|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-312 |
7.79e-178 |
|
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: 495.34 E-value: 7.79e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTArITADRMNFDGKDLLTISQKE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLF 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 243 AKPQHPYTYALLSALPE-RATGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALHS-----KVLCHYP 312
Cdd:COG0444 240 ENPRHPYTRALLSSIPRlDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREvgpghRVACHLY 315
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-319 |
2.40e-168 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 471.92 E-value: 2.40e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQ 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVD 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 241 LFAKPQHPYTYALLSALPERATGK-RLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALH----SKVLCHYPLVD 315
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKaRLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNmlagRQSKCHYPLDD 320
|
....*
gi 522082967 316 -GKPT 319
Cdd:PRK11022 321 aGRPT 325
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-261 |
1.53e-146 |
|
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: 424.10 E-value: 1.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQ 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVD 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260
....*....|....*....|.
gi 522082967 241 LFAKPQHPYTYALLSALPERA 261
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPRGD 264
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-318 |
3.35e-124 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 359.99 E-value: 3.35e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQ 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEH-LGGT-------RKEleaRAIELLGLVGIPAPESRLRAFPH 152
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWtFKGKwwqrfkwRKK---RAIELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQ 232
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 233 VERQNVVDLFAKPQHPYTYALLSALP----ERATGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALHSK-- 306
Cdd:COG4170 238 VESGPTEQILKSPHHPYTKALLRSMPdfrqPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIKgh 317
|
330
....*....|...
gi 522082967 307 -VLCHYPLVDGKP 318
Cdd:COG4170 318 eFACHFPLNMEEK 330
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-301 |
2.95e-119 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 347.48 E-value: 2.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADrMNFDGKDLLTISQ 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGS-ATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVD 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 241 LFAKPQHPYTYALLSALPE-RATGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPP 301
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRlDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPP 310
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-235 |
2.00e-106 |
|
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: 310.98 E-value: 2.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKe 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLgLVGIPAPESRLRAFPHQMSGGMNQRV 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-318 |
1.05e-102 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 305.12 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLF-------RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDL 75
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE----PTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKERRKIiGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPApeSRLRAFPHQMS 155
Cdd:COG4608 83 TGLSGRELRPL-RRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRP--EHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 236 QNVVDLFAKPQHPYTYALLSALPE---RATGKRLPsIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALHS-----KV 307
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVpdpERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREvgpghQV 318
|
330
....*....|.
gi 522082967 308 LCHYPLVDGKP 318
Cdd:COG4608 319 ACHLAEEGSGV 329
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-313 |
3.32e-97 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 291.32 E-value: 3.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQ 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKehlGGTRKE--------LEARAIELLGLVGIPAPESRLRAFPH 152
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIP---GWTYKGrwwqrfgwRKRRAIELLHRVGIKDHKDAMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQ 232
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 233 VERQNVVDLFAKPQHPYTYALLSALPERATG----KRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALHSK-- 306
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAIPDFGSAmphkSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKnh 317
|
....*...
gi 522082967 307 -VLCHYPL 313
Cdd:PRK15093 318 lYACHFPL 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-259 |
1.13e-94 |
|
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: 291.04 E-value: 1.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFET-AHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQK 81
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIiGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPApeSRLRAFPHQMSGGMNQR 161
Cdd:COG1123 336 SLREL-RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDL 241
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
250
....*....|....*...
gi 522082967 242 FAKPQHPYTYALLSALPE 259
Cdd:COG1123 493 FANPQHPYTRALLAAVPS 510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-268 |
3.01e-93 |
|
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: 287.18 E-value: 3.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MS-LLEIRNLSVEFetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITaDRMNFDGKDLLTIS 79
Cdd:COG1123 1 MTpLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERrkiiGKDISMIFQEPMTSLNPcFTVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMN 159
Cdd:COG1123 78 EALR----GRRIGMVFQDPMTQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260
....*....|....*....|....*....
gi 522082967 240 DLFAKPQhpytyaLLSALPERATGKRLPS 268
Cdd:COG1123 229 EILAAPQ------ALAAVPRLGAARGRAA 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-259 |
9.67e-86 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 270.96 E-value: 9.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWT-ARITADRM-----NFDGKDLL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAgGLVQCDKMllrrrSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 77 TISQKERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSG 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQ 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|...
gi 522082967 237 NVVDLFAKPQHPYTYALLSALPE 259
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-278 |
1.72e-85 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 267.73 E-value: 1.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARI-TADRMNFDGKDLLTIS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMN 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 522082967 240 DLFAKPQHPYTYALLSALPEratGKRLPsIPGVVPGLLD 278
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPS---GDPVP-LPEPASPLLD 277
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-259 |
4.00e-82 |
|
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: 259.23 E-value: 4.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFR-------AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITadrmnFDGKDL 75
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIR-----FDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKERRKIiGKDISMIFQEPMTSLNPCFTVGyqimEVIKE-----HLGGTRKELEARAIELLGLVGIPaPESRLRaF 150
Cdd:COG4172 350 DGLSRRALRPL-RRRMQVVFQDPFGSLSPRMTVG----QIIAEglrvhGPGLSAAERRARVAEALEEVGLD-PAARHR-Y 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 151 PHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAG 230
Cdd:COG4172 423 PHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
250 260
....*....|....*....|....*....
gi 522082967 231 QQVERQNVVDLFAKPQHPYTYALLSALPE 259
Cdd:COG4172 503 KVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-258 |
1.21e-80 |
|
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: 246.25 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQK 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVT-----FDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKiigkDISMIFQEPMTSLNPCFTVGYQIMEVIKEHlggTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQR 161
Cdd:COG1124 76 AFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDL 241
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*..
gi 522082967 242 FAKPQHPYTYALLSALP 258
Cdd:COG1124 227 LAGPKHPYTRELLAASL 243
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-256 |
3.93e-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: 3.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISqkerrkIIGKDISMIFQEPMTS 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 102 LNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 182 TALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQHPYTYALLSA 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-311 |
4.48e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 242.18 E-value: 4.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFR------AVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLL 76
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKS----TLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 77 TISqKERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIpAPESRLRaFPHQMSG 156
Cdd:PRK11308 81 KAD-PEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEHYDR-YPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIA--MMIacNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVE 234
Cdd:PRK11308 158 GQRQRIAIAraLML--DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 235 RQNVVDLFAKPQHPYTYALLSALPERATGKRLPSIP--GVVPGLLDRPTGCLFNPRCQFATDKCRSTPPALH----SKVL 308
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIKltGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRdydgRLVA 315
|
...
gi 522082967 309 CHY 311
Cdd:PRK11308 316 CFA 318
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-303 |
1.47e-76 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 238.45 E-value: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHG---------LFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGK 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 74 DLLTISQKERRKIiGKDISMIFQEPMTSLNPCFTVGYQIMEVIKE-HLGGTRKELEARAIELLGLVGI-PAPESRlraFP 151
Cdd:PRK15079 84 DLLGMKDDEWRAV-RSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINR---YP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 152 HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 232 QVERQNVVDLFAKPQHPYTYALLSALP------ERatGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPAL 303
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVPipdpdlER--NKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL 315
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-256 |
7.34e-62 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 198.39 E-value: 7.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEfeTAHGLfraVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQKer 83
Cdd:PRK10418 5 IELRNIALQ--AAQPL---VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiiGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEhLGGTRKEleARAIELLGLVGIPAPESRLRAFPHQMSGGMNQRVM 163
Cdd:PRK10418 78 ----GRKIATIMQNPRSAFNPLHTMHTHARETCLA-LGKPADD--ATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFA 243
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|...
gi 522082967 244 KPQHPYTYALLSA 256
Cdd:PRK10418 231 APKHAVTRSLVSA 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-227 |
5.43e-59 |
|
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: 189.62 E-value: 5.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKER 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGL---DRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEPmtSLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVM 163
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTA-LENVELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQ 227
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELR 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-258 |
4.48e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.05 E-value: 4.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITadrmnFDGKDLLTISQK 81
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLerPTSGSVL-----VDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIiGKDISMIFQE---------------PMtslnpcftvgyqimevikEHLGGTRKELEARAIELLGLVGIpapESR 146
Cdd:COG1135 76 ELRAA-RRKIGMIFQHfnllssrtvaenvalPL------------------EIAGVPKAEIRKRVAELLELVGL---SDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 147 LRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNV 226
Cdd:COG1135 134 ADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAV 213
|
250 260 270
....*....|....*....|....*....|..
gi 522082967 227 QYAGQQVERQNVVDLFAKPQHPYTYALLSALP 258
Cdd:COG1135 214 LENGRIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-246 |
1.36e-55 |
|
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: 181.24 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKE 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGL---ERPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKiIGKDISMIFQE--PMTSLnpcfTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQ 160
Cdd:cd03258 77 LRK-ARRRIGMIFQHfnLLSSR----TV-FENVALPLEIAGVPKAEIEERVLELLELVGL---EDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVD 240
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 522082967 241 LFAKPQ 246
Cdd:cd03258 228 VFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
6.73e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.47 E-value: 6.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQK 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGL---DRPTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMIFQEPmtSLNPCFTVGYQIMeVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQR 161
Cdd:COG1136 79 ELARLRRRHIGFVFQFF--NLLPELTALENVA-LPLLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVA 218
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-267 |
1.84e-52 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 183.13 E-value: 1.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLF-------RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDL 75
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV----ESQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKERRKIiGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIpAPESRLRaFPHQMS 155
Cdd:PRK10261 389 DTLSPGKLQAL-RRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAWR-YPHEFS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
250 260 270
....*....|....*....|....*....|..
gi 522082967 236 QNVVDLFAKPQHPYTYALLSALPERATGKRLP 267
Cdd:PRK10261 546 GPRRAVFENPQHPYTRKLMAAVPVADPSRQRP 577
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-256 |
5.47e-52 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 173.10 E-value: 5.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFR-----AVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLPwtarITADRMNFDGK 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKStlAKMLA--GIIE----PTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 74 DLLTISQKERrkiiGKDISMIFQEPMTSLNPCFTVGyQIMEV-IKEHLGGTRKELEARAIELLGLVGIpAPESRLrAFPH 152
Cdd:COG4167 76 KLEYGDYKYR----CKHIRMIFQDPNTSLNPRLNIG-QILEEpLRLNTDLTAEEREERIFATLRLVGL-LPEHAN-FYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQ 232
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 522082967 233 VERQNVVDLFAKPQHPYTYALLSA 256
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRLIES 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-260 |
4.15e-49 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 165.63 E-value: 4.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETaHGLFRA------VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKD 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAH-GGLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL----ESPSQGNVSWRGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 75 LLTISqKERRKIIGKDISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPApeSRLRAFPHQM 154
Cdd:PRK10419 76 LAKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVE 234
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260
....*....|....*....|....*..
gi 522082967 235 RQNVVDLFAKpQHPYTYALLSA-LPER 260
Cdd:PRK10419 233 TQPVGDKLTF-SSPAGRVLQNAvLPAF 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-255 |
8.04e-49 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 171.81 E-value: 8.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFR-------AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITadrmnFDGKDL 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIW-----FDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKE----RRKIigkdiSMIFQEPMTSLNPCFTVgyqiMEVIKEHLGGTRKEL-----EARAIELLGLVGIpAPESR 146
Cdd:PRK15134 350 HNLNRRQllpvRHRI-----QVVFQDPNSSLNPRLNV----LQIIEEGLRVHQPTLsaaqrEQQVIAVMEEVGL-DPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 147 LRaFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNV 226
Cdd:PRK15134 420 HR-YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*....
gi 522082967 227 QYAGQQVERQNVVDLFAKPQHPYTYALLS 255
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-256 |
5.82e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.58 E-value: 5.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKE-- 82
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL---ERPTSGRVLVDGQDLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 --RRKIigkdiSMIFQEpmtslnpcF------TVGYQI---MEvikehLGGTRK-ELEARAIELLGLVGIpapESRLRAF 150
Cdd:PRK11153 79 kaRRQI-----GMIFQH--------FnllssrTVFDNValpLE-----LAGTPKaEIKARVTELLELVGL---SDKADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 151 PHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAG 230
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
250 260
....*....|....*....|....*.
gi 522082967 231 QQVERQNVVDLFAKPQHPYTYALLSA 256
Cdd:PRK11153 218 RLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-224 |
4.17e-44 |
|
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: 150.70 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFEtaHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKERR 84
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL----GPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 85 KIIGkdisMIFQEPMTSL-NPcfTVGyqiMEVI--KEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQR 161
Cdd:cd03225 75 RKVG----LVFQNPDDQFfGP--TVE---EEVAfgLENLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVV 224
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRV 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-246 |
6.62e-43 |
|
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: 148.25 E-value: 6.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKER 83
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL----KPTSGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdisMIFQEPMTSLnpcftvgyqIMEVIKE-------HLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSG 156
Cdd:COG1122 74 RRKVG----LVFQNPDDQL---------FAPTVEEdvafgpeNLGLPREEIRERVEEALELVGL---EHLADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQ 236
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 522082967 237 NVVDLFAKPQ 246
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-246 |
6.10e-42 |
|
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: 147.21 E-value: 6.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 20 FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLlTISQKERRKIIGKDISMIFQEPM 99
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL----KPTSGTVTIDGRDI-TAKKKKKLKDLRKKVGLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 tslnpcftvgYQIME--VIKE------HLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMMIACN 171
Cdd:TIGR04521 93 ----------HQLFEetVYKDiafgpkNLGLSEEEAEERVKEALELVGLD--EEYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQ 246
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-249 |
1.52e-41 |
|
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: 144.95 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKER 83
Cdd:cd03261 1 IELRGLTKSFGGRTVL----KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL----RPDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIgKDISMIFQEP--MTSLnpcfTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGGMNQR 161
Cdd:cd03261 73 YRLR-RRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDL 241
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....*...
gi 522082967 242 FAKpQHPY 249
Cdd:cd03261 225 RAS-DDPL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
3.53e-41 |
|
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: 144.11 E-value: 3.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALM-GLLpwtaRITADRMNFDGKDLLTISQ 80
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLD----RPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQE----P-MTSL-N---PcftvgyqiMEvikehLGGtRKELEARAIELLGLVGIpapESRLRAFP 151
Cdd:COG4181 82 DARARLRARHVGFVFQSfqllPtLTALeNvmlP--------LE-----LAG-RRDARARARALLERVGL---GHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 152 HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQyAGQ 231
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLR-AGR 223
|
...
gi 522082967 232 QVE 234
Cdd:COG4181 224 LVE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-214 |
3.53e-41 |
|
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: 143.97 E-value: 3.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETahglfRAV-DSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQK 81
Cdd:COG1127 5 MIEVRNLTKSFGD-----RVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIgKDISMIFQEP--MTSLnpcfTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGGMN 159
Cdd:COG1127 76 ELYELR-RRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELSGGMR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDL 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-241 |
6.87e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.28 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE 82
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSgEVR-----VLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIigkdiSMIFQEPmtSLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRV 162
Cdd:COG1131 72 RRRI-----GYVPQEP--ALYPDLTV-RENLRFFARLYGLPRKEARERIDELLELFGL---TDAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDL 241
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.45e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 143.31 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLPwtarITADRMNFDGKDLlti 78
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKStlLRLIA--GLEK----PTSGEVLVDGKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 sqkerrKIIGKDISMIFQEPmtSLNPCFTVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGM 158
Cdd:COG1116 76 ------TGPGPDRGVVFQEP--ALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGL---AGFEDAYPHQLSGGM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-256 |
2.53e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 142.37 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNfDG--KDLLTISQ 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGC----RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR-DGqlRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLNPCFT----VGYQIMEVIKEHLGGTRkeleARAIELLGLVGIPApeSRLRAFPHQMSG 156
Cdd:PRK11701 81 AERRRLLRTEWGFVHQHPRDGLRMQVSaggnIGERLMAVGARHYGDIR----ATAGDWLERVEIDA--ARIDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER- 235
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESg 234
|
250 260
....*....|....*....|...
gi 522082967 236 --QNVVDlfaKPQHPYTYALLSA 256
Cdd:PRK11701 235 ltDQVLD---DPQHPYTQLLVSS 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
2.61e-40 |
|
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: 141.46 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLpwtaRITADRMNFDGKDLltisqk 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKStlLRIIA--GLE----RPTSGEVLVDGEPV------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 errKIIGKDISMIFQEPmtSLNPCFTVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQR 161
Cdd:cd03293 69 ---TGPGPDRGYVFQQD--ALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGL---SGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-257 |
5.01e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.59 E-value: 5.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPwtarITADRMNFDGKDLlTISQK 81
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLrCINLLEE----PDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIgKDISMIFQepmtSLN--PCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPApesRLRAFPHQMSGGMN 159
Cdd:COG1126 71 DINKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
250
....*....|....*...
gi 522082967 240 DLFAKPQHPYTYALLSAL 257
Cdd:COG1126 222 EFFENPQHERTRAFLSKV 239
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-257 |
1.18e-38 |
|
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: 138.04 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFravdSVDLEIDQGEMAAIVGESGSGKSVSMLALMG-LLPWTARITADRMNFDGKDLLTISQK 81
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCR----DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMIFQEPMTSLNPCFT----VGYQIMEVIKEHLGGTRkeleARAIELLGLVGIPApeSRLRAFPHQMSGG 157
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRDGLRMRVSaganIGERLMAIGARHYGNIR----ATAQDWLEEVEIDP--TRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQN 237
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
250 260
....*....|....*....|
gi 522082967 238 VVDLFAKPQHPYTYALLSAL 257
Cdd:TIGR02323 233 TDQVLDDPQHPYTQLLVSSI 252
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-219 |
5.43e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKE- 82
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE----RPTSGQVLVNGQDLSRLKRREi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 ---RRKIiGkdisMIFQEpmtslnpcF------TVgYQ----IMEVIkehlGGTRKELEARAIELLGLVGIpapESRLRA 149
Cdd:COG2884 75 pylRRRI-G----VVFQD--------FrllpdrTV-YEnvalPLRVT----GKSRKEIRRRVREVLDLVGL---SDKAKA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 150 FPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAE 219
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDR 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-214 |
7.20e-38 |
|
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: 134.57 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKER 83
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE----RPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkDISMIFQEPmtSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGGMNQRVM 163
Cdd:cd03259 73 ------NIGMVFQDY--ALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQ 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-213 |
1.56e-37 |
|
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: 135.17 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPWTA-RITadrmnFDGKDLLTISQ 80
Cdd:COG1120 1 MLEAENLSV----GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSSgEVL-----LDGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGkdisMIFQEPMTSLNpcFTVgyqiMEVI----KEHLGG----TRKELEA--RAIELLGLVGIpapesRLRAF 150
Cdd:COG1120 71 RELARRIA----YVPQEPPAPFG--LTV----RELValgrYPHLGLfgrpSAEDREAveEALERTGLEHL-----ADRPV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 151 pHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG1120 136 -DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-224 |
1.85e-37 |
|
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: 133.42 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLlTISQKER 83
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLL---EEPDSGTIIIDGLKL-TDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIgKDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVM 163
Cdd:cd03262 72 NELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVVAETAEVV 224
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRV 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-256 |
4.47e-37 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 134.15 E-value: 4.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLFR-----AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADRMNFDGKDL 75
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKerrkiigkdISMIFQEPMTSLNPCFTVGyQIMEV-IKEHLGGTRKELEARAIELLGLVGIPAPESRLraFPHQM 154
Cdd:PRK15112 83 SYRSQR---------IRMIFQDPSTSLNPRQRIS-QILDFpLRLNTDLEPEQREKQIIETLRQVGLLPDHASY--YPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVE 234
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 522082967 235 RQNVVDLFAKPQHPYTYALLSA 256
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLIAG 252
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-214 |
3.16e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 131.33 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPWTA-RITadrmnFDGKDLLTIS 79
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPTSgEIL-----VDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIiGKDISMIFQEPmtSLNPCFTV---------GYqiMEVIKEHLGGTRKELEARAIELLGLVGIpAPESRLRAf 150
Cdd:COG3638 72 GRALRRL-RRRIGMIFQQF--NLVPRLSVltnvlagrlGR--TSTWRSLLGLFPPEDRERALEALERVGL-ADKAYQRA- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082967 151 pHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:COG3638 145 -DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQV 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
1.12e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.99 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTAritaDRMNFDGKDLltisQKERRKIIGKDISMIFQEPmtSL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE----GTILLDGQDL----TDDERKSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 NPCFTVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIP-APESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:pfam00005 71 FPRLTVRENLRLGL-LLKGLSKREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 522082967 182 T 182
Cdd:pfam00005 150 A 150
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-231 |
2.63e-35 |
|
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: 128.24 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITadrmnFDGKDLLTISQ 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLdnPTSGEVL-----FNGQSLSKLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQepMTSLNPCFTVGYQIMevIKEHLGG-TRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMN 159
Cdd:TIGR02211 75 NERAKLRNKKLGFIYQ--FHHLLPDFTALENVA--MPLLIGKkSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGvVAETAEVVNVQYAGQ 231
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-214 |
4.29e-35 |
|
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: 128.92 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQ 80
Cdd:cd03294 18 FKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE----PTSGKVLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEpmTSLNPCFTVGYQI---MEVikehLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGG 157
Cdd:cd03294 94 KELRELRRKKISMVFQS--FALLPHRTVLENVafgLEV----QGVPRAEREERAAEALELVGL---EGWEHKYPDELSGG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDL 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-213 |
4.49e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 130.99 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLPWTA-RITadrmnFDGKDLLT 77
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTtlLRMIA--GFETPDSgRIL-----LDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISqKERRkiigkDISMIFQEP-----MTSL-NpcftVGYQImevikEHLGGTRKELEARAIELLGLVGIPAPESRlraFP 151
Cdd:COG3842 72 LP-PEKR-----NVGMVFQDYalfphLTVAeN----VAFGL-----RMRGVPKAEIRARVAELLELVGLEGLADR---YP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 152 HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-249 |
2.82e-34 |
|
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: 126.26 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetaHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKE 82
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIF-----IDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIfqepmtSLNPCFTVGYQIMEVIKeHLGGTRKELEARAIELLGLVGIPaPESRLRAFPHQMSGGMNQRV 162
Cdd:cd03295 73 LRRKIGYVIQQI------GLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLF 242
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
....*..
gi 522082967 243 AKPQHPY 249
Cdd:cd03295 225 RSPANDF 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
1.31e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLL-PWTARITadrmnFDGKDLlti 78
Cdd:COG1121 4 MPAIELENLTV----SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLpPTSGTVR-----LFGKPP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 sqKERRKIIG-----KDISMIFqePMTslnpcftvgyqIMEVIK----EHLG---GTRKELEARAIELLGLVGIPAPESR 146
Cdd:COG1121 71 --RRARRRIGyvpqrAEVDWDF--PIT-----------VRDVVLmgryGRRGlfrRPSRADREAVDEALERVGLEDLADR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 147 lrafP-HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETA 221
Cdd:COG1121 136 ----PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYF 206
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-213 |
1.80e-33 |
|
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: 123.21 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKER 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIGGL---RSVQEGSLKVLGQELHGASKKQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIiGKDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVM 163
Cdd:TIGR02982 78 VQL-RRRIGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:TIGR02982 152 IARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
5.25e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetaHGLfRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITADRMNFDGKDLLTi 78
Cdd:PRK11264 1 MSAIEVKNLVKKF---HGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRVGDITIDTARSLS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERRKIIGKDISMIFQEpmTSLNPCFTVGYQIME---VIKehlGGTRKELEARAIELLGLVGIPAPESrlrAFPHQMS 155
Cdd:PRK11264 75 QQKGLIRQLRQHVGFVFQN--FNLFPHRTVLENIIEgpvIVK---GEPKEEATARARELLAKVGLAGKET---SYPRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDL-QHKRGMalVLITHDMGVVAETAEVVNVQYAGQQVE 234
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTM--VIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|.
gi 522082967 235 RQNVVDLFAKPQHPYTYALLS 255
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFLE 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-244 |
6.98e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 123.74 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 20 FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADRmnfdgkdlLTISQKERRKIIG---KDISMIF 95
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDD--------ITITHKTKDKYIRpvrKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 96 QEPMTslnpcftvgyQIME--VIKEHLGGTR------KELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMM 167
Cdd:PRK13646 92 QFPES----------QLFEdtVEREIIFGPKnfkmnlDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 168 IACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAK 244
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-215 |
9.27e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.12 E-value: 9.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKE 82
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKL---EEITSGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RrkIIGKDISMIFQE----P-MTSLNpcfTVGYQIMEVikehLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGG 157
Cdd:PRK09493 73 R--LIRQEAGMVFQQfylfPhLTALE---NVMFGPLRV----RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMG 215
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG 197
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-214 |
1.77e-32 |
|
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: 122.15 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSveFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVsmLA--LMGLL-PWTARITadrmnFDGKDLLTISQ 80
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKST--LAklLNGLLlPTSGKVT-----VDGLDTLDEEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 -KERRKIIGkdisMIFQEPMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSG 156
Cdd:TIGR04520 72 lWEIRKKVG----MVFQNPDNQF-----VGATVEDDVAfglENLGVPREEMRKRVDEALKLVGM---EDFRDREPHLLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDM 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-231 |
3.13e-32 |
|
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: 118.65 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLltisqKER 83
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL----KPDSGEIKVLGKDI-----KKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEPmtSLNPCFTVgyqimeviKEHLggtrkelearaiellglvgipapesrlrafphQMSGGMNQRVM 163
Cdd:cd03230 68 PEEVKRRIGYLPEEP--SLYENLTV--------RENL--------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-231 |
4.80e-32 |
|
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: 118.44 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQke 82
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSIL-----IDGEDLTDLED-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPmtSLNPCFTVGYQIMevikehlggtrkelearaielLGLvgipapesrlrafphqmSGGMNQRV 162
Cdd:cd03229 70 ELPPLRRRIGMVFQDF--ALFPHLTVLENIA---------------------LGL-----------------SGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-234 |
1.02e-31 |
|
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: 118.82 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSV--SMLALMGLLPWTARITAdRMNFDGKDLLTISQK 81
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTllRLLNRLNDLIPGAPDEG-EVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 --ERRKIIGkdisMIFQEP----MTslnpcftvgyqIMEVI----KEHLGGTRKELEARAIELLGLVGIPAPESRlRAFP 151
Cdd:cd03260 76 vlELRRRVG----MVFQKPnpfpGS-----------IYDNVayglRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 152 HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
...
gi 522082967 232 QVE 234
Cdd:cd03260 218 LVE 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
1.66e-31 |
|
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: 118.82 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFEtahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKER 83
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV----EPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIiGKDISMIFQEPmtSLNPCFTVGYQI-------MEVIKEHLGGTRKELEARAIELLGLVGIpAPESRLRAfpHQMSG 156
Cdd:cd03256 74 RQL-RRQIGMIFQQF--NLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGL-LDKAYQRA--DQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAE 222
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYAD 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-218 |
2.72e-31 |
|
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: 116.38 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKER 83
Cdd:cd03214 1 EVENLSV----GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEIL-----LDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdismifqepmtslnpcftvgY--QIMEVIK-EHLggtrkelearaiellglvgipapesRLRAFpHQMSGGMNQ 160
Cdd:cd03214 72 ARKIA---------------------YvpQALELLGlAHL-------------------------ADRPF-NELSGGERQ 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVA 218
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAA 162
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-219 |
1.02e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 115.71 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLltisqKER 83
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgSIR-----VFGKPL-----EKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIG-----KDISMIFqePMTslnpcftvgyqIMEVI-------KEHLGGTRKELEARAIELLGLVGIPAPESRLRAfp 151
Cdd:cd03235 67 RKRIGyvpqrRSIDRDF--PIS-----------VRDVVlmglyghKGLFRRLSKADKAKVDEALERVGLSELADRQIG-- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 152 hQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAE 219
Cdd:cd03235 132 -ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLE 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
1.24e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.55 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL--LPWTARITADRMnFDGKDLLTI 78
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVY-LDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERRKiigkDISMIFQEPmtslNPCFTVgyQIMEVIK-----EHLGGTRKELEARAIELLGLVGI-PAPESRLRAFPH 152
Cdd:PRK14247 76 DVIELRR----RVQMVFQIP----NPIPNL--SIFENVAlglklNRLVKSKKELQERVRWALEKAQLwDEVKDRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVVNVQYAGQQ 232
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*...
gi 522082967 233 VERQNVVDLFAKPQHPYT 250
Cdd:PRK14247 224 VEWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-231 |
1.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.07 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLlEIRNLS------VEFETahglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADRMNFDGK 73
Cdd:PRK13637 1 MSI-KIENLThiymegTPFEK-----KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 74 DlltISQKERRKIIGkdisMIFQEPMtslnpcftvgYQIME--VIKE------HLGGTRKELEARAIELLGLVGIPAPES 145
Cdd:PRK13637 75 K---VKLSDIRKKVG----LVFQYPE----------YQLFEetIEKDiafgpiNLGLSEEEIENRVKRAMNIVGLDYEDY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 146 RLRAfPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVN 225
Cdd:PRK13637 138 KDKS-PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
....*.
gi 522082967 226 VQYAGQ 231
Cdd:PRK13637 217 VMNKGK 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-224 |
3.42e-30 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 114.25 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 6 IRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKERRK 85
Cdd:TIGR03608 1 LKNISKKFGDKVIL----DDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLL---EKFDSGQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 IIGKDISMIFQEpmtslnpcftvgYQIM--EVIKEHL-------GGTRKELEARAIELLGLVGIpapESRLRAFPHQMSG 156
Cdd:TIGR03608 73 FRREKLGYLFQN------------FALIenETVEENLdlglkykKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMgVVAETAEVV 224
Cdd:TIGR03608 138 GEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-246 |
3.62e-30 |
|
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: 115.13 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSV---EFEtahglfraVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTIS 79
Cdd:cd03299 1 LKVENLSKdwkEFK--------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSGKIL-----LNGKDITNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERrkiigkDISMIFQEpmTSLNPCFTVGYQIMEVIKeHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMN 159
Cdd:cd03299 68 PEKR------DISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:cd03299 136 QRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
....*..
gi 522082967 240 DLFAKPQ 246
Cdd:cd03299 216 EVFKKPK 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-254 |
8.04e-30 |
|
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: 114.36 E-value: 8.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLlEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQ 80
Cdd:cd03296 1 MSI-EVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL----ERPDSGTILFGGEDATDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERrkiigkDISMIFQEpmTSLNPCFTVGYQI---MEVIKEHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGG 157
Cdd:cd03296 72 QER------NVGFVFQH--YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQN 237
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
250
....*....|....*..
gi 522082967 238 VVDLFAKPQHPYTYALL 254
Cdd:cd03296 221 PDEVYDHPASPFVYSFL 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
9.72e-30 |
|
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: 113.69 E-value: 9.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDlltISQKER 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL----RPTSGSVLFDGED---ITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQepMTSLNPCFTVGYQIMEVIKEHLGGT---------RKELEARAIELLGLVGIpapeSRLRAFP-HQ 153
Cdd:cd03219 70 HEIARLGIGRTFQ--IPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGL----ADLADRPaGE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-270 |
1.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.12 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITAdrmnfdGKDLLTISQKERR-KIIGKDISMIFQEP 98
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTI------GERVITAGKKNKKlKPLRKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 99 MtslnpcftvgYQIME--VIKE------HLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMMIAC 170
Cdd:PRK13634 95 E----------HQLFEetVEKDicfgpmNFGVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 171 NPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQH--- 247
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDElea 242
|
250 260
....*....|....*....|....*...
gi 522082967 248 -----PYTYALLSALpERATGKRLPSIP 270
Cdd:PRK13634 243 igldlPETVKFKRAL-EEKFGISFPKPC 269
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-254 |
1.17e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.40 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLlEIRNLSVEFETahglFRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLL-PWTARITadrmnFDGKDLLT 77
Cdd:COG1118 1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTtlLRIIA--GLEtPDSGRIV-----LNGRDLFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 -ISQKERRkiIGkdisMIFQEPMtsLNPCFTVGYQIMEVIKeHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSG 156
Cdd:COG1118 69 nLPPRERR--VG----FVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAE---VVNvqyAGQQV 233
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADrvvVMN---QGRIE 213
|
250 260
....*....|....*....|.
gi 522082967 234 ERQNVVDLFAKPQHPYTYALL 254
Cdd:COG1118 214 QVGTPDEVYDRPATPFVARFL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
1.42e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTIS-QK 81
Cdd:COG4619 1 LELEGLSFRVGGKPIL----SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSgEIY-----LDGKPLSAMPpPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIigkdiSMIFQEPmtslnpcftvgyQIM-EVIKEHL-----GGTRKELEARAIELLGLVGIPapESRLRAFPHQMS 155
Cdd:COG4619 72 WRRQV-----AYVPQEP------------ALWgGTVRDNLpfpfqLRERKFDRERALELLERLGLP--PDILDKPVERLS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHD 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-213 |
1.45e-29 |
|
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: 113.49 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKER 83
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RkiigkdISMIFQEpmTSLNPCFTVGYQIMEVIKehLGGTRK-ELEARAIELLGLVGIPAPESRlraFPHQMSGGMNQRV 162
Cdd:cd03300 73 P------VNTVFQN--YALFPHLTVFENIAFGLR--LKKLPKaEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-220 |
2.91e-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: 112.12 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLltiSQKERRKI--IGKDISMIFQEpm 99
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDV---SDLRGRAIpyLRRKIGVVFQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 TSLNPCFTVGYQI---MEVIkehlGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLI 176
Cdd:cd03292 87 FRLLPDRNVYENVafaLEVT----GVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522082967 177 ADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAET 220
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTT 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-222 |
4.87e-29 |
|
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: 112.39 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKE 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV----EPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKdISMIFQE-----PMTSLNPCFT--VGYqiMEVIKEHLGGTRKELEARAIELLGLVGIpAPESRLRAfpHQMS 155
Cdd:TIGR02315 74 LRKLRRR-IGMIFQHynlieRLTVLENVLHgrLGY--KPTWRSLLGRFSEEDKERALSALERVGL-ADKAYQRA--DQLS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAE 222
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYAD 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-221 |
6.59e-29 |
|
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: 111.19 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLLTISQKE 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGGV---AALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLYGALTPSRGQVRIAGEDVNRLRGRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 ----RRKIigkdiSMIFQEpmTSLNPCFTVGYQI---MEVIkehlGGTRKELEARAIELLGLVGIpapESRLRAFPHQMS 155
Cdd:TIGR02673 74 lpllRRRI-----GVVFQD--FRLLPDRTVYENValpLEVR----GKKEREIQRRVGAALRQVGL---EHKADAFPEQLS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETA 221
Cdd:TIGR02673 140 GGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVA 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
1.18e-28 |
|
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: 111.67 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDlltIS 79
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSgRIL-----FDGRD---IT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIGKDISMIFQepMTSLNPCFTV------------GYQIMEVIKeHLGGTRK---ELEARAIELLGLVGIpapE 144
Cdd:COG0411 70 GLPPHRIARLGIARTFQ--NPRLFPELTVlenvlvaaharlGRGLLAALL-RLPRARReerEARERAEELLERVGL---A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 145 SRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVV 224
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRI 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-214 |
1.60e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.49 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFEtahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE- 82
Cdd:COG1125 3 EFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSgRIL-----IDGEDIRDLDPVEl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKI------IGkdismifqepmtsLNPCFTVGYQIMeVIKEHLGGTRKELEARAIELLGLVGIPaPESRLRAFPHQMSG 156
Cdd:COG1125 75 RRRIgyviqqIG-------------LFPHMTVAENIA-TVPRLLGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:COG1125 140 GQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDI 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-242 |
1.98e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADrmnfdGKDLLTISQKERRKIIGKDISMIFQEPM 99
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVD-----DTLITSTSKNKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 TslnpcftvgyQIME--VIK------EHLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMMIACN 171
Cdd:PRK13649 96 S----------QLFEetVLKdvafgpQNFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLF 242
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-244 |
2.03e-28 |
|
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: 110.72 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQK 81
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPDSGSIL-----IDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIigkdiSMIFQEPMtsLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGipapesrLRAFPHQ----MSGG 157
Cdd:COG4555 72 ARRQI-----GVLPDERG--LYDRLTV-RENIRYFAELYGLFDEELKKRIEELIELLG-------LEEFLDRrvgeLSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQN 237
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
....*..
gi 522082967 238 VVDLFAK 244
Cdd:COG4555 216 LDELREE 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-256 |
3.79e-28 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 109.89 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL-LPWTARITadrmnFDGKDLLTISQKE 82
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPDSGRIR-----LNGQDATRVHARD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRkiigkdISMIFQEpmTSLNPCFTVGYQI---MEVIKEhlggTRKELEARAIELLGLVGIPAPESRlraFPHQMSGGMN 159
Cdd:TIGR00968 72 RK------IGFVFQH--YALFKHLTVRDNIafgLEIRKH----PKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:TIGR00968 137 QRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPD 216
|
250
....*....|....*..
gi 522082967 240 DLFAKPQHPYTYALLSA 256
Cdd:TIGR00968 217 EVYDHPANPFVMSFLGE 233
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-213 |
4.35e-28 |
|
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: 112.05 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahglFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKER 83
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGRDITRLPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkDISMIFQEpmTSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPEsrlRAFPHQMSGGMNQRVM 163
Cdd:TIGR03265 77 ------DYGIVFQS--YALFPNLTVADNIAYGLKNR-GMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-214 |
4.82e-28 |
|
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: 110.94 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 17 HGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP---WTARITadrmnfdGKDLLTISQKERRKIigkdiSM 93
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRptsGTARVA-------GYDVVREPRKVRRSI-----GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 94 IFQEPmtSLNPCFTvGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAfphQMSGGMNQRVMIAMMIACNPR 173
Cdd:TIGR01188 71 VPQYA--SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVG---TYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522082967 174 LLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALK-EEGVTILLTTHYM 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-214 |
6.62e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.13 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PwtariTADRMNFDGKDLLTIS 79
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLdtP-----TSGDVIFNGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIGKDISMIFQepMTSLNPCFTVgyqiMEVIKEHL---GGTRKELEARAIELLGLVGIpapESRLRAFPHQMSG 156
Cdd:PRK11629 78 SAAKAELRNQKLGFIYQ--FHHLLPDFTA----LENVAMPLligKKKPAEINSRALEMLAAVGL---EHRANHRPSELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
7.48e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.57 E-value: 7.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALM-GLLPWTA-RITadrmnFDGKDLLTI 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIaGFLAPSSgEIT-----LDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 sqkerrkiiGKDISMIFQEpmTSLNPCFTV------GYQIMEVikehlggTRKELEARAIELLGLVGIPAPEsrlRAFPH 152
Cdd:COG4525 75 ---------GADRGVVFQK--DALLPWLNVldnvafGLRLRGV-------PKAERRARAEELLALVGLADFA---RRRIW 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-222 |
9.86e-28 |
|
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: 108.23 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 18 GLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKERRKIigkdiSMIFQE 97
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTSGRATVAGHDVVREPREVRRRI-----GIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PmtSLNPCFTvGYQIMEVIKEHLGGTRKELEARAIELLGLVGI-PAPESRLRAFphqmSGGMNQRVMIAMMIACNPRLLI 176
Cdd:cd03265 82 L--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLlEAADRLVKTY----SGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522082967 177 ADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMgvvaETAE 222
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYM----EEAE 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-224 |
1.61e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 105.79 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFETAHglfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKER 83
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSgEIL-----IDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKiigkDISMIFQepmtslnpcftvgyqimevikehlggtrkelearaiellglvgipapesrlrafphqMSGGMNQRVM 163
Cdd:cd00267 72 RR----RIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVV 224
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRV 150
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
3.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.02 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGL-FRAVDSVDLEIDQGEMAAIVGESGSGKSV---SMLALmgLLPWTARI----------TADRMN 69
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTfieHLNAL--LLPDTGTIewifkdeknkKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 70 FDGKDLLTISQKERRKI-----IGKDISMIFQepmtslnpcFTvGYQIMEVIKEH--------LGGTRKELEARAIELLG 136
Cdd:PRK13651 81 EKVLEKLVIQKTRFKKIkkikeIRRRVGVVFQ---------FA-EYQLFEQTIEKdiifgpvsMGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 137 LVGIPapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGV 216
Cdd:PRK13651 151 LVGLD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDN 227
|
...
gi 522082967 217 VAE 219
Cdd:PRK13651 228 VLE 230
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-311 |
5.51e-27 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 102.06 E-value: 5.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 233 VERQNVVDLFAKPQHPYTYALLSALPERA-TGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKCRSTPPAL------Hs 305
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTIKkRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALveiaegH- 81
|
....*.
gi 522082967 306 KVLCHY 311
Cdd:TIGR01727 82 RVACHL 87
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-246 |
1.59e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 17 HGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITADRMNFDGKDllTISQKERRKIiGKDISMI 94
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTLNIAGNHFDFSK--TPSDKAIREL-RRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 95 FQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLglvgipapeSRLR------AFPHQMSGGMNQRVMIA--- 165
Cdd:PRK11124 88 FQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLL---------ERLRlkpyadRFPLHLSGGQQQRVAIAral 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 166 MMiacNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVErQNVVDLFAKP 245
Cdd:PRK11124 157 MM---EPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFTQP 231
|
.
gi 522082967 246 Q 246
Cdd:PRK11124 232 Q 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-246 |
1.59e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 18 GLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITADRMNFDGKDllTISQKERRKIIGKdISMIF 95
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQK-VGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 96 QEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLglvgipapeSRLR------AFPHQMSGGMNQRVMIA---M 166
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLL---------ARLRltdkadRFPLHLSGGQQQRVAIAralM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 167 MiacNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVVAETAEVVNVQYAGQQVErQNVVDLFAKPQ 246
Cdd:COG4161 158 M---EPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQPQ 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-213 |
3.19e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHglfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKE 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF----EQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RrkiigkDISMIFQEpmTSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPESRLrafPHQMSGGMNQRV 162
Cdd:PRK11607 91 R------PINMMFQS--YALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
8-214 |
6.13e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 103.14 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 8 NLSVEFETAHGLFravdsvDLEID---QGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQK--- 81
Cdd:cd03297 1 MLCVDIEKRLPDF------TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLFDSRKKinl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 --ERRKIigkdiSMIFQEpmTSLNPCFTVGYQIMEVIKEHlggTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMN 159
Cdd:cd03297 71 ppQQRKI-----GLVFQQ--YALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:cd03297 138 QRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDL 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-255 |
7.48e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 11 VEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLL--PWTARITAD----RMNFDGKDLLTISQKERR 84
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLekPSEGSIVVNgqtiNLVRDKDGQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 85 KIIGKDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMI 164
Cdd:PRK10619 88 RLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 165 AMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAK 244
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|.
gi 522082967 245 PQHPYTYALLS 255
Cdd:PRK10619 243 PQSPRLQQFLK 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
2.06e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAhglFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA---RITADRMNFDGKDLLTIS 79
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSgevLIKGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKerrkiigkdISMIFQEPMTSLnpcFT------VGYQIMevikeHLGGTRKELEARAIELLGLVGIPAPESRLrafPHQ 153
Cdd:PRK13639 78 KT---------VGIVFQNPDDQL---FAptveedVAFGPL-----NLGLSKEEVEKRVKEALKAVGMEGFENKP---PHH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQV 233
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
250
....*....|...
gi 522082967 234 ERQNVVDLFAKPQ 246
Cdd:PRK13639 217 KEGTPKEVFSDIE 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-213 |
2.12e-25 |
|
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: 101.56 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFetaHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDlltISQKERR 84
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNGKP---IKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 85 KIIGkdisMIFQEPmtslnpcftvGYQI-MEVIKEHLGGTRKELEA---RAIELLGLVGIPAPESRLrafPHQMSGGMNQ 160
Cdd:cd03226 71 KSIG----YVMQDV----------DYQLfTDSVREELLLGLKELDAgneQAETVLKDLDLYALKERH---PLSLSGGQKQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHD 213
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHD 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-213 |
4.30e-25 |
|
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: 100.79 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKER 83
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkDISMIFQEpmTSLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVM 163
Cdd:cd03301 73 ------DIAMVFQN--YALYPHMTV-YDNIAFGLKLRKVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-235 |
5.32e-25 |
|
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: 106.07 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSvefetahglFR-------AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDL 75
Cdd:COG2274 474 IELENVS---------FRypgdsppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRIL-----IDGIDL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 76 LTISQKERRKIIGkdisMIFQEPM----TslnpcftvgyqimevIKEHLGGTRKEL-EARAIELLGLVGIpapESRLRAF 150
Cdd:COG2274 540 RQIDPASLRRQIG----VVLQDVFlfsgT---------------IRENITLGDPDAtDEEIIEAARLAGL---HDFIEAL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 151 PHQM-----------SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAE 219
Cdd:COG2274 598 PMGYdtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL 675
|
250
....*....|....*.
gi 522082967 220 TAEVVNVQyAGQQVER 235
Cdd:COG2274 676 ADRIIVLD-KGRIVED 690
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
5.41e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 103.61 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQ 80
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE----DPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERrkiigkDISMIFQEPMtsLNPCFTVgYQIM----EVIKEhlggTRKELEARAIELLGLVGIpapESRLRAFPHQMSG 156
Cdd:COG3839 73 KDR------NIAMVFQSYA--LYPHMTV-YENIafplKLRKV----PKAEIDRRVREAAELLGL---EDLLDRKPKQLSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
1.27e-24 |
|
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: 98.22 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSveFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE 82
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgEIL-----IDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdisMIFQEP----MTslnpcftvgyqIMEVIkehlggtrkelearaiellglvgipapesrlrafphqMSGGM 158
Cdd:cd03228 74 LRKNIA----YVPQDPflfsGT-----------IRENI-------------------------------------LSGGQ 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDM 214
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRL 155
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-260 |
1.64e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADRMNFDGKDLLTIsq 80
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVLSEETVWDV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 keRRKIigkdiSMIFQEPMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGG 157
Cdd:PRK13635 80 --RRQV-----GMVFQNPDNQF-----VGATVQDDVAfglENIGVPREEMVERVDQALRQVGM---EDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAEtAEVVNVQYAGQQVERQN 237
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
250 260 270
....*....|....*....|....*....|.
gi 522082967 238 VVDLFAKPQH--------PYTYALLSALPER 260
Cdd:PRK13635 224 PEEIFKSGHMlqeigldvPFSVKLKELLKRN 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
3.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.07 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLltisQK 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITI----SK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMIFQEPMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGM 158
Cdd:PRK13632 76 ENLKEIRKKIGIIFQNPDNQF-----IGATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-262 |
3.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 20 FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtARITADRMNFDGKDLLTISQKERRKIIGKDISMIFQEPM 99
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI---ISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 tslnpcftvgYQIMEVIKE--------HLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMMIACN 171
Cdd:PRK13645 101 ----------YQLFQETIEkdiafgpvNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQ----- 246
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQElltki 248
|
250
....*....|....*....
gi 522082967 247 ---HPYTYALLSALPERAT 262
Cdd:PRK13645 249 eidPPKLYQLMYKLKNKGI 267
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-278 |
4.79e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 9 LSVEFETAHGLF--------RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQ 80
Cdd:PRK13641 1 MSIKFENVDYIYspgtpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLnpcF--TVGYQIMEVIKeHLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGM 158
Cdd:PRK13641 77 NKNLKKLRKKVSLVFQFPEAQL---FenTVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNV 238
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 522082967 239 VDLFAKPQ--------HPYTYALLSALpeRATGKRLPSIPGVVPGLLD 278
Cdd:PRK13641 230 KEIFSDKEwlkkhyldEPATSRFASKL--EKGGFKFSEMPLTIDELVD 275
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-213 |
5.83e-24 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 101.33 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEF----ETAHGLFR----------------AVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPw 59
Cdd:COG4175 1 MPKIEVRNLYKIFgkrpERALKLLDqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKS-TLVrCLNRLIE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 60 tarITADRMNFDGKDLLTISQKERRKIIGKDISMIFQE----P-MTSL-NpcftVGY--QIMevikehlGGTRKELEARA 131
Cdd:COG4175 79 ---PTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQHfallPhRTVLeN----VAFglEIQ-------GVPKAERRERA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 132 IELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLIT 211
Cdd:COG4175 145 REALELVGL---AGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFIT 221
|
..
gi 522082967 212 HD 213
Cdd:COG4175 222 HD 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-224 |
6.62e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 6.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSV---SMLALmgLLPWTARITADRMNF-DGKDLLTISQKErrkiigkdiSMIFQE 97
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTiakHMNAL--LIPSEGKVYVDGLDTsDEENLWDIRNKA---------GMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PMTslnpcftvgyQIMEVI--------KEHLGGTRKELEARAIELLGLVGIPapESRLRAfPHQMSGGMNQRVMIAMMIA 169
Cdd:PRK13633 94 PDN----------QIVATIveedvafgPENLGIPPEEIRERVDESLKKVGMY--EYRRHA-PHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 170 CNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVV 224
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRII 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-213 |
1.40e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.16 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVsmlaLMGLLPWTARITADRMNFDGKDLLTISQKERRKIIGKDISMIFQEPM--TSLN 103
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKST----LLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 104 PCFTVgyQIMEVIKehlGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTA 183
Cdd:PRK10584 105 ALENV--ELPALLR---GESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|
gi 522082967 184 LDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-227 |
2.25e-23 |
|
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: 96.35 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFeTAHGL----FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMG-LLPWTARITADRmNFDGKDLLT 77
Cdd:COG4778 4 LLEVENLSKTF-TLHLQggkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRH-DGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKE----RRKiigkdismifqepmtslnpcfTVGY--QI---------MEVIKE---HLGGTRKELEARAIELLGLVG 139
Cdd:COG4778 82 ASPREilalRRR---------------------TIGYvsQFlrviprvsaLDVVAEpllERGVDREEARARARELLARLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 140 IPapeSRL-RAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVA 218
Cdd:COG4778 141 LP---ERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVRE 216
|
250
....*....|
gi 522082967 219 ETA-EVVNVQ 227
Cdd:COG4778 217 AVAdRVVDVT 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-227 |
2.28e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLLTISQK 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 E----RRKIIGkdisMIFQEpmTSLNPCFTVGyQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGG 157
Cdd:PRK10535 79 AlaqlRREHFG----FIFQR--YHLLSHLTAA-QNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQ 227
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQAERVIEIR 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-214 |
2.73e-23 |
|
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: 96.03 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTisqkeR 83
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL----RPTSGTAYINGYSIRT-----D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEPMtsLNPCFTVgyqimeviKEHL-------GGTRKELEARAIELLGLVGIPAPESRLrafPHQMSG 156
Cdd:cd03263 70 RKAARQSLGYCPQFDA--LFDELTV--------REHLrfyarlkGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDM 214
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSM 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-244 |
3.42e-23 |
|
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: 100.22 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE 82
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSgSIL-----INGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKiigkDISMIFQEP----MTslnpcftvgyqIMEVIKehLGG---TRKELEArAIELLGLvgipapESRLRAFPHQM- 154
Cdd:COG4988 409 WRR----QIAWVPQNPylfaGT-----------IRENLR--LGRpdaSDEELEA-ALEAAGL------DEFVAALPDGLd 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 ----------SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVAETAEVV 224
Cdd:COG4988 465 tplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRIL 542
|
250 260
....*....|....*....|
gi 522082967 225 NVQyAGQQVERQNVVDLFAK 244
Cdd:COG4988 543 VLD-DGRIVEQGTHEELLAK 561
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
3.44e-23 |
|
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: 94.03 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKdlltisqker 83
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK----PDSGEILVDGK---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkdismifqePMTSLNPcftvgyqimevikehlggtrkeleARAIELlglvGIpapesrlrAFPHQMSGGMNQRVM 163
Cdd:cd03216 63 --------------EVSFASP------------------------RDARRA----GI--------AMVYQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQV 233
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-249 |
3.87e-23 |
|
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: 98.65 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 9 LSVEFETAHGLFrAVDsVDLEIDQGEMAAIVGESGSGKSvSMLALM-GLL-PWTARIT-ADRMNFDGKDLLTISQKERRk 85
Cdd:TIGR02142 1 LSARFSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKT-TLIRLIaGLTrPDEGEIVlNGRTLFDSRKGIFLPPEKRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 iigkdISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLvgipapESRLRAFPHQMSGGMNQRVMIA 165
Cdd:TIGR02142 77 -----IGYVFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGI------GHLLGRLPGRLSGGEKQRVAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 166 MMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKP 245
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
....
gi 522082967 246 QHPY 249
Cdd:TIGR02142 224 DLPW 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-213 |
6.63e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglFRAvdsvDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLPwtarITADRMNFDGKDLLTISQK 81
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRF----DLTIAAGERVAILGPSGAGKStlLNLIA--GFLP----PDSGRILWNGQDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERrkiigkDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGGTRKElEARAIELLGLVGIPAPESRLrafPHQMSGGMNQR 161
Cdd:COG3840 70 ER------PVSMLFQE--NNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRL---PGQLSGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-250 |
9.10e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.50 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 25 SVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP-WTARITAD-RMNFDGKDLLTISQKERRKIIGkdisMIFQEPmtSL 102
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDgKVLYFGKDIFQIDAIKLRKEVG----MVFQQP--NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 NPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGI-PAPESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 182 TALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQHPYT 250
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
1.27e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGK--DLLTISQ 80
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ----PDSGEILLDGEpvRFRSPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRkiiGkdISMIFQEPmtSLNPCFTV------GYQIMEvikehlGGT--RKELEARAIELLGLVGIP-APESRLRafp 151
Cdd:COG1129 76 AQAA---G--IAIIHQEL--NLVPNLSVaeniflGREPRR------GGLidWRAMRRRARELLARLGLDiDPDTPVG--- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 152 hQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:COG1129 140 -DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRL 200
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-213 |
1.32e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 93.70 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEF-ETAhgLFRavdSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPwtarITADRMNFDGKDLltisq 80
Cdd:COG4133 2 MLEAENLSCRRgERL--LFS---GLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLP----PSAGEVLWNGEPI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMtsLNPCFTVGyqimevikEHL---------GGTRKELEArAIELLGLVGipapesRLRAFP 151
Cdd:COG4133 67 RDAREDYRRRLAYLGHADG--LKPELTVR--------ENLrfwaalyglRADREAIDE-ALEAVGLAG------LADLPV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 152 HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMAlVLITHD 213
Cdd:COG4133 130 RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-233 |
1.39e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.46 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP---WTARITadrmnFDGKDLL--T 77
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEGEII-----FEGEELQasN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKERrkiigKDISMIFQEPMtsLNPCFTVGYQIMevikehLGG--TRK------ELEARAIELLGLVGIPA-PESRLR 148
Cdd:PRK13549 76 IRDTER-----AGIAIIHQELA--LVKELSVLENIF------LGNeiTPGgimdydAMYLRAQKLLAQLKLDInPATPVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 149 afphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHkRGMALVLITHDMGVVAETAEVVNVQY 228
Cdd:PRK13549 143 ----NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIR 217
|
....*
gi 522082967 229 AGQQV 233
Cdd:PRK13549 218 DGRHI 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-250 |
1.79e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLAL--MGLLPWTARITADrMNFDGKDLLtiSQ 80
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGS-IVYNGHNIY--SP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPmtslNPcftVGYQIME--VIKEHLGGTR-KELEARAIE--LLGLVGIPAPESRLRAFPHQMS 155
Cdd:PRK14239 78 RTDTVDLRKEIGMVFQQP----NP---FPMSIYEnvVYGLRLKGIKdKQVLDEAVEksLKGASIWDEVKDRLHDSALGLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVliTHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLIEY 228
|
250
....*....|....*
gi 522082967 236 QNVVDLFAKPQHPYT 250
Cdd:PRK14239 229 NDTKQMFMNPKHKET 243
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-224 |
2.51e-22 |
|
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: 96.32 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLL-PWTARITadrmnFDGKDLLTISQK-----ERRKIigkdiSMIFQE 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTtlLRAIA--GLErPDSGRIR-----LGGEVLQDSARGiflppHRRRI-----GYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PmtSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLvgipapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIA 177
Cdd:COG4148 86 A--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGI------GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 522082967 178 DEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVV 224
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHV 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-214 |
2.82e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITADRMNFDGKdlltisqk 81
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHgSITLDGKPVEGP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 errkiiGKDISMIFQE----PMTSLNPCFTVGYQIMevikehlGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGG 157
Cdd:PRK11248 69 ------GAERGVVFQNegllPWRNVQDNVAFGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-242 |
2.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP---WTARItadrmnfdGKDLLTISQKERR-KIIGKDISMIFQ 96
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpteGKVTV--------GDIVVSSTSKQKEiKPVRKKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 97 EPMTSLNPCFTVgyQIMEVIKEHLGGTRKELEARAIELLGLVGIPapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLI 176
Cdd:PRK13643 92 FPESQLFEETVL--KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 177 ADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLF 242
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
3.20e-22 |
|
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: 93.27 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDlltISQKER 83
Cdd:cd03224 1 LEVENLNA----GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRD---ITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEPMtsLNPCFTVgyqimeviKEHL-----GGTRKELEARAIELLGLVgiPAPESRLRAFPHQMSGGM 158
Cdd:cd03224 70 HERARAGIGYVPEGRR--IFPELTV--------EENLllgayARRRAKRKARLERVYELF--PRLKERRKQLAGTLSGGE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETA 221
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIA 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-225 |
4.76e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVeFETAHGLFRavdSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtARITAD-RMNFDGKDLLTISQKE 82
Cdd:COG4136 2 LSLENLTI-TLGGRPLLA---PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASgEVLLNGRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRkiigkdISMIFQEPMtsLNPCFTVGYQIMEVIKEHLGgtRKELEARAIELLGLVGIPAPESRlraFPHQMSGGMNQRV 162
Cdd:COG4136 76 RR------IGILFQDDL--LFPHLSVGENLAFALPPTIG--RAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVN 225
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLD 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
8.59e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL-LPWTARITAdrmnfDGKDLLTISQKE 82
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKV-----MGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdisMIFQEP------MTSLNPCfTVGYQIMEVikehlggTRKELEARAIELLGLVGIpaPESRLRAfPHQMSG 156
Cdd:PRK13647 77 VRSKVG----LVFQDPddqvfsSTVWDDV-AFGPVNMGL-------DKDEVERRVEEALKAVRM--WDFRDKP-PYHLSY 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAETAEVVNVQYAGQQV 233
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-267 |
1.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.85 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARItadrMNFDGKDLLTISQKE 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK----VKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdisMIFQEPMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIPAPESRLrafPHQMSGGMN 159
Cdd:PRK13642 79 LRRKIG----MVFQNPDNQF-----VGATVEDDVAfgmENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVnVQYAGQQVERQNVV 239
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRIL-VMKAGEIIKEAAPS 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 522082967 240 DLFAKPQH--------PYTYALLSALpeRATGKRLP 267
Cdd:PRK13642 226 ELFATSEDmveigldvPFSSNLMKDL--RKNGFDLP 259
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-249 |
1.78e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.33 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 18 GLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMGLLpwtARITADRMNFDGKDLLTISQKERRKIIGKDISMIFQE 97
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRL---IEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 pmTSLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIA 177
Cdd:PRK10070 115 --FALMPHMTV-LDNTAFGMELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 178 DEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQHPY 249
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
2.15e-21 |
|
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: 94.87 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahglFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL---LPWTARIT-----------ADRMN 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 70 FDGK--------------DLLTISQKERRKIIgKDISMIFQEPMtSLNPCFTVGYQIMEVIKEhLGGTRKELEARAIELL 135
Cdd:TIGR03269 77 KVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEALEE-IGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 136 GLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMG 215
Cdd:TIGR03269 154 EMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
....*..
gi 522082967 216 VVAETAE 222
Cdd:TIGR03269 231 VIEDLSD 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-259 |
2.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITADrmnfdgKDLLTIS 79
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQIIID------GDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 Q--KERRKIigkdiSMIFQEPMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIPAPESRLrafPHQM 154
Cdd:PRK13650 75 NvwDIRHKI-----GMVFQNPDNQF-----VGATVEDDVAfglENKGIPHEEMKERVNEALELVGMQDFKERE---PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVnVQYAGQQVE 234
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVL-VMKNGQVES 220
|
250 260 270
....*....|....*....|....*....|...
gi 522082967 235 RQNVVDLFAKPQH--------PYTYALLSALPE 259
Cdd:PRK13650 221 TSTPRELFSRGNDllqlgldiPFTTSLVQSLRQ 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-250 |
4.91e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVsmlalmgLLpwtaRiTADRMN-------------F 70
Cdd:COG1117 12 IEVRNLNV----YYGDKQALKDINLDIPENKVTALIGPSGCGKST-------LL----R-CLNRMNdlipgarvegeilL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 71 DGKDLL--TISQKERRKIIGkdisMIFQEPmtslNPcF--------TVGYQIMEVIKehlggtRKELEARAIELLGLVGI 140
Cdd:COG1117 76 DGEDIYdpDVDVVELRRRVG----MVFQKP----NP-FpksiydnvAYGLRLHGIKS------KSELDEIVEESLRKAAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 141 PaPE--SRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVA 218
Cdd:COG1117 141 W-DEvkDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAA 217
|
250 260 270
....*....|....*....|....*....|..
gi 522082967 219 ETAEVVNVQYAGQQVERQNVVDLFAKPQHPYT 250
Cdd:COG1117 218 RVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-213 |
5.59e-21 |
|
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: 91.79 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 38 IVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKERrkiigkDISMIFQEpmTSLNPCFTVGYQIMEVIK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF----EQPDSGSIMLDGEDVTNVPPHLR------HINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 118 EHlGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQ 197
Cdd:TIGR01187 69 MR-KVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170
....*....|....*.
gi 522082967 198 DLQHKRGMALVLITHD 213
Cdd:TIGR01187 145 TIQEQLGITFVFVTHD 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-244 |
6.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLlTISQK---ERRKIIGkdisMIFQE 97
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGRIL-----FDGKPI-DYSRKglmKLRESVG----MVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PMTSLnpcFTVG-YQIMEVIKEHLGGTRKELEARAIELLGLVGIpapeSRLRAFP-HQMSGGMNQRVMIAMMIACNPRLL 175
Cdd:PRK13636 91 PDNQL---FSASvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 176 IADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAK 244
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-255 |
6.15e-21 |
|
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: 93.68 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE 82
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSgSIT-----LGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdisMIFQEPmtslnpcftvgyqimevikeHL-GGT--------RKEL-EARAIELLGLVGIpapESRLRAFPH 152
Cdd:COG4987 407 LRRRIA----VVPQRP--------------------HLfDTTlrenlrlaRPDAtDEELWAALERVGL---GDWLAALPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 -----------QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLqdLQHKRGMALVLITHDMGVVAETA 221
Cdd:COG4987 460 gldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERMD 537
|
250 260 270
....*....|....*....|....*....|....
gi 522082967 222 EVVnVQYAGQQVERQNVVDLFAkpQHPYTYALLS 255
Cdd:COG4987 538 RIL-VLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-260 |
8.09e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.63 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKS-VSMLALMGLLPWTA---RITADRMNFDGKDLLTISQKerrkiigkdISMIFQE 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKStISKLINGLLLPDDNpnsKITVDGITLTAKTVWDIREK---------VGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PMTSLnpcftVGYQIMEVIK---EHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRL 174
Cdd:PRK13640 93 PDNQF-----VGATVGDDVAfglENRAVPRPEMIKIVRDVLADVGM---LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 175 LIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGvVAETAEVVNVQYAGQQVERQNVVDLFAKPQH------- 247
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVEMlkeigld 243
|
250
....*....|....
gi 522082967 248 -PYTYALLSALPER 260
Cdd:PRK13640 244 iPFVYKLKNKLKEK 257
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-213 |
1.49e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.32 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLltisqk 81
Cdd:PRK11432 5 NFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL----EKPTEGQIFIDGEDV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMIFQE----PMTSLNPcfTVGYQImevikEHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQMSGG 157
Cdd:PRK11432 71 THRSIQQRDICMVFQSyalfPHMSLGE--NVGYGL-----KMLGVPKEERKQRVKEALELVDLAGFEDR---YVDQISGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-245 |
3.17e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEF-ETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP------WTARI-TADRMNFDGKD 74
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiQVGDIyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 75 LLTISQKERR-KIIGKDISMIFQEPMTSLnpcF--TVGYQIMevikehLG----GTRKElEARAIELLGLVGIPAPESRL 147
Cdd:PRK13631 101 TNPYSKKIKNfKELRRRVSMVFQFPEYQL---FkdTIEKDIM------FGpvalGVKKS-EAKKLAKFYLNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 148 RAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQ 227
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*...
gi 522082967 228 YAGQQVERQNVVDLFAKP 245
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQ 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
5.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWT--ARITADRMNFdGKDLLT--IS 79
Cdd:PRK14267 5 IETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeeARVEGEVRLF-GRNIYSpdVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIGkdisMIFQEPmtSLNPCFTVGYQIMEVIK-EHLGGTRKELEARAIELLGLVGI-PAPESRLRAFPHQMSGG 157
Cdd:PRK14267 80 PIEVRREVG----MVFQYP--NPFPHLTIYDNVAIGVKlNGLVKSKKELDERVEWALKKAALwDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQN 237
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250
....*....|...
gi 522082967 238 VVDLFAKPQHPYT 250
Cdd:PRK14267 232 TRKVFENPEHELT 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-218 |
5.45e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVsmlaLMGLLPWTARITADRMNFDGKDlltISQKERRKI--IGKDISMIFQEP 98
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICGIERPSAGKIWFSGHD---ITRLKNREVpfLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 99 MTSLNPCFTVGYQIMEVIKehlGGTRKELEARAIELLGLVGIPapeSRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIAD 178
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIA---GASGDDIRRRVSAALDKVGLL---DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522082967 179 EPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVA 218
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLIS 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
7.09e-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: 87.45 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLLPWTARITADRMnfdGKDLLTI 78
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKStlLSLIT--GDLPPTYGNDVRLF---GERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERRKIIGKdISMIFQEPMTSLNPCFTV----GYQIMEVIKEHlggtRKELEARAIELLGLVGIpapeSRL--RAFpH 152
Cdd:COG1119 72 DVWELRKRIGL-VSPALQLRFPRDETVLDVvlsgFFDSIGLYREP----TDEQRERARELLELLGL----AHLadRPF-G 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 153 QMSGGMNQRVMI--AMMIacNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITH 212
Cdd:COG1119 142 TLSQGEQRRVLIarALVK--DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-213 |
8.58e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.52 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKE 82
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS----PDSGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdisMIFQEpmTSLNPCFTVgyqiMEVIK---EHLGGTRKELEARAIELLGLVGIPAPESRLraFPhQMSGGMN 159
Cdd:PRK13548 74 LARRRA----VLPQH--SSLSFPFTV----EEVVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSGGEQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIA------CNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
1.11e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAhglFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQ 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGkdisMIFQEPMTSL-NPcfTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIPapESRLRAfPHQMSGGMN 159
Cdd:PRK13652 74 REVRKFVG----LVFQNPDDQIfSP--TV-EQDIAFGPINLGLDEETVAHRVSSALHMLGLE--ELRDRV-PHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVV 239
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*.
gi 522082967 240 DLFAKP 245
Cdd:PRK13652 224 EIFLQP 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-214 |
1.37e-19 |
|
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: 86.37 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDlltISQKerrkiiGKDISMIFQEpmTSL 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQ---ITEP------GPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 NPCFTVGYQIMEVIKEHLGGTRKElEARAI--ELLGLVGIPAPESRlraFPHQMSGGMNQRVMIAMMIACNPRLLIADEP 180
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKS-ERRAIveEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190
....*....|....*....|....*....|....
gi 522082967 181 TTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDV 175
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-219 |
1.67e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDlLTIS--Q 80
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY----QPDSGEILIDGKP-VRIRspR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGkdisMIFQEPMtsLNPCFTVgyqiMEVI---KEHLGGT---RKELEARAIELLGLVGIPAPesrLRAFPHQM 154
Cdd:COG3845 76 DAIALGIG----MVHQHFM--LVPNLTV----AENIvlgLEPTKGGrldRKAARARIRELSERYGLDVD---PDAKVEDL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALdvTIQaQILELLQDLQH--KRGMALVLITHDMGVVAE 219
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMA 206
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-296 |
1.83e-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: 1.83e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 233 VERQNVVDLFAKPQHPYTYALLSALPE-RATGKRLPSIPGVVPGLLDRPTGCLFNPRCQFATDKC 296
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRlDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-214 |
1.95e-19 |
|
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: 84.41 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEfetahglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKE 82
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKiigkdismifqepmtslnpcftvgyqimevikehLGgtrkelearaielLGLVgipaPESRLR-------------A 149
Cdd:cd03215 72 AIR----------------------------------AG-------------IAYV----PEDRKReglvldlsvaeniA 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 150 FPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:cd03215 101 LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSEL 164
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-219 |
2.41e-19 |
|
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: 89.09 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEF-ETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQK 81
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIiGKDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLggtRKELEAR-AIELLGLVGIPAPESR--LRAFPHQMSGGM 158
Cdd:TIGR03269 359 GRGRA-KRYIGILHQE--YDLYPHRTVLDNLTEAIGLEL---PDELARMkAVITLKMVGFDEEKAEeiLDKYPDELSEGE 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAE 219
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-235 |
5.46e-19 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.81 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKER 83
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RkiigkdISMIFQEPmtSLNPCFTVgyqiMEVIKEHLGGTRKElEARAIELLGLVGIPAPESR-LRAFphqmSGGMNQRV 162
Cdd:cd03268 73 R------IGALIEAP--GFYPNLTA----RENLRLLARLLGIR-KKRIDEVLDVVGLKDSAKKkVKGF----SLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-233 |
7.12e-19 |
|
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: 87.57 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP---WTARITadrmnFDGKDLLT-- 77
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDGEIY-----WSGSPLKAsn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKERrkiigKDISMIFQEPMtsLNPCFTVGYQIMEVIKEHLGGTRKELEA---RAIELLGLVGIPA-PESRLRAfphQ 153
Cdd:TIGR02633 72 IRDTER-----AGIVIIHQELT--LVPELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDAdNVTRPVG---D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQV 233
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-233 |
7.47e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLlEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQ 80
Cdd:PRK10851 1 MSI-EIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQTSGHIRFHGTDVSRLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRkiigkdISMIFQ-----EPMTSL-NPCFTvgyqiMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRlraFPHQM 154
Cdd:PRK10851 72 RDRK------VGFVFQhyalfRHMTVFdNIAFG-----LTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAG--QQ 232
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGniEQ 217
|
.
gi 522082967 233 V 233
Cdd:PRK10851 218 A 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-231 |
8.81e-19 |
|
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: 83.40 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetAHGlfRAVDSVDLEIDQGeMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKER 83
Cdd:cd03264 1 LQLENLTKRY--GKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP----PSSGTIRIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIigkdiSMIFQEPMTSlnPCFTVGYQI--MEVIKehlGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQR 161
Cdd:cd03264 72 RRI-----GYLPQEFGVY--PNFTVREFLdyIAWLK---GIPSKEVKARVDEVLELVNL---GDRAKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-212 |
1.01e-18 |
|
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: 83.31 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 27 DLEIDQGEMAAIVGESGSGKSvSMLALMG--LLPWTARITadrmnFDGKDLLTISQKERrkiigkDISMIFQEpmTSLNP 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKS-TLLNLIAgfETPQSGRVL-----INGVDVTAAPPADR------PVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 105 CFTVGYQIMEVIKEHLGGTRKELEARAIeLLGLVGIPAPESRLrafPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTAL 184
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTAEDRQAIEV-ALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180
....*....|....*....|....*...
gi 522082967 185 DVTIQAQILELLQDLQHKRGMALVLITH 212
Cdd:cd03298 160 DPALRAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-257 |
1.42e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA--RITAD-----RMNFDGKDLLtisqkERRKIIGkdisMIF 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyRYSGDvllggRSIFNYRDVL-----EFRRRVG----MLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 96 QEPmtslNPC-FTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGI-PAPESRLRAFPHQMSGGMNQRVMIAMMIACNPR 173
Cdd:PRK14271 108 QRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 174 LLIADEPTTALDVTIQAQILELLQDLQHKrgMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQHPYTYAL 253
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
....
gi 522082967 254 LSAL 257
Cdd:PRK14271 262 VAGL 265
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
1.90e-18 |
|
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: 86.19 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFEtahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKER 83
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdisMIFQEPmtslnpcFTVGYQIMEVIKEHLGGTRKELEARAIELLGLV----GIPAP-ESRLRAFPHQMSGGM 158
Cdd:TIGR02857 395 RDQIA----WVPQHP-------FLFAGTIAENIRLARPDASDAEIREALERAGLDefvaALPQGlDTPIGEGGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVVNV 226
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-234 |
2.60e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetaHGLfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP---WTARITadrmnFDG-----KD 74
Cdd:NF040905 1 ILEMRGITKTF---PGV-KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsYEGEIL-----FDGevcrfKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 75 lltISQKERRKIIgkdisMIFQE----PMTSlnpcftvgyqIMEVIkeHLGGTRK--------ELEARAIELLGLVGIP- 141
Cdd:NF040905 72 ---IRDSEALGIV-----IIHQElaliPYLS----------IAENI--FLGNERAkrgvidwnETNRRARELLAKVGLDe 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 142 APESRLRafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETA 221
Cdd:NF040905 132 SPDTLVT----DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVA 206
|
250
....*....|...
gi 522082967 222 EVVNVQYAGQQVE 234
Cdd:NF040905 207 DSITVLRDGRTIE 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
3.26e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTIS 79
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVL-----VAGDDVEALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKErrkiIGKDISMIFQEpmTSLNPCFTVgYQIMEVIKE-HLG--GTRKELEARAIE-LLGLVGIPAPESRlrAFPhQMS 155
Cdd:PRK09536 72 ARA----ASRRVASVPQD--TSLSFEFDV-RQVVEMGRTpHRSrfDTWTETDRAAVErAMERTGVAQFADR--PVT-SLS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVVA 218
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAA 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-213 |
6.30e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.84 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQ 80
Cdd:PRK09452 12 SPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF----ETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERrkiigkDISMIFQEpmTSLNPCFTV------GYQIMEVIKEhlggtrkELEARAIELLGLVgipapesRLRAF---- 150
Cdd:PRK09452 84 ENR------HVNTVFQS--YALFPHMTVfenvafGLRMQKTPAA-------EITPRVMEALRMV-------QLEEFaqrk 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082967 151 PHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQI-LELLQdLQHKRGMALVLITHD 213
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqNELKA-LQRKLGITFVFVTHD 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-235 |
1.17e-17 |
|
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: 80.49 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQK 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFAT-----VDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIiGkdismiFQEPMTSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPESRLRAfphQMSGGMNQR 161
Cdd:cd03266 76 ARRRL-G------FVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-233 |
1.35e-17 |
|
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: 80.02 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLlTISQKER 83
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL----PDSGEVLFDGKPL-DIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkdISMIFQEpmTSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGI-PAPESRLRafphQMSGGMNQRV 162
Cdd:cd03269 72 -------IGYLPEE--RGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELsEYANKRVE----ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQV 233
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-212 |
1.72e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.49 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahglFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGlLPwTARITADRMNFDGKDLLTISQKER 83
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HP-KYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKiigKDISMIFQEPMtslnpcftvgyQIMEVIKEHLggtrkelearaiellglvgipapesrLRAFPHQMSGGMNQRVM 163
Cdd:cd03217 75 AR---LGIFLAFQYPP-----------EIPGVKNADF--------------------------LRYVNEGFSGGEKKRNE 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITH 212
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-212 |
2.53e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.91 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLLTISQKERRKIIGkdisMIFQEP--- 98
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG----VVPQDTflf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 99 -MTslnpcftvgyqIMEVIKehLGG---TRKELEArAIELLGLvgipapESRLRAFPHQM-----------SGGMNQRVM 163
Cdd:COG1132 427 sGT-----------IRENIR--YGRpdaTDEEVEE-AAKAAQA------HEFIEALPDGYdtvvgergvnlSGGQRQRIA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITH 212
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAH 533
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-210 |
3.16e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 79.64 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDlltISQ 80
Cdd:COG0410 1 MPMLEVENLHA----GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGED---ITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISM------IFQEpMTslnpcftvgyqimevIKEHL------GGTRKELEARAIELLGLVgipaPesRLR 148
Cdd:COG0410 70 LPPHRIARLGIGYvpegrrIFPS-LT---------------VEENLllgayaRRDRAEVRADLERVYELF----P--RLK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 149 AFPHQ----MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLI 210
Cdd:COG0410 128 ERRRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLV 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-212 |
3.29e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 27 DLEIDQGEMAAIVGESGSGKSvSMLALM-GLLPwtarITADRMNFDGKDLLTISQKERrkiigkDISMIFQEpmTSLNPC 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLT----PASGSLTLNGQDHTTTPPSRR------PVSMLFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 106 FTVGYQIMEVIKEHL---GGTRKELEARAiellGLVGIPAPESRLrafPHQMSGGMNQRVMIAM-MIACNPRLLIaDEPT 181
Cdd:PRK10771 86 LTVAQNIGLGLNPGLklnAAQREKLHAIA----RQMGIEDLLARL---PGQLSGGQRQRVALARcLVREQPILLL-DEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 522082967 182 TALDVTIQAQILELLQDLQHKRGMALVLITH 212
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-273 |
7.07e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLltiSQKE 82
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSgEVL-----WDGEPL---DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIigkdismifqepmtslnpcftvGY--------QIMEVIkEHL-------GGTRKELEARAIELLGLVGIPA-PESR 146
Cdd:COG4152 70 RRRI----------------------GYlpeerglyPKMKVG-EQLvylarlkGLSKAEAKRRADEWLERLGLGDrANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 147 LRafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVtIQAQIL-ELLQDLqHKRGMALVLITHDMGVVAETAEVVN 225
Cdd:COG4152 127 VE----ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLkDVIREL-AAKGTTVIFSSHQMELVEELCDRIV 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 522082967 226 VQYAGQQVERQNVVDLfaKPQHPYTYALLSAlpeRATGKRLPSIPGVV 273
Cdd:COG4152 201 IINKGRKVLSGSVDEI--RRQFGRNTLRLEA---DGDAGWLRALPGVT 243
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-213 |
7.34e-17 |
|
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: 80.81 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 6 IRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwTARITADRMNFDGKDLLTISQKERrk 85
Cdd:TIGR03258 8 IDHLRV----AYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFV--KAAGLTGRIAIADRDLTHAPPHKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 iigkDISMIFQEpmTSLNPCFTVGYQIMEVIKEHlGGTRKELEARAIELLGLVGIPAPESRLrafPHQMSGGMNQRVMIA 165
Cdd:TIGR03258 80 ----GLALLFQN--YALFPHLKVEDNVAFGLRAQ-KMPKADIAERVADALKLVGLGDAAAHL---PAQLSGGMQQRIAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 166 MMIACNPRLLIADEPTTALDVTIQAQILELLQDLqHKR--GMALVLITHD 213
Cdd:TIGR03258 150 RAIAIEPDVLLLDEPLSALDANIRANMREEIAAL-HEElpELTILCVTHD 198
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-213 |
7.36e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.00 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVefeTAHGLfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMG-LLPWTARITadrmnFDGKDLLTISQK 81
Cdd:COG4559 1 MLEAENLSV---RLGGR-TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVR-----LNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGkdisMIFQEpmTSLNPCFTVgyqiMEVIK---EHLGGTRKELEARAIELLGLVGIPAPESRLraFPhQMSGGM 158
Cdd:COG4559 72 ELARRRA----VLPQH--SSLAFPFTV----EEVVAlgrAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSGGE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 159 NQRVMIAMMIA-----CN--PRLLIADEPTTALDVTIQAQILELLQDLQHkRGMALVLITHD 213
Cdd:COG4559 139 QQRVQLARVLAqlwepVDggPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHD 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-244 |
7.71e-17 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 78.43 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLLTISQKER 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdisMIFQEPmtslnpcFTVGYQIMEVIK-EHLGGTRKELE--ARAIELLGLVgIPAPE---SRLRAFPHQMSGG 157
Cdd:cd03251 75 RRQIG----LVSQDV-------FLFNDTVAENIAyGRPGATREEVEeaARAANAHEFI-MELPEgydTVIGERGVKLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgMALVlITHDMGVVAETAEVVnVQYAGQQVERQN 237
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTIENADRIV-VLEDGKIVERGT 219
|
....*..
gi 522082967 238 VVDLFAK 244
Cdd:cd03251 220 HEELLAQ 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
1.39e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLAL--MGLLPWTARITAdRMNFDGKDLLtisqk 81
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEG-RVEFFNQNIY----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGK---DISMIFQEP-MTSLNPCFTVGYQIMEVikehlgGTRKELEA--------RAIELLGLVgipapESRLRA 149
Cdd:PRK14258 78 ERRVNLNRlrrQVSMVHPKPnLFPMSVYDNVAYGVKIV------GWRPKLEIddivesalKDADLWDEI-----KHKIHK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 150 FPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVV----- 224
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTaffkg 226
|
250 260
....*....|....*....|....*.
gi 522082967 225 NVQYAGQQVERQNVVDLFAKPQHPYT 250
Cdd:PRK14258 227 NENRIGQLVEFGLTKKIFNSPHDSRT 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-227 |
1.50e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 76.49 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEF-ETAHGLFRavdSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKE 82
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLR---NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR----PTSGRVRLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGkdismifqepmtslnpcftvgYQIMEVikEHLGGTRKElearAIellglvgipapesrlrafphqMSGGMNQRV 162
Cdd:cd03246 74 LGDHVG---------------------YLPQDD--ELFSGSIAE----NI---------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQ 227
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLE 169
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-214 |
1.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQ-KERRKIIGkdisMIFQEPMT 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTGDFSKlQGIRKLVG----IVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 101 SLnpcftvgyqIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAF----PHQMSGGMNQRVMIAMMIACNPRLLI 176
Cdd:PRK13644 89 QF---------VGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 522082967 177 ADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDM 214
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNL 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-244 |
2.07e-16 |
|
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: 77.27 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAhglFRAVDSVDLEIDQGEMAAIVGESGSGKSVsmlaLMGLLPWTARITADRMNFDGKDLLTISQKER 83
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLFRFYDVSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdisMIFQEpmTSLnpcF--TVGYQIMeviKEHLGGTRKELE--ARAIELlglvgipapESRLRAFPHQ------ 153
Cdd:cd03253 74 RRAIG----VVPQD--TVL---FndTIGYNIR---YGRPDATDEEVIeaAKAAQI---------HDKIMRFPDGydtivg 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 -----MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVAeTAEVVNVQY 228
Cdd:cd03253 133 erglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIV-NADKIIVLK 209
|
250
....*....|....*.
gi 522082967 229 AGQQVERQNVVDLFAK 244
Cdd:cd03253 210 DGRIVERGTHEELLAK 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
3.08e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.21 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFETAH----------GLFR-------AVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLL-PwtariT 64
Cdd:COG4586 3 EVENLSKTYRVYEkepglkgalkGLFRreyreveAVDDISFTIEPGEIVGFIGPNGAGKSttIKMLT--GILvP-----T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 65 ADRMNFDGKDlltiSQKERRKIIgKDISMIF-QE--------PMTSlnpcFTVGYQIMEVIKEHLGGTRKELearaIELL 135
Cdd:COG4586 76 SGEVRVLGYV----PFKRRKEFA-RRIGVVFgQRsqlwwdlpAIDS----FRLLKAIYRIPDAEYKKRLDEL----VELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 136 GLvgipapESRLRAFPHQMSGGmnQRvM----IAMMIAcNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLIT 211
Cdd:COG4586 143 DL------GELLDTPVRQLSLG--QR-MrcelAAALLH-RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTS 212
|
....
gi 522082967 212 HDMG 215
Cdd:COG4586 213 HDMD 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-214 |
6.55e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKE 82
Cdd:PRK11231 3 LRTENLTV----GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVF-----LGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 rrkiIGKDISMIFQEPMTSlnpcftVGYQIMEVIKE----------HLGGTRKELEARAIELLGLVGIPapESRLRAfph 152
Cdd:PRK11231 74 ----LARRLALLPQHHLTP------EGITVRELVAYgrspwlslwgRLSAEDNARVNQAMEQTRINHLA--DRRLTD--- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 153 qMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDM 214
Cdd:PRK11231 139 -LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDL 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-254 |
6.94e-16 |
|
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: 76.04 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 24 DSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDLLTISQKERRKIIGkdisMIFQEPMtsLN 103
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG----LVSQEPV--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 104 PCftvgyQIMEVIKEHLGGTRKELEARAIELLGLvgipapESRLRAFPH-----------QMSGGMNQRVMIAMMIACNP 172
Cdd:cd03249 90 DG-----TIAENIRYGKPDATDEEVEEAAKKANI------HDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 173 RLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVaETAEVVNVQYAGQQVERQNVVDLFAKPQHpytYA 252
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQKGV---YA 232
|
..
gi 522082967 253 LL 254
Cdd:cd03249 233 KL 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-212 |
8.96e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTarITADRMNFDGKDLLTISQKER 83
Cdd:COG0396 1 LEIKNLHVSVEGKEIL----KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYE--VTSGSILLDGEDILELSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKiigKDISMIFQEPMTSlnPCFTVGYQIMEVIKEHLGG--TRKELEARAIELLGLVGIPapESRLR-----AFphqmSG 156
Cdd:COG0396 75 AR---AGIFLAFQYPVEI--PGVSVSNFLRTALNARRGEelSAREFLKLLKEKMKELGLD--EDFLDryvneGF----SG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDV---TIQAQILELLqdlqHKRGMALVLITH 212
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL----RSPDRGILIITH 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
1.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGkdlLTISQK 81
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----EKVKSGEIFYNN---QAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIiGKDISMIFQEPMTSLNPCfTVGYQIMEVIKEHLGGTrKELEARAIELLGLVGIPApesRLRAFPHQMSGGMNQR 161
Cdd:PRK13648 77 NFEKL-RKHIGIVFQNPDNQFVGS-IVKYDVAFGLENHAVPY-DEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 162 VMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVV 224
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVI 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-255 |
1.32e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLA---LMGLLPwTARITAdRMNFDGKDLLT-- 77
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIP-GFRVEG-KVTFHGKNLYApd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKERRKIIGkdisMIFQEPmtslNP---------CFTV---GYQimevikehlgGTRKELEARAIELLGLvgIPAPES 145
Cdd:PRK14243 84 VDPVEVRRRIG----MVFQKP----NPfpksiydniAYGArinGYK----------GDMDELVERSLRQAAL--WDEVKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 146 RLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLqhKRGMALVLITHDMGVVAETAEVV- 224
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTa 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 522082967 225 --NVQYA------GQQVERQNVVDLFAKPQHPYTYALLS 255
Cdd:PRK14243 222 ffNVELTegggryGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-213 |
1.32e-15 |
|
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: 77.79 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKE 82
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQGEVT-----LDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIgkdiSMIFQEPM---TSLNPCFTVGYQimevikehlGGTRKELEArAIELLGLvgipapESRLRAFPHQM----- 154
Cdd:TIGR02868 407 VRRRV----SVCAQDAHlfdTTVRENLRLARP---------DATDEELWA-ALERVGL------ADWLRALPDGLdtvlg 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 155 ------SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLqdLQHKRGMALVLITHD 213
Cdd:TIGR02868 467 eggarlSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
1.93e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEF------ETahglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLT 77
Cdd:COG1101 2 LELKNLSKTFnpgtvnEK-----RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP----PDSGSILIDGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKERRKIIGKdismIFQEPMTSLNPCFTvgyqimevIKEHL------GGTR-------KELEARAIELL-----GLvg 139
Cdd:COG1101 73 LPEYKRAKYIGR----VFQDPMMGTAPSMT--------IEENLalayrrGKRRglrrgltKKRRELFRELLatlglGL-- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 140 ipapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:COG1101 139 ----ENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-224 |
2.17e-15 |
|
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: 74.68 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEF----------ETAHGLFR-------AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARIT- 64
Cdd:cd03267 1 IEVSNLSKSYrvyskepgliGSLKSLFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 65 ADRMNFdgkdlltisqkERRKIIGKDISMIFQE---------PMTSLNpcftVGYQIMEVIKEHLGGTRKELeARAIELL 135
Cdd:cd03267 81 AGLVPW-----------KRRKKFLRRIGVVFGQktqlwwdlpVIDSFY----LLAAIYDLPPARFKKRLDEL-SELLDLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 136 GLVGIPApesrlrafpHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMG 215
Cdd:cd03267 145 ELLDTPV---------RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
....*....
gi 522082967 216 VVAETAEVV 224
Cdd:cd03267 216 DIEALARRV 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-212 |
2.64e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtarITADRMNFDGKDLL-TISQKERRkiIGKDI-------S 92
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLgRTVQREGR--LARDIrksrantG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 93 MIFQEpmTSLNPCFTVgyqIMEVIKEHLGGT----------RKELEARAIELLGLVGipapesrLRAFPHQ----MSGGM 158
Cdd:PRK09984 90 YIFQQ--FNLVNRLSV---LENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVG-------MVHFAHQrvstLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITH 212
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLH 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-214 |
2.64e-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: 73.78 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKERRKIIG---KDISMIFqep 98
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLDPADLRRNIGyvpQDVTLFY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 99 mTSLNPCFTVGYQImevikehlgGTRKELEaRAIELLGLvgipapESRLRAFPH-----------QMSGGMNQRVMIAMM 167
Cdd:cd03245 92 -GTLRDNITLGAPL---------ADDERIL-RAAELAGV------TDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 522082967 168 IACNPRLLIADEPTTALDVTIQAQILELLQdlQHKRGMALVLITHDM 214
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRP 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
3.01e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.35 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMG-LLPwtarITADRMNFDGKDLLTISQKER 83
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLP----PDSGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIgkdiSMIFQEPmtSLNPCFTVGyqimEVI--------KEHLGGTRKELEARAIELLGLVGIpapESRlraFPHQMS 155
Cdd:COG4604 74 AKRL----AILRQEN--HINSRLTVR----ELVafgrfpysKGRLTAEDREIIDEAIAYLDLEDL---ADR---YLDELS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-210 |
3.65e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 76.21 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNlsvefetahGLFRAVDSV-----DLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtaRITADRMN-FDGKD 74
Cdd:PRK10938 1 MSSLQISQ---------GTFRLSDTKtlqlpSLTLNAGDSWAFVGANGSGKSALARALAGELP---LLSGERQSqFSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 75 LLTISQKERRkiigkdISMIFQE---PMTSLNPCFTvGYQIMEVIKEHLggtrkELEARAIELLGLVGIPAPESRlrAFP 151
Cdd:PRK10938 69 RLSFEQLQKL------VSDEWQRnntDMLSPGEDDT-GRTTAEIIQDEV-----KDPARCEQLAQQFGITALLDR--RFK 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 152 HqMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLI 210
Cdd:PRK10938 135 Y-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-234 |
4.86e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 73.67 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 11 VEFETAHGLFRA-----VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKERRK 85
Cdd:cd03252 1 ITFEHVRFRYKPdgpviLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV----PENGRVLVDGHDLALADPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 IIGkdisMIFQEpmtslNPCFTvgyqimEVIKEHLGGTRKELEA-RAIELLGLVGIPAPESRLRAFPHQM--------SG 156
Cdd:cd03252 77 QVG----VVLQE-----NVLFN------RSIRDNIALADPGMSMeRVIEAAKLAGAHDFISELPEGYDTIvgeqgaglSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVaETAEVVNVQYAGQQVE 234
Cdd:cd03252 142 GQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTV-KNADRIIVMEKGRIVE 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-213 |
5.52e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEfeTAHGLfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDlltISQKE 82
Cdd:COG3845 257 VLEVENLSVR--DDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGED---ITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPM-TSLNPCFTVgyqimeviKEHL------------GGT--RKELEARAIELLGLVGI--PAPES 145
Cdd:COG3845 327 PRERRRLGVAYIPEDRLgRGLVPDMSV--------AENLilgryrrppfsrGGFldRKAIRAFAEELIEEFDVrtPGPDT 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 146 RLRAfphqMSGGMNQRVMIAMMIACNPRLLIADEPTTALDV----TIQAQILELlqdlqHKRGMALVLITHD 213
Cdd:COG3845 399 PARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLEL-----RDAGAAVLLISED 461
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-233 |
9.89e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.26 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVefetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALMG--LLPWTARITadrmnFDGKDLLTI 78
Cdd:PRK11831 5 ANLVDMRGVSF----TRGNRCIFDNISLTVPRGKITAIMGPSGIGKT-TLLRLIGgqIAPDHGEIL-----FDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SqKERRKIIGKDISMIFQEP--MTSLNPCFTVGYQImeviKEHLGGTRKELEARAIELLGLVGIPAPESRLrafPHQMSG 156
Cdd:PRK11831 75 S-RSRLYTVRKRMSMLFQSGalFTDMNVFDNVAYPL----REHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDmgvVAETAEVVNVQY--AGQQV 233
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD---VPEVLSIADHAYivADKKI 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
1.38e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDlltISQ 80
Cdd:PRK11614 3 KVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKD---ITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQepmtslnpcftvGYQIME--VIKEHL--GG---TRKELEARAIELLGLvgIPAPESRLRAFPHQ 153
Cdd:PRK11614 72 WQTAKIMREAVAIVPE------------GRRVFSrmTVEENLamGGffaERDQFQERIKWVYEL--FPRLHERRIQRAGT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITH---------DMGVVAETAEVV 224
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQnanqalklaDRGYVLENGHVV 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-219 |
1.54e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA----RITADRMNFdgkdlltISQKerrkiigkdISMIFQE 97
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSgtvrRAGGARVAY-------VPQR---------SEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 98 PMTSLNpCFTVGYQimevikEHLGGTR---KELEARAIELLGLVGIPAPESR-LRAfphqMSGGMNQRVMIAMMIACNPR 173
Cdd:NF040873 71 PLTVRD-LVAMGRW------ARRGLWRrltRDDRAAVDDALERVGLADLAGRqLGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522082967 174 LLIADEPTTALDVTIQAQILELLQDLqHKRGMALVLITHDMGVVAE 219
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRR 184
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
120-218 |
1.97e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 120 LGGTRKELEARAIELLGLVGIPAPESRLrafPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDL 199
Cdd:PRK10575 117 LGRFGAADREKVEEAISLVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
90
....*....|....*....
gi 522082967 200 QHKRGMALVLITHDMGVVA 218
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAA 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-212 |
2.11e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 20 FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLltisqkerrkIIGKDISMIfqepm 99
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA----LKGTPVAGCVDVPDN----------QFGREASLI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 tslnpcftvgyqimevikEHLGgtRKELEARAIELLGLVGIPAPESRLRAFPHqMSGGMNQRVMIAMMIACNPRLLIADE 179
Cdd:COG2401 104 ------------------DAIG--RKGDFKDAVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 522082967 180 PTTALDVTiQAQILEL-LQDLQHKRGMALVLITH 212
Cdd:COG2401 163 FCSHLDRQ-TAKRVARnLQKLARRAGITLVVATH 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
24-213 |
4.30e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 24 DSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL-LPWTARITAdrmnfdGKDLLTISQKerrkiigkDISMIFQEpmTSL 102
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLA------GTAPLAEARE--------DTRLMFQD--ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 NPCFTVgyqIMEVikehlG-GTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:PRK11247 93 LPWKKV---IDNV-----GlGLKGQWRDAALQALAAVGL---ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 522082967 182 TALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-232 |
9.81e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITADRmnfDGKDLLTIS 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAgNIIIDD---EDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRkiigkDISMIFQEPmtSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapeSRLR-AFPHQMSGGM 158
Cdd:PRK10895 74 ARARR-----GIGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI----EHLRdSMGQSLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDvtiQAQILELLQDLQHKRGMAL-VLIT-HDmgvVAETAEVVNVQYAGQQ 232
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVD---PISVIDIKRIIEHLRDSGLgVLITdHN---VRETLAVCERAYIVSQ 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-244 |
1.04e-13 |
|
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: 72.16 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSvsmlALMGLL-----PWTARITadrmnFDGKDLLTISQKERRKIIGkdisMIFQEpmT 100
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVTSGRIL-----IDGQDIRDVTQASLRAAIG----IVPQD--T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 101 SLnpcF--TVGYQImevIKEHLGGTRKELE--ARA------IELL--G---LVGipapESRLRafphqMSGGMNQRVMIA 165
Cdd:COG5265 442 VL---FndTIAYNI---AYGRPDASEEEVEaaARAaqihdfIESLpdGydtRVG----ERGLK-----LSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 166 MMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgMALVlITHDMGVVAETAEVVnVQYAGQQVERQNVVDLFAK 244
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLV-IAHRLSTIVDADEIL-VLEAGRIVERGTHAELLAQ 582
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-212 |
1.51e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEfeTAHGlfRA-VDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLPW-TARITADrmnfDGKDLLTISQ 80
Cdd:COG4178 363 LALEDLTLR--TPDG--RPlLEDLSLSLKPGERLLITGPSGSGKS-TLLrAIAGLWPYgSGRIARP----AGARVLFLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KerrkiigkdiSMIfqePMTSLnpcftvgyqimeviKEHL---GGTRKELEARAIELLGLVGIPAPESRL---RAFPHQM 154
Cdd:COG4178 434 R----------PYL---PLGTL--------------REALlypATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQdlQHKRGMALVLITH 212
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-256 |
1.75e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFEtahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLL-----PWTARITadrmnFDGKDLLT 77
Cdd:PRK13657 334 AVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLqrvfdPQSGRIL-----IDGTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 ISQKERRKIIGkdisMIFQEPMTsLNpcftvgyqimEVIKEHL-----GGTRKELEARAIELLGLVGIPAPESRLRAFP- 151
Cdd:PRK13657 402 VTRASLRRNIA----VVFQDAGL-FN----------RSIEDNIrvgrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 152 ---HQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVAEtAEVVNVQY 228
Cdd:PRK13657 467 ergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFD 543
|
250 260
....*....|....*....|....*...
gi 522082967 229 AGQQVERQNVVDLFAKPQHpyTYALLSA 256
Cdd:PRK13657 544 NGRVVESGSFDELVARGGR--FAALLRA 569
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-231 |
1.87e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSvefETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKS--VSMLAlmGLlpwtARITADRMNFDGKDLLTI 78
Cdd:PRK11650 1 MAGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKStlLRMVA--GL----ERITSGEIWIGGRVVNEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERrkiigkDISMIFQEpmTSLNPCFTVgYQIMEVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGM 158
Cdd:PRK11650 72 EPADR------DIAMVFQN--YALYPHMSV-RENMAYGLKIRGMPKAEIEERVAEAARILEL---EPLLDRKPRELSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQI-LElLQDLQHKRGMALVLITHDMgVVAET-AEVVNVQYAGQ 231
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHDQ-VEAMTlADRVVVMNGGV 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-228 |
1.97e-13 |
|
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: 68.72 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAhglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDL--LTISQK 81
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDItkLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRkiigkDISMIFQEPmtSLNPCFTVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIpapeSRLRAFP-HQMSGGMNQ 160
Cdd:cd03218 73 ARL-----GIGYLPQEA--SIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHI----THLRKSKaSSLSGGERR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMAlVLIT-HDmgvVAETAEVVNVQY 228
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIG-VLITdHN---VRETLSITDRAY 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
2.31e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtarITAD--RMNFDGKDL--L 76
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGL------VKPDsgRIFLDGEDIthL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 77 TISQKERRkiiGkdISMIFQEPmtSLnpcF---TVGYQIMEVIkEHLGGTRKELEARAIELLGLVGIpapeSRLRAFP-H 152
Cdd:COG1137 71 PMHKRARL---G--IGYLPQEA--SI---FrklTVEDNILAVL-ELRKLSKKEREERLEELLEEFGI----THLRKSKaY 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALD---VT-IQAQILELlqdlqHKRGMAlVLIT-HDmgvVAETAEVVN 225
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIG-VLITdHN---VRETLGICD 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-212 |
2.81e-13 |
|
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: 67.34 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSveFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMG-LLPWTARITadrmnFDGKDLLTIsQKE 82
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEIT-----LDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIgkdiSMIFQEPmtslnpcftvgYQIMEVIKEHLGgtrkelearaiellglvgipapesrlrafpHQMSGGMNQRV 162
Cdd:cd03247 73 LSSLI----SVLNQRP-----------YLFDTTLRNNLG------------------------------RRFSGGERQRL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 163 MIAMMIACNPRLLIADEPTTALDVTIQAQILELLqdLQHKRGMALVLITH 212
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITH 155
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-212 |
2.91e-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: 68.41 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWT-ARITadrmnFDGKDLLTISQKER 83
Cdd:cd03254 4 EFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQIL-----IDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGkdisMIFQEPmtslnpcFTVGYQIMEVIKehLGG--TRKELEARAIELLGL--VGIPAP---ESRLRAFPHQMSG 156
Cdd:cd03254 76 RSMIG----VVLQDT-------FLFSGTIMENIR--LGRpnATDEEVIEAAKEAGAhdFIMKLPngyDTVLGENGGNLSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITH 212
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAH 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-211 |
5.82e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.30 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMnFDGKDLltiSQKERRKIIGkdismiFQEPMTSLNPC 105
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQIL-FNGQPR---KPDQFQKCVA------YVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 106 FTVG----YQIMEVIKEHLGGTRKELEArAIELLGLVGIpapeSRLR-AFPHQMSGGMNQRVMIAMMIACNPRLLIADEP 180
Cdd:cd03234 96 LTVRetltYTAILRLPRKSSDAIRKKRV-EDVLLRDLAL----TRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 522082967 181 TTALDVTIQAQILELLQDLqhKRGMALVLIT 211
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQL--ARRNRIVILT 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-214 |
5.98e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 16 AHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKErrkiIGKDISMI 94
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVW-----LDGEHIQHYASKE----VARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 95 FQEPMTSLNpcFTVGYQIMEVIKEH---LGGTRKELE---ARAIELLGLVGIPAPESrlrafpHQMSGGMNQRVMIAMMI 168
Cdd:PRK10253 87 AQNATTPGD--ITVQELVARGRYPHqplFTRWRKEDEeavTKAMQATGITHLADQSV------DTLSGGQRQRAWIAMVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522082967 169 ACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-212 |
2.34e-12 |
|
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: 64.88 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEfeTAHGLFRA----VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwTARITADRMnFDGKDLltiS 79
Cdd:cd03213 4 LSFRNLTVT--VKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVL-INGRPL---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIGkdisMIFQEPMtsLNPCFTVgyqimevikehlggtRKELEARAiELLGLvgipapesrlrafphqmSGGMN 159
Cdd:cd03213 77 KRSFRKIIG----YVPQDDI--LHPTLTV---------------RETLMFAA-KLRGL-----------------SGGER 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522082967 160 QRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITH 212
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIH 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-222 |
3.85e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnfdgkdLLTISQKERRKIIGKDISMIFQepMTS 101
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKIT----------VLGVPVPARARLARARIGVVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 102 LNPCFTVGYQIMeVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:PRK13536 125 LDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522082967 182 TALDVTIQAQILELLQDLQhKRGMALVLITHDMgvvaETAE 222
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLL-ARGKTILLTTHFM----EEAE 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-217 |
4.24e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.40 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTI-SQK 81
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTILLRGQHIEGLpGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMI--FQEpMTSLNPCFTVGYQIMEVikEHLGG-------TRKELEA--RAIELLGLVGipapesrLRAF 150
Cdd:PRK11300 77 IARMGVVRTFQHVrlFRE-MTVIENLLVAQHQQLKT--GLFSGllktpafRRAESEAldRAATWLERVG-------LLEH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 151 PHQMSG----GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVV 217
Cdd:PRK11300 147 ANRQAGnlayGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
4.54e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEfetahglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGK--DLLTISQ 80
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKpvRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 ----------KERRK---IIGKDIS--MIfqepMTSLNPCFTVGyqimeVIKehlggtRKELEARAIELLGLVGI--PAP 143
Cdd:COG1129 324 airagiayvpEDRKGeglVLDLSIRenIT----LASLDRLSRGG-----LLD------RRRERALAEEYIKRLRIktPSP 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 144 ESRLRafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:COG1129 389 EQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSEL 454
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-217 |
6.99e-12 |
|
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: 64.41 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKdllTISQKERRKIIGKdISMIFQEPMTSL--- 102
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGK---PISQYEHKYLHSK-VSLVGQEPVLFArsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 --NPCFTVGYQIMEVIKE-----HLGGTRKELEARAIELLGLVGipapesrlrafpHQMSGGMNQRVMIAMMIACNPRLL 175
Cdd:cd03248 105 qdNIAYGLQSCSFECVKEaaqkaHAHSFISELASGYDTEVGEKG------------SQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522082967 176 IADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVV 217
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-213 |
8.17e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSvSMLALM-GLLPWTARITadrmnFDGKDLLTISQKE--RRKiigkdiSMIFQEPM 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEIL-----LNGRPLSDWSAAElaRHR------AYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 TSLN-PCFtvgyqimEVIKEHL--GGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVMIAMMI-----ACN 171
Cdd:COG4138 80 PPFAmPVF-------QYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTIN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522082967 172 P--RLLIADEPTTALDVTIQAQILELLQDLQHkRGMALVLITHD 213
Cdd:COG4138 150 PegQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHD 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-210 |
8.77e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 33 GEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMnFDGKdllTISQKERRKIIGkdisMIFQEPMtsLNPCFTVG--- 109
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL-LNGM---PIDAKEMRAISA----YVQQDDL--FIPTLTVRehl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 110 -YQIMEVIKEHLggTRKELEARAIELLGLVGI-PAPESRLRAfPHQM---SGGMNQRVMIAMMIACNPRLLIADEPTTAL 184
Cdd:TIGR00955 121 mFQAHLRMPRRV--TKKEKRERVDEVLQALGLrKCANTRIGV-PGRVkglSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180
....*....|....*....|....*.
gi 522082967 185 DVTIQAQILELLQDLQHKRGMALVLI 210
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTI 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-231 |
1.00e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVeFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP--WTARITadrmnFDGKDLLTisq 80
Cdd:TIGR02633 257 ILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVF-----INGKPVDI--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQE-PMTSLNPCFTVGYQI-MEVIKEHLGGTRKELEARaielLGLVGIPAPESRLRAFP-----HQ 153
Cdd:TIGR02633 328 RNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCFKMRIDAAAE----LQIIGSAIQRLKVKTASpflpiGR 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-245 |
1.07e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 33 GEMAAIVGESGSGKSvSMLALMGLL--PWTARITadrmnFDGKDLltiSQKERrKIIGKDISMIFQEPMTslnpcftVGY 110
Cdd:TIGR00958 507 GEVVALVGPSGSGKS-TVAALLQNLyqPTGGQVL-----LDGVPL---VQYDH-HYLHRQVALVGQEPVL-------FSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 111 QIMEVIKEHLGGTRKElearaiELLGLVGIPAPESRLRAFPH-----------QMSGGMNQRVMIAMMIACNPRLLIADE 179
Cdd:TIGR00958 570 SVRENIAYGLTDTPDE------EIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 180 PTTALDVTIQAqileLLQDLQHKRGMALVLITHDMGVVaETAEVVNVQYAGQQVERQNVVDLFAKP 245
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-221 |
1.13e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDgKDLLT--I 78
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLL----DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVL----LDDGRIIYE-QDLIVarL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERRKIIGK--------------------DIS-MIFQEPMTS-LNPCftvgYQIMEVIkEHLGGTRkeLEARAIELLG 136
Cdd:PRK11147 72 QQDPPRNVEGTvydfvaegieeqaeylkryhDIShLVETDPSEKnLNEL----AKLQEQL-DHHNLWQ--LENRINEVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 137 LVGIPaPESRLRAfphqMSGGMNQRVMIAMMIACNPRLLIADEPTTALDV-TIQAqiLE-LLQDLQHkrgmALVLITHDM 214
Cdd:PRK11147 145 QLGLD-PDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIeTIEW--LEgFLKTFQG----SIIFISHDR 213
|
....*..
gi 522082967 215 GVVAETA 221
Cdd:PRK11147 214 SFIRNMA 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-230 |
1.50e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARITadrmnFDGKDLLTISQKERRKiigkDISMIFQEPM-- 99
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLL-----FEGEDISTLKPEIYRQ----QVSYCAQTPTlf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 100 -TSLNPCFTVGYQImevikehlggtRKELEARAIELLGLVGIPAPESRLRAFPHQMSGGMNQRVMIAMMIACNPRLLIAD 178
Cdd:PRK10247 94 gDTVYDNLIFPWQI-----------RNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 522082967 179 EPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAG 230
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-212 |
1.61e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHGLfravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTarITADRMNFDGKDLLTISQKE 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAIL----RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE--VTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RrkiIGKDISMIFQEPM------------TSLNPcfTVGYQIMEVIKEHlggTRKELEARAIELLGLvgipaPESRL-RA 149
Cdd:PRK09580 75 R---AGEGIFMAFQYPVeipgvsnqfflqTALNA--VRSYRGQEPLDRF---DFQDLMEEKIALLKM-----PEDLLtRS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 150 FPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDV---TIQAQILELLQDlqHKRgmALVLITH 212
Cdd:PRK09580 142 VNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRD--GKR--SFIIVTH 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-219 |
1.79e-11 |
|
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: 62.94 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGL------------------FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RIT 64
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSgTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 65 adrmnfdgkdlltisqkerrkIIGKDISMIfqEPMTSLNPCFTvGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAP- 143
Cdd:cd03220 81 ---------------------VRGRVSSLL--GLGGGFNPELT-GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFi 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 144 ESRLRAFphqmSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAE 219
Cdd:cd03220 137 DLPVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKR 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
1.80e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 6 IRNLSVEFETAHgLFravDSVDLEIDQGEMAAIVGESGSGKSvSMLALMgllpwTARITADrmnfDGkdllTISqkeRRK 85
Cdd:COG0488 1 LENLSKSFGGRP-LL---DDVSLSINPGDRIGLVGRNGAGKS-TLLKIL-----AGELEPD----SG----EVS---IPK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 iiGKDISMIFQEPmtSLNPCFTVGYQIMEVIKE---------------------------------HLGGTrkELEARAI 132
Cdd:COG0488 60 --GLRIGYLPQEP--PLDDDLTVLDTVLDGDAElraleaeleeleaklaepdedlerlaelqeefeALGGW--EAEARAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 133 ELLGLVGIPA--PESRLRAFphqmSGGMNQRVMIAMMIACNPRLLIADEPTTALDV-TIqaqilELLQD-LQHKRGmALV 208
Cdd:COG0488 134 EILSGLGFPEedLDRPVSEL----SGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSI-----EWLEEfLKNYPG-TVL 203
|
....*
gi 522082967 209 LITHD 213
Cdd:COG0488 204 VVSHD 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-214 |
2.17e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 29 EIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITadrmnFDGKDLLTISQKE---RRKIIGKDISMIFQEPMtslnpc 105
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-----FAGQPLEAWSAAElarHRAYLSQQQTPPFAMPV------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 106 ftvgYQIMEV---IKEHLGGTRKELEaRAIELLGLvgipapESRLRAFPHQMSGGMNQRVMIAMMI-----ACNP--RLL 175
Cdd:PRK03695 87 ----FQYLTLhqpDKTRTEAVASALN-EVAEALGL------DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 522082967 176 IADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDM 214
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDL 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-246 |
2.52e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARI--TADRMNFDGKDLLTISQKerrkiigkdISMIFQEPMTSL 102
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVlwQGKPLDYSKRGLLALRQQ---------VATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 npCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGipapESRLRAFPHQ-MSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:PRK13638 91 --FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 182 TALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDLFAKPQ 246
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-241 |
3.40e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKE 82
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE----PTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIigkDISMIFQEpmTSLNPCFTVGYQIMevIKEHLggTRK----------ELEARAIELLGLVGIpapESRLRAFPH 152
Cdd:PRK09700 77 AAQL---GIGIIYQE--LSVIDELTVLENLY--IGRHL--TKKvcgvniidwrEMRVRAAMMLLRVGL---KVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQ 232
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
....*....
gi 522082967 233 VERQNVVDL 241
Cdd:PRK09700 224 VCSGMVSDV 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
3.88e-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: 60.15 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFEtAHGLFravDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGllpwtaRITADrmnfdgkdlltisqker 83
Cdd:cd03221 1 IELENLSKTYG-GKLLL---KDISLTINPGDRIGLVGRNGAGKSTLLKLIAG------ELEPD----------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 rkiigkdismifqEPMTSLNPCFTVGYqimevikehlggtrkelearaiellglvgipapesrlraFPhQMSGGMNQRVM 163
Cdd:cd03221 54 -------------EGIVTWGSTVKIGY---------------------------------------FE-QLSGGEKMRLA 80
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHkrgmALVLITHD 213
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHD 126
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-214 |
6.15e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLFRaVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP--WTARITadrmnFDGKDLlTIsqK 81
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKR-VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIF-----IDGKPV-KI--R 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKIIGKDISMIFQE-PMTSLNPCFTVGYQI-MEVIKEHLGGTR--KELEARAI--ELLGL-VGIPAPESRLRafphQM 154
Cdd:PRK13549 331 NPQQAIAQGIAMVPEDrKRDGIVPVMGVGKNItLAALDRFTGGSRidDAAELKTIleSIQRLkVKTASPELAIA----RL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSEL 465
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-219 |
6.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 6 IRNLSVEFETAHGLFRavdSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRmnfdgkdlLTISQKERRK 85
Cdd:PRK15056 9 VNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGK--------ISILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 86 IIGKD-ISMIFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRK-ELEARAIELLGLVGIPAPESRLRAFpHQMSGGMNQRVM 163
Cdd:PRK15056 74 ALQKNlVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRaKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVVAE 219
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTE 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-217 |
7.85e-11 |
|
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: 60.84 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEfetaHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLltisqKER 83
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPL-----AEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEPmtSLNPCFTVgYQIMEVIKEHLGGTRKELEArAIELLGLVG---IPApesrlrafpHQMSGGMNQ 160
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLKPELSA-LENLHFWAAIHGGAQRTIED-ALAAVGLTGfedLPA---------AQLSAGQQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVV 217
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-222 |
1.13e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.74 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLsvefETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKER 83
Cdd:PRK13537 8 IDFRNV----EKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIigkdiSMIFQepMTSLNPCFTVGYQIMeVIKEHLGGTRKELEARAIELLGLVGIpapESRLRAFPHQMSGGMNQRVM 163
Cdd:PRK13537 80 QRV-----GVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 164 IAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMgvvaETAE 222
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFM----EEAE 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-214 |
2.15e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEfetahglfrAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQK-- 81
Cdd:PRK10762 258 LKVDNLSGP---------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVTRSPQdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ---------ERRKIIGKDISMIFQEPM--TSLNPCFTVGYQImevikehlggtRKELEARAIE-LLGLVGIPAPeSRLRA 149
Cdd:PRK10762 325 langivyisEDRKRDGLVLGMSVKENMslTALRYFSRAGGSL-----------KHADEQQAVSdFIRLFNIKTP-SMEQA 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 150 FpHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:PRK10762 393 I-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEM 455
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-213 |
2.71e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGLlpwtARITADRMNFDGKDLLTISQKERrkiigkDISMIFQEpmTSLNPC 105
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGL----EDITSGDLFIGEKRMNDVPPAER------GVGMVFQS--YALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 106 FTVGYQIMEVIKehLGGTRK-ELEAR---AIELLGLVGIpapesrLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:PRK11000 90 LSVAENMSFGLK--LAGAKKeEINQRvnqVAEVLQLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 522082967 182 TALDVTIQAQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-224 |
3.45e-10 |
|
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: 59.04 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahglfRAVDS-VDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLltisqKE 82
Cdd:cd03231 1 LEADELTCERDG-----RALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP----PLAGRVLLNGGPL-----DF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPmtslnpcftvGYQIMEVIKEHL------GGTRKELEARA-IELLGLVGIPApesrlrafpHQMS 155
Cdd:cd03231 67 QRDSIARGLLYLGHAP----------GIKTTLSVLENLrfwhadHSDEQVEEALArVGLNGFEDRPV---------AQLS 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQdlQH-KRGMALVLITH-DMGVVAETAEVV 224
Cdd:cd03231 128 AGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA--GHcARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
8.42e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MS-LLEIRNLSVEF------------------ETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvSMLALM-GLLPWT 60
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIaGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 61 A-RITADrmnfdgkdlltisqkerrkiiGKDISMIfqEPMTSLNPCFTvGYQIMEVIKEHLGGTRKELEARA---IELlg 136
Cdd:COG1134 80 SgRVEVN---------------------GRVSALL--ELGAGFHPELT-GRENIYLNGRLLGLSRKEIDEKFdeiVEF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 137 lvgipapeSRLRAFPHQ----MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITH 212
Cdd:COG1134 134 --------AELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSH 204
|
....*..
gi 522082967 213 DMGVVAE 219
Cdd:COG1134 205 SMGAVRR 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-212 |
8.77e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 33 GEMAAIVGESGSGKSVSMLALMGllpwtaRITADrmNFDGKDLltISQKERRKIIGKDISMIFQEPMtsLNPCFTVGYQI 112
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG------RIQGN--NFTGTIL--ANNRKPTKQILKRTGFVTQDDI--LYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 113 MEVIKEHLGG--TRKELEARAIELLGLVGIPAPESRL--RAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTI 188
Cdd:PLN03211 162 VFCSLLRLPKslTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180
....*....|....*....|....
gi 522082967 189 QAQILELLQDLQHKrGMALVLITH 212
Cdd:PLN03211 242 AYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-212 |
9.52e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 2 SLLEIRNLSV---EFETAHGlfravdsVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTarITADRMNFDGKDLLTI 78
Cdd:CHL00131 6 PILEIKNLHAsvnENEILKG-------LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK--ILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 79 SQKERRKiigKDISMIFQEPMTslnpcfTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRL----RAFPHQ- 153
Cdd:CHL00131 77 EPEERAH---LGIFLAFQYPIE------IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLvgmdPSFLSRn 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522082967 154 ----MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITH 212
Cdd:CHL00131 148 vnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-212 |
1.62e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVefetAHG---LFRAVdSVDLEidQGEMAAIVGESGSGKSvSMLALM-GLLPwtarITADRMNFDGKDLLTIS 79
Cdd:PRK13539 3 LEGEDLAC----VRGgrvLFSGL-SFTLA--AGEALVLTGPNGSGKT-TLLRLIaGLLP----PAAGTIKLDGGDIDDPD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 80 QKERRKIIG-KDismifqepmtSLNPCFTVGyQIMEVIKEHLGGTRKELEArAIELLGLVGI---PApesrlrafpHQMS 155
Cdd:PRK13539 71 VAEACHYLGhRN----------AMKPALTVA-ENLEFWAAFLGGEELDIAA-ALEAVGLAPLahlPF---------GYLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 156 GGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDlqH-KRGMALVLITH 212
Cdd:PRK13539 130 AGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA--HlAQGGIVIAATH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
154-231 |
2.13e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 2.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQ 231
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-212 |
2.37e-09 |
|
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: 55.62 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfraVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPW-TARITADRMNfdgkDLLTISQKe 82
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPEGE----DLLFLPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 rrkiigkdismifqepmtslnPCFTVGyqimevikehlggtrkelearaiellglvgipapesRLR---AFP--HQMSGG 157
Cdd:cd03223 73 ---------------------PYLPLG------------------------------------TLReqlIYPwdDVLSGG 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 158 MNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDlqhkRGMALVLITH 212
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-234 |
2.44e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 56.65 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWtariTADRMNFDGKDLLTIS-QKE 82
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA----EEGKIEIDGIDISTIPlEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKiigkdISMIFQEPM-------TSLNPcftvgY------QIMEVIKEHLGGTrkelearaiellglvgipapesrlra 149
Cdd:cd03369 81 RSS-----LTIIPQDPTlfsgtirSNLDP-----FdeysdeEIYGALRVSEGGL-------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 150 fphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhkRGMALVLITHDMGVVAETAEVVnVQYA 229
Cdd:cd03369 125 ---NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIIDYDKIL-VMDA 198
|
....*
gi 522082967 230 GQQVE 234
Cdd:cd03369 199 GEVKE 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-244 |
3.65e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHglfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWtariTADRMNFDGKDLLTISQKER 83
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----TEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RkiigKDISMIFQEPMTSLNPCF---TVGYQIMEvikEHLGGTrkeLEarAIELLGLV-GIPAP-ESRLRAFPHQMSGGM 158
Cdd:PRK10790 414 R----QGVAMVQQDPVVLADTFLanvTLGRDISE---EQVWQA---LE--TVQLAELArSLPDGlYTPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 159 NQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKrgMALVLITHDMGVVAEtAEVVNVQYAGQQVERQNV 238
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*.
gi 522082967 239 VDLFAK 244
Cdd:PRK10790 559 QQLLAA 564
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-213 |
5.85e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.38 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFETAHgLFravDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLpwTARITADrmnfDGkdllTIsqke 82
Cdd:COG0488 315 VLELEGLSKSYGDKT-LL---DDLSLRIDRGDRIGLIGPNGAGKS----TLLKLL--AGELEPD----SG----TV---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 rrkIIGKDISMIF--QEpMTSLNPCFTVgyqiMEVIKEHLGGTRkELEARAieLLGLVGIPApeSRLRAFPHQMSGGMNQ 160
Cdd:COG0488 373 ---KLGETVKIGYfdQH-QEELDPDKTV----LDELRDGAPGGT-EQEVRG--YLGRFLFSG--DDAFKPVGVLSGGEKA 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522082967 161 RVMIAMMIACNPRLLIADEPTTALDV-TIQAqILELLQDLQhkrGmALVLITHD 213
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHD 488
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-224 |
6.64e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITadrmnfdgkdlltisQ 80
Cdd:PRK09544 2 TSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIGKDISMIFQEPMTSLnpcfTVGYQIM---EVIKEHLGGTRKELEAraiellglvgipapeSRLRAFPHQ-MSG 156
Cdd:PRK09544 63 RNGKLRIGYVPQKLYLDTTLPL----TVNRFLRlrpGTKKEDILPALKRVQA---------------GHLIDAPMQkLSG 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVV-AETAEVV 224
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVL 192
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-214 |
9.89e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGLL-PWTARIT-ADRMNFDgkdlltISQK-----ERRKIigkdiSMIFQEp 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTrPQKGRIVlNGRVLFD------AEKGiclppEKRRI-----GYVFQD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 99 mTSLNPCFTVG----YQIMEVIKEHLggtrkeleARAIELLGLvgipapESRLRAFPHQMSGGMNQRVMIAMMIACNPRL 174
Cdd:PRK11144 85 -ARLFPHYKVRgnlrYGMAKSMVAQF--------DKIVALLGI------EPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522082967 175 LIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSL 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-241 |
1.00e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA---RITADRMNFDG-KDlltiSQKerrkiigKDISMIFQ 96
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAgsiLYLGKEVTFNGpKS----SQE-------AGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 97 EpmtsLN--PCFTVGYQIM--EVIKEHLGGTR-KELEARAIELLGLVGIPAPESRLRAfphQMSGGMNQRVMIAMMIACN 171
Cdd:PRK10762 87 E----LNliPQLTIAENIFlgREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQNVVDL 241
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELK-SQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-214 |
2.22e-08 |
|
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: 56.18 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 22 AVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTAritadrmnfdGKDLltisqkerrkIIGKDISMIFQEPMTS 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS----------GTVL----------VGGKDIETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 102 LNPC---------FTVGYQIMevIKEHLGGTRKE---LEARA-IELLGLVGIPAPESRlrafphQMSGGMNQRVMIAMMI 168
Cdd:TIGR01257 1005 LGMCpqhnilfhhLTVAEHIL--FYAQLKGRSWEeaqLEMEAmLEDTGLHHKRNEEAQ------DLSGGMQRKLSVAIAF 1076
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522082967 169 ACNPRLLIADEPTTALDVTIQAQILELLqdLQHKRGMALVLITHDM 214
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-208 |
3.61e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADrMNFDGKDLLTISQ 80
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKII---GKDISMifqepmtslnPCFTVgyqimevikehlggtRKELEARAiellglvgipapesRLRAfpHQM--- 154
Cdd:cd03233 80 KYPGEIIyvsEEDVHF----------PTLTV---------------RETLDFAL--------------RCKG--NEFvrg 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 155 -SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALV 208
Cdd:cd03233 119 iSGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-244 |
3.83e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLAL------MGLLPWTARI-TADRmnfdgkdll 76
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAhv*gpdAGRRPWRF*TwCANR--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 77 tisqKERRKIIGKdismifQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAIELLGLVGIPAPESRLRAfphQMSG 156
Cdd:NF000106 81 ----RALRRTIG*------HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 157 GMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVERQ 236
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
....*...
gi 522082967 237 NVVDLFAK 244
Cdd:NF000106 227 KVDELKTK 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-244 |
4.06e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETAHGLfrAVDSVDLEIDQGEMAAIVGESGSGKSVsmlaLMGLLPWTARITADRMNFDGKDLltisQKER 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDL----RDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RKIIGKDISMIFQEpMTSLNPcfTVGYQIMEVIKEHLggTRKELEARA--------IELL--GLVGIPAPESRLrafphq 153
Cdd:PRK11176 412 LASLRNQVALVSQN-VHLFND--TIANNIAYARTEQY--SREQIEEAArmayamdfINKMdnGLDTVIGENGVL------ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgMALVlITHDMGVVAETAEVVNVQYaGQQV 233
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEKADEILVVED-GEIV 557
|
250
....*....|.
gi 522082967 234 ERQNVVDLFAK 244
Cdd:PRK11176 558 ERGTHAELLAQ 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-212 |
5.49e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.47 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVefeTAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITAdrmnfDGKDLLTISQKER 83
Cdd:PRK11174 350 IEAEDLEI---LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKI-----NGIELRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 84 RkiigKDISMIFQEPM---TSLNPCFTVGY------QIMEVIKehlggtrkelEARAIELL-----GL---VGIPApeSR 146
Cdd:PRK11174 422 R----KHLSWVGQNPQlphGTLRDNVLLGNpdasdeQLQQALE----------NAWVSEFLpllpqGLdtpIGDQA--AG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 147 LrafphqmSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQdlQHKRGMALVLITH 212
Cdd:PRK11174 486 L-------SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-234 |
2.09e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSLLEIRNLSVEFEtahGLfRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGL-LPWTARITAD--RMNFdgkdllt 77
Cdd:PRK11288 2 SPYLSFDGIGKTFP---GV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDgqEMRF------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 isqKERRKIIGKDISMIFQEpmTSLNPCFTVGYQIMEVIKEHLGG--TRKELEARAIELLGLVGIPA-PESRLRafphQM 154
Cdd:PRK11288 71 ---ASTTAALAAGVAIIYQE--LHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIdPDTPLK----YL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQYAGQQVE 234
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-214 |
2.48e-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: 50.79 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLpwtaRITADRMNFDGKDLLTISQKERRKIIGKDISMIFQEPMTsL 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 103 NPcfTVGYQImeVIKEHLGGTRKELEARAIELlglvgipAPESRLRAFPHQ---------MSGGMNQRVMIAMMIACNPR 173
Cdd:cd03290 92 NA--TVEENI--TFGSPFNKQRYKAVTDACSL-------QPDIDLLPFGDQteigerginLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522082967 174 LLIADEPTTALDV-----TIQAQILELLQDlqHKRgmALVLITHDM 214
Cdd:cd03290 161 IVFLDDPFSALDIhlsdhLMQEGILKFLQD--DKR--TLVLVTHKL 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-212 |
2.53e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNlsVEFETAHGLFRAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLP--WTAriTADRMNFDGKDLLTISQ 80
Cdd:PRK11160 338 SLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTraWDP--QQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 81 KERRKIIgkdiSMIFQEPmtslnpcftvgyqimevikeHL--GGTRKEL--------EARAIELLGLVGIPA---PESRL 147
Cdd:PRK11160 410 AALRQAI----SVVSQRV--------------------HLfsATLRDNLllaapnasDEALIEVLQQVGLEKlleDDKGL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082967 148 RAF----PHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLqdLQHKRGMALVLITH 212
Cdd:PRK11160 466 NAWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITH 532
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-197 |
2.94e-07 |
|
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: 50.57 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLSVEFETahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTA-RITadrmnFDGKDLLTISQKE 82
Cdd:cd03244 3 IEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSgSIL-----IDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIigkdISMIFQEPMT-------SLNPCftvGY----QIMEVI-----KEHLGGTRKELEARaIELLGLvgipapesr 146
Cdd:cd03244 76 LRSR----ISIIPQDPVLfsgtirsNLDPF---GEysdeELWQALervglKEFVESLPGGLDTV-VEEGGE--------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 147 lrafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQ 197
Cdd:cd03244 139 ------NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-214 |
4.79e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 5 EIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWT---ARItadrmnF----DGKDLLT 77
Cdd:NF033858 268 EARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASegeAWL------FgqpvDAGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 78 isqkeRRKiigkdismifqepmtslnpcftVGYqiM--------EV-IKEHLggtrkELEARaiellgLVGIPAPESRLR 148
Cdd:NF033858 338 -----RRR----------------------VGY--MsqafslygELtVRQNL-----ELHAR------LFHLPAAEIAAR 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 149 ---------------AFPHQMSGGMNQRVMIAmmIAC--NPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLIT 211
Cdd:NF033858 378 vaemlerfdladvadALPDSLPLGIRQRLSLA--VAVihKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFIST 455
|
...
gi 522082967 212 HDM 214
Cdd:NF033858 456 HFM 458
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-222 |
5.20e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWT-----ARITADrMNFDGKDLLTISQKE---RRKIIgkdis 92
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgARVTGD-VTLNGEPLAAIDAPRlarLRAVL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 93 mifqePMTSlNPCFTvgYQIMEVI-------KEHLGGTRKELEARAIELLGLVGIPAPESRLRAfphQMSGGMNQRVMIA 165
Cdd:PRK13547 89 -----PQAA-QPAFA--FSAREIVllgryphARRAGALTHRDGEIAWQALALAGATALVGRDVT---TLSGGELARVQFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 166 MMIA---------CNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAE 222
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHAD 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-220 |
8.48e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFEtAHGLFRAVDsvdLEIDQGEMAAIVGESGSGKSvSMLALM-GLlpwtARITADRMNFDGKDLltisQK 81
Cdd:PRK13538 1 MLEARNLACERD-ERILFSGLS---FTLNAGELVQIEGPNGAGKT-SLLRILaGL----ARPDAGEVLWQGEPI----RR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 82 ERRKiigkdismiFQEPMTSLNpcftvgyqimevikeHLGGTRKELEA--------------------RAIELLGLVG-- 139
Cdd:PRK13538 68 QRDE---------YHQDLLYLG---------------HQPGIKTELTAlenlrfyqrlhgpgddealwEALAQVGLAGfe 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 140 -IPApesrlrafpHQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLqdLQH-KRGMALVLITH-DMGV 216
Cdd:PRK13538 124 dVPV---------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL--AQHaEQGGMVILTTHqDLPV 192
|
....
gi 522082967 217 VAET 220
Cdd:PRK13538 193 ASDK 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-199 |
3.01e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLsvefeTAHGlFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDlltISQKE 82
Cdd:PRK09700 265 VFEVRNV-----TSRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK----RAGGEIRLNGKD---ISPRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIIGKDISMIFQEPM-TSLNPCFTvgyqimevIKEHLGGTRKELEARaieLLGLVGIPAPESRLRAFPHQ-------- 153
Cdd:PRK09700 332 PLDAVKKGMAYITESRRdNGFFPNFS--------IAQNMAISRSLKDGG---YKGAMGLFHEVDEQRTAENQrellalkc 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 154 ---------MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDL 199
Cdd:PRK09700 401 hsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
128-213 |
3.55e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 128 EARAIELLGLVGIPApesrlrafpHQMSGGMNQ-------RVMIAMMIACNPRLLIADEPTTALDV-TIQaqileLLQDL 199
Cdd:PRK15064 132 EARAGELLLGVGIPE---------EQHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDV 197
|
90
....*....|....
gi 522082967 200 QHKRGMALVLITHD 213
Cdd:PRK15064 198 LNERNSTMIIISHD 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-214 |
8.27e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 21 RAVDSVDLEIDQGEMAAIVGESGSGKSvsmlALMGLLPWTARITADRMNFDGKDlltISQKERRKIIGKDISMIFQEPMT 100
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAGARKIQQGRVEVLGGD---MADARHRRAVCPRIAYMPQGLGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 101 SLNPCFTVgyqimeviKEHL-------GGTRKELEARAIELLGLVGipapesrLRAFPH----QMSGGMNQRVMIammia 169
Cdd:NF033858 88 NLYPTLSV--------FENLdffgrlfGQDAAERRRRIDELLRATG-------LAPFADrpagKLSGGMKQKLGL----- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 170 C-----NPRLLIADEPTTALDVTIQAQILELLQDLQHKR-GMALVLITHDM 214
Cdd:NF033858 148 CcalihDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYM 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-224 |
1.59e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 31 DQGEMAAIVGESGSGKSVSMLALMGL--------LPWTARITADRMNF-------------------------------- 70
Cdd:PTZ00265 1192 DSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhIVFKNEHTNDMTNEqdyqgdeeqnvgmknvnefsltkeggsgedst 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 71 ----------DGKDLLTISQKERRKIIgkdiSMIFQEPMTslnpcFTVG-YQIMEVIKEHlgGTRKELEaRAIELlglvg 139
Cdd:PTZ00265 1272 vfknsgkillDGVDICDYNLKDLRNLF----SIVSQEPML-----FNMSiYENIKFGKED--ATREDVK-RACKF----- 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 140 iPAPESRLRAFPHQ-----------MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALV 208
Cdd:PTZ00265 1335 -AAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
250
....*....|....*.
gi 522082967 209 LITHDMGVVAETAEVV 224
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIV 1429
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-186 |
1.69e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.48 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 29 EIDQGEMAAIVGESGSGKS--VSMLAlmGLL-PWTARItadrmnfdGKDLLTISQKERRkiIGKDISMifqepmtslnpc 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTtfIKMLA--GVLkPDEGDI--------EIELDTVSYKPQY--IKADYEG------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 106 fTVGYQIMEVIKEHlgGTRKELEARAIELLGLVGIPapESRLRafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALD 185
Cdd:cd03237 77 -TVRDLLSSITKDF--YTHPYFKTEIAKPLQIEQIL--DREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
.
gi 522082967 186 V 186
Cdd:cd03237 148 V 148
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-259 |
1.70e-05 |
|
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: 46.15 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 1 MSL--LEIRNlsvefetahglFRAVDSVDLEIDQGeMAAIVGESGSGKSVSMLALMGLLP--WTARITAD----RMNFDG 72
Cdd:COG3593 1 MKLekIKIKN-----------FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGpsSSRKFDEEdfylGDDPDL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 73 KDL---LTISQKERR---KIIGKDISMIFQEPMTSLNPCFTVGYQ-IMEVIKEHLGGTRKELEARaIElLGLVGIPAPES 145
Cdd:COG3593 69 PEIeieLTFGSLLSRllrLLLKEEDKEELEEALEELNEELKEALKaLNELLSEYLKELLDGLDLE-LE-LSLDELEDLLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 146 RLR-------AFP-HQMSGGMNQRVMIAMMIA-------CNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMalVLI 210
Cdd:COG3593 147 SLSlriedgkELPlDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQ--VII 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 522082967 211 -THDMGVVAET--AEVVNVQYAGQQVERQNVVDLFAKPQHPYTYALLSALPE 259
Cdd:COG3593 225 tTHSPHLLSEVplENIRRLRRDSGGTTSTKLIDLDDEDLRKLLRYLGVTRSE 276
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-58 |
1.96e-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: 44.77 E-value: 1.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 4 LEIRNLSVEFETAHGL-FRAVDSVDLEIDQGEMAAIVGESGSGKSvSML-ALMGLLP 58
Cdd:cd03250 1 ISVEDASFTWDSGEQEtSFTLKDINLEVPKGELVAIVGPVGSGKS-SLLsALLGELE 56
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-213 |
2.33e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 4 LEIRNLsvefetahGLFRAVDSVDLEidqGEMAAIVGESGSGKSvSML-----ALMGLLPWTARITADRMN--------- 69
Cdd:COG0419 5 LRLENF--------RSYRDTETIDFD---DGLNLIVGPNGAGKS-TILeairyALYGKARSRSKLRSDLINvgseeasve 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 70 --------------FDGK--DLLTISQKERRKIIGKdismIFqepmtslnpcftvGYQIMEVIKEHLGGTRKELEARAIE 133
Cdd:COG0419 73 lefehggkryrierRQGEfaEFLEAKPSERKEALKR----LL-------------GLEIYEELKERLKELEEALESALEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 134 LLGLVGIpaPESRLRAF-----PHQMSGGMNQRVMIAMMIAcnprlLIADepTTALDVTIQAQILELLQDLQhkrgmalv 208
Cdd:COG0419 136 LAELQKL--KQEILAQLsgldpIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------- 198
|
....*
gi 522082967 209 LITHD 213
Cdd:COG0419 199 IITHV 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-248 |
2.48e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMgvvaETAEVVNVQYAGQQ 232
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL----STIRYANTIFVLSN 654
|
90
....*....|....*.
gi 522082967 233 VERQNVVDLFAKPQHP 248
Cdd:PTZ00265 655 RERGSTVDVDIIGEDP 670
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-235 |
2.65e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 37 AIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDlltISQKERRKIIGKDISMIFQEPMT---SLNpcftvgyQIM 113
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKL---IREGEVRAQVKLAFENANGKKYTitrSLA-------ILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 114 EVIKEHLGGTRKelearaiellglvgiPAPESRLRafphqMSGGmnQRVMIAMMIAC--------NPRLLIADEPTTALD 185
Cdd:cd03240 96 NVIFCHQGESNW---------------PLLDMRGR-----CSGG--EKVLASLIIRLalaetfgsNCGILALDEPTTNLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 186 V-TIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVNVQYAGQQVER 235
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGRQKSR 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-217 |
2.69e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 129 ARAIELL---GL----VGIPAPesrlrafphQMSGGMNQRVMIAMMI---ACNPRLLIADEPTTAL---DVtiqAQILEL 195
Cdd:TIGR00630 807 SRKLQTLcdvGLgyirLGQPAT---------TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEV 874
|
90 100
....*....|....*....|..
gi 522082967 196 LQDLQHKrGMALVLITHDMGVV 217
Cdd:TIGR00630 875 LQRLVDK-GNTVVVIEHNLDVI 895
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-228 |
3.77e-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: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 33 GEMAAIVGESGSGKSVSMLALMG-LLP----------WTARITadrmNFDGKDLltisQKERRKIIGKDISMIFQEPMTS 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPnlgkfddppdWDEILD----EFRGSEL----QNYFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 102 LNPCFTVGYQIMEVIKEHLGGTRKELearaIELLGLVGIpapesrLRAFPHQMSGGMNQRVMIAMMIACNPRLLIADEPT 181
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDEL----VDQLELRHV------LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522082967 182 TALDV----TIQAQILELLQDlqhkrGMALVLITHDMGVVAETAEVVNVQY 228
Cdd:cd03236 168 SYLDIkqrlNAARLIRELAED-----DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-214 |
6.26e-05 |
|
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: 44.78 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 29 EIDQGEMAAIVGESGSGKS--VSMLAlmgllpwtARITADRMNFDGKdlLTISQKERRkiIGKDISMifqepmtslnpcf 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTtfAKILA--------GVLKPDEGEVDED--LKISYKPQY--ISPDYDG------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 107 TVGYQIMEVIKEHLGGTRkeLEARAIELLGLVGIpaPESRLRafphQMSGGMNQRVMIAMMIACNPRLLIADEPTTALDV 186
Cdd:COG1245 417 TVEEFLRSANTDDFGSSY--YKTEIIKPLGLEKL--LDKNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180
....*....|....*....|....*...
gi 522082967 187 TIQAQILELLQDLQHKRGMALVLITHDM 214
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-228 |
7.14e-05 |
|
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: 44.39 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 32 QGEMAAIVGESGSGKSVSMLALMGLL-----------PWTARITAdrmnFDGKDLltisQKERRKIIGKDISmifqepmT 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeepSWDEVLKR----FRGTEL----QDYFKKLANGEIK-------V 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 101 SLNPcftvgyQIMEVIKEHLGGTRKELEARA---------IELLGLVGIPapESRLRafphQMSGGMNQRVMIAMMIACN 171
Cdd:COG1245 163 AHKP------QYVDLIPKVFKGTVRELLEKVdergkldelAEKLGLENIL--DRDIS----ELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDMGVVAETAEVVNVQY 228
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELA-EEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-274 |
9.31e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 20 FRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPWTARITADRMNFDGKDLLTISQKERRKII---GKDI---SM 93
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVynaETDVhfpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 94 IFQEPMTSLNPCFTVGYQIMEVIKEHLGGTRKELEARAielLGL-------VGipapesrlRAFPHQMSGGMNQRVMIAM 166
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAT---YGLshtrntkVG--------NDFVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 167 MIACNPRLLIADEPTTALDvtiQAQILELLQDLQhkrgmALVLITHDMGVVA---------ETAEVVNVQYAGQQV---E 234
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLD---SATALEFIRALK-----TSANILDTTPLVAiyqcsqdayELFDKVIVLYEGYQIyfgP 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 522082967 235 RQNVVDLFAK-----PQHPYTYALLSALPERATGKRLPSIPGVVP 274
Cdd:TIGR00956 295 ADKAKQYFEKmgfkcPDRQTTADFLTSLTSPAERQIKPGYEKKVP 339
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-266 |
9.50e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 3 LLEIRNLSVEFetahGLFRAVDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLPwtarITADRMNFDGKDLLTISQKE 82
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP----PDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 83 RRKIigkDISMIFQEPMtsLNPCFTVgyqimeviKEHLggtrkelearaieLLGLVGIPAPESRLRAFPHQMSGGMN--- 159
Cdd:PRK15439 83 AHQL---GIYLVPQEPL--LFPNLSV--------KENI-------------LFGLPKRQASMQKMKQLLAALGCQLDlds 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 160 ----------QRVMIAMMIACNPRLLIADEPTTALDV----TIQAQILELLQdlqhkRGMALVLITHDMGVVAETAEVVN 225
Cdd:PRK15439 137 sagslevadrQIVEILRGLMRDSRILILDEPTASLTPaeteRLFSRIRELLA-----QGVGIVFISHKLPEIRQLADRIS 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 522082967 226 VQyagqqveRQNVVDLFAKPQHPYTYALLSALPERATGKRL 266
Cdd:PRK15439 212 VM-------RDGTIALSGKTADLSTDDIIQAITPAAREKSL 245
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
154-214 |
1.87e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEM 451
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
153-213 |
1.91e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHkrgmALVLITHD 213
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-217 |
3.80e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082967 154 MSGGMNQRVMIAMMIAC---NPRLLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVV 217
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV 875
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
121-216 |
7.32e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 121 GGTRKELEARAIELLGlVGIPAPESRLRAfphqMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQ 200
Cdd:PRK11288 369 NRWEAENADRFIRSLN-IKTPSREQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA 443
|
90 100
....*....|....*....|
gi 522082967 201 hKRGMALVLITHD----MGV 216
Cdd:PRK11288 444 -AQGVAVLFVSSDlpevLGV 462
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-213 |
9.18e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 9.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082967 140 IPAPESRLRAFPHQMSGGMNQRVMIAMMIA---CNPR-LLIADEPTTALDVTIQAQILELLQDLQHKRGMALVlITHD 213
Cdd:cd03227 64 VAAVSAELIFTRLQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHL 140
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
153-213 |
1.33e-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: 40.69 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDV-TIQAqiLEllQDLQHKRGMALVlITHD 213
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA--LE--EALLNFAGCAVV-ISHD 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-228 |
1.63e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522082967 153 QMSGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQHKRgmALVLITHDMGVVAETAEVVNVQY 228
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-226 |
2.25e-03 |
|
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: 38.46 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082967 154 MSGGMNQRVMIAMMIACNPR--LLIADEPTTALDVTIQAQILELLQDLQHKrGMALVLITHDMGVVAETAEVVNV 226
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
155-214 |
3.44e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 155 SGGMNQRVMIAMMIACNPRLLIADEPTTALDVTIQAQILELLQDLQhKRGMALVLITHDM 214
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSEL 464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
154-213 |
5.27e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 5.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 154 MSGGMNQRVMIAMMIACNPRLLIADEPTTALDVtiqaQILELLQDLQHKRGMALVLITHD 213
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-212 |
6.88e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.19 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 23 VDSVDLEIDQGEMAAIVGESGSGKSVSMLALMGLLP-WTARITADRmnfDGKdLLTISQKE-------RRKIIGKDISMI 94
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTKPA---KGK-LFYVPQRPymtlgtlRDQIIYPDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 95 FQEPmtslnpcftvgyqimevikehlGGTRKELEArAIELLGLVGIPAPE---SRLRAFPHQMSGGMNQRVMIAMMIACN 171
Cdd:TIGR00954 544 MKRR----------------------GLSDKDLEQ-ILDNVQLTHILEREggwSAVQDWMDVLSGGEKQRIAMARLFYHK 600
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522082967 172 PRLLIADEPTTALDVTIQAQILELLQDLqhkrGMALVLITH 212
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
150-225 |
7.99e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082967 150 FP-HQMSGGMNQRVMIAMMIA---CNPRLLIADEPTTALDVTIQAQILELLQDLQHKRGMALVLITHDMGVVAETAEVVN 225
Cdd:COG1106 198 LPlSEESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTELLDAFLELLR 277
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-56 |
9.01e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 37.86 E-value: 9.01e-03
10 20 30
....*....|....*....|....*....|.
gi 522082967 26 VDLEIDQGEMAAIVGESGSGKSVSMLALMGL 56
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
|
| |
