|
Name |
Accession |
Description |
Interval |
E-value |
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
7-251 |
1.48e-110 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 318.32 E-value: 1.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSY 86
Cdd:COG4138 1 LQLNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 87 IPILKVFQYVGLFSPNTVFSA---GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQVWDKQQCEGKFILLDEP 163
Cdd:COG4138 81 PFAMPVFQYLALHQPAGASSEaveQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 164 TNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIFMSEIKLSHSA 243
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVE 240
|
....*...
gi 2697035156 244 SHRVWQVI 251
Cdd:COG4138 241 GHRWLIPT 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
7-248 |
1.71e-91 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 270.27 E-value: 1.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSY 86
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 87 IPILKVFQYVGLFSP---NTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQVWDKQQCEGKFILLDEP 163
Cdd:PRK03695 81 PFAMPVFQYLTLHQPdktRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 164 TNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIFMSEIKLSHSA 243
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVE 240
|
....*
gi 2697035156 244 SHRVW 248
Cdd:PRK03695 241 GHPML 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-233 |
1.96e-52 |
|
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: 170.61 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI--DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:COG1120 1 MLEAENLSVgyGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVSYIPILKVFQYV--------GLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqq 152
Cdd:COG1120 81 PQEPPAPFGLTVRELValgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 153 cEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSD 231
Cdd:COG1120 155 -EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEE 233
|
..
gi 2697035156 232 IF 233
Cdd:COG1120 234 VY 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-218 |
2.25e-49 |
|
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: 160.29 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 8 DIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQ 82
Cdd:cd03214 1 EVENLSVGyggrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 83 LVSYipilkvfqyvglfspntvfsagvferlcsdFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDE 162
Cdd:cd03214 81 ALEL------------------------------LGLAHLADRPFNELSGGERQRVLLARALAQ-------EPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 163 PTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-251 |
2.71e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.48 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:COG4559 2 LEAENLSvrLGGRTLldDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELtPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QlvsYIPI---LKVFQYVGL-----FSPNTVFSAGVFERLcSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQVWDKQQC 153
Cdd:COG4559 82 Q---HSSLafpFTVEEVVALgraphGSSAAQDRQIVREAL-ALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 154 EGKFILLDEPTNNLDII-QQAMLDKwIKYFCDCLGTVIMSGHDLshsykN-----ASCIWMIKQGQLVAVGKPECIMTEK 227
Cdd:COG4559 158 GPRWLFLDEPTSALDLAhQHAVLRL-ARQLARRGGGVVAVLHDL-----NlaaqyADRILLLHQGRLVAQGTPEEVLTDE 231
|
250 260
....*....|....*....|....
gi 2697035156 228 NLSDIFMSEIKLSHSASHRVWQVI 251
Cdd:COG4559 232 LLERVYGADLRVLAHPEGGCPQVL 255
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
1.27e-34 |
|
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: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNITI--DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHiaqlsQ 75
Cdd:COG1121 1 MMMMPAIELENLTVsyGGRPVleDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFGKPPRRAR-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQLVSY---IPIlKVFQYV--GLFSpntvfSAGVFERLCSD-----------FQLTSLLSKPINQLSGGEWQRVR 139
Cdd:COG1121 76 RIGYVPQRAEVdwdFPI-TVRDVVlmGRYG-----RRGLFRRPSRAdreavdealerVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 140 IVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQ----AMLDKWIKYFCdclgTVIMSGHDLSHSYKNASCIWMIKQGqLV 215
Cdd:COG1121 150 LARALAQ-------DPDLLLLDEPFAGVDAATEealyELLRELRREGK----TILVVTHDLGAVREYFDRVLLLNRG-LV 217
|
250 260
....*....|....*....|....*...
gi 2697035156 216 AVGKPECIMTEKNLSDIFMSEIKLSHSA 243
Cdd:COG1121 218 AHGPPEEVLTPENLSRAYGGPVALLAHG 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-247 |
3.52e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.65 E-value: 3.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:COG4604 2 IEIKNVSkrYGGKVVldDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKVFQYVGlfspntvF-----SAGvfeRLCSD-----------FQLTSLLSKPINQLSGGEWQRVRIVAAFL 145
Cdd:COG4604 82 QENHINSRLTVRELVA-------FgrfpySKG---RLTAEdreiideaiayLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 146 QvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHsyknASC----IWMIKQGQLVAVGKP 220
Cdd:COG4604 152 Q-------DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGkTVVIVLHDINF----ASCyadhIVAMKDGRVVAQGTP 220
|
250 260
....*....|....*....|....*..
gi 2697035156 221 ECIMTEKNLSDIFMSEIKLSHSASHRV 247
Cdd:COG4604 221 EEIITPEVLSDIYDTDIEVEEIDGKRI 247
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-238 |
6.53e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.48 E-value: 6.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT--IDTRLV--NVSAQVLTGEqIH-ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyHIAQLSQQRAYL 80
Cdd:COG1131 1 IEVRGLTkrYGDKTAldGVSLTVEPGE-IFgLLGPNGAGKTTTIRMLLGLLrPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVSYIPILKVFQYVGLFS-----PNTVFSAgVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEG 155
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFArlyglPRKEARE-RIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL-------HDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 156 KFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPEcIMTEKNLSDIFMS 235
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD-ELKARLLEDVFLE 229
|
...
gi 2697035156 236 EIK 238
Cdd:COG1131 230 LTG 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-251 |
9.82e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.57 E-value: 9.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSYIPILKVFQYVGL 98
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELsPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 -FSPNTvFSAGVFERLCSDF----QLTSLLSKPINQLSGGEWQRVRIVAAFLQVWdKQQCEGKFILLDEPTNNLDIIQQA 173
Cdd:PRK13548 100 gRAPHG-LSRAEDDALVAAAlaqvDLAHLAGRDYPQLSGGEQQRVQLARVLAQLW-EPDGPPRWLLLDEPTSALDLAHQH 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 174 MLDKWIKYFC-DCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIFMSEIKLSHSASHRVWQVI 251
Cdd:PRK13548 178 HVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQPHPETGAPLVL 256
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-229 |
3.77e-30 |
|
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: 112.43 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT---IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQrayl 80
Cdd:COG1122 1 IELENLSfsyPGGTPAldDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDGKDITKKNLRELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 sqlVSYipilkVFQYvglfsPNT-VFSAGVFE---------------------RLCSDFQLTSLLSKPINQLSGGEWQRV 138
Cdd:COG1122 77 ---VGL-----VFQN-----PDDqLFAPTVEEdvafgpenlglpreeirerveEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 ---RIVAaflqvwdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:COG1122 144 aiaGVLA----------MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
250
....*....|....
gi 2697035156 216 AVGKPECIMTEKNL 229
Cdd:COG1122 214 ADGTPREVFSDYEL 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-195 |
5.05e-30 |
|
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: 111.42 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI--DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyHIAQLSQQRAYLS 81
Cdd:COG4133 3 LEAENLSCrrGERLLfsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKVFQYVGLFSP--NTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFL---QVWdkqqcegk 156
Cdd:COG4133 82 HADGLKPELTVRENLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLspaPLW-------- 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2697035156 157 fiLLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHD 195
Cdd:COG4133 154 --LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-213 |
1.03e-28 |
|
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: 107.94 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYlsqlvsyipilkVFQY- 95
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGL------------VFQNp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 -VGLFSPnTVFSAGVF----------------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFI 158
Cdd:cd03225 85 dDQFFGP-TVEEEVAFglenlglpeeeieervEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA-------MDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 159 LLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQ 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-214 |
1.56e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.90 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:COG4619 1 LELEGLSFRvggkPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QlvsyIPIL----------KVFQYVGL-FSPNTVfsAGVFERLCSDfqlTSLLSKPINQLSGGEWQRVRIVAAFLQvwdk 150
Cdd:COG4619 81 Q----EPALwggtvrdnlpFPFQLRERkFDRERA--LELLERLGLP---PDILDKPVERLSGGERQRLALIRALLL---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 151 qqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQL 214
Cdd:COG4619 148 ---QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-242 |
9.87e-27 |
|
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: 104.01 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP--VGGDILIGGRSIRQYHIAQLSQQRAY 79
Cdd:COG1119 3 LLELRNVTVrrgGKTILdDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 LSQ-LVSYIPI-LKVFQYV--GLFSpntvfSAGVF-----------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAF 144
Cdd:COG1119 83 VSPaLQLRFPRdETVLDVVlsGFFD-----SIGLYreptdeqreraRELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 145 LQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDcLG--TVIMSGHDL-------SHsyknascIWMIKQGQLV 215
Cdd:COG1119 158 VK-------DPELLILDEPTAGLDLGARELLLALLDKLAA-EGapTLVLVTHHVeeippgiTH-------VLLLKDGRVV 222
|
250 260
....*....|....*....|....*..
gi 2697035156 216 AVGKPECIMTEKNLSDIFMSEIKLSHS 242
Cdd:COG1119 223 AAGPKEEVLTSENLSEAFGLPVEVERR 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-233 |
1.27e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 5 LIIDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAY 79
Cdd:PRK11231 1 MTLRTENLTVgygTKRILnDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 LSQ------------LVSY--IPILKVFqyvGLFSPNtvfSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFL 145
Cdd:PRK11231 81 LPQhhltpegitvreLVAYgrSPWLSLW---GRLSAE---DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 146 QvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:PRK11231 155 Q-------DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
....*...
gi 2697035156 226 EKNLSDIF 233
Cdd:PRK11231 228 PGLLRTVF 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-238 |
1.37e-26 |
|
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: 103.40 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYhIAQLSQQRAYLSQLVSYIPILKVFQYV 96
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPDSGSILIDGEDVRKE-PREARRQIGVLPDERGLYDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSP-NTVFS---AGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQ 172
Cdd:COG4555 96 RYFAElYGLFDeelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH-------DPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 173 AMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIM---TEKNLSDIFMSEIK 238
Cdd:COG4555 169 RLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAFVALIG 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-221 |
4.78e-26 |
|
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: 106.00 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI-----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:COG4988 337 IELEDVSFsypggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQlVSYIP-------------------ILKVFQYVGLfspntvfsagvferlcSDF--QLTSLLSKPIN----QLSGGEW 135
Cdd:COG4988 417 PQ-NPYLFagtirenlrlgrpdasdeeLEAALEAAGL----------------DEFvaALPDGLDTPLGeggrGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 136 QRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDI-----IQQAMLDkwikyfcdcLG---TVIMSGHDLsHSYKNASCIW 207
Cdd:COG4988 480 QRLALARALLR-------DAPLLLLDEPTAHLDAeteaeILQALRR---------LAkgrTVILITHRL-ALLAQADRIL 542
|
250
....*....|....
gi 2697035156 208 MIKQGQLVAVGKPE 221
Cdd:COG4988 543 VLDDGRIVEQGTHE 556
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-213 |
9.51e-26 |
|
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: 98.86 E-value: 9.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 16 TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQraylsqlVSYIPilkvfq 94
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRR-------IGYVP------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 yvglfspntvfsagvferlcsdfqltsllskpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAM 174
Cdd:cd00267 80 ----------------------------------QLSGGQRQRVALARALLL-------NPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 2697035156 175 LDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQ 213
Cdd:cd00267 119 LLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-165 |
1.71e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.10 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSYIPILKVFQ---- 94
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGlLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREnlrl 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 95 YVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPI----NQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTN 165
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALL-------TKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-225 |
2.69e-25 |
|
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: 103.83 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITIDTR------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP----VGGDILIGGRSIRQYHIAQLSQ 75
Cdd:COG1123 4 LLEVRDLSVRYPggdvpaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQ--LVSYIPiLKVFQYVGLFSPNTVFSAGVF----ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwd 149
Cdd:COG1123 84 RIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEArarvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA---- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 150 kqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:COG1123 159 ---LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-233 |
1.41e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI---DTRLVN-VSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:PRK09536 4 IDVSDLSVefgDTTVLDgVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKVFQYV--------GLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqc 153
Cdd:PRK09536 84 QDTSLSFEFDVRQVVemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 154 EGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIF 233
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-218 |
3.40e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 96.45 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 9 IKNITI--DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYH--IAQLSQQRAYLS 81
Cdd:cd03235 2 VEDLTVsyGGHPVleDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPLEKERkrIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLvsyiPILkVFQYV--GLFSPntvfsAGVFERL-CSDFQ----------LTSLLSKPINQLSGGEWQRVRIVAAFLQvw 148
Cdd:cd03235 82 DF----PIS-VRDVVlmGLYGH-----KGLFRRLsKADKAkvdealervgLSELADRQIGELSGGQQQRVLLARALVQ-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 149 dkqqcEGKFILLDEPTNNLDIIQQA----MLDKWIKYFCdclgTVIMSGHDLSHSYKNASCIWMIKQGqLVAVG 218
Cdd:cd03235 150 -----DPDLLLLDEPFAGVDPKTQEdiyeLLRELRREGM----TILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-213 |
6.92e-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: 94.37 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQlvsyIPILkvfqyv 96
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAYVPQ----DPFL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspntvFSAGVFErlcsdfqltsllskpiNQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD-----IIQ 171
Cdd:cd03228 88 --------FSGTIRE----------------NILSGGQRQRIAIARALLR-------DPPILILDEATSALDpeteaLIL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2697035156 172 QAMLdkwiKYFCDClgTVIMSGHDLShSYKNASCIWMIKQGQ 213
Cdd:cd03228 137 EALR----ALAKGK--TVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-233 |
8.14e-23 |
|
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: 93.40 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI-----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQR--- 77
Cdd:cd03256 1 IEVENLSKtypngKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKGKALRQLRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYLSQLVSYIPILKVFQYV---------------GLFSPNTVFSAgvFERLcSDFQLTSLLSKPINQLSGGEWQRVRIVA 142
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrstwrslfGLFPKEEKQRA--LAAL-ERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 143 AFLQvwdkqqcEGKFILLDEPTNNLDII--QQAMLDkwIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGK 219
Cdd:cd03256 158 ALMQ-------QPKLILADEPVASLDPAssRQVMDL--LKRINREEGiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
250
....*....|....
gi 2697035156 220 PECImTEKNLSDIF 233
Cdd:cd03256 229 PAEL-TDEVLDEIY 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-221 |
9.19e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI--DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQ-----LSQQR- 77
Cdd:COG3840 2 LRLDDLTYryGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLpPDSGRILWNGQDLTALPPAErpvsmLFQENn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 --AYLSqlvsyipilkVFQYVGL-FSPNTVFSAGVFERL---CSDFQLTSLLS-KPiNQLSGGEWQRVRIVAAFLQvwdK 150
Cdd:COG3840 82 lfPHLT----------VAQNIGLgLRPGLKLTAEQRAQVeqaLERVGLAGLLDrLP-GQLSGGQRQRVALARCLVR---K 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 151 QQCegkfILLDEPTNNLDI-IQQAMLDkWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:COG3840 148 RPI----LLLDEPFSALDPaLRQEMLD-LVDELCRERGlTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-214 |
2.07e-22 |
|
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: 90.53 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyHIAQLSQQRAYLS 81
Cdd:cd03230 1 IEVRNLSkrYGKKTAldDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKVFQYVglfspntvfsagvferlcsdfqltsllskpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLD 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLH-------DPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 162 EPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQL 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-218 |
1.01e-21 |
|
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: 90.47 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGR---SIRQYHIAQLSQQRAYLSQLVSYIPILKVF 93
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAGLvpwKRRKKFLRRIGVVFGQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYV----GLfsPNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDI 169
Cdd:cd03267 117 YLLaaiyDL--PPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH-------EPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2697035156 170 IQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03267 187 VAQENIRNFLKEYNRERGtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-227 |
1.08e-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: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQlVSYIpilkvfqyv 96
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ-RPHL--------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspntvFSAGVFERL------CSDFQLTSLLSK----------------PI----NQLSGGEWQRVRIVAAFLQvwdk 150
Cdd:COG4987 421 --------FDTTLRENLrlarpdATDEELWAALERvglgdwlaalpdgldtWLgeggRRLSGGERRRLALARALLR---- 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 151 qqcEGKFILLDEPTNNLDII-QQAMLDKWIKYFCDclGTVIMSGHDLSHsYKNASCIWMIKQGQLVAVGKPECIMTEK 227
Cdd:COG4987 489 ---DAPILLLDEPTEGLDAAtEQALLADLLEALAG--RTVLLITHRLAG-LERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-213 |
2.45e-21 |
|
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: 87.63 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSirqyhIAQLSQQRAYLS 81
Cdd:cd03229 1 LELKNVSKRygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDGED-----LTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYipilkVFQYVGLFSPNTVFSAGVFerlcsdfqltsllskpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLD 161
Cdd:cd03229 76 RRIGM-----VFQDFALFPHLTVLENIAL------------------GLSGGQQQRVALARALAM-------DPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 162 EPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQ 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-221 |
3.48e-21 |
|
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: 92.20 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAY 79
Cdd:COG2274 474 IELENVSFrypgDSPPVldNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsqlvsyipilkVFQYVGLFSPN-----TVFSAGV-FERL---CSDFQLTSLLSK-------PI----NQLSGGEWQRVR 139
Cdd:COG2274 554 ------------VLQDVFLFSGTireniTLGDPDAtDEEIieaARLAGLHDFIEAlpmgydtVVgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 140 IVAAFLQvwdkqqcEGKFILLDEPTNNLD-----IIQQAMLdkwiKYFCDClgTVIMSGHDLSHSyKNASCIWMIKQGQL 214
Cdd:COG2274 622 IARALLR-------NPRILILDEATSALDaeteaIILENLR----RLLKGR--TVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
....*..
gi 2697035156 215 VAVGKPE 221
Cdd:COG2274 688 VEDGTHE 694
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-195 |
1.15e-20 |
|
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: 87.16 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRA----YLSQLVSYIPILKV 92
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVRVDGTDISKLSEKELAAFRRrhigFVFQSFNLLPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYVGL---FSPNTVFSA-GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLD 168
Cdd:cd03255 100 LENVELpllLAGVPKKERrERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA-------NDPKIILADEPTGNLD 172
|
170 180 190
....*....|....*....|....*....|...
gi 2697035156 169 -----IIQQAMLDkwikyFCDCLG-TVIMSGHD 195
Cdd:cd03255 173 setgkEVMELLRE-----LNKEAGtTIVVVTHD 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
3.23e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.87 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENklIIDIKNIT-------IDTR-LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIA 71
Cdd:COG1136 1 MSP--LLELRNLTksygtgeGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 72 QLSQQRAylsQLVSYipilkVFQYVGLFSPNTVFS--------AGV--------FERLCSDFQLTSLLSKPINQLSGGEW 135
Cdd:COG1136 79 ELARLRR---RHIGF-----VFQFFNLLPELTALEnvalplllAGVsrkerrerARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 136 QRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLD-----IIQQAMLDkwikyFCDCLG-TVIMSGHDLsHSYKNASCIWMI 209
Cdd:COG1136 151 QRVAIARALV-------NRPKLILADEPTGNLDsktgeEVLELLRE-----LNRELGtTIVMVTHDP-ELAARADRVIRL 217
|
....*..
gi 2697035156 210 KQGQLVA 216
Cdd:COG1136 218 RDGRIVS 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-225 |
9.08e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.65 E-value: 9.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP---------VGGDILIGGRSIRQYHIAQLSQQRAYLSQL----- 83
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 84 ---VSYIPILKVFQYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQVW--DKQQCEGKFI 158
Cdd:PRK13547 97 afsAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWppHDAAQPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 159 LLDEPTNNLDII-QQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:PRK13547 177 LLDEPTAALDLAhQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
1.22e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 4 KLIIDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIgGRSIRqyhIAQLSQQRA 78
Cdd:COG0488 313 KKVLELEGLSKsygDKTLLdDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDSGTVKL-GETVK---IGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 79 YL----------SQLVSYIPILKVFQYVG--LFSPNTVFsagvferlcsdfqltsllsKPINQLSGGEWQRVRIVAAFLQ 146
Cdd:COG0488 389 ELdpdktvldelRDGAPGGTEQEVRGYLGrfLFSGDDAF-------------------KPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 147 vwdkqqcEGKFILLDEPTNNLDI-----IQQAmLDKWikyfcdcLGTVIMSGHD---LShsyKNASCIWMIKQGQLV 215
Cdd:COG0488 450 -------PPNVLLLDEPTNHLDIetleaLEEA-LDDF-------PGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-218 |
2.07e-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: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTR----LVNVSAQVLTGeqIH-ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAqLSQQRAYL 80
Cdd:cd03264 1 LQLENLTKRYGkkraLDGVSLTLGPG--MYgLLGPNGAGKTTLMRILATLTpPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVSYIPILKVFQ---YVGLFS--PNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEG 155
Cdd:cd03264 78 PQEFGVYPNFTVREfldYIAWLKgiPSKEVKARV-DEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG-------DP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 156 KFILLDEPTNNLD---------IIQQAMLDKwikyfcdclgTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03264 150 SILIVDEPTAGLDpeerirfrnLLSELGEDR----------IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-173 |
8.20e-19 |
|
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: 82.54 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI-------DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyhiaqlSQQR 77
Cdd:COG1124 2 LEVRNLSVsygqggrRVPVLkDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTR------RRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYLSQlVSYipilkVFQ-YVGLFSPN-TVFSA--------GVFE------RLCSDFQLT-SLLSKPINQLSGGEWQRVRI 140
Cdd:COG1124 76 AFRRR-VQM-----VFQdPYASLHPRhTVDRIlaeplrihGLPDreeriaELLEQVGLPpSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190
....*....|....*....|....*....|...
gi 2697035156 141 VAAFLqvwdkqqCEGKFILLDEPTNNLDIIQQA 173
Cdd:COG1124 150 ARALI-------LEPELLLLDEPTSALDVSVQA 175
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-209 |
2.07e-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: 83.88 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 15 DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSIRQYHIAQLSQQRAYLSQlVSYIPILKVF 93
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTeGSIAVNGVPLADADADSWRDQIAWVPQ-HPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLFSPNTVFSA--GVFERLCSDFQLTSL---LSKPI----NQLSGGEWQRVRIVAAFLQVwdkqqceGKFILLDEPT 164
Cdd:TIGR02857 414 ENIRLARPDASDAEirEALERAGLDEFVAALpqgLDTPIgeggAGLSGGQAQRLALARAFLRD-------APLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDclG-TVIMSGHDLSHSYkNASCIWMI 209
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GrTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-221 |
2.31e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 81.23 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHIaqlsQQRAyls 81
Cdd:cd03296 3 IEVRNVSKRfgdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPV----QERN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlVSYipilkVFQYVGLFSPNTVFSAGVF--------------------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIV 141
Cdd:cd03296 76 --VGF-----VFQHYALFRHMTVFDNVAFglrvkprserppeaeirakvHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 142 AAfLQVwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:cd03296 149 RA-LAV------EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
.
gi 2697035156 221 E 221
Cdd:cd03296 222 D 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-217 |
3.72e-18 |
|
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: 79.01 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsiRQYHIAqlsqqraylsqlvsyipilkvfqyv 96
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkPDSGEILVDG---KEVSFA------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfSPNTVFSAGVFerlcsdfqltsllskPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLD 176
Cdd:cd03216 68 ---SPRDARRAGIA---------------MVYQLSVGERQMVEIARALAR-------NARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2697035156 177 KWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAV 217
Cdd:cd03216 123 KVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-225 |
3.75e-18 |
|
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: 80.81 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSYIPILKVFQYVGL 98
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEENIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 F-SPNTVFSAGVFERLcsdFQLTSLLSKPIN--------QLSGGEWQRV---RIVAAflqvwdkqqcEGKFILLDEPTNN 166
Cdd:cd03295 99 VpKLLKWPKEKIRERA---DELLALVGLDPAefadryphELSGGQQQRVgvaRALAA----------DPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 167 LDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-218 |
4.26e-18 |
|
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: 79.87 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSI-----RQYHIAQLSQQ 76
Cdd:cd03259 1 LELKGLSKtygSVRALdDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEILIDGRDVtgvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 77 RAYLsqlvsyiPILKVFQYVGL-----FSPNTVFSAGVFERLcSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkq 151
Cdd:cd03259 81 YALF-------PHLTVAENIAFglklrGVPKAEIRARVRELL-ELVGLEGLLNRYPHELSGGQQQRVALARALAR----- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 152 qcEGKFILLDEPTNNLD-IIQQAMLDKwIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03259 148 --EPSLLLLDEPLSALDaKLREELREE-LKELQRELGiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-168 |
7.90e-18 |
|
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: 79.62 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG----GDILIGGRSIR----QYHIAQLSQQRAYLSQL-----V 84
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQPRKpdqfQKCVAYVRQDDILLPGLtvretL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 85 SYIPILKvfqyVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:cd03234 103 TYTAILR----LPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW-------DPKVLILDEPT 171
|
....
gi 2697035156 165 NNLD 168
Cdd:cd03234 172 SGLD 175
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-215 |
1.05e-17 |
|
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: 78.84 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 8 DIKNITIDTR-----LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyHIAQLSQQRAYLS 81
Cdd:cd03226 1 RIENISFSYKkgteiLDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILK-VFQYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILL 160
Cdd:cd03226 78 QDVDYQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL-------SGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 161 DEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-221 |
1.43e-17 |
|
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: 81.49 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLsQLV------SYIPILKV 92
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRRSLRELRRRV-QMVfqdpysSLNPRMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYV--GLFSPNTVFSAGVFER---LCSDFQL-TSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNN 166
Cdd:COG1123 362 GDIIaePLRLHGLLSRAERRERvaeLLERVGLpPDLADRYPHELSGGQRQRVAIARALA-------LEPKLLILDEPTSA 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 167 LDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRELGlTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-228 |
1.91e-17 |
|
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: 78.70 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiaQLSQQRAYls 81
Cdd:cd03261 1 IELRGLTKSfggrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIDGEDIS-----GLSEAELY-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlvsyiPILK----VFQYVGLFSPNTVFSAGVF----ERLCSDFQLTSLLSKPIN-------------QLSGGEWQRV-- 138
Cdd:cd03261 74 ------RLRRrmgmLFQSGALFDSLTVFENVAFplreHTRLSEEEIREIVLEKLEavglrgaedlypaELSGGMKKRVal 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 -RIVAAflqvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVA 216
Cdd:cd03261 148 aRALAL----------DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
250
....*....|..
gi 2697035156 217 VGKPECIMTEKN 228
Cdd:cd03261 218 EGTPEELRASDD 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
2.35e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.98 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQraylsqlVSYipilkVFQYVGL 98
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRfYDPTSGRILIDGVDIRDLTLESLRRQ-------IGV-----VPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 FSpNTVFS--------------------AGvferlCSDFqLTSL---LSKPINQ----LSGGEWQRVRIVAAFLQvwdkq 151
Cdd:COG1132 426 FS-GTIREnirygrpdatdeeveeaakaAQ-----AHEF-IEALpdgYDTVVGErgvnLSGGQRQRIAIARALLK----- 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 152 qcEGKFILLDEPTNNLD-----IIQQAmLDKWIKyfcdclG-TVIMSGHDLShSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:COG1132 494 --DPPILILDEATSALDteteaLIQEA-LERLMK------GrTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHE 559
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-218 |
2.66e-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: 77.71 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIR---QYHIAQLSQQRA 78
Cdd:cd03269 1 LEVENVTKRfgrvTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDGKPLDiaaRNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 79 -Y-----LSQLVsYIPILKvfqyvGLfspNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqq 152
Cdd:cd03269 81 lYpkmkvIDQLV-YLAQLK-----GL---KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH------ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 153 cEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03269 146 -DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
11-218 |
4.77e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.34 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 11 NITIDTRLVNVSAQV---LTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGR----SIRQYHIAqlSQQR--AYL 80
Cdd:cd03297 3 CVDIEKRLPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTvlfdSRKKINLP--PQQRkiGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVSYIPILKVFQyvglfspNTVFSAGV---------FERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkq 151
Cdd:cd03297 81 FQQYALFPHLNVRE-------NLAFGLKRkrnredrisVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAA----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 152 qcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03297 149 --QPELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-236 |
6.05e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIR--------QYHIAQLSQQRAYLSQLVSYIPIL 90
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIIIDDEDISllplharaRRGIGYLPQEASIFRRLSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 91 KVFQYVGLFSPNTvfSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFlqvwdkqQCEGKFILLDEPTNNLDII 170
Cdd:PRK10895 101 AVLQIRDDLSAEQ--REDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL-------AANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 171 QQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIFMSE 236
Cdd:PRK10895 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGE 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-195 |
6.77e-17 |
|
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: 75.18 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI--DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaqlsqqrayls 81
Cdd:cd03221 1 IELENLSKtyGGKLLlkDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVTWGSTVK---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlVSYIPilkvfqyvglfspntvfsagvferlcsdfqltsllskpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLD 161
Cdd:cd03221 65 --IGYFE----------------------------------------QLSGGEKMRLALAKLLLE-------NPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|....
gi 2697035156 162 EPTNNLDIIQQAMLDKWIKYFcdcLGTVIMSGHD 195
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY---PGTVILVSHD 126
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-218 |
7.78e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 76.78 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITIDTR--------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRsirqyHIAQLSQ- 75
Cdd:cd03257 1 LLEVKNLSVSFPtgggsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGK-----DLLKLSRr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQLVSYIP----------------ILKVFQYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVR 139
Cdd:cd03257 76 LRKIRRKEIQMVFqdpmsslnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 140 IVAAFLqvwdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03257 156 IARALA-------LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGlTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-221 |
8.34e-17 |
|
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: 76.99 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTR---LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiAQLSQQRaylsQ 82
Cdd:cd03299 1 LKVENLSKDWKefkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSGKILLNGKDI-----TNLPPEK----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 83 LVSYIPilkvfQYVGLFSPNTVF---SAGVFERLCS-------------DFQLTSLLSKPINQLSGGEWQRVRIVAAFLq 146
Cdd:cd03299 72 DISYVP-----QNYALFPHMTVYkniAYGLKKRKVDkkeierkvleiaeMLGIDHLLNRKPETLSGGEQQRVAIARALV- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 147 vwdkqqCEGKFILLDEPTNNLDIIQQA----MLDKWIKYFCDclgTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:cd03299 146 ------VNPKILLLDEPFSALDVRTKEklreELKKIRKEFGV---TVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-229 |
1.20e-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: 76.42 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI--DTR-----LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRA 78
Cdd:cd03249 1 IEFKNVSFryPSRpdvpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERfYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 79 YLSQLvsyiPILkvfqYVGLFSPNTVFSAG-----VFERLCSDFQLTSLLSKPIN-----------QLSGGEWQRVRIVA 142
Cdd:cd03249 81 LVSQE----PVL----FDGTIAENIRYGKPdatdeEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 143 AFLQvwdkqqcEGKFILLDEPTNNLD-----IIQQAmLDKWIKYFcdclgTVIMSGHDLShSYKNASCIWMIKQGQLVAV 217
Cdd:cd03249 153 ALLR-------NPKILLLDEATSALDaesekLVQEA-LDRAMKGR-----TTIVIAHRLS-TIRNADLIAVLQNGQVVEQ 218
|
250
....*....|..
gi 2697035156 218 GKPECIMTEKNL 229
Cdd:cd03249 219 GTHDELMAQKGV 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-194 |
1.72e-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: 74.56 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVsyipilkvfqyv 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVRLDGADISQWDPNELGDHVGYLPQDD------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspnTVFSAGVFErlcsdfqltsllskpiNQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLD 176
Cdd:cd03246 86 ------ELFSGSIAE----------------NILSGGQRQRLGLARALYG-------NPRILVLDEPNSHLDVEGERALN 136
|
170
....*....|....*...
gi 2697035156 177 KWIKYFCDCLGTVIMSGH 194
Cdd:cd03246 137 QAIAALKAAGATRIVIAH 154
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-196 |
2.27e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSirqyHIAQLSQQraylSQLVSYIPI------- 89
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLrPTSGTVRRAGGA----RVAYVPQR----SEVPDSLPLtvrdlva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 90 LKVFQYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDI 169
Cdd:NF040873 80 MGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-------EADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 2697035156 170 IQQAMLDKWIKYFCDCLGTVIMSGHDL 196
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-218 |
2.82e-16 |
|
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: 75.22 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 22 SAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGrsirQYHIAQLSQQR--AYLSQLVSYIPILKVFQYVGL 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRVLING----VDVTAAPPADRpvSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 -FSPNTVFSA---GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD-IIQQA 173
Cdd:cd03298 94 gLSPGLKLTAedrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVR-------DKPVLLLDEPFAALDpALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2697035156 174 MLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-236 |
4.23e-16 |
|
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: 76.69 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 12 ITIDTRLvnvSAQVLTGeqihILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaQLSQQRAYLS---QLVSYi 87
Cdd:TIGR02142 14 LDADFTL---PGQGVTA----IFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTL------FDSRKGIFLPpekRRIGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 88 pilkVFQYVGLFSPNTVFS--------------AGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqc 153
Cdd:TIGR02142 80 ----VFQEARLFPHLSVRGnlrygmkrarpserRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLS------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 154 EGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGT-VIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDI 232
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
....
gi 2697035156 233 FMSE 236
Cdd:TIGR02142 229 ARED 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-226 |
6.63e-16 |
|
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: 74.99 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQ-QRAYLSQlvsyipilkVFQYVG 97
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPTSGKVLIDGQDIAAMSRKELRElRRKKISM---------VFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 LFsP------NTVFS---AGV-----FERLCSDFQLTSL---LSKPINQLSGGEWQRV---RIVAAFLQVWdkqqcegkf 157
Cdd:cd03294 113 LL-PhrtvleNVAFGlevQGVpraerEERAAEALELVGLegwEHKYPDELSGGMQQRVglaRALAVDPDIL--------- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 158 iLLDEPTNNLD-IIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTE 226
Cdd:cd03294 183 -LMDEAFSALDpLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-223 |
1.17e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 73.81 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQyhiaqlsqqrayls 81
Cdd:cd03300 1 IELENVSKfyggFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDITN-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlvsyIPILK-----VFQYVGLFSPNTVFSAGVF----------------ERLCSDFQLTSLLSKPINQLSGGEWQRVRI 140
Cdd:cd03300 67 -----LPPHKrpvntVFQNYALFPHLTVFENIAFglrlkklpkaeikervAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 141 VAAFLqvwdkqqCEGKFILLDEPTNNLDI-IQQAMLDKwIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03300 142 ARALV-------NEPKVLLLDEPLGALDLkLRKDMQLE-LKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
....*
gi 2697035156 219 KPECI 223
Cdd:cd03300 214 TPEEI 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-220 |
2.48e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 9 IKNITIDtrlvnVSAQVLTGeqihILGANGAGKSTLLAAISGYL-PVGGDILIGGRSI--RQYHIAQLSQQRAYLSQlvs 85
Cdd:PRK13638 17 LKGLNLD-----FSLSPVTG----LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLdySKRGLLALRQQVATVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 86 yIPILKVFqYVGLFSpNTVFSA---GVFERLCS---DFQLT-----SLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCE 154
Cdd:PRK13638 85 -DPEQQIF-YTDIDS-DIAFSLrnlGVPEAEITrrvDEALTlvdaqHFRHQPIQCLSHGQKKRVAIAGALV-------LQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 155 GKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-233 |
2.86e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSYIPILKVFQYV-- 96
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTVFS------AGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDII 170
Cdd:PRK10253 105 GRYPHQPLFTrwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 171 QQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIF 233
Cdd:PRK10253 178 HQIDLLELLSELNREKGyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-228 |
3.98e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAIS-GYLPVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSyipilkvfqyv 96
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVH----------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspntVFSAGVFERL------CSDFQLTSLL-----------SKPIN--------QLSGGEWQRVRIVAAFLQvwdkq 151
Cdd:PRK11160 425 -------LFSATLRDNLllaapnASDEALIEVLqqvgleklledDKGLNawlgeggrQLSGGEQRRLGIARALLH----- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 152 qcEGKFILLDEPTNNLD---------IIQQAMLDKwikyfcdclgTVIMSGHDLsHSYKNASCIWMIKQGQLVAVGKPEC 222
Cdd:PRK11160 493 --DAPLLLLDEPTEGLDaeterqileLLAEHAQNK----------TVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQE 559
|
....*.
gi 2697035156 223 IMTEKN 228
Cdd:PRK11160 560 LLAQQG 565
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-225 |
4.12e-15 |
|
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: 72.19 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIaqlsQQRAYLSqlVSYIP---------- 88
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDITKLPM----HKRARLG--IGYLPqeasifrklt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 89 ----ILKVFQYVGLfspNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPT 164
Cdd:cd03218 92 veenILAVLEIRGL---SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA-------TNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDC-LGTVImSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRgIGVLI-TDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-218 |
6.17e-15 |
|
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: 70.80 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsirqYHIAQLSQQrayLSQLVSYIPilkvfQYV 96
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDG-----VPVSDLEKA---LSSLISVLN-----QRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSpntvfsagvferlcsdfqlTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD-IIQQAML 175
Cdd:cd03247 85 YLFD-------------------TTLRNNLGRRFSGGERQRLALARILLQ-------DAPIVLLDEPTVGLDpITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2697035156 176 DKWIKYFCDclGTVIMSGHDLShSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03247 139 SLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-218 |
1.04e-14 |
|
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: 71.08 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 17 RLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQraylsqlVSYIPilkvfQY 95
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTSGSVLLDGTDIRQLDPADLRRN-------IGYVP-----QD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFS----PNTVFSAGVF--ERLCSDFQLTSL----------LSKPIN----QLSGGEWQRVRIVAAFLQvwdkqqcEG 155
Cdd:cd03245 87 VTLFYgtlrDNITLGAPLAddERILRAAELAGVtdfvnkhpngLDLQIGergrGLSGGQRQAVALARALLN-------DP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 156 KFILLDEPTNNLDIIQQAM----LDKWIkyfcdCLGTVIMSGHDLShSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERlkerLRQLL-----GDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-171 |
1.05e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 33 ILGANGAGKSTLLAAISGYL---------PVGGDILI---GGRSIRQYhIAQLSQQR---AYLSQLVSYIPilKVFQ-YV 96
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELipnlgdyeeEPSWDEVLkrfRGTELQNY-FKKLYNGEikvVHKPQYVDLIP--KVFKgKV 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 97 G--LfspNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQ 171
Cdd:PRK13409 181 RelL---KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPTSYLDIRQ 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-221 |
1.13e-14 |
|
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: 71.10 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAYlsqlvsyipilkVFQYV 96
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQKGQILIDGIDIRDISRKSLRSMIGV------------VLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSpNTVF----------SAGVFERLCSDFQLTSLLSKPIN-----------QLSGGEWQRVRIVAAFLQvwdkqqcEG 155
Cdd:cd03254 87 FLFS-GTIMenirlgrpnaTDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLR-------DP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 156 KFILLDEPTNNLD-----IIQQAML----DKwikyfcdclgTVIMSGHDLShSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:cd03254 159 KILILDEATSNIDtetekLIQEALEklmkGR----------TSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHD 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-206 |
1.16e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 24 QVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsirQYHIAQLSQQR--AYLSQLVSYIPILKVFQYVGL-F 99
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLtPASGSLTLNG----QDHTTTPPSRRpvSMLFQENNLFSHLTVAQNIGLgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 100 SPNTVFSA---GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdKQQcegKFILLDEPTNNLD-IIQQAML 175
Cdd:PRK10771 97 NPGLKLNAaqrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV----REQ---PILLLDEPFSALDpALRQEML 169
|
170 180 190
....*....|....*....|....*....|..
gi 2697035156 176 dKWIKYFCDCLG-TVIMsghdLSHSYKNASCI 206
Cdd:PRK10771 170 -TLVSQVCQERQlTLLM----VSHSLEDAARI 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-218 |
1.49e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.47 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 21 VSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsIRQYHIAQLSQQR-AYLSQLVSYIPILKVFQYVGL 98
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDG--FDVVKEPAEARRRlGFVSDSTGLYDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 FS-----PNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQA 173
Cdd:cd03266 102 FAglyglKGDELTARL-EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH-------DPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2697035156 174 MLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-215 |
1.76e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQ------QRaylSQLVSYIPILKV 92
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvPTSGEVRVLGYVPFKRRKEFARRigvvfgQR---SQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQyvgLFS-----PNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGewQRVR--IVAAFLQvwdkqqcEGKFILLDEPTN 165
Cdd:COG4586 117 FR---LLKaiyriPDAEYKKRL-DELVELLDLGELLDTPVRQLSLG--QRMRceLAAALLH-------RPKILFLDEPTI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2697035156 166 NLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGtTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-221 |
2.14e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRsirQYHIAQLSQQRAyls 81
Cdd:COG1118 3 IEVRNISKrfgSFTLLdDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRIVLNGR---DLFTNLPPRERR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlVSYipilkVFQYVGLFsPN-TVF---SAG--------------VfERLCSDFQLTSLLSKPINQLSGGEWQRV---RI 140
Cdd:COG1118 77 --VGF-----VFQHYALF-PHmTVAeniAFGlrvrppskaeirarV-EELLELVQLEGLADRYPSQLSGGQRQRValaRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 141 VAAflqvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKW-IKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGK 219
Cdd:COG1118 148 LAV----------EPEVLLLDEPFGALDAKVRKELRRWlRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
..
gi 2697035156 220 PE 221
Cdd:COG1118 218 PD 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-233 |
3.97e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 33 ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSYIPILKVFQYVGLFSPNTVFSAGVF- 110
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQpPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFg 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 111 -------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVaafLQVWDKQQCegkfILLDEPTNNLDIIQQAMLDKWIKYFC 183
Cdd:PRK10575 122 aadrekvEEAISLVGLKPLAHRLVDSLSGGERQRAWIA---MLVAQDSRC----LLLDEPTSALDIAHQVDVLALVHRLS 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2697035156 184 DCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIF 233
Cdd:PRK10575 195 QERGlTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-182 |
4.37e-14 |
|
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: 69.74 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSirqyhiaqlsqqraylsqlVSYIPilkvfQYVGLFSPNTV-- 104
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLkPDEGDIEIELDT-------------------VSYKP-----QYIKADYEGTVrd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 105 FSAGVFERLCSD----------FQLTSLLSKPINQLSGGEWQRVRIVAAFLQVWDkqqcegkFILLDEPTNNLDIIQQAM 174
Cdd:cd03237 81 LLSSITKDFYTHpyfkteiakpLQIEQILDREVPELSGGELQRVAIAACLSKDAD-------IYLLDEPSAYLDVEQRLM 153
|
....*...
gi 2697035156 175 LDKWIKYF 182
Cdd:cd03237 154 ASKVIRRF 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-164 |
4.83e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 69.00 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRqyhiAQLSQQRAYLSqlVSYIPilkvfQYV 96
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDIT----GLPPHERARAG--IGYVP-----EGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTV---FSAGVFERLCSDFQ------------LTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLD 161
Cdd:cd03224 85 RIFPELTVeenLLLGAYARRRAKRKarlervyelfprLKERRKQLAGTLSGGEQQMLAIARALMS-------RPKLLLLD 157
|
...
gi 2697035156 162 EPT 164
Cdd:cd03224 158 EPS 160
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-219 |
5.11e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIrqyhiAQLSQQRaylsqlvsyIPILK----- 91
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDL-----SRLKRRE---------IPYLRrrigv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 VFQYVGLFSPNTVFS--------AGVFERLCSD--------FQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEG 155
Cdd:COG2884 84 VFQDFRLLPDRTVYEnvalplrvTGKSRKEIRRrvrevldlVGLSDKAKALPHELSGGEQQRVAIARALVN-------RP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 156 KFILLDEPTNNLDiiqQAMLDKWIKYFCD--CLG-TVIMSGHDLS--HSYKnASCIwMIKQGQLVAVGK 219
Cdd:COG2884 157 ELLLADEPTGNLD---PETSWEIMELLEEinRRGtTVLIATHDLElvDRMP-KRVL-ELEDGRLVRDEA 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-195 |
5.18e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 9 IKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILI----------------GGRSIRQ 67
Cdd:COG0488 1 LENLSksFGGRPLldDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELePDSGEVSIpkglrigylpqeppldDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 68 Y------HIAQLSQQRAYLSQLVS--------YIPILKVFQYVGLFS-PNTVfsagvfERLCSDFQLT-SLLSKPINQLS 131
Cdd:COG0488 81 TvldgdaELRALEAELEELEAKLAepdedlerLAELQEEFEALGGWEaEARA------EEILSGLGFPeEDLDRPVSELS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 132 GGEWQRVRIVAAFLQVWDkqqcegkFILLDEPTNNLDIIQQAMLDKWIKYFcdcLGTVIMSGHD 195
Cdd:COG0488 155 GGWRRRVALARALLSEPD-------LLLLDEPTNHLDLESIEWLEEFLKNY---PGTVLVVSHD 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-219 |
7.32e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI---DTRLVN-VSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLsqqrAYL 80
Cdd:COG4152 1 MLELKGLTKrfgDKTAVDdVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEVLWDGEPLDPEDRRRI----GYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 -------------SQLVsYIPILKvfqyvGLfSPNTVFSAGvfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqv 147
Cdd:COG4152 77 peerglypkmkvgEQLV-YLARLK-----GL-SKAEAKRRA--DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL-- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 148 wdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHsyknAS--C--IWMIKQGQLVAVGK 219
Cdd:COG4152 146 -----HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMEL----VEelCdrIVIINKGRKVLSGS 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-229 |
7.52e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:PRK11174 350 IEAEDLEIlspdGKTLAgPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QlvsyIPIL---KVFQYVGLFSPN--------TVFSAGVferlcSDF--QLTSLLSKPINQ----LSGGEWQRVRIVAAF 144
Cdd:PRK11174 430 Q----NPQLphgTLRDNVLLGNPDasdeqlqqALENAWV-----SEFlpLLPQGLDTPIGDqaagLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 145 LQvwdkqqcEGKFILLDEPTNNLDI---------IQQAMLDKwikyfcdclgTVIMSGHDLShSYKNASCIWMIKQGQLV 215
Cdd:PRK11174 501 LQ-------PCQLLLLDEPTASLDAhseqlvmqaLNAASRRQ----------TTLMVTHQLE-DLAQWDQIWVMQDGQIV 562
|
250
....*....|....
gi 2697035156 216 AVGKPECIMTEKNL 229
Cdd:PRK11174 563 QQGDYAELSQAGGL 576
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-168 |
9.17e-14 |
|
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: 68.30 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiaqlsQQRAYLSQLVSYIP-------ILK 91
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYINGYSIR--------TDRKAARQSLGYCPqfdalfdELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 VFQYVGLFS-----PNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNN 166
Cdd:cd03263 92 VREHLRFYArlkglPKSEIKEEV-ELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG-------GPSVLLLDEPTSG 163
|
..
gi 2697035156 167 LD 168
Cdd:cd03263 164 LD 165
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-168 |
1.02e-13 |
|
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: 68.38 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNIT--------IDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHIAQLSQQ 76
Cdd:cd03258 1 MIELKNVSkvfgdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 77 RaylsQLVSYIpilkvFQYVGLFSPNTVFS--------AGVfERLCSDFQLTSLL----------SKPiNQLSGGEWQRV 138
Cdd:cd03258 81 R----RRIGMI-----FQHFNLLSSRTVFEnvalpleiAGV-PKAEIEERVLELLelvgledkadAYP-AQLSGGQKQRV 149
|
170 180 190
....*....|....*....|....*....|
gi 2697035156 139 RIVAAFlqvwdkqQCEGKFILLDEPTNNLD 168
Cdd:cd03258 150 GIARAL-------ANNPKVLLCDEATSALD 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-197 |
1.05e-13 |
|
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: 68.27 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiaQLSQQRAYLSQLVSYIPILKVFQYVgL 98
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTSGEVLVDGEPVT-----GPGPDRGYVFQQDALLPWLTVLDNV-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 FSPNTVFSAG-----VFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD----- 168
Cdd:cd03293 96 LGLELQGVPKaeareRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV-------DPDVLLLDEPFSALDaltre 168
|
170 180
....*....|....*....|....*....
gi 2697035156 169 IIQQAMLDKWIKYfcdcLGTVIMSGHDLS 197
Cdd:cd03293 169 QLQEELLDIWRET----GKTVLLVTHDID 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-218 |
1.83e-13 |
|
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: 67.28 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRsirqyhiaqlsqqrayls 81
Cdd:cd03301 1 VELENVTKrfgnVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEEPTSGRIYIGGR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qLVSYIP-----ILKVFQYVGLFSPNTVFSAGVF----------------ERLCSDFQLTSLLSKPINQLSGGEWQRVRI 140
Cdd:cd03301 63 -DVTDLPpkdrdIAMVFQNYALYPHMTVYDNIAFglklrkvpkdeidervREVAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 141 VAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03301 142 GRAIVR-------EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGtTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-196 |
2.46e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL-PVGGDILIggrSIRqyhiaqlsqqraylsqlVSYIPilkvfQYVGLFSPNTV-- 104
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDP---ELK-----------------ISYKP-----QYIKPDYDGTVed 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 105 FSAGVFERLCSDF---------QLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAML 175
Cdd:PRK13409 420 LLRSITDDLGSSYykseiikplQLERLLDKNVKDLSGGELQRVAIAACLSR-------DADLYLLDEPSAHLDVEQRLAV 492
|
170 180
....*....|....*....|..
gi 2697035156 176 DKWIKYFCDCLG-TVIMSGHDL 196
Cdd:PRK13409 493 AKAIRRIAEEREaTALVVDHDI 514
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-221 |
3.82e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP----VGGDILIGGRSIRQYHIAQLSqqrAYLSQLVSYIPILKVF 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkGSGSVLLNGMPIDAKEMRAIS---AYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVgLFS-----PNTVFSAGVFERLCSDFQLTSLLS---------KPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFIL 159
Cdd:TIGR00955 118 EHL-MFQahlrmPRRVTKKEKRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLT-------DPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 160 LDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHD-LSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-223 |
4.32e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSirqyhiaqLSQQRAYL 80
Cdd:PRK11607 19 LLEIRNLTksFDGQHAvdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVD--------LSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SqlvsyiPILKVFQYVGLFSPNTVFSAGVF----ERLCSD---FQLTSLLS----------KPiNQLSGGEWQRVRIVAA 143
Cdd:PRK11607 91 R------PINMMFQSYALFPHMTVEQNIAFglkqDKLPKAeiaSRVNEMLGlvhmqefakrKP-HQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 144 FLQvwdkqqcEGKFILLDEPTNNLDiiqQAMLDKWIKYFCDCL----GTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGK 219
Cdd:PRK11607 164 LAK-------RPKLLLLDEPMGALD---KKLRDRMQLEVVDILervgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....
gi 2697035156 220 PECI 223
Cdd:PRK11607 234 PEEI 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-221 |
4.74e-13 |
|
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: 66.44 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG------YLPVGGDILIGGRSIRQYHIAQLSQQ 76
Cdd:cd03260 1 IELRDLNVyygdKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 77 RAylsqlvsyipILKVFQyvglfSPNtVFSAGVFE--------RLCSDFQLTS-----LLSK-----------PINQLSG 132
Cdd:cd03260 81 RR----------VGMVFQ-----KPN-PFPGSIYDnvayglrlHGIKLKEELDerveeALRKaalwdevkdrlHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 133 GEWQRVRIVAAfLQVwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLgTVIMSGHDLSHSYKNASCIWMIKQG 212
Cdd:cd03260 145 GQQQRLCLARA-LAN------EPEVLLLDEPTSALDPISTAKIEELIAELKKEY-TIVIVTHNMQQAARVADRTAFLLNG 216
|
....*....
gi 2697035156 213 QLVAVGKPE 221
Cdd:cd03260 217 RLVEFGPTE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
6.84e-13 |
|
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: 65.85 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI---DTRLVN-VSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyHIAQLSQQRAYLS 81
Cdd:cd03265 1 IEVENLVKkygDFEAVRgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKVFQYVGLFS-----PNTVFSAGVfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGK 156
Cdd:cd03265 80 QDLSVDDELTGWENLYIHArlygvPGAERRERI-DELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-------RPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 157 FILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-196 |
6.87e-13 |
|
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: 67.89 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 33 ILGANGAGKSTLLAAISGYL---------PVGGDILI----GgrSIRQYHIAQLSQQR---AYLSQLVSYIPilKVFQyv 96
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELkpnlgdydeEPSWDEVLkrfrG--TELQDYFKKLANGEikvAHKPQYVDLIP--KVFK-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspNTVFSA-------GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDI 169
Cdd:COG1245 178 -----GTVRELlekvderGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*..
gi 2697035156 170 IQQAMLDKWIKYFCDCLGTVIMSGHDL 196
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-168 |
7.37e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITIDTR----LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQyHIAQLSQQRAYL 80
Cdd:PRK13540 1 MLDVIELDFDYHdqplLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVSYIPILKVFQYVgLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVrivaAFLQVWdkqQCEGKFILL 160
Cdd:PRK13540 80 GHRSGINPYLTLRENC-LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQV----ALLRLW---MSKAKLWLL 151
|
....*...
gi 2697035156 161 DEPTNNLD 168
Cdd:PRK13540 152 DEPLVALD 159
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-233 |
7.96e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 16 TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSIRQyhiAQLSQQRAYLSQ----------LV 84
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAsGKISILGQPTRQ---ALQKNLVAYVPQseevdwsfpvLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 85 SYIPILKVFQYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ-------QGQVILLDEPF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKqGQLVAVGKPECIMTEKNLSDIF 233
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-197 |
8.02e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.24 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL----------PVGGDIliggrsIRQYHIAQLSQqraYLSQLVS--YIPILKVfQY 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddpPDWDEI------LDEFRGSELQN---YFTKLLEgdVKVIVKP-QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFsPNTVFSA-----------GVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:cd03236 96 VDLI-PKAVKGKvgellkkkderGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR-------DADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLS 197
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
18-197 |
9.75e-13 |
|
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: 65.35 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYH---IAQLSQQraylsqlvsyipILKVF 93
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALtPSRGQVRIAGEDVNRLRgrqLPLLRRR------------IGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLFSPNTVFS--AGVFE--RLCSDF---------QLTSLLSK----PInQLSGGEWQRVRIVAAFLQvwdkqqcEGK 156
Cdd:TIGR02673 86 QDFRLLPDRTVYEnvALPLEvrGKKEREiqrrvgaalRQVGLEHKadafPE-QLSGGEQQRVAIARAIVN-------SPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2697035156 157 FILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLS 197
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLS 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-218 |
1.23e-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: 64.49 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP---VGGDILIGGRSIRQYHIAQLSqqrAYLSQLVSYIPILKVFQ 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglgVSGEVLINGRPLDKRSFRKII---GYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 YVglfspntVFSAGvferlcsdfqltsllskpINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAM 174
Cdd:cd03213 102 TL-------MFAAK------------------LRGLSGGERKRVSIALELVS-------NPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2697035156 175 LDKWIKYFCDCLGTVIMSGHDLSHS-YKNASCIWMIKQGQLVAVG 218
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEiFELFDKLLLLSQGRVIYFG 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-176 |
1.24e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTRLV---NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-----GDILIGGR-----SIRQYHIAQL 73
Cdd:PRK10418 5 IELRNIALQAAQPlvhGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtaGRVLLDGKpvapcALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 74 SQQ-----------RAY-------LSQLVSYIPILKVFQYVGLFSPNTVFSAGVFErlcsdfqltsllskpinqLSGGEW 135
Cdd:PRK10418 85 MQNprsafnplhtmHTHaretclaLGKPADDATLTAALEAVGLENAARVLKLYPFE------------------MSGGML 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2697035156 136 QRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLDIIQQA-MLD 176
Cdd:PRK10418 147 QRMMIALALL-------CEAPFIIADEPTTDLDVVAQArILD 181
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-168 |
1.33e-12 |
|
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: 65.15 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 12 ITIdtrLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSirqyhIAQLSQ-QRAYL-SQLVSY-- 86
Cdd:COG4181 25 LTI---LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQD-----LFALDEdARARLrARHVGFvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 87 -----IPILKVFQYVGLfsPNTVFSAG-VFERlcsdfqLTSLLSK----------PiNQLSGGEWQRVRIVAAFLqvwdk 150
Cdd:COG4181 97 qsfqlLPTLTALENVML--PLELAGRRdARAR------ARALLERvglghrldhyP-AQLSGGEQQRVALARAFA----- 162
|
170
....*....|....*...
gi 2697035156 151 qqCEGKFILLDEPTNNLD 168
Cdd:COG4181 163 --TEPAILFADEPTGNLD 178
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
1.71e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNI-------TIDTR--LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSirqyhIAQLSQ 75
Cdd:COG1101 1 MLELKNLsktfnpgTVNEKraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILIDGKD-----VTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 -QRAylsQLVSyipilKVFQ--YVGLfSPN-TV---------------FSAGV-------FERLCSDFQLtSL---LSKP 126
Cdd:COG1101 76 yKRA---KYIG-----RVFQdpMMGT-APSmTIeenlalayrrgkrrgLRRGLtkkrrelFRELLATLGL-GLenrLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 127 INQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD-------------IIQQAMLdkwikyfcdclgTVIMSG 193
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLT-------KPKLLLLDEHTAALDpktaalvleltekIVEENNL------------TTLMVT 206
|
250 260
....*....|....*....|..
gi 2697035156 194 HDLSHSYKNASCIWMIKQGQLV 215
Cdd:COG1101 207 HNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-195 |
2.16e-12 |
|
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: 64.35 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYH---IAQLSQQRAYLSQLVSYIPILKVF 93
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGlFSPNTVFSAG--VFERLCSDFQLTSLLSK----PiNQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNL 167
Cdd:cd03292 97 ENVA-FALEVTGVPPreIRKRVPAALELVGLSHKhralP-AELSGGEQQRVAIARAIVN-------SPTILIADEPTGNL 167
|
170 180
....*....|....*....|....*...
gi 2697035156 168 DIIQQAMLDKWIKYFCDCLGTVIMSGHD 195
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-229 |
2.46e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.74 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQyhiaQLSQ 75
Cdd:PRK09452 9 SSLSPLVELRGISksFDGKEVisNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQDITH----VPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRaylsqlvsyiPILKVFQYVGLFSPNTVF-----------------SAGVFERLcSDFQLTSLLSKPINQLSGGEWQRV 138
Cdd:PRK09452 85 NR----------HVNTVFQSYALFPHMTVFenvafglrmqktpaaeiTPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 RIVAAflqVWDKQqcegKFILLDEPTNNLDI-IQQAMLDKwIKYFCDCLG-TVIMSGHD----LSHSYKnascIWMIKQG 212
Cdd:PRK09452 154 AIARA---VVNKP----KVLLLDESLSALDYkLRKQMQNE-LKALQRKLGiTFVFVTHDqeeaLTMSDR----IVVMRDG 221
|
250
....*....|....*...
gi 2697035156 213 QLVAVGKPECIMTE-KNL 229
Cdd:PRK09452 222 RIEQDGTPREIYEEpKNL 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-168 |
3.69e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSirqyhIAQLS-QQRAy 79
Cdd:COG3842 5 ALELENVSKrygDVTALdDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILLDGRD-----VTGLPpEKRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsqlVSYipilkVFQ-YvGLFsPN-TVF--------SAGV--------FERLCSDFQLTSLLSKPINQLSGGEWQRV--- 138
Cdd:COG3842 79 ----VGM-----VFQdY-ALF-PHlTVAenvafglrMRGVpkaeirarVAELLELVGLEGLADRYPHQLSGGQQQRVala 147
|
170 180 190
....*....|....*....|....*....|
gi 2697035156 139 RIVAaflqvwdkqqCEGKFILLDEPTNNLD 168
Cdd:COG3842 148 RALA----------PEPRVLLLDEPLSALD 167
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.78e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENklIIDIKNITI----DTR-LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLS 74
Cdd:PRK13647 1 MDN--IIEVEDLHFrykdGTKaLKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 75 QQRAYlsqlvsyipilkVFQyvglfSP-NTVFSAGVFE---------RLCSD------------FQLTSLLSKPINQLSG 132
Cdd:PRK13647 79 SKVGL------------VFQ-----DPdDQVFSSTVWDdvafgpvnmGLDKDeverrveealkaVRMWDFRDKPPYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 133 GEWQRVRIvAAFLQVwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQG 212
Cdd:PRK13647 142 GQKKRVAI-AGVLAM------DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
250
....*....|....*..
gi 2697035156 213 QLVAVGKPEcIMTEKNL 229
Cdd:PRK13647 215 RVLAEGDKS-LLTDEDI 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-219 |
4.26e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 64.02 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRsirqyHIAQLSQQRAYLSQLVSYIPILKVFQYV 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGK-----QITEPGPDRMVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLfSPNTVFS-------AGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFlqvwdkqQCEGKFILLDEPTNNLDI 169
Cdd:TIGR01184 76 AL-AVDRVLPdlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARAL-------SIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 170 I-----QQAMLDKWIKYFCdclgTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGK 219
Cdd:TIGR01184 148 LtrgnlQEELMQIWEEHRV----TVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-229 |
4.26e-12 |
|
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: 63.79 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAI-SGYLPVGGDILIGGRSIRQYhiaqlsqQRAYLSQLVSYIPilkvfQYV 96
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYDVSSGSILIDGQDIREV-------TLDSLRRAIGVVP-----QDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSpNTVFSAGVFERL-CSDFQL----------TSLLSKPIN----------QLSGGEWQRVRIVAAFLQvwdkqqcEG 155
Cdd:cd03253 85 VLFN-DTIGYNIRYGRPdATDEEVieaakaaqihDKIMRFPDGydtivgerglKLSGGEKQRVAIARAILK-------NP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 156 KFILLDEPTNNLDI-----IQQAMLDKwikyfcdCLG-TVIMSGHDLShSYKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:cd03253 157 PILLLDEATSALDThtereIQAALRDV-------SKGrTTIVIAHRLS-TIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-229 |
4.49e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 30 QIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLsqqRAYLSqLVSYIPILKVF-----QYVGlFSPNT 103
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGEPITKENIREV---RKFVG-LVFQNPDDQIFsptveQDIA-FGPIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 104 VF--SAGVFERLCSDFQ---LTSLLSKPINQLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDEPTNNLDIIQQAMLDKW 178
Cdd:PRK13652 107 LGldEETVAHRVSSALHmlgLEELRDRVPHHLSGGEKKRVAI-AGVIAM------EPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 179 IKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:PRK13652 180 LNDLPETYGmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-180 |
5.01e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.11 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyhiaqLSQQRAYlsqlvsyipilkVFQYV 96
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLaPSSGEITLDGVPVTG-----PGADRGV------------VFQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFsP------NTVFS---AGV--------FERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFlqvwdkqQCEGKFIL 159
Cdd:COG4525 86 ALL-PwlnvldNVAFGlrlRGVpkaerrarAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL-------AADPRFLL 157
|
170 180
....*....|....*....|....*.
gi 2697035156 160 LDEPTNNLDI-----IQQAMLDKWIK 180
Cdd:COG4525 158 MDEPFGALDAltreqMQELLLDVWQR 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-229 |
5.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqYHIAQLsqqraylsqlvsyipiLKVFQYV 96
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPIK-YDKKSL----------------LEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 G---------LFSPnTVFSAGVF-------------ERLCSDFQLTSLL---SKPINQLSGGEWQRVRIvAAFLQVwdkq 151
Cdd:PRK13639 81 GivfqnpddqLFAP-TVEEDVAFgplnlglskeeveKRVKEALKAVGMEgfeNKPPHHLSGGQKKRVAI-AGILAM---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 152 qcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:PRK13639 155 --KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-194 |
5.62e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyHIAQLSQQRAYLSQLVSYIPILKVFQyv 96
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDI---DDPDVAEACHYLGHRNAMKPALTVAE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspNTVFSAGVF--------ERLCsDFQLTSLLSKPINQLSGGeWQR----VRIVAAFLQVWdkqqcegkfiLLDEPT 164
Cdd:PRK13539 93 -----NLEFWAAFLggeeldiaAALE-AVGLAPLAHLPFGYLSAG-QKRrvalARLLVSNRPIW----------ILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDCLGTVIMSGH 194
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-168 |
6.61e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 64.69 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsirqYHIAQLSQQRayLSQLVSYIPilkvfQYV 96
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQGEVTLDG-----VPVSSLDQDE--VRRRVSVCA-----QDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLfspntvFSAGVFERL------CSDFQLTSLLSK-----PINQL---------------SGGEWQRVRIVAAFLQvwdk 150
Cdd:TIGR02868 419 HL------FDTTVRENLrlarpdATDEELWAALERvgladWLRALpdgldtvlgeggarlSGGERQRLALARALLA---- 488
|
170
....*....|....*...
gi 2697035156 151 qqcEGKFILLDEPTNNLD 168
Cdd:TIGR02868 489 ---DAPILLLDEPTEHLD 503
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-168 |
8.29e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNI--TIDTR--LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQ 75
Cdd:PRK10247 2 QENSPLLQLQNVgyLAGDAkiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QraylsqlVSYipilkVFQYVGLFSpNTVFSAGVF-----------ERLCSD---FQL-TSLLSKPINQLSGGEWQRVRI 140
Cdd:PRK10247 82 Q-------VSY-----CAQTPTLFG-DTVYDNLIFpwqirnqqpdpAIFLDDlerFALpDTILTKNIAELSGGEKQRISL 148
|
170 180
....*....|....*....|....*...
gi 2697035156 141 VAAFlqvwdkqQCEGKFILLDEPTNNLD 168
Cdd:PRK10247 149 IRNL-------QFMPKVLLLDEITSALD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-195 |
1.27e-11 |
|
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: 64.19 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 5 LIIDIKNIT--IDTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGgrsiRQYHIAQLSQQRAY 79
Cdd:TIGR03719 321 KVIEAENLTkaFGDKLLidDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIG----ETVKLAYVDQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 LS------QLVS----YIPILKV----FQYVGLFSpntvFSAGvferlcsDFQltsllsKPINQLSGGEWQRVRIvAAFL 145
Cdd:TIGR03719 397 LDpnktvwEEISggldIIKLGKReipsRAYVGRFN----FKGS-------DQQ------KKVGQLSGGERNRVHL-AKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 146 QVwdkqqcEGKFILLDEPTNNLDI-----IQQAMLDkwikyFCDClgTVIMSgHD 195
Cdd:TIGR03719 459 KS------GGNVLLLDEPTNDLDVetlraLEEALLN-----FAGC--AVVIS-HD 499
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
1.73e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaqlSQQRAYLSQLVSYIPIlkVFQyvglfSP-NTVF 105
Cdd:PRK13636 32 GEVTAILGGNGAGKSTLFQNLNGILkPSSGRILFDGKPI--------DYSRKGLMKLRESVGM--VFQ-----DPdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 106 SAGVFE---------------------RLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:PRK13636 97 SASVYQdvsfgavnlklpedevrkrvdNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM-------EPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGlTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-163 |
1.77e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 17 RLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIaqlsQQRAYLSqlVSYIP----- 88
Cdd:COG1137 16 RTVvkDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLPM----HKRARLG--IGYLPqeasi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 89 ---------ILKVFQYVGLfspntvfSAGV----FERLCSDFQLTSLLSKPINQLSGGEWQRV---RIVAAflqvwdkqq 152
Cdd:COG1137 90 frkltvednILAVLELRKL-------SKKEreerLEELLEEFGITHLRKSKAYSLSGGERRRVeiaRALAT--------- 153
|
170
....*....|.
gi 2697035156 153 cEGKFILLDEP 163
Cdd:COG1137 154 -NPKFILLDEP 163
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-221 |
1.99e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHiaqlSQQRAyls 81
Cdd:PRK10851 3 IEIANIKKsfgrTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVSRLH----ARDRK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 qlVSYipilkVFQYVGLFSPNTVFSAGVF--------ER------------LCSDFQLTSLLSKPINQLSGGEWQRVRIV 141
Cdd:PRK10851 76 --VGF-----VFQHYALFRHMTVFDNIAFgltvlprrERpnaaaikakvtqLLEMVQLAHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 142 AAfLQVwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:PRK10851 149 RA-LAV------EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
.
gi 2697035156 221 E 221
Cdd:PRK10851 222 D 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-194 |
2.17e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.35 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 21 VSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSirqyhiaqLSQQRAYLSQLVSYI---PILKvfqyv 96
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGP--------LDFQRDSIARGLLYLghaPGIK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSP--NTVF------SAGVFERLcSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQ---VWdkqqcegkfiLLDEPTN 165
Cdd:cd03231 86 TTLSVleNLRFwhadhsDEQVEEAL-ARVGLNGFEDRPVAQLSAGQQRRVALARLLLSgrpLW----------ILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 2697035156 166 NLDIIQQAMLDKWIKYFCDCLGTVIMSGH 194
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
2.18e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKlIIDIKNITI------DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQL 73
Cdd:PRK13635 1 MKEE-IIRVEHISFrypdaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 74 SQQraylsqlvsyipILKVF-----QYVGlfspNTVFSAGVF-------------ERLCSDFQL---TSLLSKPINQLSG 132
Cdd:PRK13635 80 RRQ------------VGMVFqnpdnQFVG----ATVQDDVAFglenigvpreemvERVDQALRQvgmEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 133 GEWQRVRI---VAAflqvwdkqqcEGKFILLDEPTNNLDII-QQAMLDKwIKYFCDCLG-TVIMSGHDLSHSYKnASCIW 207
Cdd:PRK13635 144 GQKQRVAIagvLAL----------QPDIIILDEATSMLDPRgRREVLET-VRQLKEQKGiTVLSITHDLDEAAQ-ADRVI 211
|
250
....*....|....*.
gi 2697035156 208 MIKQGQLVAVGKPECI 223
Cdd:PRK13635 212 VMNKGEILEEGTPEEI 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-194 |
2.32e-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: 61.22 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHiAQLSQQRAYLSQLVSYIPILKVFQyvgl 98
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPELSALE---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 fspNTVFsagvFERLCSDFQ-----------LTSLLSKPINQLSGGEWQRVrivaAFLQVWDKQQcegKFILLDEPTNNL 167
Cdd:TIGR01189 93 ---NLHF----WAAIHGGAQrtiedalaavgLTGFEDLPAAQLSAGQQRRL----ALARLWLSRR---PLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 2697035156 168 DIIQQAMLDKWIKYFCDCLGTVIMSGH 194
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-196 |
2.61e-11 |
|
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: 63.26 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRsirqyhiaqlsqqraylsqlVSYIPilkvfQYVGLFSPNTV-- 104
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLK--------------------ISYKP-----QYISPDYDGTVee 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 105 --------------FSAGVFERLcsdfQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDII 170
Cdd:COG1245 421 flrsantddfgssyYKTEIIKPL----GLEKLLDKNVKDLSGGELQRVAIAACLSR-------DADLYLLDEPSAHLDVE 489
|
170 180
....*....|....*....|....*..
gi 2697035156 171 QQAMLDKWIKYFCDCLG-TVIMSGHDL 196
Cdd:COG1245 490 QRLAVAKAIRRFAENRGkTAMVVDHDI 516
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-225 |
2.95e-11 |
|
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: 61.30 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEqIH-ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSI---RQYHIAQLSQQRAYlsQLVSYIPILKVFQ 94
Cdd:cd03219 18 DVSFSVRPGE-IHgLIGPNGAGKTTLFNLISGFLrPTSGSVLFDGEDItglPPHEIARLGIGRTF--QIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 --YVGLF--SPNTVFSAGVF----------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILL 160
Cdd:cd03219 95 nvMVAAQarTGSGLLLARARreereareraEELLERVGLADLADRPAGELSYGQQRRLEIARALAT-------DPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 161 DEPTNNLDIIQQAMLDKWIKYFCDcLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRE-RGiTVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-220 |
3.24e-11 |
|
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: 60.97 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTR------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQray 79
Cdd:cd03244 3 IEFKNVSLRYRpnlppvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsqlVSYIPilkvfQYVGLFS--------PNTVFSAGVFERLCSDFQLTSLLSKPI-----------NQLSGGEWQRVRI 140
Cdd:cd03244 80 ----ISIIP-----QDPVLFSgtirsnldPFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 141 VAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIK-YFCDClgTVIMSGHDLsHSYKNASCIWMIKQGQLVAVGK 219
Cdd:cd03244 151 ARALLR-------KSKILVLDEATASVDPETDALIQKTIReAFKDC--TVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
.
gi 2697035156 220 P 220
Cdd:cd03244 221 P 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-164 |
3.43e-11 |
|
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: 61.15 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQ---YHIAQLSqqraylsqlVSYIPilkvfQY 95
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIRFDGEDITGlppHRIARLG---------IGYVP-----EG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFSPNTV---------------FSAGVFERLCSDF-QLTSLLSKPINQLSGGEwqrvrivaaflqvwdkQQ------- 152
Cdd:COG0410 87 RRIFPSLTVeenlllgayarrdraEVRADLERVYELFpRLKERRRQRAGTLSGGE----------------QQmlaigra 150
|
170
....*....|....
gi 2697035156 153 --CEGKFILLDEPT 164
Cdd:COG0410 151 lmSRPKLLLLDEPS 164
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-223 |
4.79e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRsirqyHIAQLSqqraylSQLVSYIPILKVFQYVGL 98
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTGGTILLRGQ-----HIEGLP------GHQIARMGVVRTFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 FSPNTV---------------FSAGVF--------ERLCSDFQ--------LTSLLSKPINQLSGGEWQRVRIVaaflqv 147
Cdd:PRK11300 92 FREMTVienllvaqhqqlktgLFSGLLktpafrraESEALDRAatwlervgLLEHANRQAGNLAYGQQRRLEIA------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 148 wdkqQC---EGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECI 223
Cdd:PRK11300 166 ----RCmvtQPEILMLDEPAAGLNPKETKELDELIAELRNEHNvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-224 |
8.56e-11 |
|
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: 60.44 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEqIH-ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSI---RQYHIAQLSQQRAYlsQLVSYIPILKVFQ 94
Cdd:COG0411 22 DVSLEVERGE-IVgLIGPNGAGKTTLFNLITGFYrPTSGRILFDGRDItglPPHRIARLGIARTF--QNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 YV---GLFSPNTVFSAGVF----------------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEG 155
Cdd:COG0411 99 NVlvaAHARLGRGLLAALLrlprarreereareraEELLERVGLADRADEPAGNLSYGQQRRLEIARALA-------TEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 156 KFILLDEPT---NNLDIiqQAMLDkWIKYFCDCLG-TVIMSGHD------LSHSyknascIWMIKQGQLVAVGKPECIM 224
Cdd:COG0411 172 KLLLLDEPAaglNPEET--EELAE-LIRRLRDERGiTILLIEHDmdlvmgLADR------IVVLDFGRVIAEGTPAEVR 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-218 |
9.26e-11 |
|
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: 59.54 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrQYHIAQLSQqrayLSQLVSY---IPILKVF 93
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGKSY-QKNIEALRR----IGALIEApgfYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLFSPNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQA 173
Cdd:cd03268 91 ENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLG-------NPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2697035156 174 MLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG 218
Cdd:cd03268 164 ELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-226 |
1.06e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 61.21 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI------DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYhiaqlsqQRAY 79
Cdd:TIGR01842 317 LSVENVTIvppggkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiWPPTSGSVRLDGADLKQW-------DRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 LSQLVSYIPilkvfQYVGLFS---------------PNTVFSA----GVFE---RLCSDFQlTSLLSKPINqLSGGEWQR 137
Cdd:TIGR01842 390 FGKHIGYLP-----QDVELFPgtvaeniarfgenadPEKIIEAaklaGVHElilRLPDGYD-TVIGPGGAT-LSGGQRQR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 138 VRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLShSYKNASCIWMIKQGQLVAV 217
Cdd:TIGR01842 463 IALARALYG-------DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARF 534
|
....*....
gi 2697035156 218 GKPECIMTE 226
Cdd:TIGR01842 535 GERDEVLAK 543
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-218 |
1.36e-10 |
|
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: 59.55 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI------DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAY 79
Cdd:cd03251 1 VEFKNVTFrypgdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 LSQlvsyipilKVFqyvgLFSpNTVFSAGVFERL---------------CSDF--QLTSLLSKPIN----QLSGGEWQRV 138
Cdd:cd03251 81 VSQ--------DVF----LFN-DTVAENIAYGRPgatreeveeaaraanAHEFimELPEGYDTVIGergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 RIVAAFLQvwdkqqcEGKFILLDEPTNNLD-----IIQQAmLDKWIKYfcdclGTVIMSGHDLShSYKNASCIWMIKQGQ 213
Cdd:cd03251 148 AIARALLK-------DPPILILDEATSALDteserLVQAA-LERLMKN-----RTTFVIAHRLS-TIENADRIVVLEDGK 213
|
....*
gi 2697035156 214 LVAVG 218
Cdd:cd03251 214 IVERG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
1.37e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.00 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 3 NKLIIDIKNITIDTR------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaqlsq 75
Cdd:PRK13632 4 KSVMIKVENVSFSYPnsennaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKIDGITI---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQLVSYIPIlkVF-----QYVGL-------FS-PNTVFSAGVFERLCSDF----QLTSLLSKPINQLSGGEWQRV 138
Cdd:PRK13632 74 SKENLKEIRKKIGI--IFqnpdnQFIGAtveddiaFGlENKKVPPKKMKDIIDDLakkvGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 RIvAAFLQVwdkqqcEGKFILLDEPTnnldiiqqAMLD----KWIKYFCDCL-----GTVIMSGHDLSHSYKNASCIWMi 209
Cdd:PRK13632 152 AI-ASVLAL------NPEIIIFDEST--------SMLDpkgkREIKKIMVDLrktrkKTLISITHDMDEAILADKVIVF- 215
|
250 260 270
....*....|....*....|....*....|
gi 2697035156 210 KQGQLVAVGKPECIMTEKNlsdiFMSEIKL 239
Cdd:PRK13632 216 SEGKLIAQGKPKEILNNKE----ILEKAKI 241
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-239 |
1.38e-10 |
|
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: 60.14 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT------IDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRqyHIAQLSQQRay 79
Cdd:TIGR04520 1 IEVENVSfsypesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGlLLPTSGKVTVDGLDTL--DEENLWEIR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsQLVSYipilkVF-----QYVGlfspNTV-----FSagvFERLC--------------SDFQLTSLLSKPINQLSGGEW 135
Cdd:TIGR04520 77 --KKVGM-----VFqnpdnQFVG----ATVeddvaFG---LENLGvpreemrkrvdealKLVGMEDFRDREPHLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 136 QRVRIvAAFLQVwdkqqcEGKFILLDEPTnnldiiqqAMLD--------KWIKYFCDCLG-TVIMSGHDLSHSyKNASCI 206
Cdd:TIGR04520 143 QRVAI-AGVLAM------RPDIIILDEAT--------SMLDpkgrkevlETIRKLNKEEGiTVISITHDMEEA-VLADRV 206
|
250 260 270
....*....|....*....|....*....|...
gi 2697035156 207 WMIKQGQLVAVGKPECIMTEKNLsdifMSEIKL 239
Cdd:TIGR04520 207 IVMNKGKIVAEGTPREIFSQVEL----LKEIGL 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-216 |
1.45e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.89 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAaISGYL--PVGGDILIGGRSIRQYHIAQLSQQR----AYLSQLVSYIPILK 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdkPTSGTYRVAGQDVATLDADALAQLRrehfGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 VFQYVGLfsPNTVFSAGVFERLCSDFQLTSLL------SKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTN 165
Cdd:PRK10535 103 AAQNVEV--PAVYAGLERKQRLLRAQELLQRLgledrvEYQPSQLSGGQQQRVSIARALMN-------GGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2697035156 166 NLDIIQQAMLDKWIKYFCDCLGTVIMSGHDlSHSYKNASCIWMIKQGQLVA 216
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-164 |
1.70e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEqIH-ILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQlSQQR--AYLSQLVSYIPILKVFQ- 94
Cdd:COG1129 22 GVSLELRPGE-VHaLLGENGAGKSTLMKILSGvYQPDSGEILLDGEPVRFRSPRD-AQAAgiAIIHQELNLVPNLSVAEn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 -YVGLFSPNTVF---------SAGVFERLCSDFQLTSLLSkpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:COG1129 100 iFLGREPRRGGLidwramrrrARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSR-------DARVLILDEPT 168
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-168 |
1.73e-10 |
|
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: 59.08 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGyL--PVGGDILIGGRSI--RQYHIAQLSQQRAYLSQLVSYIPILKVF 93
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LeePDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLfSPNTVFSAGVFE------RLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNL 167
Cdd:cd03262 95 ENITL-APIKVKGMSKAEaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM-------NPKVMLFDEPTSAL 166
|
.
gi 2697035156 168 D 168
Cdd:cd03262 167 D 167
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-194 |
1.81e-10 |
|
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: 58.69 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEqIH-ILGANGAGKSTLLAAISG---YLPVGGDILIGGRSirqyhIAQLS-QQRAYLSQLVSyipilkv 92
Cdd:cd03217 16 LKGVNLTIKKGE-VHaLMGPNGSGKSTLAKTIMGhpkYEVTEGEILFKGED-----ITDLPpEERARLGIFLA------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYvglfsPNTVfsAGVferlcsdfQLTSLLsKPINQ-LSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQ 171
Cdd:cd03217 83 FQY-----PPEI--PGV--------KNADFL-RYVNEgFSGGEKKRNEILQLLLL-------EPDLAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|...
gi 2697035156 172 QAMLDKWIKYFCDCLGTVIMSGH 194
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITH 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-167 |
2.22e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGeQIHIL-GANGAGKSTLLAAISG-YLPVGGDILIGGRSIR-QYHIAQLSQQRAYLSQLVSYIPILKVFQ 94
Cdd:PRK11288 20 LDDISFDCRAG-QVHALmGENGAGKSTLLKILSGnYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 --YVGLFsPNtvfSAGVFERLCSDFQLTSLLSK---------PINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEP 163
Cdd:PRK11288 99 nlYLGQL-PH---KGGIVNRRLLNYEAREQLEHlgvdidpdtPLKYLSIGQRQMVEIAKALAR-------NARVIAFDEP 167
|
....
gi 2697035156 164 TNNL 167
Cdd:PRK11288 168 TSSL 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-220 |
2.63e-10 |
|
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: 60.41 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 34 LGANGAGKSTLLAAISGYLP-VGGDILIGGRSI-------RQyHIAQLSQQRAYLSQLVSYIPILKVFQYVGLFSPNTVF 105
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPpTSGTVLVGGKDIetnldavRQ-SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 106 SagvFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD-IIQQAMLDKWIKYFCD 184
Cdd:TIGR01257 1041 E---MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG-------DAKVVVLDEPTSGVDpYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....*.
gi 2697035156 185 clGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:TIGR01257 1111 --RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-229 |
4.54e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAylsqLVSYIPIL------KVFQYVGLFS 100
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNlYQPTGGQVLLDGVPLVQYDHHYLHRQVA----LVGQEPVLfsgsvrENIAYGLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 101 PNTVFSAGVFERLCSDF--QLTSLLSKPI----NQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAM 174
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFimEFPNGYDTEVgekgSQLSGGQKQRIAIARALVR-------KPRVLILDEATSALDAECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 175 LDKWikyfcDCLG--TVIMSGHDLsHSYKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:TIGR00958 656 LQES-----RSRAsrTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-226 |
4.62e-10 |
|
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: 59.43 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKN-----ITIDTRLV----NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP---------VGGD--------IL 59
Cdd:TIGR03269 279 IIKVRNvskryISVDRGVVkavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsgevnvrVGDEwvdmtkpgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 60 IGGRSIRqyHIAQLSQQ------RAYLSQLVSYIPILKVFQYVGLFSPNTVFSAGVFERlcsdfQLTSLLSKPINQLSGG 133
Cdd:TIGR03269 359 GRGRAKR--YIGILHQEydlyphRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEE-----KAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 134 EWQRVrivaAFLQVWDKqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQG 212
Cdd:TIGR03269 432 ERHRV----ALAQVLIK---EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEqTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|....
gi 2697035156 213 QLVAVGKPECIMTE 226
Cdd:TIGR03269 505 KIVKIGDPEEIVEE 518
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-227 |
4.98e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNItidtRLVNVSAQVLTGEQIHI--------LGANGAGKSTLLAAISGYLP------VGGDILIGGRSIRQYHIAQ 72
Cdd:PRK14247 4 IEIRDL----KVSFGQVEVLDGVNLEIpdntitalMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 73 LSQQRAYLSQLVSYIPILKVFQYVGL-FSPNTVFS--AGVFERLCSDFQLTSL-------LSKPINQLSGGEWQRVRIVA 142
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALgLKLNRLVKskKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 143 AFlqvwdkqQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLgTVIMSGHDLSHSYKNASCIWMIKQGQLVAVG---- 218
Cdd:PRK14247 160 AL-------AFQPEVLLADEPTANLDPENTAKIESLFLELKKDM-TIVLVTHFPQQAARISDYVAFLYKGQIVEWGptre 231
|
250
....*....|..
gi 2697035156 219 ---KPECIMTEK 227
Cdd:PRK14247 232 vftNPRHELTEK 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-164 |
5.23e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEqIH-ILGANGAGKSTLLAAISG-YLPVGGDILIGGrsiRQYHIAQLSQQRAYlsqlvsyiPILKVFQYVG 97
Cdd:COG3845 23 DVSLTVRPGE-IHaLLGENGAGKSTLMKILYGlYQPDSGEILIDG---KPVRIRSPRDAIAL--------GIGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 LFSPNTVF---------SAGVF----------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFI 158
Cdd:COG3845 91 LVPNLTVAenivlglepTKGGRldrkaarariRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR-------GARIL 163
|
....*.
gi 2697035156 159 LLDEPT 164
Cdd:COG3845 164 ILDEPT 169
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-215 |
5.26e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHiaqlSQQRAYLSQLVSYIpilkvFQYV 96
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLK----NREVPFLRRQIGMI-----FQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTVFS--------AG-----VFERLCSDFQLTSLLSKPIN---QLSGGEWQRVRIVAAFLQvwdkqqcEGKFILL 160
Cdd:PRK10908 89 HLLMDRTVYDnvaipliiAGasgddIRRRVSAALDKVGLLDKAKNfpiQLSGGEQQRVGIARAVVN-------KPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 161 DEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-225 |
5.44e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYH--IAQLSQQRA 78
Cdd:PRK09493 1 MIEFKNVSKHfgptQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEItSGDLIVDGLKVNDPKvdERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 79 YLSQLVSYIPILKVFQYVgLFSPNTVFSAGVFErlcSDFQLTSLLSK----------PiNQLSGGEWQRVRIVAAfLQVw 148
Cdd:PRK09493 81 MVFQQFYLFPHLTALENV-MFGPLRVRGASKEE---AEKQARELLAKvglaerahhyP-SELSGGQQQRVAIARA-LAV- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 149 dkqqcEGKFILLDEPTNNLDI-IQQAMLdKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:PRK09493 154 -----KPKLMLFDEPTSALDPeLRHEVL-KVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-194 |
7.17e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 56.39 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI-----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSirqyHIAQLSqQRAYL 80
Cdd:cd03223 1 IELENLSLatpdgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGsGRIGMPEGE----DLLFLP-QRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLVsyipilkvfqyvglfspntvfsagvferlcsdfqLTSLLSKPINQ-LSGGEWQRVRIVAAFLQvwdkqqcEGKFIL 159
Cdd:cd03223 76 PLGT----------------------------------LREQLIYPWDDvLSGGEQQRLAFARLLLH-------KPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 2697035156 160 LDEPTNNLDI-IQQAMLDKWIKYFCdclgTVIMSGH 194
Cdd:cd03223 115 LDEATSALDEeSEDRLYQLLKELGI----TVISVGH 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-195 |
1.10e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYL-PVGGDI-LIGGRSIRQYHIAQLSQQRA------YLSQLVSYIPILKVFQYVGLF 99
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELaPVSGEIgLAKGIKLGYFAQHQLEFLRAdesplqHLARLAPQELEQKLRDYLGGF 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 100 SpntvfsagvferlcsdFQlTSLLSKPINQLSGGEwqRVRIVAAfLQVWDKQQcegkFILLDEPTNNLDI-IQQAMLDKW 178
Cdd:PRK10636 418 G----------------FQ-GDKVTEETRRFSGGE--KARLVLA-LIVWQRPN----LLLLDEPTNHLDLdMRQALTEAL 473
|
170
....*....|....*..
gi 2697035156 179 IkyfcDCLGTVIMSGHD 195
Cdd:PRK10636 474 I----DFEGALVVVSHD 486
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-167 |
1.14e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG---GDILIGGRSIRQYHIAQlSQQR- 77
Cdd:PRK13549 5 LLEMKNITKTfggvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyeGEIIFEGEELQASNIRD-TERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 -AYLSQLVSYIPILKVFQyvGLFSPNTVFSAGVF---------ERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFlqv 147
Cdd:PRK13549 84 iAIIHQELALVKELSVLE--NIFLGNEITPGGIMdydamylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL--- 158
|
170 180
....*....|....*....|
gi 2697035156 148 wDKQqceGKFILLDEPTNNL 167
Cdd:PRK13549 159 -NKQ---ARLLILDEPTASL 174
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-196 |
1.17e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 57.02 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI------DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiaQLSQQ 76
Cdd:COG1116 7 ALELRGVSKrfptggGGVTAldDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVDGKPVT-----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 77 RAYlsqlvsyipilkVFQYVGLFsP------NTVF---SAGVF--------ERLCSDFQLTSLLSKPINQLSGGEWQRVR 139
Cdd:COG1116 82 RGV------------VFQEPALL-PwltvldNVALgleLRGVPkaerreraRELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 140 IVAAFLQvwdkqqcEGKFILLDEPTNNLDII-----QQAMLDKWIKyfcdcLG-TVIMSGHDL 196
Cdd:COG1116 149 IARALAN-------DPEVLLMDEPFGALDALtrerlQDELLRLWQE-----TGkTVLFVTHDV 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-168 |
1.38e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.07 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI----DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAI-------SGYLPVgGDILI-GGRSIRQyhiaQLS 74
Cdd:PRK11264 4 IEVKNLVKkfhgQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV-GDITIdTARSLSQ----QKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 75 QQRAyLSQLVSYipilkVFQYVGLFSPNTVFSaGVFE---------RLCSDFQLTSLLSK----------PiNQLSGGEW 135
Cdd:PRK11264 79 LIRQ-LRQHVGF-----VFQNFNLFPHRTVLE-NIIEgpvivkgepKEEATARARELLAKvglagketsyP-RRLSGGQQ 150
|
170 180 190
....*....|....*....|....*....|...
gi 2697035156 136 QRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD 168
Cdd:PRK11264 151 QRVAIARALAM-------RPEVILFDEPTSALD 176
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-227 |
1.40e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 57.12 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHIAQLSQQRAYLsQLVsyipilkvFQ-Y 95
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLeKPAQGTVSFRGQDLYQLDRKQRRAFRRDV-QLV--------FQdS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFSPNTVFSAGVFERLcsdFQLTSL----------------------LSKPINQLSGGEWQRVRIVAAFlqvwdkqQC 153
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPL---RHLTSLdeseqkariaelldmvglrsedADKLPRQLSGGQLQRINIARAL-------AV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 154 EGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTV-IMSGHDLSHSYKNASCIWMIKQGQLVAvgkpECIMTEK 227
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVE----ECDVAQL 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-195 |
1.53e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 4 KLIIDIKNITI---DTRLV-NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRsirqYHIAQLSQQRA 78
Cdd:PRK11147 317 KIVFEMENVNYqidGKQLVkDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRIHCGTK----LEVAYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 79 YL-------------SQLV----------SYipiLKVFqyvgLFSPNTVFSagvferlcsdfqltsllskPINQLSGGEW 135
Cdd:PRK11147 393 ELdpektvmdnlaegKQEVmvngrprhvlGY---LQDF----LFHPKRAMT-------------------PVKALSGGER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 136 QRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKyfcDCLGTVIMSGHD 195
Cdd:PRK11147 447 NRLLLARLFLK-------PSNLLILDEPTNDLDVETLELLEELLD---SYQGTVLLVSHD 496
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-215 |
1.77e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 16 TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIrqyhiAQL--SQQRAYLS--QLVsyipil 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPL-----AKLnrAQRKAFRRdiQMV------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 91 kvFQ-YVGLFSPNTVFSAGVFERLcsdFQLTSL----------------------LSKPINQLSGGEWQRVRIVAAFlqv 147
Cdd:PRK10419 95 --FQdSISAVNPRKTVREIIREPL---RHLLSLdkaerlarasemlravdlddsvLDKRPPQLSGGQLQRVCLARAL--- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 148 wdkqQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTV-IMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:PRK10419 167 ----AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-168 |
2.18e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.01 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRsirqyhiaqlsqqraylsqLVSYIPILK-----VFQYVGLFsP 101
Cdd:COG3839 29 GEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILIGGR-------------------DVTDLPPKDrniamVFQSYALY-P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 102 N-TVF--------SAGV------------FERLcsdfQLTSLLSKPINQLSGGEWQRV---R-IVAaflqvwdkqqcEGK 156
Cdd:COG3839 89 HmTVYeniafplkLRKVpkaeidrrvreaAELL----GLEDLLDRKPKQLSGGQRQRValgRaLVR-----------EPK 153
|
170
....*....|..
gi 2697035156 157 FILLDEPTNNLD 168
Cdd:COG3839 154 VFLLDEPLSNLD 165
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-224 |
2.18e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNITIDTRlvNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQR-- 77
Cdd:PRK10070 29 LSKEQILEKTGLSLGVK--DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 --AYLSQLVSYIPILKVFQyvglfspNTVFS---AGVFERLCSDFQLTSLLSKPI--------NQLSGGEWQRVRIVAAF 144
Cdd:PRK10070 107 kiAMVFQSFALMPHMTVLD-------NTAFGmelAGINAEERREKALDALRQVGLenyahsypDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 145 LQVWDkqqcegkFILLDEPTNNLD-IIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECI 223
Cdd:PRK10070 180 AINPD-------ILLMDEAFSALDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
.
gi 2697035156 224 M 224
Cdd:PRK10070 253 L 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-169 |
2.26e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 33 ILGANGAGKSTLLAAISGYL-PVGGDILIGgrsiRQYHIAQLSQQRAYLS------QLVS----YIPILKV----FQYVG 97
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEqPDSGTIKIG----ETVKLAYVDQSRDALDpnktvwEEISggldIIKVGNReipsRAYVG 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 98 LFSpntvFSAGvferlcsDFQltsllsKPINQLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDEPTNNLDI 169
Cdd:PRK11819 431 RFN----FKGG-------DQQ------KKVGVLSGGERNRLHL-AKTLKQ------GGNVLLLDEPTNDLDV 478
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-218 |
2.33e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAIS-GYLPVGGDILIGGRSIRQYHIAQLSQQraylsqlvsyipILKVFQYVGL 98
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDGTDIRTVTRASLRRN------------IAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 F---------------SPNTVFSAGvfERL-CSDFqltsLLSKPI----------NQLSGGEWQRVRIVAAFLQvwdkqq 152
Cdd:PRK13657 421 FnrsiednirvgrpdaTDEEMRAAA--ERAqAHDF----IERKPDgydtvvgergRQLSGGERQRLAIARALLK------ 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 153 cEGKFILLDEPTNNLDIIQQAMLDKWIkyfcDCLG---TVIMSGHDLShSYKNASCIWMIKQGQLVAVG 218
Cdd:PRK13657 489 -DPPILILDEATSALDVETEAKVKAAL----DELMkgrTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-225 |
2.58e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 5 LIIDIKNItidtrLVNVSAQVLTGEQIHILGANGAGKSTLLAAIS-------GYLPVGGDILIGGRSIRQYHIAQLSQQR 77
Cdd:PRK14246 18 LYINDKAI-----LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYLSQLVSYIPILKVFQYVGL-FSPNTVFSAGVFERLCSDF--------QLTSLLSKPINQLSGGEWQRVRIVAAFlqvw 148
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYpLKSHGIKEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARAL---- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 149 dkqQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSgHDLSHSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:PRK14246 169 ---ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-221 |
3.48e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID--TRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:PRK11831 7 LVDMRGVSFTrgNRCIfdNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIaPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQLvsyipilkvFQYVGLFSPNTVFSAGVF-----ERLCSDFQLTSLLSK-------------PiNQLSGGEWQRVRIVA 142
Cdd:PRK11831 87 SML---------FQSGALFTDMNVFDNVAYplrehTQLPAPLLHSTVMMKleavglrgaaklmP-SELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 143 AFlqvwdkqQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:PRK11831 157 AI-------ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-168 |
3.63e-09 |
|
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: 55.52 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILI--GGRSIRqyhIAQLSQQR---------AYLSQLVSYI 87
Cdd:COG4778 29 GVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVrhDGGWVD---LAQASPREilalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 88 PILKVFQYVGlfSPntVFSAGV------------FERLCSDFQLTSLlskPINQLSGGEWQRVRIVAAFLQVWdkqqceg 155
Cdd:COG4778 106 PRVSALDVVA--EP--LLERGVdreearararelLARLNLPERLWDL---PPATFSGGEQQRVNIARGFIADP------- 171
|
170
....*....|...
gi 2697035156 156 KFILLDEPTNNLD 168
Cdd:COG4778 172 PLLLLDEPTASLD 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-63 |
3.87e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.47 E-value: 3.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGR 63
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRVEVNGR 88
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-244 |
5.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsirqYHIAQLSQQRAyLSQLVSYIPIlkVFQY- 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAG-----YHITPETGNKN-LKKLRKKVSL--VFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 -VGLFSpNTVF--------SAGVFERLCSDFQL---------TSLLSKPINQLSGGEWQRVRI--VAAFlqvwdkqqcEG 155
Cdd:PRK13641 95 eAQLFE-NTVLkdvefgpkNFGFSEDEAKEKALkwlkkvglsEDLISKSPFELSGGQMRRVAIagVMAY---------EP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 156 KFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKN-LSDIFM 234
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYL 244
|
250
....*....|
gi 2697035156 235 SEIKLSHSAS 244
Cdd:PRK13641 245 DEPATSRFAS 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-167 |
5.19e-09 |
|
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: 55.99 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG---GDILIGGRSIRQYHIAQLSQQR- 77
Cdd:TIGR02633 1 LLEMKGIVKTfggvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYLSQLVSYIPILKVFQyvGLFSPNTVFSAGVF----------ERLCSDFQLTSL-LSKPINQLSGGEWQRVRIVAAFlq 146
Cdd:TIGR02633 81 VIIHQELTLVPELSVAE--NIFLGNEITLPGGRmaynamylraKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKAL-- 156
|
170 180
....*....|....*....|.
gi 2697035156 147 vwDKQqceGKFILLDEPTNNL 167
Cdd:TIGR02633 157 --NKQ---ARLLILDEPSSSL 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-229 |
5.39e-09 |
|
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: 55.18 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAYLSQlvsyipilkvfqyv 96
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfsPNTVFSAGVFE------------------RLCSDFQLTSLLSKPINQ--------LSGGEWQRVRIVAAFLQvwdk 150
Cdd:cd03252 84 ----ENVLFNRSIRDnialadpgmsmervieaaKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIH---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 151 qqcEGKFILLDEPTNNLD-----IIQQAMLDKwikyfcdCLG-TVIMSGHDLShSYKNASCIWMIKQGQLVAVGKPECIM 224
Cdd:cd03252 156 ---NPRILIFDEATSALDyesehAIMRNMHDI-------CAGrTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
....*
gi 2697035156 225 TEKNL 229
Cdd:cd03252 225 AENGL 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-168 |
7.94e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHIAQLSQQR----AYLSQLVSYIPILKV 92
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAELRnqklGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYVGLfspnTVFSAGVFERLCSDFQLTSL----LSKPIN----QLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:PRK11629 105 LENVAM----PLLIGKKKPAEINSRALEMLaavgLEHRANhrpsELSGGERQRVAIARALVN-------NPRLVLADEPT 173
|
....
gi 2697035156 165 NNLD 168
Cdd:PRK11629 174 GNLD 177
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-169 |
8.59e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNI--TIDTRLV--NVSAQVLTGEqIH-ILGANGAGKSTLLAAISG---YLPVGGDILIGGRSIRQYHIAQ 72
Cdd:CHL00131 2 NKNKPILEIKNLhaSVNENEIlkGLNLSINKGE-IHaIMGPNGSGKSTLSKVIAGhpaYKILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 73 LSQQRAYLSqlvsyipilkvFQYvglfsPNTVfsAGV---------------------------FERLCSDFQLTSL--- 122
Cdd:CHL00131 81 RAHLGIFLA-----------FQY-----PIEI--PGVsnadflrlaynskrkfqglpeldplefLEIINEKLKLVGMdps 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2697035156 123 -LSKPINQ-LSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLDI 169
Cdd:CHL00131 143 fLSRNVNEgFSGGEKKRNEILQMAL-------LDSELAILDETDSGLDI 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-223 |
1.73e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKS-TLLAAISGYLPVGGDILIGGRSIRQY--HIAQLSQQRAYLSQLVSYIPILKVFQYv 96
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKMLLRRRsrQVIELSEQSAAQMRHVRGADMAMIFQE- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTVFSAGvfERLCSDFQL-------------------------TSLLSKPINQLSGGEWQRVRIVAAFlqvwdkq 151
Cdd:PRK10261 113 PMTSLNPVFTVG--EQIAESIRLhqgasreeamveakrmldqvripeaQTILSRYPHQLSGGMRQRVMIAMAL------- 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 152 QCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGT-VIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECI 223
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-194 |
2.02e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI------DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:TIGR01271 1218 MDVQGLTAkyteagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQlvsyipilKVFQYVGLF----SPNTVFSAGVFERLCSDFQLTSLLSKPINQL-----------SGGEWQRVRIVAAFL 145
Cdd:TIGR01271 1298 PQ--------KVFIFSGTFrknlDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2697035156 146 QvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKY-FCDClgTVIMSGH 194
Cdd:TIGR01271 1370 S-------KAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNC--TVILSEH 1410
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-196 |
2.54e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI------DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:cd03289 3 MTVKDLTAkyteggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQlvsyipilKVFQYVGLF----SPNTVFSAGVFERLCSDFQLTSLLSKPINQL-----------SGGEWQRVRIVAAFL 145
Cdd:cd03289 83 PQ--------KVFIFSGTFrknlDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 146 QvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKY-FCDClgTVIMSGHDL 196
Cdd:cd03289 155 S-------KAKILLLDEPSAHLDPITYQVIRKTLKQaFADC--TVILSEHRI 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-251 |
2.62e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQRAYLSQlvsyIPIL---KVF 93
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQ----DPVLfdgTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLF---SPNTVFSA----GVFERLCSDFQ-LTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGK-FILLDEPT 164
Cdd:PTZ00243 1402 QNVDPFleaSSAEVWAAlelvGLRERVASESEgIDSRVLEGGSNYSVGQRQLMCMARALLK-------KGSgFILMDEAT 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 165 NNLD-----IIQQAMLDKWIKYfcdclgTVIMSGHDLsHSYKNASCIWMIKQGQLVAVGKP-ECIMtekNLSDIFMSEIK 238
Cdd:PTZ00243 1475 ANIDpaldrQIQATVMSAFSAY------TVITIAHRL-HTVAQYDKIIVMDHGAVAEMGSPrELVM---NRQSIFHSMVE 1544
|
250
....*....|....
gi 2697035156 239 -LSHSASHRVWQVI 251
Cdd:PTZ00243 1545 aLGRSEAKRFLQLV 1558
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
5-168 |
2.69e-08 |
|
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: 53.57 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 5 LIIDIK----NITIDTRLvNVSAQVLTGeqihILGANGAGKSTLLAAISGYL-PVGGDILIGGR----SIRQYHIAqlSQ 75
Cdd:COG4148 3 LEVDFRlrrgGFTLDVDF-TLPGRGVTA----LFGPSGSGKTTLLRAIAGLErPDSGRIRLGGEvlqdSARGIFLP--PH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAylsqlVSYipilkVFQYVGLFSPNTV---------FSAGV-----FERLCSDFQLTSLLSKPINQLSGGEWQRVRIV 141
Cdd:COG4148 76 RRR-----IGY-----VFQEARLFPHLSVrgnllygrkRAPRAerrisFDEVVELLGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180
....*....|....*....|....*..
gi 2697035156 142 AAFLqvwdkqqCEGKFILLDEPTNNLD 168
Cdd:COG4148 146 RALL-------SSPRLLLMDEPLAALD 165
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-194 |
3.44e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiaqlsQQR-AYLSQLVsyipilkvfqYVG 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEVLWQGEPIR--------RQRdEYHQDLL----------YLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 -------LFSP--NTVFSAGVFERLcSDFQLTSLLSK---------PINQLSGGewQRVRIVAAFLQV-----Wdkqqce 154
Cdd:PRK13538 81 hqpgiktELTAleNLRFYQRLHGPG-DDEALWEALAQvglagfedvPVRQLSAG--QQRRVALARLWLtraplW------ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2697035156 155 gkfiLLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGH 194
Cdd:PRK13538 152 ----ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-175 |
3.59e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.66 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDT-----RLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG---------YLPVGGDILIggrsirqyhiaq 72
Cdd:COG4178 363 LALEDLTLRTpdgrpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriARPAGARVLF------------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 73 LSqQRAY-----LSQLVSYiP----------ILKVFQYVGLfspntvfsagvfERLCSDFQLTSLLSkpiNQLSGGEWQR 137
Cdd:COG4178 431 LP-QRPYlplgtLREALLY-PataeafsdaeLREALEAVGL------------GHLAERLDEEADWD---QVLSLGEQQR 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 2697035156 138 VRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAML 175
Cdd:COG4178 494 LAFARLLLH-------KPDWLFLDEATSALDEENEAAL 524
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-226 |
3.71e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGG----RSIRQYHIAQLSQQRAYLSQLvsyiPILKV 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDivvsSTSKQKEIKPVRKKVGVVFQF----PESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYVGL----FSP-NTVFSAGVFERLCSD-FQLTSL----LSKPINQLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDE 162
Cdd:PRK13643 98 FEETVLkdvaFGPqNFGIPKEKAEKIAAEkLEMVGLadefWEKSPFELSGGQMRRVAI-AGILAM------EPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 163 PTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTE 226
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-221 |
4.39e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISgYL--PVGGDILIGGRSIR-------QYHIAQLSQQRAYLSQLVsyip 88
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-FLekPSEGSIVVNGQTINlvrdkdgQLKVADKNQLRLLRTRLT---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 89 ilKVFQYVGLFSPNTVFSaGVFERLCSDFQLTSLLSK--------------------PINqLSGGEWQRVRIVAAFLQvw 148
Cdd:PRK10619 96 --MVFQHFNLWSHMTVLE-NVMEAPIQVLGLSKQEAReravkylakvgideraqgkyPVH-LSGGQQQRVSIARALAM-- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 149 dkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPE 221
Cdd:PRK10619 170 -----EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
4.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENklIIDIKNITIDTR-------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQ 72
Cdd:PRK13650 1 MSN--IIEVKNLTFKYKedqekytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 73 LSQQraylsqlvsyipILKVF-----QYVGLfspnTVFSAGVF-------------ERLCSDFQLTSLL---SKPINQLS 131
Cdd:PRK13650 79 IRHK------------IGMVFqnpdnQFVGA----TVEDDVAFglenkgipheemkERVNEALELVGMQdfkEREPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 132 GGEWQRVRIVAAFlqvwdkqQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMiK 210
Cdd:PRK13650 143 GGQKQRVAIAGAV-------AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVM-K 214
|
250
....*....|.
gi 2697035156 211 QGQLVAVGKPE 221
Cdd:PRK13650 215 NGQVESTSTPR 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-214 |
4.84e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 30 QIHILGANGAGKSTLLAAISGYL-PVGGDILiggRSIR-------QYHIAQL---SQQRAYLSQLVSYIPILKVFQYVGL 98
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELqPSSGTVF---RSAKvrmavfsQHHVDGLdlsSNPLLYMMRCFPGVPEQKLRAHLGS 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 99 FspntvfsaGVferlcsdfqLTSLLSKPINQLSGGEWQRVrivaAFLQVWDKQQcegKFILLDEPTNNLDIIQQAMLDKW 178
Cdd:PLN03073 614 F--------GV---------TGNLALQPMYTLSGGQKSRV----AFAKITFKKP---HILLLDEPSNHLDLDAVEALIQG 669
|
170 180 190
....*....|....*....|....*....|....*.
gi 2697035156 179 IKYFcdcLGTVIMSGHDLSHSYKNASCIWMIKQGQL 214
Cdd:PLN03073 670 LVLF---QGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-168 |
4.95e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGyLPVG--GDILIGGRSIRQYHIAQLSQQRA----YLSQLVSYIPILK 91
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGssGEVSLVGQPLHQMDEEARAKLRAkhvgFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 VFQYVGLFS----PNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFlqvwdkqQCEGKFILLDEPTNNL 167
Cdd:PRK10584 105 ALENVELPAllrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-------NGRPDVLFADEPTGNL 177
|
.
gi 2697035156 168 D 168
Cdd:PRK10584 178 D 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-248 |
5.92e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 30 QIH-ILGANGAGKSTLLAAISGYL-PVGGDILIGGRsirqyHIAQLSQQRAYlsQLVSYIpilkVFQYVGLFSPNTVFSA 107
Cdd:PRK15439 38 EVHaLLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGN-----PCARLTPAKAH--QLGIYL----VPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 108 GVF---ERLCSDFQLTSLLSKPINQLSggewqrVRIVAAFLQVWDKQQCE--------GKFILLDEPTNNLDIIQ----- 171
Cdd:PRK15439 107 ILFglpKRQASMQKMKQLLAALGCQLD------LDSSAGSLEVADRQIVEilrglmrdSRILILDEPTASLTPAEterlf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 172 ---QAMLDKWIkyfcdclGTVIMSgHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDIFMSEIKLSHSASHRVW 248
Cdd:PRK15439 181 sriRELLAQGV-------GIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKSLSASQKLW 252
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-196 |
6.43e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYLS 81
Cdd:PRK09544 4 LVSLENVSVSfgqrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 82 QLVSYIPILKvfqyvglfsPNtVFSAGVFERLcSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLD 161
Cdd:PRK09544 84 LTVNRFLRLR---------PG-TKKEDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLN-------RPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2697035156 162 EPTNNLDIIQQAMLDKWIKYFCDCLG-TVIMSGHDL 196
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDL 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-168 |
8.72e-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: 51.11 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 10 KNITIDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG----YLPVGGDILIGGrsiRQYHIAQLSQQR--AYLSQL 83
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVEGDIHYNG---IPYKEFAEKYPGeiIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 84 VSYIPILKVFQYVglfspntvfsagvferlcsDFQLTSLLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEP 163
Cdd:cd03233 92 DVHFPTLTVRETL-------------------DFALRCKGNEFVRGISGGERKRVSIAEALV-------SRASVLCWDNS 145
|
....*
gi 2697035156 164 TNNLD 168
Cdd:cd03233 146 TRGLD 150
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
1.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.56 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyhiAQLSQQRayLSQLVSYIPIlkVFQyv 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTIGERVIT----AGKKNKK--LKPLRKKVGI--VFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glFSPNTVFSAGVFERLC---SDFQLT-------------------SLLSKPINQLSGGEWQRVRIvAAFLQVwdkqqcE 154
Cdd:PRK13634 93 --FPEHQLFEETVEKDICfgpMNFGVSeedakqkaremielvglpeELLARSPFELSGGQMRRVAI-AGVLAM------E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 155 GKFILLDEPTNNLDII-QQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKNlsdiF 233
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKgRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD----E 239
|
....*..
gi 2697035156 234 MSEIKLS 240
Cdd:PRK13634 240 LEAIGLD 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-220 |
2.11e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.18 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGrsirqyhiaqlsqqraylsQLVSYIPILK-----VF 93
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFIGE-------------------KRMNDVPPAErgvgmVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLFSPNTVFS--------AGV--------FERLCSDFQLTSLLSKPINQLSGGEWQRVRI----VAaflqvwdkqqc 153
Cdd:PRK11000 82 QSYALYPHLSVAEnmsfglklAGAkkeeinqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIgrtlVA----------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 154 EGKFILLDEPTNNLDI-------IQQAMLDKWIKyfcdclGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvqmrIEISRLHKRLG------RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-168 |
2.41e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGyL--PVGGDILIGGRSIRQYHIAQLSQQRaylsQLVSYIpilkvFQY 95
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL-LerPTSGRVLVDGQDLTALSEKELRKAR----RQIGMI-----FQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFSPNTVFS--------AG---------VFERLcsdfQLTSLLSK----PiNQLSGGEWQRVRIVAAFlqvwdkqQCE 154
Cdd:PRK11153 91 FNLLSSRTVFDnvalplelAGtpkaeikarVTELL----ELVGLSDKadryP-AQLSGGQKQRVAIARAL-------ASN 158
|
170
....*....|....
gi 2697035156 155 GKFILLDEPTNNLD 168
Cdd:PRK11153 159 PKVLLCDEATSALD 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-197 |
2.78e-07 |
|
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: 50.44 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNIT----IDTRLV----NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP----VGGDILIGGRSIRQYHIAQL 73
Cdd:COG0444 1 LLEVRNLKvyfpTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 74 sqqRAYLSQLVSYI---------PILKV--------------------------FQYVGLFSPntvfsagvfERLCSDFq 118
Cdd:COG0444 81 ---RKIRGREIQMIfqdpmtslnPVMTVgdqiaeplrihgglskaeareraielLERVGLPDP---------ERRLDRY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 119 ltsllskPiNQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLDIIQQA----MLDKwikyFCDCLG-TVIMSG 193
Cdd:COG0444 148 -------P-HELSGGMRQRVMIARALA-------LEPKLLIADEPTTALDVTIQAqilnLLKD----LQRELGlAILFIT 208
|
....
gi 2697035156 194 HDLS 197
Cdd:COG0444 209 HDLG 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-63 |
2.98e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 49.84 E-value: 2.98e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGR 63
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPDSGTVTVRGR 84
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-220 |
3.32e-07 |
|
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: 49.33 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRqyHIAqlsqqrayLSQLVSYIPILKvfQYV 96
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDIS--TIP--------LEDLRSSLTIIP--QDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTVFSAGVFERLcSDFQLTSLL--SKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAM 174
Cdd:cd03369 92 TLFSGTIRSNLDPFDEY-SDEEIYGALrvSEGGLNLSQGQRQLLCLARALLK-------RPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2697035156 175 LDKWI-KYFCDclGTVIMSGHDLsHSYKNASCIWMIKQGQLVAVGKP 220
Cdd:cd03369 164 IQKTIrEEFTN--STILTIAHRL-RTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-214 |
7.11e-07 |
|
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: 48.62 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYHIAQLSQQRAylsqLVSYIPILkvfqYV 96
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQGGQVLLDGKPISQYEHKYLHSKVS----LVGQEPVL----FA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFSPNTVFSAGV--FERLCSDFQ------LTSLLSKPI--------NQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILL 160
Cdd:cd03248 102 RSLQDNIAYGLQScsFECVKEAAQkahahsFISELASGYdtevgekgSQLSGGQKQRVAIARALIR-------NPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 161 DEPTNNLDIIQQAMLDKWIkYFCDCLGTVIMSGHDLShSYKNASCIWMIKQGQL 214
Cdd:cd03248 175 DEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-195 |
8.09e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYlpvggDILIGGRSIRQ--YHIAQLSQQ---------RAYLSQLVSY 86
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKDFNGEARPQpgIKVGYLPQEpqldptktvRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 87 IP-ILKVFQ--YVGLFSPNTVFSAGVFE--RL------CSDFQLTSLLS------------KPINQLSGGEWQRVRIVAA 143
Cdd:TIGR03719 96 IKdALDRFNeiSAKYAEPDADFDKLAAEqaELqeiidaADAWDLDSQLEiamdalrcppwdADVTKLSGGERRRVALCRL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 144 FLQVWDkqqcegkFILLDEPTNNLDIIQQAMLDKWIKYFCdclGTVIMSGHD 195
Cdd:TIGR03719 176 LLSKPD-------MLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTHD 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-218 |
9.49e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI-----DTR-LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQRAy 79
Cdd:PRK11176 342 IEFRNVTFtypgkEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIdEGEILLDGHDLRDYTLASLRNQVA- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsqLVSyipilkvfQYVGLFSP----NTVFSA-GVFER----------LCSDF--QLTSLLSKPINQ----LSGGEWQRV 138
Cdd:PRK11176 421 ---LVS--------QNVHLFNDtianNIAYARtEQYSReqieeaarmaYAMDFinKMDNGLDTVIGEngvlLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 139 RIVAAFLQvwdkqqcEGKFILLDEPTNNLD-----IIQQAmLDKWIKYfcdclGTVIMSGHDLShSYKNASCIWMIKQGQ 213
Cdd:PRK11176 490 AIARALLR-------DSPILILDEATSALDteserAIQAA-LDELQKN-----RTSLVIAHRLS-TIEKADEILVVEDGE 555
|
....*
gi 2697035156 214 LVAVG 218
Cdd:PRK11176 556 IVERG 560
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-178 |
9.90e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSirqyhIAQLSQQRAYlsqlvsyipilkVFQYV 96
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqHGSITLDGKP-----VEGPGAERGV------------VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 GLFS-----PNTVFS---AGV--FERLCSDFQLTSLL------SKPINQLSGGEWQRV---RIVAAFLQVwdkqqcegkf 157
Cdd:PRK11248 80 GLLPwrnvqDNVAFGlqlAGVekMQRLEIAHQMLKKVglegaeKRYIWQLSGGQRQRVgiaRALAANPQL---------- 149
|
170 180
....*....|....*....|....*.
gi 2697035156 158 ILLDEPTNNLDI-----IQQAMLDKW 178
Cdd:PRK11248 150 LLLDEPFGALDAftreqMQTLLLKLW 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-215 |
1.04e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAIS-------GYLPVGGDILIG-------------------------GRSIRQYHiaQLSQ 75
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNgevllddGRIIYEQDLIVArlqqdpprnvegtvydfvaegieeqAEYLKRYH--DISH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAY------LSQLVSyipILKVFQYVGLFSpntvfsagvFE-RLCSDFQLTSL-LSKPINQLSGGeWQRVRIVAAFLQv 147
Cdd:PRK11147 107 LVETdpseknLNELAK---LQEQLDHHNLWQ---------LEnRINEVLAQLGLdPDAALSSLSGG-WLRKAALGRALV- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 148 wdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFcdcLGTVIMSGHDLSHSYKNASCIWMIKQGQLV 215
Cdd:PRK11147 173 -----SNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-172 |
1.13e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYHIAQLSQQRAYL----SQLVSYIPILKV 92
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRATSGRIVFDGKDITDWQTAKIMREAVAIvpegRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYVGLFSPNTVFSagvfERLCSDFQLTSLLSKPINQ----LSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLD 168
Cdd:PRK11614 101 LAMGGFFAERDQFQ----ERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMS-------QPRLLLLDEPSLGLA 169
|
....*.
gi 2697035156 169 --IIQQ 172
Cdd:PRK11614 170 piIIQQ 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-196 |
1.14e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 4 KLIIDIKNITI--DTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIR--------QYHIAQ 72
Cdd:PRK09700 263 ETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRaGGEIRLNGKDISprspldavKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 73 LSQQRA--------YLSQLVSYIPILKVFQY---VGLFSPNTvfSAGVFERLCSDFQLT-SLLSKPINQLSGGEWQRVrI 140
Cdd:PRK09700 343 ITESRRdngffpnfSIAQNMAISRSLKDGGYkgaMGLFHEVD--EQRTAENQRELLALKcHSVNQNITELSGGNQQKV-L 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2697035156 141 VAAFLQvwdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDL 196
Cdd:PRK09700 420 ISKWLC------CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-226 |
1.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.51 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaqlSQQRAYLSQLVSYIPIlkVFQY- 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDI--------TDKKVKLSDIRKKVGL--VFQYp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 -VGLFSpNTVFSAGVF-------------ERLCSDFQLTSL-----LSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGK 156
Cdd:PRK13637 93 eYQLFE-ETIEKDIAFgpinlglseeeieNRVKRAMNIVGLdyedyKDKSPFELSGGQKRRVAIAGVVAM-------EPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2697035156 157 FILLDEPTNNLD------IIQQamldkwIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTE 226
Cdd:PRK13637 165 ILILDEPTAGLDpkgrdeILNK------IKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-228 |
1.72e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSI----RQYHIAQLSQQRAylsqLVSYIPILKV 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDITIthktKDKYIRPVRKRIG----MVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 93 FQYVG----LFSPNTvFSAGVFERLCSDFQL-------TSLLSKPINQLSGGEWQRVRIVAAFLQVWDkqqcegkFILLD 161
Cdd:PRK13646 99 FEDTVereiIFGPKN-FKMNLDEVKNYAHRLlmdlgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPD-------IIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 162 EPTNNLDIIQQAMLDKWIKYF-CDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPECIMTEKN 228
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-173 |
2.56e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITI------DTRLV--NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV------GGDILIGG--------- 62
Cdd:PRK15134 5 LLAIENLSVafrqqqTVRTVvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGesllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 63 --RSIRQYHIAQLSQQraylsQLVSYIP--------------------------ILKVFQYVGLFSPNTvfsagvfeRLc 114
Cdd:PRK15134 85 tlRGVRGNKIAMIFQE-----PMVSLNPlhtlekqlyevlslhrgmrreaargeILNCLDRVGIRQAAK--------RL- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 115 SDFQltsllskpiNQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQA 173
Cdd:PRK15134 151 TDYP---------HQLSGGERQRVMIAMALLT-------RPELLIADEPTTALDVSVQA 193
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-232 |
2.56e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGrsIRQYHIAQLSQQRaylsQLVSYIPILKVFQYV 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSG--IDTGDFSKLQGIR----KLVGIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 G-------LFSPNTVFSAGV-----FERLCSDFQLTSLLSKPINQLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDEPT 164
Cdd:PRK13644 92 GrtveedlAFGPENLCLPPIeirkrVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL-AGILTM------EPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 165 NNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLsHSYKNASCIWMIKQGQLVAVGKPECIMTEKNLSDI 232
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-195 |
2.71e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 123 LSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCdclGTVIMSGHD 195
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLAQALI-------CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ---GTLILISHD 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-168 |
2.73e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 21 VSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSI-----RQYHIAQlsqqraylsqlvsyipilkVFQ 94
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERItSGEIWIGGRVVnelepADRDIAM-------------------VFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 YVGLFSPNTVF-----------------------SAGVFErlcsdfqLTSLLS-KPiNQLSGGEWQRV---R-IV---AA 143
Cdd:PRK11650 84 NYALYPHMSVRenmayglkirgmpkaeieervaeAARILE-------LEPLLDrKP-RELSGGQRQRVamgRaIVrepAV 155
|
170 180
....*....|....*....|....*
gi 2697035156 144 FlqvwdkqqcegkfiLLDEPTNNLD 168
Cdd:PRK11650 156 F--------------LFDEPLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
33-252 |
2.90e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.54 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 33 ILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyHIAQLSQQRAYLSQLVSYIPILK-----VFQYVG--------- 97
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIkSKYGTIQVGDIYIGD-KKNNHELITNPYSKKIKNFKELRrrvsmVFQFPEyqlfkdtie 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 ---LFSPNTVFSAGVFERLCSDFQLT------SLLSKPINQLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDEPTNNLD 168
Cdd:PRK13631 136 kdiMFGPVALGVKKSEAKKLAKFYLNkmglddSYLERSPFGLSGGQKRRVAI-AGILAI------QPEILIFDEPTAGLD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 169 IIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPecimteknlSDIFMSEIKLSHS--ASHR 246
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP---------YEIFTDQHIINSTsiQVPR 279
|
....*.
gi 2697035156 247 VWQVIN 252
Cdd:PRK13631 280 VIQVIN 285
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-222 |
3.76e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.93 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT----IDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAI-------SGYLPVGGDILIGGRSIRQYHIAQLSQ 75
Cdd:PRK11124 3 IQLNGINcfygAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQLVSYIPILKVFQ--------YVGLFSPNTVFSAgvfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQv 147
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQnlieapcrVLGLSKDQALARA---EKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 148 wdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPEC 222
Cdd:PRK11124 159 ------EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-222 |
3.80e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 46.54 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNIT----IDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGG------RSIRQYHIAQLSQ 75
Cdd:COG4161 3 IQLKNINcfygSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLeTPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 76 QRAYLSQLVSYIPILKVFQ--------YVGLFSPNTVFSAgvfERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQv 147
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnlieapckVLGLSKEQAREKA---MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 148 wdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKPEC 222
Cdd:COG4161 159 ------EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASH 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-67 |
4.27e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 4.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 18 LVNVSAQVLTGEqIH-ILGANGAGKSTLLAAISGYLPVG---GDILIGG-----RSIRQ 67
Cdd:NF040905 17 LDDVNLSVREGE-IHaLCGENGAGKSTLMKVLSGVYPHGsyeGEILFDGevcrfKDIRD 74
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-175 |
4.43e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 15 DTRLVNVSAQVL-TGEQIHILGANGAGKSTLLAAISGYLPvggdILIGGRSIRQYHIAQLSQQRayLSQLVSyipilKVF 93
Cdd:PRK10938 15 DTKTLQLPSLTLnAGDSWAFVGANGSGKSALARALAGELP----LLSGERQSQFSHITRLSFEQ--LQKLVS-----DEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QY--VGLFSP--------------NTVFSAGVFERLCSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKF 157
Cdd:PRK10938 84 QRnnTDMLSPgeddtgrttaeiiqDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMS-------EPDL 156
|
170
....*....|....*...
gi 2697035156 158 ILLDEPTNNLDIIQQAML 175
Cdd:PRK10938 157 LILDEPFDGLDVASRQQL 174
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-226 |
4.56e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.72 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGGRSIRQYhiAQLSQQRA-------YLSQLVSYIPILK 91
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPVPSR--ARHARQRVgvvpqfdNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 VF-QYVGLfspntvFSAGVFERLCSDFQLTSLLSK---PINQLSGGEWQRVRIVAAFLQVWDkqqcegkFILLDEPTNNL 167
Cdd:PRK13537 103 VFgRYFGL------SAAAARALVPPLLEFAKLENKadaKVGELSGGMKRRLTLARALVNDPD-------VLVLDEPTTGL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 168 DIIQQAMLDKWIKYFCDCLGTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKP-ECIMTE 226
Cdd:PRK13537 170 DPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPhALIESE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-169 |
5.30e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITIDTRLVNVSAQVLTGEqihIL---GANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQR-AYL 80
Cdd:COG1129 256 VLEVEGLSVGGVVRDVSFSVRAGE---ILgiaGLVGAGRTELARALFGADPAdSGEIRLDGKPVRIRSPRDAIRAGiAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQ------LVS--------YIPILKVFQYVGLFSPNTVfsAGVFERLCSDFQL-TSLLSKPINQLSGGEWQRV---RIVA 142
Cdd:COG1129 333 PEdrkgegLVLdlsireniTLASLDRLSRGGLLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVvlaKWLA 410
|
170 180
....*....|....*....|....*..
gi 2697035156 143 AflqvwdkqqcEGKFILLDEPTNNLDI 169
Cdd:COG1129 411 T----------DPKVLILDEPTRGIDV 427
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
5-169 |
5.81e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 5 LIIDIK------NITIDTRLvnvSAQVLTGeqihILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQyhiaqlSQQR 77
Cdd:PRK11144 2 LELNFKqqlgdlCLTVNLTL---PAQGITA----IFGRSGAGKTSLINAISGLTrPQKGRIVLNGRVLFD------AEKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYLsqlvsyiPILK-----VFQYVGLFSPNTV----------FSAGVFERLCSDFQLTSLLSK-PINqLSGGEWQRVRIV 141
Cdd:PRK11144 69 ICL-------PPEKrrigyVFQDARLFPHYKVrgnlrygmakSMVAQFDKIVALLGIEPLLDRyPGS-LSGGEKQRVAIG 140
|
170 180
....*....|....*....|....*...
gi 2697035156 142 AAFLQvwdkqqcEGKFILLDEPTNNLDI 169
Cdd:PRK11144 141 RALLT-------APELLLMDEPLASLDL 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-176 |
6.13e-06 |
|
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: 46.99 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLSQQRAYLsQLV------SYIP----- 88
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRM-QVVfqdpfgSLSPrmtvg 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 89 ----------------------ILKVFQYVGLfSPNTvfsagvferlcsdfqltslLSKPINQLSGGEWQRVRIVAAfLQ 146
Cdd:COG4172 383 qiiaeglrvhgpglsaaerrarVAEALEEVGL-DPAA-------------------RHRYPHEFSGGQRQRIAIARA-LI 441
|
170 180 190
....*....|....*....|....*....|.
gi 2697035156 147 VwdkqqcEGKFILLDEPTNNLDI-IQQAMLD 176
Cdd:COG4172 442 L------EPKLLVLDEPTSALDVsVQAQILD 466
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-196 |
7.19e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYLP----VGGDILIGGRSIRQYHIAQLSQQRAylsQLVSYIpilkvFQyvglfSPNT 103
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLAangrIGGSATFNGREILNLPEKELNKLRA---EQISMI-----FQ-----DPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 104 VFSA--GVFERLCSDFQLTSLLSK--------------------------PiNQLSGGEWQRVRIVAAFLqvwdkqqCEG 155
Cdd:PRK09473 109 SLNPymRVGEQLMEVLMLHKGMSKaeafeesvrmldavkmpearkrmkmyP-HEFSGGMRQRVMIAMALL-------CRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2697035156 156 KFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGT-VIMSGHDL 196
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDL 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-218 |
9.12e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSIRQYhiaQLSQQRAYLSqLVSYIPIL---KVF 93
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSeGDIRFHDIPLTKL---QLDSWRSRLA-VVSQTPFLfsdTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 94 QYVGLFSPNTVFS--------AGVFE---RLCSDFQlTSLLSKPInQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDE 162
Cdd:PRK10789 407 NNIALGRPDATQQeiehvarlASVHDdilRLPQGYD-TEVGERGV-MLSGGQKQRISIARALL-------LNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 163 PTNNLD------IIQQamLDKWIKYfcdclGTVIMSGHDLShSYKNASCIWMIKQGQLVAVG 218
Cdd:PRK10789 478 ALSAVDgrtehqILHN--LRQWGEG-----RTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-230 |
9.74e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.60 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 10 KNITIDTRLVNV---SAQVLTGEQIHI--------LGANGAGKSTLLAAISGYLP------VGGDILIGGRSIRQYHI-- 70
Cdd:PRK14267 1 MKFAIETVNLRVyygSNHVIKGVDLKIpqngvfalMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 71 AQLSQQRAYLSQLVSYIPILKVFQYV--GLFSPNTVFSAG-VFERLCSDFQLTSL-------LSKPINQLSGGEWQRVRI 140
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVaiGVKLNGLVKSKKeLDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 141 VAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLgTVIMSGHDLSHSYKNASCIWMIKQGQLVAVGK- 219
Cdd:PRK14267 161 ARALAM-------KPKILLMDEPTANIDPVGTAKIEELLFELKKEY-TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPt 232
|
250
....*....|....*..
gi 2697035156 220 ------PECIMTEKNLS 230
Cdd:PRK14267 233 rkvfenPEHELTEKYVT 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-219 |
1.01e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 16 TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP---VGGDILIGGRSIRQyhiaQLSQQRAYLSQ---LVSYIPI 89
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTK----QILKRTGFVTQddiLYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 90 LKVFQYVGLFS-PNTVF---SAGVFERLCSDFQLTS-----LLSKPINQLSGGEWQRVRIVAAFLqvwdkqqCEGKFILL 160
Cdd:PLN03211 158 RETLVFCSLLRlPKSLTkqeKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEML-------INPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 161 DEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHD-LSHSYKNASCIWMIKQGQLVAVGK 219
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
19-196 |
1.09e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 19 VNVSAQVLT-GEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIrqyhiaqlsqqraylsqlvSYIPilkvfQYV 96
Cdd:cd03222 15 LLVELGVVKeGEVIGIVGPNGTGKTTAVKILAGQLiPNGDNDEWDGITP-------------------VYKP-----QYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 97 glfspntvfsagvferlcsdfqltsllskpinQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPTNNLDIIQQAMLD 176
Cdd:cd03222 71 --------------------------------DLSGGELQRVAIAAALLR-------NATFYLFDEPSAYLDIEQRLNAA 111
|
170 180
....*....|....*....|.
gi 2697035156 177 KWIKYFCD-CLGTVIMSGHDL 196
Cdd:cd03222 112 RAIRRLSEeGKKTALVVEHDL 132
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
123-197 |
1.85e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 1.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2697035156 123 LSKPINQLSGGEWQRVRIvAAFLQvwdkQQCEGKFILLDEPTNNLDIIQQAMLDKWIKYFCDCLGTVIMSGHDLS 197
Cdd:cd03238 81 LGQKLSTLSGGELQRVKL-ASELF----SEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-168 |
1.92e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.07 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNIT----IDTRLV----NVSAQVLTGEqIH-ILGANGAGKSTLLAAISGyL--PVGGDILIGGRSIRQYHIAQLS 74
Cdd:COG1135 1 MIELENLSktfpTKGGPVtaldDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINL-LerPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 75 QQRaylsQLVSYIpilkvFQYVGLFSPNTVFS--------AG---------VFERLcsdfQLTSLLSK----PiNQLSGG 133
Cdd:COG1135 79 AAR----RKIGMI-----FQHFNLLSSRTVAEnvalpleiAGvpkaeirkrVAELL----ELVGLSDKadayP-SQLSGG 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 2697035156 134 EWQRV---RIVAAflqvwdkqqcEGKFILLDEPTNNLD 168
Cdd:COG1135 145 QKQRVgiaRALAN----------NPKVLLCDEATSALD 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-167 |
2.01e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEqIH-ILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRQYH---IAQLSQQR 77
Cdd:PRK09700 6 ISMAGIGKSfgpvHALKSVNLTVYPGE-IHaLLGENGAGKSTLMKVLSGiHEPTKGTITINNINYNKLDhklAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 78 AYlsQLVSYIPILKVFQ--YVGLFSPNTVFSAGV----FERLCSDFQLTSL-----LSKPINQLSGGEWQRVRIVAAFLq 146
Cdd:PRK09700 85 IY--QELSVIDELTVLEnlYIGRHLTKKVCGVNIidwrEMRVRAAMMLLRVglkvdLDEKVANLSISHKQMLEIAKTLM- 161
|
170 180
....*....|....*....|.
gi 2697035156 147 vwdkqqCEGKFILLDEPTNNL 167
Cdd:PRK09700 162 ------LDAKVIIMDEPTSSL 176
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-221 |
2.34e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 123 LSKPINQLSGGEWQRVRIvAAFLQVWDKqqceGK-FILLDEPTNNL---DIIQ-----QAMLDKwikyfcdclG-TVIMS 192
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKL-AKELSKRST----GRtLYILDEPTTGLhfdDIKKllevlQRLVDK---------GnTVVVI 888
|
90 100 110
....*....|....*....|....*....|....*
gi 2697035156 193 GHDLsHSYKNASCIWMI------KQGQLVAVGKPE 221
Cdd:TIGR00630 889 EHNL-DVIKTADYIIDLgpeggdGGGTVVASGTPE 922
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-77 |
2.39e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 2.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQR 77
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLaPDAGEVHYRMRDGQLRDLYALSEAE 82
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-203 |
2.79e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 16 TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSqqraYLSQLVSYIPILKVFQ 94
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNINNIAKPYCT----YIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 95 YVGLFSpNTVFSAGVFERLCSDFQLTSLLSKPINQLSGGeWQRVRIVAAFLqvwdkqQCEGKFILLDEPTNNLDIIQQAM 174
Cdd:PRK13541 90 NLKFWS-EIYNSAETLYAAIHYFKLHDLLDEKCYSLSSG-MQKIVAIARLI------ACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|....*....
gi 2697035156 175 LDKWIKYFCDCLGTVIMSGHdLSHSYKNA 203
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH-LESSIKSA 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
4.51e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGRSIRQYHIAQLSQQraYLSQLVSYIPILK----- 91
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlPDTGTIEWIFKDEKNKKKTKEKEK--VLEKLVIQKTRFKkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 92 ---------VFQYV--GLFSP----NTVF---SAGV-----FERLCSDFQLTSL----LSKPINQLSGGEWQRVRIvAAF 144
Cdd:PRK13651 101 keirrrvgvVFQFAeyQLFEQtiekDIIFgpvSMGVskeeaKKRAAKYIELVGLdesyLQRSPFELSGGQKRRVAL-AGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 145 LQVwdkqqcEGKFILLDEPTNNLDII-QQAMLDkwIKYFCDCLG-TVIMSGHDLSHSYKNASCIWMIKQGQLVAVGKpec 222
Cdd:PRK13651 180 LAM------EPDFLVFDEPTAGLDPQgVKEILE--IFDNLNKQGkTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD--- 248
|
250
....*....|....*...
gi 2697035156 223 imTEKNLSDI-FMSEIKL 239
Cdd:PRK13651 249 --TYDILSDNkFLIENNM 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-76 |
4.59e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITI---DTRLVN-VSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG--GDILIGGR---------SIRQyHIA 71
Cdd:PRK10938 261 IVLNNGVVsynDRPILHnLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysNDLTLFGRrrgsgetiwDIKK-HIG 339
|
....*
gi 2697035156 72 QLSQQ 76
Cdd:PRK10938 340 YVSSS 344
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-162 |
4.82e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIrqyhiaQLSQQRAYLSQLVSyipilkVFQYVGLF------- 99
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILLDGKPV------TAEQPEDYRKLFSA------VFTDFHLFdqllgpe 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 100 --SPNTVFSAGVFERL-------CSDFQLTSLlskpinQLSGGEWQRVRIVAAFLQVWDkqqcegkFILLDE 162
Cdd:PRK10522 417 gkPANPALVEKWLERLkmahkleLEDGRISNL------KLSKGQKKRLALLLALAEERD-------ILLLDE 475
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-223 |
5.19e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQLS--QQRAYLSQLVSYIpilkvFQYvG 97
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISekERRNLVGAEVAMI-----FQD-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 LFSPNTVFSAG--VFE------------RLCSDFQLTSLLSKP---------INQLSGGEWQRVRIVAAFlqvwdkqQCE 154
Cdd:PRK11022 99 MTSLNPCYTVGfqIMEaikvhqggnkktRRQRAIDLLNQVGIPdpasrldvyPHQLSGGMSQRVMIAMAI-------ACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2697035156 155 GKFILLDEPTNNLDIIQQA-----MLDKWIKyfcDCLGTVIMSgHDLSHSYKNASCIWMIKQGQLVAVGKPECI 223
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAqiielLLELQQK---ENMALVLIT-HDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-169 |
7.17e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 28 GEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSIRQyhiAQLSQQRAYLSQLVSYIPILKVFQyvglfspNTVFS 106
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATR---GDRSRFMAYLGHLPGLKADLSTLE-------NLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2697035156 107 AGVFERLCSDFQ--------LTSLLSKPINQLSGGEWQRVrivaAFLQVWdkqQCEGKFILLDEPTNNLDI 169
Cdd:PRK13543 107 CGLHGRRAKQMPgsalaivgLAGYEDTLVRQLSAGQKKRL----ALARLW---LSPAPLWLLDEPYANLDL 170
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-92 |
8.46e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.23 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 4 KLIIDIKNI--TIDTR------LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG---GDILIGGRSIRQYhiaq 72
Cdd:cd03232 1 GSVLTWKNLnyTVPVKggkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvitGEILINGRPLDKN---- 76
|
90 100
....*....|....*....|
gi 2697035156 73 LSQQRAYLSQLVSYIPILKV 92
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNLTV 96
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-233 |
8.60e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.85 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 25 VLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQyHIAQLSQQRAYLSQLVSYIPILKVFQYVGLFSPNT 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVtSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 104 VFSAGVFERLcSDFQLTSL-LSKPINQL----SGGEWQRVRIVAAFLqvwdkqQCEgKFILLDEPTNNLDIIQQAMLdkW 178
Cdd:TIGR01257 2041 GVPAEEIEKV-ANWSIQSLgLSLYADRLagtySGGNKRKLSTAIALI------GCP-PLVLLDEPTTGMDPQARRML--W 2110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 179 ikyfcDCLGTVIMSGHDL---SHSYKnaSCIWMIKQGQLVAVGKPECIMTEKNLSDIF 233
Cdd:TIGR01257 2111 -----NTIVSIIREGRAVvltSHSME--ECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-176 |
9.01e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITID-----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQLSQQRay 79
Cdd:COG3845 257 VLEVENLSVRddrgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPaSGSIRLDGEDITGLSPRERRRLG-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 80 lsqlVSYIP------------------ILKvFQYVGLFSPNTVFSAGVF----ERLCSDFQL-TSLLSKPINQLSGGEWQ 136
Cdd:COG3845 335 ----VAYIPedrlgrglvpdmsvaenlILG-RYRRPPFSRGGFLDRKAIrafaEELIEEFDVrTPGPDTPARSLSGGNQQ 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2697035156 137 RVrIVA-AFLQvwdkqqcEGKFILLDEPTNNLDI-----IQQAMLD 176
Cdd:COG3845 410 KV-ILArELSR-------DPKLLIAAQPTRGLDVgaiefIHQRLLE 447
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
124-229 |
1.28e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 124 SKPINqLSGGEWQRVRIvAAFLQVwdkqqcEGKFILLDEPTNNLD---------IIQQAMLDKWIkyfcdclgTVIMSGH 194
Cdd:PRK13640 139 SEPAN-LSGGQKQRVAI-AGILAV------EPKIIILDESTSMLDpagkeqilkLIRKLKKKNNL--------TVISITH 202
|
90 100 110
....*....|....*....|....*....|....*
gi 2697035156 195 DLSHSyKNASCIWMIKQGQLVAVGKPECIMTEKNL 229
Cdd:PRK13640 203 DIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
126-195 |
2.29e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 126 PINQLSGGEWQRVRIVAAFLQVWDkqqcegkFILLDEPTNNLDIIQQAMLDKWIKYFcdcLGTVIMSGHD 195
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPD-------MLLLDEPTNHLDAESVAWLEQFLHDY---PGTVVAVTHD 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-78 |
2.84e-04 |
|
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: 41.73 E-value: 2.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG-YLPVGGDILIGGRSIRqyHIAQLSQQRA 78
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfYDVTSGRILIDGQDIR--DVTQASLRAA 433
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
126-228 |
4.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 126 PINQLSGGEWQRVRIvAAFLQvwdKQQCEGKFILLDEPTNNL---DIIQ-----QAMLDKwikyfcdclG-TVIMSGHDL 196
Cdd:COG0178 823 PATTLSGGEAQRVKL-ASELS---KRSTGKTLYILDEPTTGLhfhDIRKllevlHRLVDK---------GnTVVVIEHNL 889
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2697035156 197 ShsyknasciwMIKQ---------------GQLVAVGKPECIMTEKN 228
Cdd:COG0178 890 D----------VIKTadwiidlgpeggdggGEIVAEGTPEEVAKVKA 926
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-221 |
4.06e-04 |
|
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: 41.33 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITID----TRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISG---YLPVGGDIL-----------------IG- 61
Cdd:TIGR03269 1 IEVKNLTKKfdgkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIIyhvalcekcgyverpskVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 62 -----GRSIRQYHIAQLSQQRAYLSQLVSYIPILkvFQYV-GLFSPNTVF----------------SAGVFERLCSDFQL 119
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLSDKLRRRIRKRIAIM--LQRTfALYGDDTVLdnvlealeeigyegkeAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 120 TSLLSKPINQLSGGEWQRVrivaaflqVWDKQQCEGKFILL-DEPTNNLD-----IIQQAMLDKWIKYFCdclgTVIMSG 193
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRV--------VLARQLAKEPFLFLaDEPTGTLDpqtakLVHNALEEAVKASGI----SMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 2697035156 194 H------DLSHsyknaSCIWmIKQGQLVAVGKPE 221
Cdd:TIGR03269 227 HwpevieDLSD-----KAIW-LENGEIKEEGTPD 254
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-174 |
4.72e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 7 IDIKNITIDTR-----LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG-GDILIGGRSIRQYHIAQLSQQRAYL 80
Cdd:PRK10790 341 IDIDNVSFAYRddnlvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 SQlvsyIPIL---KVFQYVGL---FSPNTVFSA------GVFERLCSDfQLTSLLSKPINQLSGGEWQRVRIVAAFLQVw 148
Cdd:PRK10790 421 QQ----DPVVladTFLANVTLgrdISEEQVWQAletvqlAELARSLPD-GLYTPLGEQGNNLSVGQKQLLALARVLVQT- 494
|
170 180 190
....*....|....*....|....*....|.
gi 2697035156 149 dkqqceGKFILLDEPTNNLD-----IIQQAM 174
Cdd:PRK10790 495 ------PQILILDEATANIDsgteqAIQQAL 519
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-176 |
5.02e-04 |
|
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: 40.82 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 1 MENKLIIDIKNITID-------TRLV-NVSAQVLTGEQIHILGANGAGKS-TLLAAIsGYLP-----VGGDILIGGRSIR 66
Cdd:COG4172 1 MMSMPLLSVEDLSVAfgqgggtVEAVkGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPdpaahPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 67 QYHIAQLSQQRAylsQLVSYIpilkvFQyvglfSP----NTVFSAG--VFERLCSDFQLT---------SLLS------- 124
Cdd:COG4172 80 GLSERELRRIRG---NRIAMI-----FQ-----EPmtslNPLHTIGkqIAEVLRLHRGLSgaaararalELLErvgipdp 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 125 -KPIN----QLSGGEWQRVRIVAAFLqvwdkqqCEGKFILLDEPTNNLDI-IQQAMLD 176
Cdd:COG4172 147 eRRLDayphQLSGGQRQRVMIAMALA-------NEPDLLIADEPTTALDVtVQAQILD 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-83 |
5.15e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 5.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVG----GDILIGGRSIR---QYHIAQLSQQRAYLSQL 83
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGvitgGDRLVNGRPLDssfQRSIGYVQQQDLHLPTS 851
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-180 |
6.67e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 40.02 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 3 NKLI--IDIKNITI--DTR--LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSirQYHIAQLSQQ 76
Cdd:PRK14258 2 SKLIpaIKVNNLSFyyDTQkiLEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRV--EFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 77 RAYLSQLVSYIPIlkVFQYVGLFsPNTVFSA-----------------GVFERLCSDFQL----TSLLSKPINQLSGGEW 135
Cdd:PRK14258 80 RVNLNRLRRQVSM--VHPKPNLF-PMSVYDNvaygvkivgwrpkleidDIVESALKDADLwdeiKHKIHKSALDLSGGQQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2697035156 136 QRVRIVAAFlqvwdkqQCEGKFILLDEPTNNLDIIQQAMLDKWIK 180
Cdd:PRK14258 157 QRLCIARAL-------AVKPKVLLMDEPCFGLDPIASMKVESLIQ 194
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-53 |
1.12e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|....
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP 53
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-225 |
1.36e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 25 VLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRSIRQYHIAQlsqqrayLSQLVSYIPilkvfQYVGLFSPNT 103
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELeKGRIMIDDCDVAKFGLTD-------LRRVLSIIP-----QSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 104 VFS---------AGVFERL----------CSDFQLTSLLSKPINQLSGGEWQRVRIVAAFLQvwdkqqcEGKFILLDEPT 164
Cdd:PLN03232 1327 RFNidpfsehndADLWEALerahikdvidRNPFGLDAEVSEGGENFSVGQRQLLSLARALLR-------RSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 165 NNLDIIQQAMLDKWIK-YFCDClgTVIMSGHDLShSYKNASCIWMIKQGQLVAVGKPECIMT 225
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIReEFKSC--TMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-63 |
1.53e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.00 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2697035156 20 NVSAQVLTGEQIHILGANGAGKSTLLAAISGYL-PVGGDILIGGR 63
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDH 75
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
123-220 |
1.59e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 123 LSKPINQLSGGEWQRVRIvAAFLQvwdKQQCEGKFILLDEPTNNL---DIiqQAMLDKwIKYFCDCLGTVIMSGHDLsHS 199
Cdd:cd03271 163 LGQPATTLSGGEAQRIKL-AKELS---KRSTGKTLYILDEPTTGLhfhDV--KKLLEV-LQRLVDKGNTVVVIEHNL-DV 234
|
90 100
....*....|....*....|....*....
gi 2697035156 200 YKNASciWMI--------KQGQLVAVGKP 220
Cdd:cd03271 235 IKCAD--WIIdlgpeggdGGGQVVASGTP 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-169 |
1.90e-03 |
|
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: 39.04 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 17 RLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLP--VGGDILIGGR---------SIRQyHIAQLSQQRaylsQLVS 85
Cdd:TIGR02633 275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKpvdirnpaqAIRA-GIAMVPEDR----KRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 86 YIPILKVFQYVGL-----FSPNTVFSAGVfERLCSDFQLTSLLSK------PINQLSGGEWQRVrIVAAFLQVwdkqqcE 154
Cdd:TIGR02633 350 IVPILGVGKNITLsvlksFCFKMRIDAAA-ELQIIGSAIQRLKVKtaspflPIGRLSGGNQQKA-VLAKMLLT------N 421
|
170
....*....|....*
gi 2697035156 155 GKFILLDEPTNNLDI 169
Cdd:TIGR02633 422 PRVLILDEPTRGVDV 436
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-176 |
2.66e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.22 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIrqYHIAQLSQQRAYLSQLVSYIPIlkVFQYVG 97
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIV--YNGHNIYSPRTDTVDLRKEIGM--VFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 98 LFsPNTVFS--------AGVFERLCSDFQL-TSLLSKPINQ------------LSGGEWQRVrIVAAFLQVwdkqqcEGK 156
Cdd:PRK14239 97 PF-PMSIYEnvvyglrlKGIKDKQVLDEAVeKSLKGASIWDevkdrlhdsalgLSGGQQQRV-CIARVLAT------SPK 168
|
170 180
....*....|....*....|
gi 2697035156 157 FILLDEPTNNLDIIQQAMLD 176
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIE 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-169 |
3.17e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 17 RLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPvG---GDILIGGR--SIR------QYHIAQLSQQRaylsQLVS 85
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-GrweGEIFIDGKpvKIRnpqqaiAQGIAMVPEDR----KRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 86 YIPILKVFQYVGLFSPNTVFSAGVF----ERLCSDFQLTSLLSK------PINQLSGGEWQRVrIVAAFLQVwdkqqcEG 155
Cdd:PRK13549 352 IVPVMGVGKNITLAALDRFTGGSRIddaaELKTILESIQRLKVKtaspelAIARLSGGNQQKA-VLAKCLLL------NP 424
|
170
....*....|....
gi 2697035156 156 KFILLDEPTNNLDI 169
Cdd:PRK13549 425 KILILDEPTRGIDV 438
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
6-174 |
3.78e-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: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 6 IIDIKNITIDT----RLVN-VSAQVLTGEQIHILGANGAGKSTLLAAISGYLPVGGDILIGGRSIRQYHIAQlsqqRAYL 80
Cdd:TIGR00954 451 GIKFENIPLVTpngdVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ----RPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 81 S-----QLVSYIPILKVFQYVGlfspntvFSAGVFERLCSDFQLTSLLSKPI---------NQLSGGEWQRVRIVAAFLQ 146
Cdd:TIGR00954 527 TlgtlrDQIIYPDSSEDMKRRG-------LSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYH 599
|
170 180
....*....|....*....|....*....
gi 2697035156 147 vwdkqqcEGKFILLDEPTNNLDI-IQQAM 174
Cdd:TIGR00954 600 -------KPQFAILDECTSAVSVdVEGYM 621
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-180 |
5.09e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV--GGDILIGGRSirqyhiaqlsqqrAYLSQlVSYIPILKVFQY 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVVIRGTV-------------AYVPQ-VSWIFNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2697035156 96 VGLFSPntvFSAGVFER------LCSDFQL------TSLLSKPINqLSGGEWQRVRIVAAFLQVWDkqqcegkFILLDEP 163
Cdd:PLN03130 699 ILFGSP---FDPERYERaidvtaLQHDLDLlpggdlTEIGERGVN-ISGGQKQRVSMARAVYSNSD-------VYIFDDP 767
|
170
....*....|....*...
gi 2697035156 164 TNNLDI-IQQAMLDKWIK 180
Cdd:PLN03130 768 LSALDAhVGRQVFDKCIK 785
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-86 |
7.13e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.20 E-value: 7.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2697035156 27 TGEQIHILGANGAGKSTLLAAISGYL--PVGGDILIGGRSIRQYHIAQLSQQRAYLSQLVSY 86
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS 62
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-76 |
7.66e-03 |
|
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: 36.68 E-value: 7.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2697035156 10 KNITIDTRLVNVSAQVLTGEQIHILGANGAGKSTLLAAISGYLPV-GGDILIGGRsirqyhIAQLSQQ 76
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKlSGSVSVPGS------IAYVSQE 74
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-62 |
8.59e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.18 E-value: 8.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLLAAISGY-LPVGGDILIGG 62
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKG 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-45 |
8.63e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.02 E-value: 8.63e-03
10 20
....*....|....*....|....*...
gi 2697035156 18 LVNVSAQVLTGEQIHILGANGAGKSTLL 45
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLL 50
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-67 |
9.73e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 36.69 E-value: 9.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2697035156 6 IIDIKNITIDTR----LVNVSAQVLTGEQIHILGANGAGKSTLLAAISG---YLPVGGDILIGGRSIRQ 67
Cdd:PRK09580 1 MLSIKDLHVSVEdkaiLRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTGGTVEFKGKDLLE 69
|
|
| |
