM--SSL 102
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVgfQLGETLRvhmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTT 182
Cdd:PRK10584 104 NALENV--ELPALLR---GESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522061013 183 ALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQyAGQKVEEQ 236
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLV-NGQLQEEA 228
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-256 |
2.24e-29 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 112.59 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL----EQPDSGRIRLNGQDATRVHARDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RrivgkdMAMIFQEpmSSLNPCFTV--GFQLGETLRVHmglNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQR 161
Cdd:TIGR00968 73 K------IGFVFQH--YALFKHLTVrdNIAFGLEIRKH---PKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:TIGR00968 139 VALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
250
....*....|....*
gi 522061013 242 FRDPHHPYTAALLAA 256
Cdd:TIGR00968 219 YDHPANPFVMSFLGE 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-224 |
2.73e-29 |
|
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: 111.73 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtsSGLFRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQ- 82
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 ---RRRIvgkdmAMIFQEpmSSLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMS 159
Cdd:cd03292 74 pylRRKI-----GVVFQD--FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRV 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-214 |
4.30e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.83 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISAR 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL----DTPTSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQepMSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQR 161
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIG-KKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-226 |
5.52e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 113.25 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 18 GLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRRRIvgkdmAMIFQE 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL----RPTSGTARVAGYDVVREPRKVRRSI-----GIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 98 PmsSLNPCFTVGfqlgETLRVH---MGLNRKERRQRSIELLNLVGIPAPEDRLSNfphQMSGGMSQRVMIAMALACNPKL 174
Cdd:TIGR01188 75 A--SVDEDLTGR----ENLEMMgrlYGLPKDEAEERAEELLELFELGEAADRPVG---TYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 522061013 175 LIADEPTTALDVTIQAQILDlLVRLQKEQGMALVLITHDMGVVAETAERVQV 226
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWD-YIRALKEEGVTILLTTHYMEEADKLCDRIAI 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-265 |
8.31e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGIS-- 79
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 --ARQRRRIVGkdmaMIFQE--PMSSLNPCFTVgfqlgETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMS 155
Cdd:PRK10535 79 alAQLRREHFG----FIFQRyhLLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAEtAERVQVQYAGQKVEE 235
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
250 260 270
....*....|....*....|....*....|
gi 522061013 236 QPVRalfrdPHHPYTAALLAALPERAKVGQ 265
Cdd:PRK10535 225 PPAQ-----EKVNVAGGTEPVVNTASGWRQ 249
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-248 |
9.94e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.60 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 11 VEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDLR---------GISAR 81
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQE-----PMSSLNPCFTVGFQLgetlrvhMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSG 156
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHfnlwsHMTVLENVMEAPIQV-------LGLSKQEARERAVKYLAKVGID--ERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
250
....*....|..
gi 522061013 237 PVRALFRDPHHP 248
Cdd:PRK10619 235 APEQLFGNPQSP 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-257 |
1.22e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSglfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISA 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF----EQPTAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRvHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQ 160
Cdd:PRK11607 89 YQR------PINMMFQS--YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTI----QAQILDLLVRLqkeqGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|.
gi 522061013 237 PVRALFRDPHHPYTAALLAAL 257
Cdd:PRK11607 233 EPEEIYEHPTTRYSAEFIGSV 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-244 |
1.33e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 115.41 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP---WTAKITadrmqFDGQDLRG 77
Cdd:PRK13549 3 EYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEGEII-----FEGEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQRRRivgKDMAMIFQEPMssLNPCFTVG---FqLGETLRVHMGLNRKERRQRSIELLNLVGIPA-PEDRLSNFphq 153
Cdd:PRK13549 74 SNIRDTER---AGIAIIHQELA--LVKELSVLeniF-LGNEITPGGIMDYDAMYLRAQKLLAQLKLDInPATPVGNL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 mSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:PRK13549 145 -GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
250
....*....|.
gi 522061013 234 EEQPVRALFRD 244
Cdd:PRK13549 223 GTRPAAGMTED 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
1.60e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.32 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITAD--RMQFDGQDLrgISARQRRRIVgkdmamiFQEP 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKgePIKYDKKSL--LEVRKTVGIV-------FQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 99 MSSL-NPCFTVGFQLGEtlrVHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQRVMIAMALACNPKLLIA 177
Cdd:PRK13639 88 DDQLfAPTVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 178 DEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-254 |
1.99e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.84 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsgLFRAvdgvSLACDKGEILSIVGESGSGKS--VAMLAlmGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRF----DLTIAAGERVAILGPSGAGKStlLNLIA--GFLP----PDSGRILWNGQDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVHMGLNRKERrQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQR 161
Cdd:COG3840 70 ER------PVSMLFQE--NNLFPHLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGLAGLLDRL---PGQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|...
gi 522061013 242 FRDPHHPYTAALL 254
Cdd:COG3840 218 LDGEPPPALAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-256 |
4.49e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 109.35 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTV---EFQtssglfraVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDLRGIS 79
Cdd:cd03299 1 LKVENLSKdwkEFK--------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSGKIL-----LNGKDITNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRvHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMS 159
Cdd:cd03299 68 PEKR------DISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:cd03299 136 QRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
250
....*....|....*..
gi 522061013 240 ALFRDPHHPYTAALLAA 256
Cdd:cd03299 216 EVFKKPKNEFVAEFLGF 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-224 |
6.71e-28 |
|
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: 107.73 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFqtsSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDlrgISARQRR 84
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNGKP---IKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 85 RIVGkdmaMIFQEPmsslnpcftvGFQL-GETLR--VHMGLNRKERRQRSIE-LLNLVGIPAPEDRLsnfPHQMSGGMSQ 160
Cdd:cd03226 71 KSIG----YVMQDV----------DYQLfTDSVReeLLLGLKELDAGNEQAEtVLKDLDLYALKERH---PLSLSGGQKQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
7.18e-28 |
|
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: 107.98 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqfdgqdLRGISARQ 82
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSgTAY----------INGYSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQEpmSSLNPCFTVGfqlgETLRVHM---GLNRKERRQRSIELLNLVGIPAPEDRLSnfpHQMSGGMS 159
Cdd:cd03263 69 DRKAARQSLGYCPQF--DALFDELTVR----EHLRFYArlkGLPKSEIKEEVELLLRVLGLTDKANKRA---RTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-249 |
1.45e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 17 SGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRRRIVGKDMAMIFQ 96
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI----EPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 97 EpmSSLNPCFTV------GFQLGetlrvhmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALAC 170
Cdd:PRK10070 114 S--FALMPHMTVldntafGMELA-------GINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 171 NPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDPHHPY 249
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
2.81e-27 |
|
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: 104.82 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR-- 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLY----KPDSGEILVDGKEVSFASPRda 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIvgkdmAMIfqepmsslnpcftvgfqlgetlrvhmglnrkerrqrsiellnlvgipapedrlsnfpHQMSGGMSQR 161
Cdd:cd03216 73 RRAGI-----AMV---------------------------------------------------------YQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-231 |
7.36e-27 |
|
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: 105.45 E-value: 7.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 24 DGVSLACD---KGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR-----QRRRIvgkdmAMIF 95
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLFDSRKKinlppQQRKI-----GLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 96 QEpmSSLNPCFTVGFQLGETLRVHmglNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVMIAMALACNPKLL 175
Cdd:cd03297 82 QQ--YALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 176 IADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-225 |
1.14e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVeFQTSSGLFRavdGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtAKITAD-RMQFDGQDLRGISARQ 82
Cdd:COG4136 2 LSLENLTI-TLGGRPLLA---PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASgEVLLNGRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRriVGkdmaMIFQEPMssLNPCFTVGFQLGETLRVhmGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRV 162
Cdd:COG4136 76 RR--IG----ILFQDDL--LFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQ 225
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLD 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-257 |
1.59e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakiTAD--RMQFDGQDLRGI 78
Cdd:COG3845 3 PPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY------QPDsgEILIDGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQ-RRRIVGkdmaMIFQEPMssLNPCFTV--GFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMS 155
Cdd:COG3845 73 SPRDaIALGIG----MVHQHFM--LVPNLTVaeNIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAK---VEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALdvTIQ--AQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
250 260
....*....|....*....|....
gi 522061013 234 EEQPVRALfrdphhpyTAALLAAL 257
Cdd:COG3845 221 GTVDTAET--------SEEELAEL 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-234 |
1.79e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.25 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 20 FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakITADRMQFDGQ-----DLRGISARQRRRivgKDMAMI 94
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-----ISETGQTIVGDyaipaNLKKIKEVKRLR---KEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 95 FQEPMSSLnpcftvgFQlgETLR-------VHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQRVMIAMA 167
Cdd:PRK13645 96 FQFPEYQL-------FQ--ETIEkdiafgpVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 168 LACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-226 |
2.13e-26 |
|
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: 102.85 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTveFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLRGISARQ 82
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgEIL-----IDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVgkdmAMIFQEPmsslnpcftvgFQLGETLRvhmglnrkErrqrsiellNLvgipapedrlsnfphqMSGGMSQRV 162
Cdd:cd03228 74 LRKNI----AYVPQDP-----------FLFSGTIR--------E---------NI----------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVAEtAERVQV 226
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIV 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-213 |
2.39e-26 |
|
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: 103.71 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSgLFRavdGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakitadrmQFDGQ-DLRGISA 80
Cdd:COG4133 1 MMLEAENLSCRRGERL-LFS---GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP----------PSAGEvLWNGEPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPMssLNPCFTVGfqlgETLRVHMGLNRKERRQRSI-ELLNLVGIPAPEDRLsnfPHQMSGGMS 159
Cdd:COG4133 67 RDAREDYRRRLAYLGHADG--LKPELTVR----ENLRFWAALYGLRADREAIdEALEAVGLAGLADLP---VRQLSAGQK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRlQKEQGMALVLITHD 213
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-245 |
2.55e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.11 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:PRK11432 7 VVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL----EKPTEGQIFIDGEDVTHRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVM 163
Cdd:PRK11432 79 ------DICMVFQS--YALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFR 243
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
..
gi 522061013 244 DP 245
Cdd:PRK11432 227 QP 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-266 |
3.75e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.18 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwTAKITADRMQFDGQdLRGISAR 81
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVL----DQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM---NDKVSGYRYSGDVL-LGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVG--KDMAMIFQEPmsslNPC-FTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGI-PAPEDRLSNFPHQMSGG 157
Cdd:PRK14271 92 NYRDVLEfrRRVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAERVQVQYAGQKVEEQP 237
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|....*....
gi 522061013 238 VRALFRDPHHPYTAALLAALPERAKVGQR 266
Cdd:PRK14271 246 TEQLFSSPKHAETARYVAGLSGDVKDAKR 274
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-235 |
4.75e-26 |
|
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: 103.22 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADrmqfdgqdlrGISAR 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVD----------GFDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIPAPEDRLSNfphQMSGGMSQR 161
Cdd:cd03266 71 KEPAEARRRLGFVSDS--TGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-214 |
5.61e-26 |
|
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: 108.77 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTveFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDLRGISARQ 82
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRIL-----IDGIDLRQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEPmsslnpcftvgFQLGETLR--VHMGlNRKERRQRSIELLNLVGIpapEDRLSNFPHQM------ 154
Cdd:COG2274 547 LRRQIG----VVLQDV-----------FLFSGTIRenITLG-DPDATDEEIIEAARLAGL---HDFIEALPMGYdtvvge 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 155 -----SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqkEQGMALVLITHDM 214
Cdd:COG2274 608 ggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRL 670
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-233 |
5.87e-26 |
|
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: 102.74 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKItadrmQFDGqdlRGISARQ 82
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEV-----LFDG---KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIvgkdmAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRV 162
Cdd:cd03269 69 RNRI-----GYLPEE--RGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLEL---SEYANKRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVtIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-252 |
6.56e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.96 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLAL--MG-LLPwTAKITAdRMQFDGQDlrgI 78
Cdd:COG1117 10 PKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLIP-GARVEG-EILLDGED---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQ------RRRIvgkdmAMIFQEPmsslNPcF--------TVGfqlgetLRVHMGLNRKERRQRSIELLNLVGIPaPE 144
Cdd:COG1117 81 YDPDvdvvelRRRV-----GMVFQKP----NP-FpksiydnvAYG------LRLHGIKSKSELDEIVEESLRKAALW-DE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 145 --DRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAE 222
Cdd:COG1117 144 vkDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSD 221
|
250 260 270
....*....|....*....|....*....|
gi 522061013 223 RVQVQYAGQKVEEQPVRALFRDPHHPYTAA 252
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-245 |
6.56e-26 |
|
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: 105.95 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakiTAD--RMQFDGQDL----RGIS-ARQRRRIvgkdmAMIFQEP 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLE------RPDsgRIRLGGEVLqdsaRGIFlPPHRRRI-----GYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 99 msSLNPCFTVGfqlgETLRVhmGLNRKERRQRSI---ELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLL 175
Cdd:COG4148 87 --RLFPHLSVR----GNLLY--GRKRAPRAERRIsfdEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 176 IADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-250 |
1.07e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLLP-WTAKITAD-RMQFDGQDLRGISARQRRRIVGkdmaMIFQEPmsSLN 103
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDgKVLYFGKDIFQIDAIKLRKEVG----MVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 104 PCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGI-PAPEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTT 182
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 183 ALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDPHHPYT 250
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-231 |
1.69e-25 |
|
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: 100.58 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEfqtssglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRivgKDMAMIFQEpmsslnpcftvgfqlgetlRVHMGLNRkerrQRSIELlNLVgipapedrlsnFPHQMSGGMSQR 161
Cdd:cd03215 71 DAIR---AGIAYVPED-------------------RKREGLVL----DLSVAE-NIA-----------LSSLLSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-250 |
3.09e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.16 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLAL--MGLLPWTAKITADrMQFDGQDLrgIS 79
Cdd:PRK14239 4 PILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGS-IVYNGHNI--YS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIVGKDMAMIFQEPmsslNPC-FTVGFQLGETLRVHmGLNRKERRQRSIELlNLVGIPAPE---DRLSNFPHQMS 155
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQP----NPFpMSIYENVVYGLRLK-GIKDKQVLDEAVEK-SLKGASIWDevkDRLHDSALGLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVliTHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLIEY 228
|
250
....*....|....*
gi 522061013 236 QPVRALFRDPHHPYT 250
Cdd:PRK14239 229 NDTKQMFMNPKHKET 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
3.91e-25 |
|
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: 101.21 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVefqtSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISA 80
Cdd:COG0410 1 MPMLEVENLHA----GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RqrrRIVGKDMAM------IFqepmSSLnpcfTVGfqlgETLRVHMGLNRKERRQRSI--ELLNLVgiPAPEDRLSNFPH 152
Cdd:COG0410 73 H---RIARLGIGYvpegrrIF----PSL----TVE----ENLLLGAYARRDRAEVRADleRVYELF--PRLKERRRQRAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQK 232
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
250
....*....|....
gi 522061013 233 VEEQPVRALFRDPH 246
Cdd:COG0410 215 VLEGTAAELLADPE 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-244 |
6.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVA---MLALmgLLPWTAKITADRMqfDGQDLRGI-SARQRrrivgkdMAMIFQE 97
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGL--DTSDEENLwDIRNK-------AGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 98 PMSSLNPCFT---VGFQlGETLrvhmGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQRVMIAMALACNPKL 174
Cdd:PRK13633 94 PDNQIVATIVeedVAFG-PENL----GIPPEEIRERVDESLKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 175 LIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAEtAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-254 |
7.06e-25 |
|
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: 102.57 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 38 IVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARqrRRIVGkdmaMIFQEpmSSLNPCFTVGFQLGETLR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF----EQPDSGSIMLDGEDVTNVPPH--LRHIN----MVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 118 VHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLV 197
Cdd:TIGR01187 69 MR-KVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 198 RLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDPHHPYTAALL 254
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-259 |
8.35e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 8.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQ 82
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEPMSSlnpcFT-------VGFQLGetlrvHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMS 155
Cdd:PRK13650 79 IRHKIG----MVFQNPDNQ----FVgatveddVAFGLE-----NKGIPHEEMKERVNEALELVGMQDFKERE---PARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAeTAERVQVQYAGQKVEE 235
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
250 260 270
....*....|....*....|....*....|..
gi 522061013 236 QPVRALFRDPHH--------PYTAALLAALPE 259
Cdd:PRK13650 222 STPRELFSRGNDllqlgldiPFTTSLVQSLRQ 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
9.30e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.22 E-value: 9.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGkdmaMIFQEPMSSlnpcF---TV----GFQLgETLRVhmglNRKERRQRSIELLNLVGIpapEDRLSNFPHQM 154
Cdd:PRK13632 80 EIRKKIG----IIFQNPDNQ----FigaTVeddiAFGL-ENKKV----PPKKMKDIIDDLAKKVGM---EDYLDKEPQNL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
1.80e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISA 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSK---EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGkdmaMIFQEPMSSL-NPCFTVGFQLGETlrvHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMS 159
Cdd:PRK13652 74 REVRKFVG----LVFQNPDDQIfSPTVEQDIAFGPI---NLGLDEETVAHRVSSALHMLGL---EELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*.
gi 522061013 240 ALFRDP 245
Cdd:PRK13652 224 EIFLQP 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-235 |
2.05e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.44 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQD-LRGISARQ 82
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSyQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RrrivgkdMAMIFQEPmsSLNPCFTVGFQLGETLRVHMGlnRKERRQRSIELLNLVGIPapEDRLSNFphqmSGGMSQRV 162
Cdd:cd03268 73 R-------IGALIEAP--GFYPNLTARENLRLLARLLGI--RKKRIDEVLDVVGLKDSA--KKKVKGF----SLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-224 |
2.69e-24 |
|
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: 99.08 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGisarqrrriVGKDMAMIFQEpmSSL 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQITE---------PGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVGFQLGETL-RVHMGLNRKERRQRSIELLNLVGIPAPEDRlsnFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:TIGR01184 66 LPWLTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 522061013 182 TALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRV 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-242 |
2.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKItadrMQFDGQDLRGISARQ 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK----VKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEPMSSLnpcftVGFQLGETLRVHM---GLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMS 159
Cdd:PRK13642 79 LRRKIG----MVFQNPDNQF-----VGATVEDDVAFGMenqGIPREEMIKRVDEALLAVNM---LDFKTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 160 QRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAeTAERVQVQYAGQKVEEQPVR 239
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPS 225
|
...
gi 522061013 240 ALF 242
Cdd:PRK13642 226 ELF 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-241 |
4.35e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVefqTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:COG3845 256 VVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRivgKDMAMIFQEPMSS-LNPCFTV------GFQLGETLRVHMGLNRKERRQRSIELLNLVGI--PAPEDRLSNfph 152
Cdd:COG3845 329 ERRR---LGVAYIPEDRLGRgLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVrtPGPDTPARS--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 qMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQK 232
Cdd:COG3845 403 -LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
....*....
gi 522061013 233 VEEQPVRAL 241
Cdd:COG3845 481 VGEVPAAEA 489
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-230 |
4.52e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQR 83
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQTSGHIRFHGTDVSRLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RriVGkdmaMIFQEpmSSLNPCFTVGFQLGETLRVhmgLNRKER------RQRSIELLNLVGIPAPEDRlsnFPHQMSGG 157
Cdd:PRK10851 75 K--VG----FVFQH--YALFRHMTVFDNIAFGLTV---LPRRERpnaaaiKAKVTQLLEMVQLAHLADR---YPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-244 |
5.49e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL-LPWTAKITADrmqfdGQDLRGISARQ 82
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVM-----GREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEPMSSLnpcFT------VGFQlgetlRVHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSG 156
Cdd:PRK13647 77 VRSKVG----LVFQDPDDQV---FSstvwddVAFG-----PVNMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
....*...
gi 522061013 237 PVRALFRD 244
Cdd:PRK13647 221 DKSLLTDE 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-234 |
6.09e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 102.18 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFqtsSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP---WTAKITadrmqFDGQ--DLRG 77
Cdd:NF040905 1 ILEMRGITKTF---PGV-KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsYEGEIL-----FDGEvcRFKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQRRRIVgkdmaMIFQEpmSSLNPCFTVG---FqLGETLRVHMGLNRKERRQRSIELLNLVGIP-APEDRLSNfphq 153
Cdd:NF040905 72 IRDSEALGIV-----IIHQE--LALIPYLSIAeniF-LGNERAKRGVIDWNETNRRARELLAKVGLDeSPDTLVTD---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:NF040905 140 IGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
.
gi 522061013 234 E 234
Cdd:NF040905 219 E 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-241 |
6.16e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLrgiSARQ 82
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSgEVL-----WDGEPL---DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIvG---------KDMamifqepmsslnpcfTVGFQL---GEtLRvhmGLNRKERRQRSIELLNLVGIPA-PEDRLsn 149
Cdd:COG4152 70 RRRI-GylpeerglyPKM---------------KVGEQLvylAR-LK---GLSKAEAKRRADEWLERLGLGDrANKKV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 150 fpHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVtIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYA 229
Cdd:COG4152 128 --EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
250
....*....|..
gi 522061013 230 GQKVEEQPVRAL 241
Cdd:COG4152 205 GRKVLSGSVDEI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-244 |
7.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PwtakiTADRMQFDGQDLRGISARQRRRIVGKDMAMIFQEPM 99
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvP-----TQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 100 SSLnpcF--TV------GFQlgetlrvHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQRVMIAMALACN 171
Cdd:PRK13649 96 SQL---FeeTVlkdvafGPQ-------NFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 172 PKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-249 |
8.24e-24 |
|
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: 100.19 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 34 EILSIVGESGSGKSVAMLALMGLL-PWTAKIT-ADRMQFDGQDLRGISARQRRrivgkdMAMIFQEpmSSLNPCFTVGFQ 111
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVlNGRTLFDSRKGIFLPPEKRR------IGYVFQE--ARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 112 LGETLRVHMGLNRKERRQRSIELLNLvgipapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQ 191
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGI------GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 192 ILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDPHHPY 249
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-244 |
2.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDL----RGIsaRQRRRIVGkdmaMIFQE 97
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKPIdysrKGL--MKLRESVG----MVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 98 PMSSLnpcFTVG-FQLGETLRVHMGLNRKERRQRSIELLNLVGIpapeDRLSNFP-HQMSGGMSQRVMIAMALACNPKLL 175
Cdd:PRK13636 91 PDNQL---FSASvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 176 IADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-235 |
2.24e-23 |
|
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: 100.65 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTssglFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL---LPWTAKIT-----------ADRMQ 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 70 FDGQ--------------DLRGISARQRRRIVgKDMAMIFQEPmsslnpcftvgFQLGETLRV---------HMGLNRKE 126
Cdd:TIGR03269 77 KVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRT-----------FALYGDDTVldnvlealeEIGYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 127 RRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMA 206
Cdd:TIGR03269 145 AVGRAVDLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS 221
|
250 260
....*....|....*....|....*....
gi 522061013 207 LVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:TIGR03269 222 MVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
2.52e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGL-FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQ 82
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP----PDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKdmamIFQEPMSSLNPCFTVGFQL------GETLRVHMGLNRKERR--QRSIELLNLvGIpapEDRLSNFPHQM 154
Cdd:COG1101 78 RAKYIGR----VFQDPMMGTAPSMTIEENLalayrrGKRRGLRRGLTKKRRElfRELLATLGL-GL---ENRLDTKVGLL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
4.13e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEF-QTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP------WTAKI-TADRMQFDGQD 74
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiQVGDIyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGIS-----ARQRRRIVGkdmaMIFQEPMsslnpcftvgFQL-GETLR-------VHMGLNRKERRQRSIELLNLVGIP 141
Cdd:PRK13631 101 TNPYSkkiknFKELRRRVS----MVFQFPE----------YQLfKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 142 apEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRlQKEQGMALVLITHDMGVVAETA 221
Cdd:PRK13631 167 --DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|....*
gi 522061013 222 ERVQVQYAGQKVEEQPVRALFRDPH 246
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
1.22e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGL-FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKI-----------TADRMQF 70
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlPDTGTIewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 71 DGQDLRgISARQRRRI-----VGKDMAMIFQepmsslnpcFTvGFQLGE-TLR-------VHMGLNRKERRQRSIELLNL 137
Cdd:PRK13651 83 VLEKLV-IQKTRFKKIkkikeIRRRVGVVFQ---------FA-EYQLFEqTIEkdiifgpVSMGVSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 138 VGIPapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVV 217
Cdd:PRK13651 152 VGLD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNV 228
|
....*..
gi 522061013 218 AETAERV 224
Cdd:PRK13651 229 LEWTKRT 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-234 |
1.51e-22 |
|
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: 97.95 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEF-QTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFDGQDL--RGI 78
Cdd:TIGR03269 278 PIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMtkPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQRrriVGKDMAMIFQEpmSSLNPCFTVGFQLGETlrVHMGLNRKERRQRSIELLNLVGIPAPEDR--LSNFPHQMSG 156
Cdd:TIGR03269 358 DGRGR---AKRYIGILHQE--YDLYPHRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKAEeiLDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
1.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWT--AKITADRMQFdGQDLRG--IS 79
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLF-GRNIYSpdVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIVGkdmaMIFQEPmsslNPC--------FTVGFQLGETLRVHMGLN-RKERRQRSIELLNLVgipapEDRLSNF 150
Cdd:PRK14267 80 PIEVRREVG----MVFQYP----NPFphltiydnVAIGVKLNGLVKSKKELDeRVEWALKKAALWDEV-----KDRLNDY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 PHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqgMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLG 224
|
250 260
....*....|....*....|
gi 522061013 231 QKVEEQPVRALFRDPHHPYT 250
Cdd:PRK14267 225 KLIEVGPTRKVFENPEHELT 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-213 |
1.94e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.55 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSglfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISA 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF----ETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVgipapedRLSNF----PHQMSG 156
Cdd:PRK09452 84 ENR------HVNTVFQS--YALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMV-------QLEEFaqrkPHQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-241 |
2.00e-22 |
|
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: 97.91 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVefqTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:COG4988 335 PSIELEDVSF---SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRivgkDMAMIFQEPmsslnpcftvgFQLGETLRVHMGLNRKER-RQRSIELLNLVGIpapEDRLSNFPHQM------ 154
Cdd:COG4988 408 SWRR----QIAWVPQNP-----------YLFAGTIRENLRLGRPDAsDEELEAALEAAGL---DEFVAALPDGLdtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 -----SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITHDMGVVAEtAERVQVQYA 229
Cdd:COG4988 470 ggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDD 546
|
250
....*....|..
gi 522061013 230 GQKVEEQPVRAL 241
Cdd:COG4988 547 GRIVEQGTHEEL 558
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-276 |
2.18e-22 |
|
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: 96.22 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 6 IENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwTAKITADRMQFDGQDLRGISARQRrr 85
Cdd:TIGR03258 8 IDHLRVAYGANTVL----DDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFV--KAAGLTGRIAIADRDLTHAPPHKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 86 ivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVHMgLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIA 165
Cdd:TIGR03258 80 ----GLALLFQN--YALFPHLKVEDNVAFGLRAQK-MPKADIAERVADALKLVGL---GDAAAHLPAQLSGGMQQRIAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 166 MALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKE-QGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:TIGR03258 150 RAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDA 229
|
250 260 270
....*....|....*....|....*....|....*
gi 522061013 245 PHHPYTAALLAA---LPERAKVGQRLPSIAGVVPG 276
Cdd:TIGR03258 230 PADGFAAEFLGAaniLPAIALGITEAPGLVDVSCG 264
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-224 |
2.48e-22 |
|
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: 93.27 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEF---QTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTAKITADRmQFDGQDLRG 77
Cdd:COG4778 3 TLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRH-DGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQ----RRRivgkdmamifqepmsslnpcfTVGF--QLgetLRV---------------HMGLNRKERRQRSIELLN 136
Cdd:COG4778 82 ASPREilalRRR---------------------TIGYvsQF---LRViprvsaldvvaepllERGVDREEARARARELLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 137 LVGIPapeDRL-SNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMG 215
Cdd:COG4778 138 RLNLP---ERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEE 213
|
....*....
gi 522061013 216 VVAETAERV 224
Cdd:COG4778 214 VREAVADRV 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-231 |
3.11e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.64 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGeILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP----PSSGTIRIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkdmAMIFQEPMssLNPCFTVGFQLgETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVM 163
Cdd:cd03264 72 RRI-----GYLPQEFG--VYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNL---GDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-245 |
3.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRRRIVGKDMAMIFQEPMS 100
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 SLnpcF--TV--GFQLGEtlrVHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLI 176
Cdd:PRK13641 97 QL---FenTVlkDVEFGP---KNFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 177 ADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-235 |
3.48e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEfqtssglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QR-----------RRIVGkdmamIFQE-------PMSSLNPCFTVGFqlgetlrvhmgLNRKERRQRSIELLNLVGI--P 141
Cdd:COG1129 323 DAiragiayvpedRKGEG-----LVLDlsireniTLASLDRLSRGGL-----------LDRRRERALAEEYIKRLRIktP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 142 APEDRLSNfphqMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETA 221
Cdd:COG1129 387 SPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLS 461
|
250
....*....|....
gi 522061013 222 ERVQVQYAGQKVEE 235
Cdd:COG1129 462 DRILVMREGRIVGE 475
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-224 |
1.02e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS----PDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 Q--RRRivgkdmAMIFQEpmSSLNPCFTVgfqlgetlR--VHMGL----NRKERRQRSI-ELLNLVGIPAPEDRlsnFPH 152
Cdd:PRK13548 73 ElaRRR------AVLPQH--SSLSFPFTV--------EevVAMGRaphgLSRAEDDALVaAALAQVDLAHLAGR---DYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 153 QMSGGMSQRVMIAMALA------CNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRI 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-245 |
2.30e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTA---KITADRMQFDGQDLRGIsaRQRRRIVgkdmamiFQE 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNpnsKITVDGITLTAKTVWDI--REKVGIV-------FQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 98 PMSSLnpcftVGFQLGETlrVHMGL-NRKERRQRSIEL----LNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNP 172
Cdd:PRK13640 93 PDNQF-----VGATVGDD--VAFGLeNRAVPRPEMIKIvrdvLADVGM---LDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 173 KLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGvVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-244 |
7.24e-21 |
|
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: 92.97 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP---WTAKItadrmQFDGQDLRGIS 79
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDGEI-----YWSGSPLKASN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRivgKDMAMIFQEPMssLNPCFTV--GFQLGETLRVHMGL-NRKERRQRSIELLNLVGIPApeDRLSNFPHQMSG 156
Cdd:TIGR02633 72 IRDTER---AGIVIIHQELT--LVPELSVaeNIFLGNEITLPGGRmAYNAMYLRAKNLLRELQLDA--DNVTRPVGDYGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTiQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQ 236
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATK 223
|
....*...
gi 522061013 237 PVRALFRD 244
Cdd:TIGR02633 224 DMSTMSED 231
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-299 |
1.19e-20 |
|
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: 84.72 E-value: 1.19e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 233 VEEQPVRALFRDPHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVECDR 299
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRK 69
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-243 |
1.37e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSS----------GLFR-------AVDGVSLACDKGEILSIVGESGSGKS--VAMLAlmGLL-PwtakiT 64
Cdd:COG4586 3 EVENLSKTYRVYEkepglkgalkGLFRreyreveAVDDISFTIEPGEIVGFIGPNGAGKSttIKMLT--GILvP-----T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 65 ADRMQFDGQDlrgiSARQRRRIVgKDMAMIF-QEPmsslnpcftvgfQL------GETLRVH---MGLNRKERRQRS--- 131
Cdd:COG4586 76 SGEVRVLGYV----PFKRRKEFA-RRIGVVFgQRS------------QLwwdlpaIDSFRLLkaiYRIPDAEYKKRLdel 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 132 IELLNLvgipapEDRLSNFPHQMSGGmsQRvM---IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALV 208
Cdd:COG4586 139 VELLDL------GELLDTPVRQLSLG--QR-MrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTIL 209
|
250 260 270
....*....|....*....|....*....|....*
gi 522061013 209 LITHDMGVVAETAERVQVQYAGQKVEEQPVRALFR 243
Cdd:COG4586 210 LTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-244 |
1.64e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 6 IENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADRMQFDGQDLRGISarqrr 84
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLR----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 85 rivgKDMAMIFQEPMSSLNPCfTVGFQLGETLRVHMgLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMI 164
Cdd:PRK13648 83 ----KHIGIVFQNPDNQFVGS-IVKYDVAFGLENHA-VPYDEMHRRVSEALKQVDM---LERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 165 AMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAEtAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-213 |
3.37e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITadrmqFDGQDLRGISARQ--RRRivgkdmAMIFQEpms 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEIL-----LNGRPLSDWSAAElaRHR------AYLSQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 SLNPCFTVGFQLgetLRVHM--GLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMAL-----ACNP- 172
Cdd:COG4138 78 QSPPFAMPVFQY---LALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPe 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522061013 173 -KLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHD 213
Cdd:COG4138 152 gQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHD 192
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
3.45e-20 |
|
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: 88.22 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLlpwtakITADRMQFDGQDLR---- 76
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKS----TLLSL------ITGDLPPTYGNDVRlfge 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 ---GISARQ-RRRI--VGKDMAMIFQEPMSSLNpcfTV--GFqlgetlrvH--MGLNRK---ERRQRSIELLNLVGIPAP 143
Cdd:COG1119 67 rrgGEDVWElRKRIglVSPALQLRFPRDETVLD---VVlsGF--------FdsIGLYREptdEQRERARELLELLGLAHL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 144 EDRLsnFpHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITH 212
Cdd:COG1119 136 ADRP--F-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
3.45e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.25 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQ 82
Cdd:COG4559 1 MLEAENLSVRLGGR----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL----TPSSGEVRLNGRPLAAWSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 --RRRIVgkdMAmifQEpmSSLNPCFTVG--FQLGetlRVHMGLNRKERRQRSIELLNLVGIPAPEDRlsNFPhQMSGGM 158
Cdd:COG4559 73 laRRRAV---LP---QH--SSLAFPFTVEevVALG---RAPHGSSAAQDRQIVREALALVGLAHLAGR--SYQ-TLSGGE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 159 SQRVMIAMALA-----CN--PKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERV 224
Cdd:COG4559 139 QQRVQLARVLAqlwepVDggPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRI 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-226 |
1.25e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.23 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSS----------GLFR-------AVDGVSLACDKGEILSIVGESGSGKSVAM-------------LAL 53
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkSLFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLkilsgllqptsgeVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 54 MGLLPWTAKItadrmqfdgQDLRGISArqrrrIVGKDMAMIFQEPmsslnpcftvgfqLGETLRVHMGLNR------KER 127
Cdd:cd03267 81 AGLVPWKRRK---------KFLRRIGV-----VFGQKTQLWWDLP-------------VIDSFYLLAAIYDlpparfKKR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 128 RQRSIELLNLvgipapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMAL 207
Cdd:cd03267 134 LDELSELLDL------EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTV 207
|
250
....*....|....*....
gi 522061013 208 VLITHDMGVVAETAERVQV 226
Cdd:cd03267 208 LLTSHYMKDIEALARRVLV 226
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-297 |
1.93e-19 |
|
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: 80.91 E-value: 1.93e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 233 VEEQPVRALFRDPHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHGRPTGCLFAPRCGFATVEC 297
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-224 |
2.94e-19 |
|
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: 84.85 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 27 SLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTAKITadrmqFDGQDLRGISARQRrrivgkDMAMIFQEpmSSLNPC 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVL-----INGVDVTAAPPADR------PVSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 106 FTVgFQ---LGETLRVHMglnRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQRVMIAMALACNPKLLIADEPTT 182
Cdd:cd03298 85 LTV-EQnvgLGLSPGLKL---TAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522061013 183 ALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-224 |
2.97e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.37 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITadrmqFDGQDLRGISARQ--RRRivgkdmAMIFQepmsSLN 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-----FAGQPLEAWSAAElaRHR------AYLSQ----QQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 104 PCFTVG-FQLgetLRVHMGLNRKERRQRSI--ELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMAL-----ACNP--K 173
Cdd:PRK03695 80 PPFAMPvFQY---LTLHQPDKTRTEAVASAlnEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522061013 174 LLIADEPTTALDVTiQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:PRK03695 154 LLLLDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
4.07e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISA 80
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL----TPTAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQrrriVGKDMAMIFQEPMSSLNpcFTVgfqlgETLrVHMG----LNR----KERRQRSIE-LLNLVGIPAPEDRLSNfp 151
Cdd:PRK09536 73 RA----ASRRVASVPQDTSLSFE--FDV-----RQV-VEMGrtphRSRfdtwTETDRAAVErAMERTGVAQFADRPVT-- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 152 hQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVA 218
Cdd:PRK09536 139 -SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAA 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-223 |
2.05e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 27 SLACDKGEILSIVGESGSGKSvAMLALM-GLLPwtakITADRMQFDGQDLRGISARQRrrivgkDMAMIFQEpmSSLNPC 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLT----PASGSLTLNGQDHTTTPPSRR------PVSMLFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 106 FTVGFQLGETLRVHMGLNRKERRQRSiELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALD 185
Cdd:PRK10771 86 LTVAQNIGLGLNPGLKLNAAQREKLH-AIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 522061013 186 VTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAER 223
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPR 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-224 |
3.78e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLeIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitadrmqfdGQDLRGISAR 81
Cdd:PRK11247 12 PLL-LNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA----------GELLAGTAPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRivgKDMAMIFQEpmSSLNPCFTVGFQLGETLRVHMglnrkerRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQR 161
Cdd:PRK11247 77 AEAR---EDTRLMFQD--ARLLPWKKVIDNVGLGLKGQW-------RDAALQALAAVGL---ADRANEWPAALSGGQKQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-231 |
5.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLF-RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR 81
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----QPTEGKVTVGDIVVSSTSKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQEPMSSL-NPCFTVGFQLGETlrvHMGLNRKERRQRSIELLNLVGIPapEDRLSNFPHQMSGGMSQ 160
Cdd:PRK13643 77 KEIKPVRKKVGVVFQFPESQLfEETVLKDVAFGPQ---NFGIPKEKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGH 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-214 |
5.80e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDLRGISARQ 82
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVF-----LGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 rrriVGKDMAMIFQEPMS----SLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPapEDRLSNfphqMSGGM 158
Cdd:PRK11231 74 ----LARRLALLPQHHLTpegiTVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLA--DRRLTD----LSGGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDM 214
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDL 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-238 |
7.83e-18 |
|
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: 80.26 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEfqtsSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGlLPwTAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HP-KYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRivgKDMAMIFQEPmsslnPCFTvGFQLGETLR-VHMGLnrkerrqrsiellnlvgipapedrlsnfphqmSGGMSQRV 162
Cdd:cd03217 75 AR---LGIFLAFQYP-----PEIP-GVKNADFLRyVNEGF--------------------------------SGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHdMGVVAE--TAERVQVQYAGQKVEEQPV 238
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH-YQRLLDyiKPDRVHVLYDGRIVKSGDK 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-224 |
1.02e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDLRGISARQ----RRRIvgkdmAMIFQ 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQI-----GMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 97 EPMSSLNPcfTVGFQLGETLRVhMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLI 176
Cdd:PRK10908 87 DHHLLMDR--TVYDNVAIPLII-AGASGDDIRRRVSAALDKVGL---LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 522061013 177 ADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRM 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-234 |
1.10e-17 |
|
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: 83.66 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTveFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:COG4987 332 PSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVgkdmAMIFQEPmsslnPCFTvgfqlgETLR--VHMGlnrkeRRQRS----IELLNLVGIpapEDRLSNFPH--- 152
Cdd:COG4987 406 DLRRRI----AVVPQRP-----HLFD------TTLRenLRLA-----RPDATdeelWAALERVGL---GDWLAALPDgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 --------QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkeQGMALVLITHDMgVVAETAERV 224
Cdd:COG4987 463 twlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRL-AGLERMDRI 539
|
250
....*....|
gi 522061013 225 QVQYAGQKVE 234
Cdd:COG4987 540 LVLEDGRIVE 549
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-262 |
1.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADRMQF-DGQDLRGIsarqrRRIVGkdmaMIFQEPM 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSGIDTgDFSKLQGI-----RKLVG----IVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 100 SSLnpcftvgfqLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNF----PHQMSGGMSQRVMIAMALACNPKLL 175
Cdd:PRK13644 88 TQF---------VGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 176 IADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVaETAERVQVQYAGQKVEEQPVRALFRDPHHPYTAALLA 255
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPP 236
|
....*..
gi 522061013 256 ALPERAK 262
Cdd:PRK13644 237 SLIELAE 243
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-235 |
1.70e-17 |
|
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: 80.28 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 24 DGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQRRRIVGkdmaMIFQEPMssLN 103
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG----LVSQEPV--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 104 PCfTVGFQLGetlrvhMGLNR--KERRQRSIELLNLvgipapEDRLSNFPH-----------QMSGGMSQRVMIAMALAC 170
Cdd:cd03249 90 DG-TIAENIR------YGKPDatDEEVEEAAKKANI------HDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 171 NPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVaETAERVQVQYAGQKVEE 235
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQ 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-231 |
1.73e-17 |
|
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: 78.80 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTveFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR----PTSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMamifQEpmsslnpcftvgfqlgetlrvhmglnrkerrqrsIELL------NLvgipapedrlsnfphqMSGG 157
Cdd:cd03246 75 GDHVGYLP----QD----------------------------------DELFsgsiaeNI----------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAEtAERVQVQYAGQ 231
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-231 |
3.10e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTvefqtSSGlfraVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQ- 82
Cdd:PRK10762 258 LKVDNLS-----GPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVTRSPQDg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 ----------RRRIVGKDMAMIFQEPMSslnpcFTVgfqLGETLRVHMGLNRKERRQ---RSIELLNlVGIPAPEDRLSN 149
Cdd:PRK10762 325 langivyiseDRKRDGLVLGMSVKENMS-----LTA---LRYFSRAGGSLKHADEQQavsDFIRLFN-IKTPSMEQAIGL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 150 fphqMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYA 229
Cdd:PRK10762 396 ----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHE 470
|
..
gi 522061013 230 GQ 231
Cdd:PRK10762 471 GR 472
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
4.18e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSvAMLALMG-LLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLP----PDSGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkdMAMIFQEPmsSLNPCFTVGfQLgetlrVHMG--------LNRKERR--QRSIELLNLVGIpapEDRlsnFPHQ 153
Cdd:COG4604 74 AKR----LAILRQEN--HINSRLTVR-EL-----VAFGrfpyskgrLTAEDREiiDEAIAYLDLEDL---ADR---YLDE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-224 |
5.75e-17 |
|
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: 81.56 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVefqTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQR 83
Cdd:TIGR02857 322 LEFSGVSV---AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVgkdmAMIFQEPmsslnpcftvgFQLGETLRVHMGLNRKE-------RRQRSIELLNLV-GIPAPED-RLSNFPHQM 154
Cdd:TIGR02857 395 RDQI----AWVPQHP-----------FLFAGTIAENIRLARPDasdaeirEALERAGLDEFVaALPQGLDtPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkeQGMALVLITHDMGVVAEtAERV 224
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRI 526
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
6.44e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLAL--MGLLPWTAKITAdRMQFDGQDL--R 76
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEG-RVEFFNQNIyeR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GISARQRRRIVgkdmAMIFQEPmsSLNPcFTVGFQLGETLRVhMGLNRKerrqrsIELLNLV--GIPAPE--DRLSNFPH 152
Cdd:PRK14258 80 RVNLNRLRRQV----SMVHPKP--NLFP-MSVYDNVAYGVKI-VGWRPK------LEIDDIVesALKDADlwDEIKHKIH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 Q----MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQY 228
Cdd:PRK14258 146 KsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
250 260
....*....|....*....|....*..
gi 522061013 229 A-----GQKVEEQPVRALFRDPHHPYT 250
Cdd:PRK14258 226 GnenriGQLVEFGLTKKIFNSPHDSRT 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-235 |
6.56e-17 |
|
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: 78.81 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglFRAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLFRFYDVSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGkdmaMIFQEpmsslnpcfTVGFQlgETLRVHMGLNRKERRQrsIELLNLVGIPAPEDRLSNFPHQ---------- 153
Cdd:cd03253 74 RRAIG----VVPQD---------TVLFN--DTIGYNIRYGRPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgergl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 -MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVAeTAERVQVQYAGQK 232
Cdd:cd03253 137 kLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRI 213
|
...
gi 522061013 233 VEE 235
Cdd:cd03253 214 VER 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-242 |
1.03e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDlrgISA 80
Cdd:PRK11614 3 KVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLCGDPRATSGRIVFDGKD---ITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQepmsslnpcftvGFQLGETLRVHMGL-------NRKERRQRSIELLNLvgIPAPEDRLSNFPHQ 153
Cdd:PRK11614 72 WQTAKIMREAVAIVPE------------GRRVFSRMTVEENLamggffaERDQFQERIKWVYEL--FPRLHERRIQRAGT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
....*....
gi 522061013 234 EEQPVRALF 242
Cdd:PRK11614 217 LEDTGDALL 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-231 |
1.32e-16 |
|
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: 77.58 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQR 83
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIvgkDMAMIFQEPmsSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIPAPEDRLSnfpHQMSGGMSQRVM 163
Cdd:cd03218 73 ARL---GIGYLPQEA--SIFRKLTVEENILAVLEIR-GLSKKEREEKLEELLEEFHITHLRKSKA---SSLSGGERRRVE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 164 IAMALACNPKLLIADEPTTALD----VTIQAQILDLlvrlqKEQGMAlVLIT-HDMGVVAETAERVQVQYAGQ 231
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDpiavQDIQKIIKIL-----KDRGIG-VLITdHNVRETLSITDRAYIIYEGK 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-212 |
1.99e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 25 GVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMqFDGqdlRGISARQRRRIVgkdmAMIFQEPMssLNP 104
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL-LNG---MPIDAKEMRAIS----AYVQQDDL--FIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 105 CFTVGFQLGETLRVHMG--LNRKERRQRSIELLNLVGIPAPEDRLSNFPHQM---SGGMSQRVMIAMALACNPKLLIADE 179
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPrrVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVkglSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|....
gi 522061013 180 PTTALDVTIQAQILDLLVRL-QKeqGMALVLITH 212
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIH 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-210 |
2.27e-16 |
|
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: 76.93 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwTAKITADRMQFDGQDLrgiSARQR 83
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQILFNGQPR---KPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGkdmamiFQEPMSSLNPCFTVGfqlgETLR--VHMGLNR----KERRQR-SIELLNLVGIpapEDRLSNFPHQMSG 156
Cdd:cd03234 80 QKCVA------YVRQDDILLPGLTVR----ETLTytAILRLPRkssdAIRKKRvEDVLLRDLAL---TRIGGNLVKGISG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLI 210
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-212 |
4.98e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 78.67 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKS-VAMLaLMGLLPwtakITADRMQFDGQDLRGISARQRRRIVGkdmaMIFQEPms 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKStLVNL-LLRFYD----PTSGRILIDGVDIRDLTLESLRRQIG----VVPQDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 slnpcftvgFQLGETLRVHMGLNRKER-RQRSIELLNLVGIpapEDRLSNFPHQM-----------SGGMSQRVMIAMAL 168
Cdd:COG1132 424 ---------FLFSGTIRENIRYGRPDAtDEEVEEAAKAAQA---HEFIEALPDGYdtvvgergvnlSGGQRQRIAIARAL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522061013 169 ACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITH 212
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-226 |
5.85e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtsSGLFrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISAR 81
Cdd:PRK11300 4 PLLSVSGLMMRF---GGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QrrrIVGKDMAMIFQ-----EPMSSLnpcftvgfqlgETLRV--HMGLN--------------RKERR--QRSIELLNLV 138
Cdd:PRK11300 76 Q---IARMGVVRTFQhvrlfREMTVI-----------ENLLVaqHQQLKtglfsgllktpafrRAESEalDRAATWLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 139 GIPAPEDRLSNfphQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVA 218
Cdd:PRK11300 142 GLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM 218
|
....*...
gi 522061013 219 ETAERVQV 226
Cdd:PRK11300 219 GISDRIYV 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-231 |
6.25e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitaDRMQFDGQDLRGISA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRivgKDMAMIFQEPmsSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSnfpHQMSGGMSQ 160
Cdd:PRK10895 73 HARAR---RGIGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGERR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-231 |
6.92e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEfqtssGlFRavdGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISAR 81
Cdd:PRK15439 267 PVLTVEDLTGE-----G-FR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRP----ARGGRIMLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QR-----------RRIVGkdmamIFQEPMSSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIellnlvGIpapedRLSNf 150
Cdd:PRK15439 334 QRlarglvylpedRQSSG-----LYLDAPLAWNVCALTHNRRGFWIKPARENAVLERYRRAL------NI-----KFNH- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 PHQ----MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERVQV 226
Cdd:PRK15439 397 AEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLV 475
|
....*
gi 522061013 227 QYAGQ 231
Cdd:PRK15439 476 MHQGE 480
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-220 |
8.00e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtakITAD--RMQFDGQDLRGI 78
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGL------VKPDsgRIFLDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 SARQRRRivgkdMAMIF--QEPmsSLnpcF---TVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQ 153
Cdd:COG1137 71 PMHKRAR-----LGIGYlpQEA--SI---FrklTVEDNILAVLELR-KLSKKEREERLEELLEEFGI---THLRKSKAYS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALD---VT-IQAQILDLlvrlqKEQGMAlVLIT-HDmgvVAET 220
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIG-VLITdHN---VRET 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-235 |
1.03e-15 |
|
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: 75.34 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQR 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGkdmaMIFQEPmsslnpcftvgFQLGETLRVHMGLNR----KERRQRSIELLNLvgipapEDRLSNFPH------- 152
Cdd:cd03251 75 RRQIG----LVSQDV-----------FLFNDTVAENIAYGRpgatREEVEEAARAANA------HEFIMELPEgydtvig 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 ----QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgMALVlITHDMGVVaETAERVQVQY 228
Cdd:cd03251 134 ergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTI-ENADRIVVLE 210
|
....*..
gi 522061013 229 AGQKVEE 235
Cdd:cd03251 211 DGKIVER 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-224 |
1.24e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtakITADRMQFDGQDLRGISARQ 82
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTVQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVG---KDMAM---IFQE-----PMSSLNPCFtVGfQLGET--LRVHMGLNRKERRQRSIELLNLVGipapedrLSN 149
Cdd:PRK09984 74 EGRLARdirKSRANtgyIFQQfnlvnRLSVLENVL-IG-ALGSTpfWRTCFSWFTREQKQRALQALTRVG-------MVH 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 150 FPHQ----MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:PRK09984 145 FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERI 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-245 |
1.39e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 33 GEILSIVGESGSGKS-VAMLALMGLLPWTAKITadrmqFDGQDLRGISARQRRRIVgkdmAMIFQEPmsslnpcftVGFQ 111
Cdd:TIGR00958 507 GEVVALVGPSGSGKStVAALLQNLYQPTGGQVL-----LDGVPLVQYDHHYLHRQV----ALVGQEP---------VLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 112 LGETLRVHMGLNRKERRqrsiELLNLVGIPAPEDRLSNFPH-----------QMSGGMSQRVMIAMALACNPKLLIADEP 180
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDE----EIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 181 TTALDVTIQAqildLLVRLQKEQGMALVLITHDMGVVaETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:TIGR00958 645 TSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-231 |
1.52e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLFRaVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP--WTAKITadrmqFDGQDLR----- 76
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKR-VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIF-----IDGKPVKirnpq 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 -----GISA----RQRRRIVgKDMAMIFQEPMSSLNPcFTvgfqlgetlrvHMGLNRKERRQRSI--ELLNL-VGIPAPE 144
Cdd:PRK13549 334 qaiaqGIAMvpedRKRDGIV-PVMGVGKNITLAALDR-FT-----------GGSRIDDAAELKTIleSIQRLkVKTASPE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 145 DRLSNfphqMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERV 224
Cdd:PRK13549 401 LAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRV 475
|
....*..
gi 522061013 225 QVQYAGQ 231
Cdd:PRK13549 476 LVMHEGK 482
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-212 |
3.46e-15 |
|
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: 72.97 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQ--TSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwTAKITADRMqFDGQDLrgiSAR 81
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVL-INGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGkdmaMIFQEPMssLNPCFTVGfqlgETLRVHMGLnrkerrqRSIellnlvgipapedrlsnfphqmSGGMSQR 161
Cdd:cd03213 79 SFRKIIG----YVPQDDI--LHPTLTVR----ETLMFAAKL-------RGL----------------------SGGERKR 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLITH 212
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIH 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-233 |
7.46e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL-LPWTAKITADRMQFDGQDLRgISA 80
Cdd:PRK09700 4 PYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINYNKLDHK-LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIfqEPMSSLNPCFtVGFQLgeTLRVhMGLN---RKERRQRSIELLNLVGIPA-PEDRLSNfphqMSG 156
Cdd:PRK09700 79 QLGIGIIYQELSVI--DELTVLENLY-IGRHL--TKKV-CGVNiidWREMRVRAAMMLLRVGLKVdLDEKVAN----LSI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-233 |
8.13e-15 |
|
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: 72.24 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtaKITADRMQFDGQDLRGISARQRRRIVGkdmaMIFQEPM-- 99
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLDPADLRRNIG----YVPQDVTlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 100 -SSLNPCFTVGFQLGETLRVhmglnrkerrqrsIELLNLVGIpapEDRLSNFPH-----------QMSGGMSQRVMIAMA 167
Cdd:cd03245 91 yGTLRDNITLGAPLADDERI-------------LRAAELAGV---TDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 168 LACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITHDMGVVaETAERVQVQYAGQKV 233
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-212 |
8.18e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEfqtssglfraVD------GVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWtaKITADRMQFDGQDLRG 77
Cdd:COG0396 1 LEIKNLHVS----------VEgkeilkGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKY--EVTSGSILLDGEDILE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQRRRivgKDMAMIFQEPMSslnpcftV-GFQLGETLRVHMGLNRKER------RQRSIELLNLVGIPapEDRLS-- 148
Cdd:COG0396 69 LSPDERAR---AGIFLAFQYPVE-------IpGVSVSNFLRTALNARRGEElsarefLKLLKEKMKELGLD--EDFLDry 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 149 ---NFphqmSGGMSQRVMIAMALACNPKLLIADEPTTALDvtIQA-QILDLLVRLQKEQGMALVLITH 212
Cdd:COG0396 137 vneGF----SGGEKKRNEILQMLLLEPKLAILDETDSGLD--IDAlRIVAEGVNKLRSPDRGILIITH 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-235 |
1.13e-14 |
|
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: 72.52 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQRRRIVGkdmaMIFQEPMss 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV----PENGRVLVDGHDLALADPAWLRRQVG----VVLQENV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 lnpcftvgfQLGETLRVHMGLNRKE-RRQRSIELLNLVGipaPEDRLSNFPH-----------QMSGGMSQRVMIAMALA 169
Cdd:cd03252 87 ---------LFNRSIRDNIALADPGmSMERVIEAAKLAG---AHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 170 CNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVaETAERVQVQYAGQKVEE 235
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQ 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-234 |
1.65e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQ 82
Cdd:PRK13657 334 AVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRivgkDMAMIFQEPMsSLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELlnlvgIPAPEDRLSNFP----HQMSGGM 158
Cdd:PRK13657 407 LRR----NIAVVFQDAG-LFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF-----IERKPDGYDTVVgergRQLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVAEtAERVQVQYAGQKVE 234
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-233 |
2.00e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 24 DGVSLACDKGEILSIVGESGSGKSvAMLALMG--LLPWTAKItadrmQFDGQDLRGISaRQRRRIVGKDMAMIFQEpmSS 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKT-TLLRLIGgqIAPDHGEI-----LFDGENIPAMS-RSRLYTVRKRMSMLFQS--GA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 LNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLsnfPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 522061013 182 TALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVqYAGQKV 233
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYI-VADKKI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-219 |
2.01e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitadrmqfdgqdlrGISARQRRRIVgkdmAMIFQEpmSS 101
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS---------------GTVRRAGGARV----AYVPQR--SE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 LNPCFTVgfqlgeTLR--VHMGL---------NRKERRQRSIELLNLVGIpapeDRLSNFP-HQMSGGMSQRVMIAMALA 169
Cdd:NF040873 66 VPDSLPL------TVRdlVAMGRwarrglwrrLTRDDRAAVDDALERVGL----ADLAGRQlGELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522061013 170 CNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAE 219
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRR 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-231 |
2.74e-14 |
|
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: 73.32 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLFRaVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP--WTAKITADRMQFDGQD-LRGIS 79
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKR-VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKPVDIRNpAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 A--------RQRRRIVgkdmamifqepmsslnPCFTVGFQLgeTLRVhmgLNRKERRQRSIELLNLVGIPAPEDRLS--- 148
Cdd:TIGR02633 336 AgiamvpedRKRHGIV----------------PILGVGKNI--TLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKvkt 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 149 ---NFP-HQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERV 224
Cdd:TIGR02633 395 aspFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRV 473
|
....*..
gi 522061013 225 QVQYAGQ 231
Cdd:TIGR02633 474 LVIGEGK 480
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-252 |
4.22e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLA---LMGLLPwTAKITAdRMQFDGQDL--RG 77
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIP-GFRVEG-KVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 78 ISARQRRRIVGkdmaMIFQEPmsslNP---------CFTV---GFQ--LGETLrvhmglnrkERRQRSIELLNLVgipap 143
Cdd:PRK14243 84 VDPVEVRRRIG----MVFQKP----NPfpksiydniAYGArinGYKgdMDELV---------ERSLRQAALWDEV----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 144 EDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQgMALVLITHDMGVVAETAE- 222
Cdd:PRK14243 142 KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQ-YTIIIVTHNMQQAARVSDm 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 522061013 223 ----RVQVQYAGQK----VEEQPVRALFRDPHHPYTAA 252
Cdd:PRK14243 220 taffNVELTEGGGRygylVEFDRTEKIFNSPQQQATRD 257
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-212 |
7.77e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVefQTSSGlfRA-VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPW-TAKITadrmqfdgqdlrgisar 81
Cdd:COG4178 363 LALEDLTL--RTPDG--RPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIA----------------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 qrrRIVGKDMAMIFQEPMsslnpcftvgFQLGeTLR---VHMGLNRKERRQRSIELLNLVGIPAPEDRLS---NFPHQMS 155
Cdd:COG4178 422 ---RPAGARVLFLPQRPY----------LPLG-TLRealLYPATAEAFSDAELREALEAVGLGHLAERLDeeaDWDQVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrLQKEQGMALVLITH 212
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-245 |
9.70e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDLRGISARQRRRIVgkdmAMIFQE-PMSSlnp 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKST----LLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV----AYLPQQlPAAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 105 cftvGFQLGETLRV-----HMGLNR--KERRQRSIELLNLVGIPAPEDRLSNfphQMSGGMSQRVMIAMALACNPKLLIA 177
Cdd:PRK10575 99 ----GMTVRELVAIgrypwHGALGRfgAADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 178 DEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRDP 245
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-244 |
1.35e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtsSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLR--GIS 79
Cdd:PRK10762 3 ALLQLKGIDKAF---PGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT----RDAGSILYLGKEVTfnGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRIvgkdmAMIFQEpmssLN--PCFTVG---FqLGETLRVHMG-LNRKERRQRSIELLNLVGIPAPEDRLSNfphQ 153
Cdd:PRK10762 75 SSQEAGI-----GIIHQE----LNliPQLTIAeniF-LGREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVG---E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKV 233
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
250
....*....|.
gi 522061013 234 EEQPVRALFRD 244
Cdd:PRK10762 221 AEREVADLTED 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-213 |
1.41e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENltVEFQTSSGLFraVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDLRGISA 80
Cdd:PRK10247 6 PLLQLQN--VGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLL-----FEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVgkdmAMIFQEPMsslnpcftvgfQLGETLRVHMGLN---RKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGG 157
Cdd:PRK10247 77 EIYRQQV----SYCAQTPT-----------LFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFALPDTILTKNIAELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 158 MSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-222 |
1.42e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitadrmqfdgqdlrGISA 80
Cdd:PRK09544 2 TSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE---------------GVIK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDMAMIFQEPmsslnpcfTVGFQLGETLRVHMGLNRKE-----RRQRSIELLNlvgipAPEDRLSnfphqms 155
Cdd:PRK09544 63 RNGKLRIGYVPQKLYLDT--------TLPLTVNRFLRLRPGTKKEDilpalKRVQAGHLID-----APMQKLS------- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVV-AETAE 222
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-224 |
1.87e-13 |
|
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: 68.71 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGL------------------FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KIT 64
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSgTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 65 adrmqfdgqdlrgisarqrrrIVGKDMAMIFqepmsslnpcFTVGFQLGETLR-------VHMGLNRKERRQRSIELLNL 137
Cdd:cd03220 81 ---------------------VRGRVSSLLG----------LGGGFNPELTGReniylngRLLGLSRKEIDEKIDEIIEF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 138 VGIPAPEDR-LSNFphqmSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvRLQKEQGMALVLITHDMGV 216
Cdd:cd03220 130 SELGDFIDLpVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSS 204
|
....*...
gi 522061013 217 VAETAERV 224
Cdd:cd03220 205 IKRLCDRA 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-235 |
3.79e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADRMQFDGQdlrgisARQRRRIVGkdmaMIFQepMSS 101
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKITVLGVPVPAR------ARLARARIG----VVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 LNPCFTVGfqlgETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:PRK13536 125 LDLEFTVR----ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522061013 182 TALDVTIQAQILDLLvRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEE 235
Cdd:PRK13536 201 TGLDPHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-241 |
4.87e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGiSARQRRRIVGkdmaMIFQepMSSL 102
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVPS-RARHARQRVG----VVPQ--FDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVGfqlgETLRV---HMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADE 179
Cdd:PRK13537 92 DPDFTVR----ENLLVfgrYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 180 PTTALDVTIQAQILDLLVRLQKeQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRAL 241
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-235 |
6.31e-13 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 67.25 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWT-AKITadrmqFDGQDLRGISARQRRRIVGkdmaMIFQEPms 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQIL-----IDGIDIRDISRKSLRSMIG----VVLQDT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 slnpcftvgFQLGETLRVHMGLNRKE-RRQRSIELLNLVGIpapEDRLSNFP-----------HQMSGGMSQRVMIAMAL 168
Cdd:cd03254 87 ---------FLFSGTIMENIRLGRPNaTDEEVIEAAKEAGA---HDFIMKLPngydtvlgengGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 169 ACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqGMALVLITHDMGVVAEtAERVQVQYAGQKVEE 235
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-279 |
1.28e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFqtsSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL-LPwtakiTADRMQFDGQDLRGIS 79
Cdd:PRK11288 2 SPYLSFDGIGKTF---PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQP-----DAGSILIDGQEMRFAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRrriVGKDMAMIFQEpmSSLNPCFTVG--FQLGEtLRVHMG-LNRKERRQRSIELLNLVGIPA-PEDRLSNfphqMS 155
Cdd:PRK11288 73 TTAA---LAAGVAIIYQE--LHLVPEMTVAenLYLGQ-LPHKGGiVNRRLLNYEAREQLEHLGVDIdPDTPLKY----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTiQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEe 235
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAR-EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 522061013 236 qpvralfrdpHHPYTAALLAALPERAKVGQRLPSIAGVVPGQHG 279
Cdd:PRK11288 221 ----------TFDDMAQVDRDQLVQAMVGREIGDIYGYRPRPLG 254
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-231 |
1.28e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 15 TSSGLFRAVD-----GVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITadrmqFDGQDL----RGISA-RQR 83
Cdd:PRK13638 4 TSDLWFRYQDepvlkGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVL-----WQGKPLdyskRGLLAlRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 rrivgkdMAMIFQEPMSSLnpCFT-VGFQLGETLRvHMGLNRKERRQRSIELLNLVGIpapedrlSNFPHQ----MSGGM 158
Cdd:PRK13638 79 -------VATVFQDPEQQI--FYTdIDSDIAFSLR-NLGVPEAEITRRVDEALTLVDA-------QHFRHQpiqcLSHGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 159 SQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQkEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-231 |
2.23e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 35 ILSIVGESGSGKSVAMLALMGLL-PWTAKIT-ADRMQFDGQdlRGIS-ARQRRRIvgkdmAMIFQEpmSSLNPCFTVGFQ 111
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTrPQKGRIVlNGRVLFDAE--KGIClPPEKRRI-----GYVFQD--ARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 112 LgetlrvHMGLNRKERRQ--RSIELLnlvGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQ 189
Cdd:PRK11144 97 L------RYGMAKSMVAQfdKIVALL---GI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522061013 190 AQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-231 |
2.43e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTvefQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISA 80
Cdd:PRK11650 1 MAGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRrrivgkDMAMIFQEpmSSLNPCFTVGFQLGETLRVHmGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQ 160
Cdd:PRK11650 74 ADR------DIAMVFQN--YALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILEL---EPLLDRKPRELSGGQRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMgVVAET-AERVQVQYAGQ 231
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ-VEAMTlADRVVVMNGGV 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-226 |
3.77e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTvefqtsSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGllpwTAKITADRMQFDGQDlrgISAR 81
Cdd:PRK09700 264 TVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG----VDKRAGGEIRLNGKD---ISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAMIFQepmSSLNPCFTVGFQLGETLRVH-----------MGL--NRKERR--QRSIELLNLvGIPAPEDR 146
Cdd:PRK09700 331 SPLDAVKKGMAYITE---SRRDNGFFPNFSIAQNMAISrslkdggykgaMGLfhEVDEQRtaENQRELLAL-KCHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 147 LSnfphQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQV 226
Cdd:PRK09700 407 IT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAV 481
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
7.97e-12 |
|
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: 65.84 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTSSglfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKITADrmQFDGQDLRGISA 80
Cdd:TIGR02868 333 PTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQGEVTLD--GVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRRIVGKDmAMIFqepmsslnpcftvgfqlGETLRVHMGLNRKERRQRSI-ELLNLVG----IPAPEDRLSNFPHQM- 154
Cdd:TIGR02868 408 RRRVSVCAQD-AHLF-----------------DTTVRENLRLARPDATDEELwAALERVGladwLRALPDGLDTVLGEGg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 155 ---SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrLQKEQGMALVLITHD 213
Cdd:TIGR02868 470 arlSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-234 |
8.88e-12 |
|
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: 63.59 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWtakiTADRMQFDGQDLRGISARQR 83
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA----EEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRivgkDMAMIFQEPM-------SSLNPcftvgF------QLGETLRVHMGlnrkerrqrsieLLNLvgipapedrlsnf 150
Cdd:cd03369 81 RS----SLTIIPQDPTlfsgtirSNLDP-----FdeysdeEIYGALRVSEG------------GLNL------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 151 phqmSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDlLVRlQKEQGMALVLITHDMGVVAETAeRVQVQYAG 230
Cdd:cd03369 127 ----SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK-TIR-EEFTNSTILTIAHRLRTIIDYD-KILVMDAG 199
|
....
gi 522061013 231 QKVE 234
Cdd:cd03369 200 EVKE 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-223 |
1.16e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 5 EIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWT---AKItadrmqFdGQ--DLRGIS 79
Cdd:NF033858 268 EARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASegeAWL------F-GQpvDAGDIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRrriVGKdmamifqepMSSlnpcftvGFQLGETLRVH---------MGLNRKERRQRSIELLNLVGIPAPEDRLsnf 150
Cdd:NF033858 337 TRRR---VGY---------MSQ-------AFSLYGELTVRqnlelharlFHLPAAEIAARVAEMLERFDLADVADAL--- 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 151 PHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGvvaEtAER 223
Cdd:NF033858 395 PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN---E-AER 463
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-224 |
3.03e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEfQTSSGLFravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLrgisaRQR 83
Cdd:cd03231 1 LEADELTCE-RDGRALF---SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP----PLAGRVLLNGGPL-----DFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMAMIFQEP--MSSLNPCftvgfqlgETLRVHMGLNRKERRQrsiELLNLVGIPAPEDRLSnfpHQMSGGMSQR 161
Cdd:cd03231 68 RDSIARGLLYLGHAPgiKTTLSVL--------ENLRFWHADHSDEQVE---EALARVGLNGFEDRPV---AQLSAGQQRR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 162 VMIAMALACNPKLLIADEPTTALDVTIQAQILDlLVRLQKEQGMALVLITH-DMGVVAETAERV 224
Cdd:cd03231 134 VALARLLLSGRPLWILDEPTTALDKAGVARFAE-AMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-230 |
5.92e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.74 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLlpwtAKITADRMQFDGQDLRGISARQRRriVGkdmaMIFQEpmSSLNPC 105
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGL----EDITSGDLFIGEKRMNDVPPAERG--VG----MVFQS--YALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 106 FTVGFQLGETLRVhMGLNRKERRQR---SIELLNLVGIpapedrLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTT 182
Cdd:PRK11000 90 LSVAENMSFGLKL-AGAKKEEINQRvnqVAEVLQLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 522061013 183 ALDVTIQAQILDLLVRLQKEQGMALVLITHDMgVVAET-AERVQVQYAG 230
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQ-VEAMTlADKIVVLDAG 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-212 |
6.07e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 23 VDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLP---WTAKITADRMQFDGQDLRgisarqRRRIVGKDmamifqepm 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTKQILK------RTGFVTQD--------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 100 SSLNPCFTVGFQL--GETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRL--SNFPHQMSGGMSQRVMIAMALACNPKLL 175
Cdd:PLN03211 149 DILYPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*..
gi 522061013 176 IADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITH 212
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
152-213 |
6.28e-11 |
|
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: 59.77 E-value: 6.28e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 152 HQMSGGMSQRVMIAMALACNPKLLIADEPTTALDV-TIQAqildLLVRLQKEQGmALVLITHD 213
Cdd:cd03221 69 EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALKEYPG-TVILVSHD 126
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-210 |
6.73e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 12 EFQTSSGLFRAVDGVSLACDK-----GEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQRRRI 86
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSltlnaGDSWAFVGANGSGKSALARALAGELP----LLSGERQSQFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 87 VgkdmAMIFQE---PMSSLNPCFTvgfqlGETLRvHMGLNRKERRQRSIELLNLVGIPAPEDRlsNFPHqMSGGMSQRVM 163
Cdd:PRK10938 79 V----SDEWQRnntDMLSPGEDDT-----GRTTA-EIIQDEVKDPARCEQLAQQFGITALLDR--RFKY-LSTGETRKTL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeQGMALVLI 210
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLV 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-223 |
7.17e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRgiSARQRRRiVGKDMAMIFQepms 100
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAGARKIQQGRVEVLGGDMA--DARHRRA-VCPRIAYMPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 slnpcftvGfqLGE----TLRVH---------MGLNRKERRQRSIELLNLVGipapedrLSNFPH----QMSGGMSQRVM 163
Cdd:NF033858 84 --------G--LGKnlypTLSVFenldffgrlFGQDAAERRRRIDELLRATG-------LAPFADrpagKLSGGMKQKLG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQ-GMALVLITHDMgvvaETAER 223
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYM----EEAER 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-246 |
8.88e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWT-----AKITADrMQFDGQDLRGISARQ--RRRIV---GKD 90
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgARVTGD-VTLNGEPLAAIDAPRlaRLRAVlpqAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 91 MAMIFQEPMSSLNPCFTVGFQLGETlrvhmglnrkERRQRSI--ELLNLVGIPAPEDRLSNfphQMSGGMSQRVMIAMAL 168
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGAL----------THRDGEIawQALALAGATALVGRDVT---TLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 169 A---------CNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVR 239
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....*..
gi 522061013 240 ALFRDPH 246
Cdd:PRK13547 241 DVLTPAH 247
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
154-214 |
9.25e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 9.25e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDM 214
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-212 |
1.01e-10 |
|
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: 59.47 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVefQTSSGLFRaVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPW-TAKITadrmqfdgqdlrgisarq 82
Cdd:cd03223 1 IELENLSL--ATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIG------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 rrRIVGKDMAMIFQEPMsslnpcFTVGfqlgeTLRvhmglnrkerrqrsiELLNLvgipaPEDRlsnfphQMSGGMSQRV 162
Cdd:cd03223 60 --MPEGEDLLFLPQRPY------LPLG-----TLR---------------EQLIY-----PWDD------VLSGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522061013 163 MIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrlqKEQGMALVLITH 212
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-226 |
1.36e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.56 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 11 VEFQTSSGLFR------AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQRR 84
Cdd:cd03248 12 VKFQNVTFAYPtrpdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 85 RIVgkdmAMIFQEPM---SSLNPCFTVGFQLGETLRVhmglnrKERRQRSIELLNLVGIP-APEDRLSNFPHQMSGGMSQ 160
Cdd:cd03248 88 SKV----SLVGQEPVlfaRSLQDNIAYGLQSCSFECV------KEAAQKAHAHSFISELAsGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 161 RVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrLQKEQGMALVLITHDMGVVaETAERVQV 226
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQAL--YDWPERRTVLVIAHRLSTV-ERADQILV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-217 |
2.65e-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: 58.91 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEfqtsSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRgisarQR 83
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR----PDSGEVRWNGTPLA-----EQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMAMIFQEPmsSLNPCFTVGfqlgETLRVHMGLNRKERRQRSiELLNLVGIPAPEDRLSnfpHQMSGGMSQRVM 163
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLKPELSAL----ENLHFWAAIHGGAQRTIE-DALAAVGLTGFEDLPA---AQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQiLDLLVRLQKEQGMALVLITH-DMGVV 217
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVAL-LAGLLRAHLARGGIVLLTTHqDLGLV 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-264 |
5.15e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSvamlALMGLLPWTAKITADRMQFDGQDLRGISARQ--RRRIV-----GKDMAMIfqep 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaiRAGIMlcpedRKAEGII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 99 msslnPCFTVGFQLGETLRVH---MGL---NRKERR--QRSIELLNlVGIPAPEDRLSNfphqMSGGMSQRVMIAMALAC 170
Cdd:PRK11288 344 -----PVHSVADNINISARRHhlrAGClinNRWEAEnaDRFIRSLN-IKTPSREQLIMN----LSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 171 NPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPvRALFrDPHhpyt 250
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA-REQA-TER---- 486
|
250
....*....|....
gi 522061013 251 AALLAALPERAKVG 264
Cdd:PRK11288 487 QALSLALPRTSAAV 500
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-219 |
8.30e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakitadRMQFDGQDLRGISARQRRRivgkdMAMIFQEPMSS 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---------RLASGKISILGQPTRQALQ-----KNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 -LNPCFTVgfqLGETLRV-----HMGLNR---KERRQRSIELLNLVGipapedrLSNFPH----QMSGGMSQRVMIAMAL 168
Cdd:PRK15056 88 eVDWSFPV---LVEDVVMmgrygHMGWLRrakKRDRQIVTAALARVD-------MVEFRHrqigELSGGQKKRVFLARAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522061013 169 ACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAE 219
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTE 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-196 |
9.87e-10 |
|
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: 57.89 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTA-KITadrmqFDGQDLRGISARQ 82
Cdd:cd03244 3 IEFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSgSIL-----IDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 -RRRIvgkdmAMIFQEPM-------SSLNPC--FTVGfQLGETL-RVHMglnrKERRQRSIELLNLVgipaPEDRLSNFp 151
Cdd:cd03244 76 lRSRI-----SIIPQDPVlfsgtirSNLDPFgeYSDE-ELWQALeRVGL----KEFVESLPGGLDTV----VEEGGENL- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 522061013 152 hqmSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLL 196
Cdd:cd03244 141 ---SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-220 |
1.66e-09 |
|
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: 58.99 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPL------LEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQD 74
Cdd:COG4618 322 MPLprpkgrLSVENLTVVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP----PTAGSVRLDGAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 75 LRGISARQRRRIVG---KDMAMI----------FQEPmsslnpcftvgfqlgetlrvhmglnrkeRRQRSIELLNLVGIp 141
Cdd:COG4618 396 LSQWDREELGRHIGylpQDVELFdgtiaeniarFGDA----------------------------DPEKVVAAAKLAGV- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 142 apEDRLSNFP-----------HQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLI 210
Cdd:COG4618 447 --HEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVI 523
|
250
....*....|
gi 522061013 211 THDMGVVAET 220
Cdd:COG4618 524 THRPSLLAAV 533
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-241 |
1.84e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqtssGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLAL------MGLLPWTAKI-TADRmqfdgqdlr 76
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAhv*gpdAGRRPWRF*TwCANR--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 gisaRQRRRIVGKDMAMIF--QEPMSSLNPCFTVGFQLGetlrvhmgLNRKERRQRSIELLNLVGIPAPEDRLSNfphQM 154
Cdd:NF000106 81 ----RALRRTIG*HRPVR*grRESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAA---KY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDlLVRLQKEQGMALVLITHDMGVVAETAERVQVQYAGQKVE 234
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWD-EVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
....*..
gi 522061013 235 EQPVRAL 241
Cdd:NF000106 225 DGKVDEL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-231 |
2.89e-09 |
|
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: 58.49 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPLLEIENLTVEFQTSSGlfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAkitadrmqfdGQDLRGisa 80
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS----------GTVLVG--- 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 rqrrrivGKDMAMIFQEPMSSLNPC--FTVGFQ---LGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSNFPHQMS 155
Cdd:TIGR01257 991 -------GKDIETNLDAVRQSLGMCpqHNILFHhltVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLS 1063
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrLQKEQGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:TIGR01257 1064 GGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-212 |
5.81e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVefqTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADrmqfdGQDLRGISARQR 83
Cdd:PRK11174 350 IEAEDLEI---LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIN-----GIELRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRivgkDMAMIFQEPmsslnpcftvgfQLGE-TLRVHMGLNRKERRQRSIE-LLNLVGIpapedrlSNFPHQM------- 154
Cdd:PRK11174 422 RK----HLSWVGQNP------------QLPHgTLRDNVLLGNPDASDEQLQqALENAWV-------SEFLPLLpqgldtp 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 155 --------SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITH 212
Cdd:PRK11174 479 igdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH 542
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-212 |
7.85e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 8 NLTVEFQTSSGLF---------RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADRMQFD--GQDLR 76
Cdd:COG2401 22 DLSERVAIVLEAFgvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNqfGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GISArqrrriVGKDmamifqepmsslnpcftvgfqlGETLRVhmglnrkerrqrsIELLNLVGIPAPEDRLSNFPHqMSG 156
Cdd:COG2401 102 LIDA------IGRK----------------------GDFKDA-------------VELLNAVGLSDAVLWLRRFKE-LST 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 157 GMSQRVMIAMALACNPKLLIADEPTTALDVTiQAQILDLLV-RLQKEQGMALVLITH 212
Cdd:COG2401 140 GQKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARNLqKLARRAGITLVVATH 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-235 |
1.00e-08 |
|
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: 54.24 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLpwtakitadrmqfdgqdLRGISARQR 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKS----TLLQLL-----------------TGDLKPQQG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVGKDMAMIFQEPMSSLnpcFTVGFQlgetlRVHMglnrkerrqRSIELLNLVGIpapedrlsnfphQMSGGMSQRVM 163
Cdd:cd03247 58 EITLDGVPVSDLEKALSSL---ISVLNQ-----RPYL---------FDTTLRNNLGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 164 IAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITHDMGVVaETAERVQVQYAGQKVEE 235
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGI-EHMDKILFLENGKIIMQ 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
2.27e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 6 IENLTVEFQTSSgLFravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtakiTADrmqfDGQdlrgISARQRRR 85
Cdd:COG0488 1 LENLSKSFGGRP-LL---DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL------EPD----SGE----VSIPKGLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 86 IvgkdmAMIFQEPmsSLNPCFTVgfqLGETLRVHMGLNRKERRQRSIE-------------------------------- 133
Cdd:COG0488 63 I-----GYLPQEP--PLDDDLTV---LDTVLDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweaeara 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 134 --LLNLVGIP-APEDR-LSNFphqmSGGMSQRVMIAMALACNPKLLIADEPTTALDV-TIQaqildLLVR-LQKEQGmAL 207
Cdd:COG0488 133 eeILSGLGFPeEDLDRpVSEL----SGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEfLKNYPG-TV 202
|
....*.
gi 522061013 208 VLITHD 213
Cdd:COG0488 203 LVVSHD 208
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-212 |
2.75e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLtvefQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWtaKITADRMQFDGQDLRGISAR 81
Cdd:CHL00131 6 PILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAY--KILEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIvGKDMAmiFQEPMSslnpcfTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSN----FPHQ---- 153
Cdd:CHL00131 80 ERAHL-GIFLA--FQYPIE------IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGmdpsFLSRnvne 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 154 -MSGGMSQRVMI-AMALAcNPKLLIADEPTTALDV---TIQAQILDLLVRLQKeqgmALVLITH 212
Cdd:CHL00131 151 gFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITH 209
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-212 |
3.78e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWtaKITADRMQFDGQDLRGISARQ 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAIL----RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RrriVGKDMAMIFQEPMSSlnPCFTVGFQLGETLRVhmglNRKERRQRSIELLNLVGIPAPEDRLSNFPHQM-------- 154
Cdd:PRK09580 75 R---AGEGIFMAFQYPVEI--PGVSNQFFLQTALNA----VRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvg 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 155 -SGGMSQRVMIAMALACNPKLLIADEPTTALDVTiQAQILDLLVRLQKEQGMALVLITH 212
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-212 |
4.33e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 25 GVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQDLRGISARQRRRIVGKDMAMifqEPMSSL-- 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP----PAAGTIKLDGGDIDDPDVAEACHYLGHRNAM---KPALTVae 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 NPCFTVGFQLGETLRVHMGLNRkerrqrsIELLNLVGIPApedrlsnfpHQMSGGMSQRVMIAMALACNPKLLIADEPTT 182
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEA-------VGLAPLAHLPF---------GYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 522061013 183 ALDVTIQAQILDlLVRLQKEQGMALVLITH 212
Cdd:PRK13539 157 ALDAAAVALFAE-LIRAHLAQGGIVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-224 |
4.82e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.16 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQ------------------TSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvAMLALM-GLLPWTakit 64
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIaGILEPT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 65 adrmqfdgqdlRGiSARQRRRIVgkdmAMIfqEPMSSLNPCFTvGFQ---LGETLrvhMGLNRKERRQRsiellnlvgip 141
Cdd:COG1134 80 -----------SG-RVEVNGRVS----ALL--ELGAGFHPELT-GREniyLNGRL---LGLSRKEIDEK----------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 142 apEDR------LSNFPHQ----MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLIT 211
Cdd:COG1134 127 --FDEivefaeLGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVS 203
|
250
....*....|...
gi 522061013 212 HDMGVVAETAERV 224
Cdd:COG1134 204 HSMGAVRRLCDRA 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-225 |
6.28e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEfqtsSG---LFRavdGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKItadrmQFDGQDLRgi 78
Cdd:PRK13538 1 MLEARNLACE----RDeriLFS---GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEV-----LWQGEPIR-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 79 saRQRrrivgkdmamifQEPMSSLnpcFTVGFQLG--------ETLRVHMGLNRKERRQRSIELLNLVGIPAPEDRLSnf 150
Cdd:PRK13538 67 --RQR------------DEYHQDL---LYLGHQPGikteltalENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPV-- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 151 pHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMAlVLITH-DMGVVAETAERVQ 225
Cdd:PRK13538 128 -RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHqDLPVASDKVRKLR 201
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
37-235 |
7.73e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.57 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 37 SIVGESGSGKSVAMLALMGLLPWtakiTADRMQFDGQDLRGISARQRRRIVgkdmAMIFQEPMSslnpcftvgfqLGETL 116
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPL----TEGEIRLDGRPLSSLSHSVLRQGV----AMVQQDPVV-----------LADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 117 RVHMGLNRKERRQRSIELLNLVgipapedRLSNFPHQMSGGM-------------SQRVMIAMA--LACNPKLLIADEPT 181
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETV-------QLAELARSLPDGLytplgeqgnnlsvGQKQLLALArvLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522061013 182 TALDVTIQAQILDLLvRLQKEQgMALVLITHDMGVVAEtAERVQVQYAGQKVEE 235
Cdd:PRK10790 505 ANIDSGTEQAIQQAL-AAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-212 |
7.81e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.68 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENltVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSvamlALMGLLP--WTAkiTADRMQFDGQDLRGIS 79
Cdd:PRK11160 337 VSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTraWDP--QQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 80 ARQRRRivgkdmamifqepmsslnpCFTVGFQ----LGETLRVHMGL-NRKERRQRSIELLNLVGIpapEDRLSNFP--- 151
Cdd:PRK11160 409 EAALRQ-------------------AISVVSQrvhlFSATLRDNLLLaAPNASDEALIEVLQQVGL---EKLLEDDKgln 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 152 -------HQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLvrLQKEQGMALVLITH 212
Cdd:PRK11160 467 awlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITH 532
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-244 |
1.10e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 21 RAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLpwtAKITADrMQFDGQDLRGISARQrrrIVGKDMAMIFQEPMS 100
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY---QKDSGS-ILFQGKEIDFKSSKE---ALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 101 SLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELLNLVGIPA-PEDRLSNFP-HQMsggmsQRVMIAMALACNPKLLIAD 178
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIdPRAKVATLSvSQM-----QMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 179 EPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAETAERVQVQYAGQKVEEQPVRALFRD 244
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-217 |
1.16e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 13 FQTSSGLFR-AVDGVSLACDKGEILSIVGESGSGKSVAMLALMGL-LPWTAKItadrmqfdgqDLRGiSArqrrrivgkd 90
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTV----------DIKG-SA---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 91 mAMIfqEPMSSLNPCFTvGFQLGETLRVHMGLNRKERRQRSIELLNLVGIpapedrlSNFPHQ----MSGGMSQRVMIAM 166
Cdd:PRK13545 88 -ALI--AISSGLNGQLT-GIENIELKGLMMGLTKEKIKEIIPEIIEFADI-------GKFIYQpvktYSSGMKSRLGFAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522061013 167 ALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVV 217
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQV 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
111-224 |
1.33e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 111 QLGETLRvHMGLNRKERR-QRSIELLNLvgipAPEDRLSnfphQMSGGMSQRVMIAMALACNPKLLIADEPTTALDV-TI 188
Cdd:PRK11147 122 KLQEQLD-HHNLWQLENRiNEVLAQLGL----DPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIeTI 192
|
90 100 110
....*....|....*....|....*....|....*.
gi 522061013 189 qaqilDLLVRLQKEQGMALVLITHDMGVVAETAERV 224
Cdd:PRK11147 193 -----EWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-212 |
1.78e-07 |
|
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: 50.70 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 7 ENLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPW---TAKITADRMqfdgqdlrgISARQR 83
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGrktAGVITGEIL---------INGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 ----RRIVGkdmamiFQEPMSSLNPCFTVgfqlGETLRVHM---GLNRKERRqrsiellnlvgipapedrlsnfphqmsg 156
Cdd:cd03232 74 dknfQRSTG------YVEQQDVHSPNLTV----REALRFSAllrGLSVEQRK---------------------------- 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 157 gmsqRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITH 212
Cdd:cd03232 116 ----RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIH 166
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-208 |
2.33e-07 |
|
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: 50.72 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 8 NLTVEFQTSSGLFRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPWTAKITADrMQFDGQDLRGISARQRRRIv 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIPYKEFAEKYPGEI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 88 gkdmamIFQEPMSSLNPCFTVGfqlgETLRVHMGLNRKErrqrsiellNLVGIpapedrlsnfphqmSGGMSQRVMIAMA 167
Cdd:cd03233 86 ------IYVSEEDVHFPTLTVR----ETLDFALRCKGNE---------FVRGI--------------SGGERKRVSIAEA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522061013 168 LACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALV 208
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-214 |
5.36e-07 |
|
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: 49.64 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 13 FQTSSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTAKITADRMQFDGQDLRGISARQRRRIvgkdm 91
Cdd:cd03290 8 FSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 92 AMIFQEPMSsLNPCFTVGFQLGETLRvhmglnrKERRQRSIELLNLvgipAPEDRLSNFPHQ---------MSGGMSQRV 162
Cdd:cd03290 82 AYAAQKPWL-LNATVEENITFGSPFN-------KQRYKAVTDACSL----QPDIDLLPFGDQteigerginLSGGQRQRI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 163 MIAMALACNPKLLIADEPTTALDV-----TIQAQILDLLvrlqKEQGMALVLITHDM 214
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFL----QDDKRTLVLVTHKL 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-219 |
1.28e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 20 FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakITADRMQFDGQ-DLRGISARQRRRIVGKDmamifqep 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS----PTVGKVDRNGEvSVIAISAGLSGQLTGIE-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 99 msslnpcfTVGFQLgetlrVHMGLNRKERRQRSIELLNLvgipapeDRLSNFPHQ----MSGGMSQRVMIAMALACNPKL 174
Cdd:PRK13546 105 --------NIEFKM-----LCMGFKRKEIKAMTPKIIEF-------SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 522061013 175 LIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAE 219
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQ 208
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-223 |
1.54e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 32 KGEILSIVGESGSGKSVAMLALMGLLPwtakitadrmqfdgqdlrgisaRQRRRIVGKDMAMIFQEPMSSLNPCFTVGfq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG----------------------PPGGGVIYIDGEDILEEVLDQLLLIIVGG-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 112 lgetlrvhmglnrkerrqrsiellnlvgipapedrlsnFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQ 191
Cdd:smart00382 57 --------------------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*..
gi 522061013 192 ILDL-----LVRLQKEQGMALVLITHDMGVVAETAER 223
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-235 |
1.58e-06 |
|
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: 49.82 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 24 DGVSLACDKGEILSIVGESGSGKS-VAMLaLMGLLpwtaKITADRMQFDGQDLRGISARQRRRIVGkdmaMIFQEpmssl 102
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKStLARL-LFRFY----DVTSGRILIDGQDIRDVTQASLRAAIG----IVPQD----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 103 npcfTVGFQlgETLRVHMGLNR----KERRQRSIELLNLvgipapEDRLSNFPHQM-----------SGGMSQRVMIAMA 167
Cdd:COG5265 441 ----TVLFN--DTIAYNIAYGRpdasEEEVEAAARAAQI------HDFIESLPDGYdtrvgerglklSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 168 LACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgMALVlITHDMGVVAEtAERVQVQYAGQKVEE 235
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLV-IAHRLSTIVD-ADEILVLEAGRIVER 573
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-234 |
2.39e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGLfrAVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQDLRGISARQR 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 84 RRIVgkdmAMIFQEpMSSLNpcftvgfqlgETLRVHMGLNRKERRQRSiELLNLVGIPAPEDRLSNFPH----------- 152
Cdd:PRK11176 416 RNQV----ALVSQN-VHLFN----------DTIANNIAYARTEQYSRE-QIEEAARMAYAMDFINKMDNgldtvigengv 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgMALVlITHDMGVVaETAERVQVQYAGQK 232
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTI-EKADEILVVEDGEI 556
|
..
gi 522061013 233 VE 234
Cdd:PRK11176 557 VE 558
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-217 |
6.20e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 139 GIPAPedrlsnfphQMSGGMSQRVMIAMAL---ACNPKLLIADEPTTAL---DVtiqAQILDLLVRLqKEQGMALVLITH 212
Cdd:TIGR00630 824 GQPAT---------TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEVLQRL-VDKGNTVVVIEH 890
|
....*
gi 522061013 213 DMGVV 217
Cdd:TIGR00630 891 NLDVI 895
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-224 |
9.78e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.98 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFQTssglfRAV-DGVSLACDKGEILSIVGESGSGKSvamlALMGLLpwtakitADRMQFDGqdlrGisa 80
Cdd:COG0488 314 KVLELEGLSKSYGD-----KTLlDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLL-------AGELEPDS----G--- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 rqrRRIVGKDMamifqepmsslnpcfTVGF--QLGETLRVHM-------GLNRKERRQRSIELLNLVGIPApeDRLSNFP 151
Cdd:COG0488 371 ---TVKLGETV---------------KIGYfdQHQEELDPDKtvldelrDGAPGGTEQEVRGYLGRFLFSG--DDAFKPV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 152 HQMSGGMSQRVMIAMALACNPKLLIADEPTTALDV-TIQAqildLLVRLQKEQGmALVLITHDMGVVAETAERV 224
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-230 |
1.02e-05 |
|
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: 47.32 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGlfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlpwTAKITADRMqfdgqdlrgisarq 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD---TTVTSGDAT-------------- 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 rrrIVGKDMAMIFQEPMSSLNPC--FTVGFQLgETLRVHMGLNRKERRQRSIEL-------LNLVGIPAPEDRLSNfphQ 153
Cdd:TIGR01257 1998 ---VAGKSILTNISDVHQNMGYCpqFDAIDDL-LTGREHLYLYARLRGVPAEEIekvanwsIQSLGLSLYADRLAG---T 2070
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAG 230
Cdd:TIGR01257 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-213 |
1.20e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 1.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 152 HQMSGGMSQRVMIAMALA---CNPK-LLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVlITHD 213
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHL 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-212 |
1.46e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLL------------PWTAKITADRMQ------------------------ 69
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNDMTNEQDYqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 70 --------------FDGQDLRGISARQRRRIvgkdMAMIFQEPMSsLNPCFTVGFQLGETLRVHMGLNRKERRQRSIELL 135
Cdd:PTZ00265 1267 gedstvfknsgkilLDGVDICDYNLKDLRNL----FSIVSQEPML-FNMSIYENIKFGKEDATREDVKRACKFAAIDEFI 1341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 136 NlvGIPAPED-RLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITH 212
Cdd:PTZ00265 1342 E--SLPNKYDtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-212 |
2.72e-05 |
|
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: 44.38 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFQTSSGL-FRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakitadrmqfdgqdlrgisARQ 82
Cdd:cd03250 1 ISVEDASFTWDSGEQEtSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---------------------KLS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQEP--MS-SL--NPCFTVGFqlgetlrvhmglnRKERRQRSIELLNLVgipapEDrLSNFPHQ---- 153
Cdd:cd03250 60 GSVSVPGSIAYVSQEPwiQNgTIreNILFGKPF-------------DEERYEKVIKACALE-----PD-LEILPDGdlte 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 154 -------MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITH 212
Cdd:cd03250 121 igekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTH 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-214 |
2.84e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakitadRMQFDGQDLRGISArqrrriVGKDMAMIFQEPMSSlNPC 105
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS--------HAETSSVVIRGSVA------YVPQVSWIFNATVRE-NIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 106 FTVGFQlgetlrvhmglnrKERRQRSIEllnlvgIPAPEDRLSNFPHQ-----------MSGGMSQRVMIAMALACNPKL 174
Cdd:PLN03232 701 FGSDFE-------------SERYWRAID------VTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522061013 175 LIADEPTTALDVTIQAQILDLLVRlQKEQGMALVLITHDM 214
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQL 800
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-217 |
3.42e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 3.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVV 217
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
130-213 |
3.63e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 130 RSIELLNLVGIPApedrlsnfpHQMSGGMSQ-------RVMIAMALACNPKLLIADEPTTALDV-TIQ--AQILDllvrl 199
Cdd:PRK15064 134 RAGELLLGVGIPE---------EQHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDInTIRwlEDVLN----- 199
|
90
....*....|....
gi 522061013 200 QKEQGMalVLITHD 213
Cdd:PRK15064 200 ERNSTM--IIISHD 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-228 |
3.66e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.66 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 33 GEILSIVGESGSGKSVAMLALMG-LLP----------WTAKITAdrmqFDGQDLRGISARqrrrIVGKDMAMIFQEPMSS 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPnlgkfddppdWDEILDE----FRGSELQNYFTK----LLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 102 LNPCFTVGfqlgetlRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPT 181
Cdd:cd03236 98 LIPKAVKG-------KVGELLKKKDERGKLDELVDQLEL---RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 522061013 182 TALDVTiQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQY 228
Cdd:cd03236 168 SYLDIK-QRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-194 |
3.76e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 26 VSLACDKGEILSIVGESGSGKSVAMLALMG-LLPWTAKItadrmqfdgqdlrgisaRQRRRIvgkdmamifqepmsSLNP 104
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKI-----------------KHSGRI--------------SFSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 105 CFTvgFQLGETLR--VHMGLNRKERRQRSIellnlVGIPAPEDRLSNFPHQ-----------MSGGMSQRVMIAMALACN 171
Cdd:TIGR01271 494 QTS--WIMPGTIKdnIIFGLSYDEYRYTSV-----IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKD 566
|
170 180
....*....|....*....|...
gi 522061013 172 PKLLIADEPTTALDVTIQAQILD 194
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIFE 589
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
139-218 |
5.56e-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: 44.14 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 139 GIPAPEdrlsnfphqMSGGMSQRVMIAMAL---ACNPKLLIADEPTTAL---DVtiqAQILDLLVRLqKEQGMALVLITH 212
Cdd:cd03271 164 GQPATT---------LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDV---KKLLEVLQRL-VDKGNTVVVIEH 230
|
....*.
gi 522061013 213 DMGVVA 218
Cdd:cd03271 231 NLDVIK 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-231 |
5.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSsglfraVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtaKITADrMQFDGQDLRGISARQ 82
Cdd:PRK10982 250 ILEVRNLTSLRQPS------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE---KSAGT-ITLHGKKINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 rrrIVGKDMAMIFQEPMSS-----LNPCFTVGFQLGETLRVHMGL--NRKERR--QRSIELLNlVGIPAPEDRLSNfphq 153
Cdd:PRK10982 320 ---AINHGFALVTEERRSTgiyayLDIGFNSLISNIRNYKNKVGLldNSRMKSdtQWVIDSMR-VKTPGHRTQIGS---- 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGVVAETAERVQVQYAGQ 231
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-213 |
6.21e-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: 43.36 E-value: 6.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 153 QMSGG------MSQRVMIAMALACNPKLLIADEPTTALDV-TIQAQILDLLVRLQKEQGMALVLITHD 213
Cdd:cd03240 115 RCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-224 |
7.03e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 7.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522061013 154 MSGGMSQRVMIAMALACNPK--LLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVaETAERV 224
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVL-SSADWI 158
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-213 |
8.27e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 128 RQRSIELLNlvGIPAPEDRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDvtiqaqiLDLLVRLQK----EQ 203
Cdd:PRK10636 126 RSRAASLLH--GLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksYQ 196
|
90
....*....|
gi 522061013 204 GmALVLITHD 213
Cdd:PRK10636 197 G-TLILISHD 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-237 |
1.05e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMLALMGLlPWTAKITAdRMQFDGQDlrgISARQ 82
Cdd:NF040905 257 VFEVKNWTVYHPLHPER-KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR-SYGRNISG-TVFKDGKE---VDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGKDMAMIFQEpmsslnpcftvgfqlgetlRVHMGLNRKERRQRSIELLNLVGI-------PAPEDRLSN-FPHQM 154
Cdd:NF040905 331 VSDAIDAGLAYVTED-------------------RKGYGLNLIDDIKRNITLANLGKVsrrgvidENEEIKVAEeYRKKM 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 155 --------------SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVVAET 220
Cdd:NF040905 392 niktpsvfqkvgnlSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGM 470
|
250
....*....|....*..
gi 522061013 221 AERVQVQYAGQKVEEQP 237
Cdd:NF040905 471 CDRIYVMNEGRITGELP 487
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-228 |
1.22e-04 |
|
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: 42.17 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQVQY 228
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
1.55e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.75 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 4 LEIENLTVEFqTSSGlfRAV-DGVSLACDKGEILSIVGESGSGKSVAMLALMGLLPwtakiTADRMQFDGQDLRGISARQ 82
Cdd:TIGR01271 1218 MDVQGLTAKY-TEAG--RAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-----TEGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 83 RRRIVGkdmaMIFQEPmsslnpcftvgFQLGETLRVHMGLNRKERRQRSIELLNLVGIpapEDRLSNFPHQ--------- 153
Cdd:TIGR01271 1290 WRKAFG----VIPQKV-----------FIFSGTFRKNLDPYEQWSDEEIWKVAEEVGL---KSVIEQFPDKldfvlvdgg 1351
|
170 180 190
....*....|....*....|....*....|....*....
gi 522061013 154 --MSGGMSQRVMIAMALACNPKLLIADEPTTALD-VTIQ 189
Cdd:TIGR01271 1352 yvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
155-226 |
2.04e-04 |
|
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: 42.85 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQV 226
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-227 |
7.09e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 22 AVDGVSLACDKGEILSIVGESGSGKSVamlaLMGLLPWTAKITADRMQFDGQ---DLRGISARQRRRIVGkdmamifQEP 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKST----LLSLIQRHFDVSEGDIRFHDIpltKLQLDSWRSRLAVVS-------QTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 99 msslnpcftvgFQLGETLRVHMGLNRKERRQRSIEllNLVGIPAPEDRLSNFPH-----------QMSGGMSQRVMIAMA 167
Cdd:PRK10789 399 -----------FLFSDTVANNIALGRPDATQQEIE--HVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 168 LACNPKLLIADEPTTALDVTIQAQILDLLVrlQKEQGMALVLITHDMGVVAETAERVQVQ 227
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTEASEILVMQ 523
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-217 |
8.21e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 8.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 154 MSGGMSQRVMIAMALAC---NPKLLIADEPTTALDVTIQAQILDLLVRLqKEQGMALVLITHDMGVV 217
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVV 875
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-185 |
1.20e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 128 RQRSIELLNLVGIPApedRLSNFP-HQMSGGMSQRVMIAMALACNPKLLIADEPTTALD 185
Cdd:PRK10938 378 QKLAQQWLDILGIDK---RTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-212 |
1.49e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 3 LLEIENLTVEFQTSSGLfravDGVSLACDKGEILSIVGESGSGKSVAMLALMGLL-PWTAKItadrmQFDGQDL-RGISA 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLL----QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEI-----LFERQSIkKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 81 RQRRrivgkdmaMIFQEPMSSLNPCFTVG----FQLgETLRVHMGLNrkerrqrsiELLNLVGIpapeDRLSNFP-HQMS 155
Cdd:PRK13540 72 YQKQ--------LCFVGHRSGINPYLTLRenclYDI-HFSPGAVGIT---------ELCRLFSL----EHLIDYPcGLLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522061013 156 GGMSQRVMIAMALACNPKLLIADEPTTALDvtiQAQILDLLVRLQ--KEQGMALVLITH 212
Cdd:PRK13540 130 SGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
145-231 |
1.95e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 145 DRLSNFPHQMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKeqgmALVLITHDMGVVAETAERV 224
Cdd:PRK10636 422 DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDL 497
|
....*..
gi 522061013 225 QVQYAGQ 231
Cdd:PRK10636 498 YLVHDGK 504
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-228 |
2.18e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQgmALVLITHDMGVVAETAERVQVQY 228
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
155-226 |
2.42e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 155 SGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEQGMALVLITHDMGVVAETAERVQV 226
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-212 |
2.80e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 1 MPL--LEIENltvefqtssglFRAVDGVSLACDKGeILSIVGESGSGKSVAMLALMGLLP--WTAKITADRMqFDGQDLR 76
Cdd:COG3593 1 MKLekIKIKN-----------FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGpsSSRKFDEEDF-YLGDDPD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 77 GIS-----------ARQRRRIVGKDMAMIFQEPMSSLNPCFTVGFQ--------------LGETLRVHMGLNRKERRQRS 131
Cdd:COG3593 68 LPEieieltfgsllSRLLRLLLKEEDKEELEEALEELNEELKEALKalnellseylkellDGLDLELELSLDELEDLLKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 132 IELLNLVGIPAPEDRLsnfphqmsgGMSQRVMIAMALAC---------NPKLLIADEPTTALDVTIQAQILDLLVRLQKE 202
Cdd:COG3593 148 LSLRIEDGKELPLDRL---------GSGFQRLILLALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEK 218
|
250
....*....|.
gi 522061013 203 QGMalVLI-TH 212
Cdd:COG3593 219 PNQ--VIItTH 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-226 |
3.14e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 2 PLLEIENLTVEFqtsSGLfRAVDGVSLACDKGEILSIVGESGSGKSVAMlalmgllpwtaKITADRMQFDGQDLRGISAR 81
Cdd:PRK15439 10 PLLCARSISKQY---SGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLM-----------KIIAGIVPPDSGTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 82 QRRRIVGKDMAM----IFQEPMssLNPCFTVgfqlgeTLRVHMGLNRKERRQRSIE-LLNLVGipapedrlSNFPHQMSG 156
Cdd:PRK15439 75 CARLTPAKAHQLgiylVPQEPL--LFPNLSV------KENILFGLPKRQASMQKMKqLLAALG--------CQLDLDSSA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522061013 157 GM-----SQRVMIAMALACNPKLLIADEPTTALdvtIQAQILDLLVRLQK--EQGMALVLITHDMGVVAETAERVQV 226
Cdd:PRK15439 139 GSlevadRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISV 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
154-244 |
3.27e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.54 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKE-QGMALVLITHDMGVVAETaERVQVQYAGQK 232
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
90
....*....|...
gi 522061013 233 VEEQPVRALF-RD 244
Cdd:TIGR00957 840 SEMGSYQELLqRD 852
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-216 |
3.32e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.00 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRLQKEqGMALVLITHDMGV 216
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAI 274
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
154-213 |
4.13e-03 |
|
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: 38.76 E-value: 4.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDvtiqAQILDLLVR-LQKEQGmALVLITHD 213
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPG-TVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
153-213 |
4.75e-03 |
|
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: 38.76 E-value: 4.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522061013 153 QMSGGMSQRVMIAMALACNPKLLIADEPTTALDV-TIQAqildLLVRLQKEQGMALVlITHD 213
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA----LEEALLNFAGCAVV-ISHD 499
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-211 |
6.34e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.57 E-value: 6.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 522061013 154 MSGGMSQRVMIAMALACNPKLLIADEPTTALDVTIQAQILDLLVRlQKEQGMALVLIT 211
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVT 797
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
154-217 |
7.22e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 7.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522061013 154 MSGGMSQRVMIAMALA---CNPKLLIADEPTTAL---DVtiqAQILDLLVRLqKEQGMALVLITHDMGVV 217
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVLHRL-VDKGNTVVVIEHNLDVI 892
|
|
| |
