|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-234 |
4.14e-73 |
|
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: 222.21 E-value: 4.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV-RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT-QADRSQLAKHVGLM 91
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LALqisEPATLL 168
Cdd:COG1122 81 FQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagvLAM---EPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 169 LDEPFASLDLLSQARLA---AQLEDSGHQILVSTHLLEHVYG-FERVLWLEQGRVRADGPGREICEAYAE 234
Cdd:COG1122 158 LDEPTAGLDPRGRRELLellKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
24-218 |
1.26e-53 |
|
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: 171.88 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS-QLAKHVGLMFQNPDDQIIF 101
Cdd:cd03225 11 DGARPALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLVFQNPDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 PTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQ 181
Cdd:cd03225 91 PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 182 ARLAA---QLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGR 218
Cdd:cd03225 171 RELLEllkKLKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-236 |
1.46e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQ 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIfGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPddqIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL-LALqISEPATLLLD 170
Cdd:COG1131 81 EP---ALYPdlTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLaLAL-LHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 171 EPFASLDLLSQARLAAQLE---DSGHQILVSTHLLEHV-YGFERVLWLEQGRVRADGPGREICEAYAEDV 236
Cdd:COG1131 157 EPTSGLDPEARRELWELLRelaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEDV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
25-240 |
5.41e-43 |
|
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: 145.77 E-value: 5.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMfqnPDDQIIFP- 102
Cdd:COG4555 12 GKVPALKDVSFTAKDGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL---PDERGLYDr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 -TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQ 181
Cdd:COG4555 89 lTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 182 A---RLAAQLEDSGHQILVSTH---LLEHVygFERVLWLEQGRVRADGPGREICEAYAEDVRERA 240
Cdd:COG4555 169 RllrEILRALKKEGKTVLFSSHimqEVEAL--CDRVVILHKGKVVAQGSLDELREEIGEENLEDA 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-231 |
1.24e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLM 91
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIAsgEL-VALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQNPDdqiIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LAlqiSEPAT 166
Cdd:COG1118 81 FQHYA---LFPhmTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALaraLA---VEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 167 LLLDEPFASLDllsqARLAAQLE--------DSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEA 231
Cdd:COG1118 155 LLLDEPFGALD----AKVRKELRrwlrrlhdELGGTTVFVTHDQEEALELaDRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-228 |
3.43e-40 |
|
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: 139.02 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGLMF 92
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPddQIIFP-TVAEELAFSLTAR----GETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LAlQisEP 164
Cdd:COG1120 82 QEP--PAPFGlTVRELVALGRYPHlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIaraLA-Q--EP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 165 ATLLLDEPFASLDLLSQARLAAQL----EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLrrlaRERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-218 |
1.73e-38 |
|
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: 132.99 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQ 93
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEAlALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPDdqiIFP--TVAEELAFSLTARGetRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:COG4133 83 ADG---LKPelTVRENLRFWAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2539771384 172 PFASLDLLSQARLAAQLED---SGHQILVSTHlLEHVYGFERVLWLEQGR 218
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhlaRGGAVLLTTH-QPLELAAARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-237 |
8.16e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 8.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 11 SSHSIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRsqlaKHV 88
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPpgEF-VAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNPDDQIIFP-TVAEELAFSLTAR----GETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL-LALqIS 162
Cdd:COG1121 78 GYVPQRAEVDWDFPiTVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLaRAL-AQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 163 EPATLLLDEPFASLDLLSQARLAAQLE---DSGHQILVSTHLLEHVYG-FERVLWLEQGRVrADGPGRE------ICEAY 232
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEEvltpenLSRAY 235
|
....*
gi 2539771384 233 AEDVR 237
Cdd:COG1121 236 GGPVA 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-223 |
3.43e-37 |
|
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: 129.95 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQ 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPddqIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqISEPATLLLD 170
Cdd:cd03259 80 DY---ALFPhlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALArAL-AREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 171 EPFASLDLLSQARLAAQLEDSGHQ-----ILVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElgittIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-228 |
3.55e-37 |
|
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: 136.57 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPK---QGRVVVHGCD-TQADRSQLAKHV 88
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETvALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDlLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:COG1123 86 GMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 169 LDEPFASLDLLSQARLAAQL----EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLrelqRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-231 |
3.58e-36 |
|
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: 133.88 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT----QADRSQLAKHVGLMFQNPDDQ 98
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETlGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLRELRRRVQMVFQDPYSS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 99 iIFP--TVAEELAFSLTARGE-TRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCL---LALqisEPATLLLDE 171
Cdd:COG1123 355 -LNPrmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIaraLAL---EPKLLILDE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 172 PFASLDLLSQARLAAQLED----SGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEA 231
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDlqreLGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-222 |
4.61e-35 |
|
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: 124.51 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV----RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqADRSQLAKHVG 89
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFvALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNPddqIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqISEPAT 166
Cdd:cd03293 77 YVFQQD---ALLPwlTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALArAL-AVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 167 LLLDEPFASLDLLS----QARLAAQLEDSGHQILVSTH-LLEHVYGFERVLWLEQ--GRVRAD 222
Cdd:cd03293 153 LLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHdIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-190 |
6.98e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.20 E-value: 6.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 9 TVSSHSIRLDAVTLV----RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqADRSQ 83
Cdd:COG1116 2 SAAAPALELRGVSKRfptgGGGVTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAKHVGLMFQNPDdqiIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALq 160
Cdd:COG1116 78 PGPDRGVVFQEPA---LLPwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIArAL- 153
|
170 180 190
....*....|....*....|....*....|
gi 2539771384 161 ISEPATLLLDEPFASLDLLSQARLAAQLED 190
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLR 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-223 |
1.05e-34 |
|
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: 123.54 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQlakHVGLMfq 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIfGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN---RIGYL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 nPDDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:cd03269 76 -PEERGLYPkmKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 172 PFASLDLLSQ---ARLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03269 155 PFSGLDPVNVellKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-219 |
1.17e-33 |
|
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: 119.42 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQ 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIyGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPDdqiIFPTvaeelafsLTARgetrqaarqqarEFLarrgleawagravsELSQGQRQQVCL-LALqISEPATLLLDEP 172
Cdd:cd03230 81 EPS---LYEN--------LTVR------------ENL--------------KLSGGMKQRLALaQAL-LHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 173 FASLDLLSQAR---LAAQLEDSGHQILVSTHLLEHV-YGFERVLWLEQGRV 219
Cdd:cd03230 123 TSGLDPESRREfweLLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
29-200 |
2.62e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 119.06 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 29 VFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLA---KHVGLMFQNPDDQIIFPTV 104
Cdd:TIGR01166 7 VLKGLNFAAERgEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLerrQRVGLVFQDPDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 105 AEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARL 184
Cdd:TIGR01166 87 DQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQM 166
|
170
....*....|....*....
gi 2539771384 185 AA---QLEDSGHQILVSTH 200
Cdd:TIGR01166 167 LAilrRLRAEGMTVVISTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-223 |
1.57e-32 |
|
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: 117.78 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQL-----AKHVGLMFQNpddQIIFP--TVA 105
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQ---YALFPhlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 106 EELAFSLtaRGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLA 185
Cdd:cd03297 94 ENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2539771384 186 AQLED-----SGHQILVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:cd03297 172 PELKQikknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-233 |
1.78e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.83 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtQADRSQLAKHVGLMf 92
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRIGYL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 qnPDDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLD 170
Cdd:COG4152 77 --PEERGLYPkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 171 EPFASLD-----LLSQARLaaQLEDSGHQILVSTHLLEHVygfER----VLWLEQGRVRADGPGREICEAYA 233
Cdd:COG4152 155 EPFSGLDpvnveLLKDVIR--ELAAKGTTVIFSSHQMELV---EElcdrIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-223 |
2.18e-32 |
|
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: 117.63 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 16 RLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRsqlaKHVGLMFQN 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFlAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDDQIIFP-TVAEELAFSLTAR----GETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVcLLALQI-SEPATLL 168
Cdd:cd03235 77 RSIDRDFPiSVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV-LLARALvQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 169 LDEPFASLDLLSQA---RLAAQLEDSGHQILVSTHLLEHVYG-FERVLWLEqGRVRADG 223
Cdd:cd03235 156 LDEPFAGVDPKTQEdiyELLRELRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-225 |
2.82e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV-RGSRTVFEGLTLDLQ--EMRIgLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK---H 87
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEkgEFVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 88 VGLMFQnpdDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqISEP 164
Cdd:COG2884 81 IGVVFQ---DFRLLPdrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIArAL-VNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 165 ATLLLDEPFASLD-LLSQ--ARLAAQLEDSGHQILVSTH---LLEHVYGfeRVLWLEQGRVRADGPG 225
Cdd:COG2884 157 ELLLADEPTGNLDpETSWeiMELLEEINRRGTTVLIATHdleLVDRMPK--RVLELEDGRLVRDEAR 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-222 |
5.82e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.68 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGS----RTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK- 86
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEagEF-VAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDiSSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 87 ---HVGLMFQNPDdqiIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALq 160
Cdd:COG1136 84 rrrHIGFVFQFFN---LLPelTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIArAL- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 161 ISEPATLLLDEPFASLDLLSQARLAAQL----EDSGHQILVSTH---LLEHvygFERVLWLEQGRVRAD 222
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLrelnRELGTTIVMVTHdpeLAAR---ADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-189 |
2.39e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 11 SSHSIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA----DRsql 84
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEpgEF-VALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppeKR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 85 akHVGLMFQNPDdqiIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LAL 159
Cdd:COG3842 78 --NVGMVFQDYA---LFPhlTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALaraLAP 152
|
170 180 190
....*....|....*....|....*....|
gi 2539771384 160 qisEPATLLLDEPFASLDLlsQARLAAQLE 189
Cdd:COG3842 153 ---EPRVLLLDEPLSALDA--KLREEMREE 177
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-223 |
3.85e-31 |
|
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: 114.21 E-value: 3.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQN 94
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDdqiIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEP 172
Cdd:cd03264 81 FG---VYPnfTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 173 FASLDLLSQARLAAQLED--SGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03264 158 TAGLDPEERIRFRNLLSElgEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-228 |
9.46e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 9.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDL-QEMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDDQIIF 101
Cdd:PRK13652 14 SGSKEALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPiTKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 PTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQ 181
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 182 ARLAAQLED----SGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13652 174 KELIDFLNDlpetYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
39-228 |
1.78e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 39 EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLA---KHVGLMFQNPDDQIIFPTVAEELAFSLTAR 115
Cdd:PRK13639 29 EM-VALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrKTVGIVFQNPDDQLFAPTVEEDVAFGPLNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 116 GETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLL--SQ-ARLAAQLEDSG 192
Cdd:PRK13639 108 GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMgaSQiMKLLYDLNKEG 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 2539771384 193 HQILVSTHL--LEHVYGfERVLWLEQGRVRADGPGREI 228
Cdd:PRK13639 188 ITIIISTHDvdLVPVYA-DKVYVMSDGKIIKEGTPKEV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-227 |
2.50e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGL 90
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRpgEV-VAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 MFQNPddQIIFP-TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQV------CLLALQISE 163
Cdd:PRK13548 81 LPQHS--SLSFPfTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVqlarvlAQLWEPDGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 164 PATLLLDEPFASLDLLSQ---ARLAAQL-EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGRE 227
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQhhvLRLARQLaHERGLAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTPAE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-228 |
3.71e-30 |
|
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: 112.21 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADRSQLAKHVG 89
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEIlAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNP---DDQiifpTVAEELAFSL---TARGETRQaaRQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LALq 160
Cdd:cd03261 81 MLFQSGalfDSL----TVFENVAFPLrehTRLSEEEI--REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALaraLAL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 161 isEPATLLLDEPFASLDLLSQ---ARLAAQLEDS-GHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:cd03261 154 --DPELLLYDEPTAGLDPIASgviDDLIRSLKKElGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-224 |
3.84e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMF 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELtAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPddQIIFP-TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LAlQISEPAT-- 166
Cdd:COG4559 82 QHS--SLAFPfTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLarvLA-QLWEPVDgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 167 ---LLLDEPFASLDLLSQ---ARLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGP 224
Cdd:COG4559 159 prwLFLDEPTSALDLAHQhavLRLARQLARRGGGVVAVLHDLNLAAQYaDRILLLHQGRLVAQGT 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-219 |
5.33e-30 |
|
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: 111.43 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV--RGSRTVF--EGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLA-- 85
Cdd:cd03255 1 IELKNLSKTygGGGEKVQalKGVSLSIEkgEF-VAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSEKELAaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 86 --KHVGLMFQNPddQII-FPTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqI 161
Cdd:cd03255 80 rrRHIGFVFQSF--NLLpDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIArAL-A 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 162 SEPATLLLDEPFASLDLLSQAR----LAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-231 |
8.20e-30 |
|
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: 111.82 E-value: 8.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGS----RTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHV 88
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPgESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNPDDqIIFP--TVAEELAFSLTARGETRQAARqqAREFLARRGL-EAWAGRAVSELSQGQRQQVCLL-ALqISEP 164
Cdd:COG1124 82 QMVFQDPYA-SLHPrhTVDRILAEPLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIArAL-ILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 165 ATLLLDEPFASLDLLSQARLAAQLEDSGHQ-----ILVStHLLEHVYGF-ERVLWLEQGRVRADGPGREICEA 231
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErgltyLFVS-HDLAVVAHLcDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-223 |
9.49e-30 |
|
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: 109.45 E-value: 9.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 16 RLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGLMFQ 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIvGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NpddqiifptvaeelafsltargetrqaarqqarefLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:cd03214 81 A-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 174 ASLDLLSQARLAAQL----EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03214 126 SHLDIAHQIELLELLrrlaRERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
42-223 |
1.31e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.00 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLA---KHVGLMFQNPDDQIIFPTVAEELAFSLTARGET 118
Cdd:PRK13644 31 IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT-GDFSKLQgirKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 119 RQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA---RLAAQLEDSGHQI 195
Cdd:PRK13644 110 PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIavlERIKKLHEKGKTI 189
|
170 180
....*....|....*....|....*...
gi 2539771384 196 LVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:PRK13644 190 VYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-219 |
1.41e-29 |
|
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: 110.04 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdTQADRSQLAKHVGLMFQNPDDQIIFP 102
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIiALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERRKSIGYVMQDVDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 TVAEELAFSLTARGetrqAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA 182
Cdd:cd03226 88 SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 183 RLAA---QLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRV 219
Cdd:cd03226 164 RVGElirELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-228 |
2.95e-29 |
|
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: 115.32 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLV--RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVG 89
Cdd:COG2274 473 DIELENVSFRypGDSPPVLDNISLTIKPgERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQnpDDQIIFPTVAEELAFSLTARGETR--QAARQ-QAREFLARR--GLEAWAGRAVSELSQGQRQQVCLL-ALqISE 163
Cdd:COG2274 553 VVLQ--DVFLFSGTIRENITLGDPDATDEEiiEAARLaGLHDFIEALpmGYDTVVGEGGSNLSGGQRQRLAIArAL-LRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 164 PATLLLDEPFASLDLLSQARLAAQLEDSGHQ--ILVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-228 |
3.91e-29 |
|
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: 109.45 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 28 TVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKH-VGLMFQNPDdqiIFP-- 102
Cdd:cd03219 14 VALDDVSFSVRPGEIhGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDiTGLPPHEIARLgIGRTFQIPR---LFPel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 TVAEEL----------AFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL-LALqISEPATLLLDE 171
Cdd:cd03219 91 TVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIaRAL-ATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 172 PFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:cd03219 170 PAAGLNPEETEELAElirELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-174 |
4.46e-29 |
|
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: 106.96 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 30 FEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDdqiIFP--TVA 105
Cdd:pfam00005 1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQ---LFPrlTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 106 EELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAV----SELSQGQRQQVCLLALQISEPATLLLDEPFA 174
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-228 |
7.53e-29 |
|
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: 109.02 E-value: 7.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVV-VHGCDT-QADRSQLAKHVGLM 91
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPgEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRgGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 fqNPDDQIIFP--TVAEEL---AF--SLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVcLL--ALqIS 162
Cdd:COG1119 84 --SPALQLRFPrdETVLDVvlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV-LIarAL-VK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 163 EPATLLLDEPFASLDLLSQARLAAQLEDSGHQ-----ILVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEgaptlVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-223 |
1.06e-27 |
|
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: 105.53 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVT----LVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVG 89
Cdd:cd03266 2 ITADALTkrfrDVKKTVQAVDGVSFTVKPGEVtGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMfqnPDDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATL 167
Cdd:cd03266 82 FV---SDSTGLYDrlTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 168 LLDEPFASLDLLSQARL---AAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03266 159 LLDEPTTGLDVMATRALrefIRQLRALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-223 |
1.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 31 EGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDDQIIFPTVAEEL 108
Cdd:PRK13647 22 KGLSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSKVGLVFQDPDDQVFSSTVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 109 AFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAA-- 186
Cdd:PRK13647 102 AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEil 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2539771384 187 -QLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:PRK13647 182 dRLHNQGKTVIVATHDVDLAAEWaDQVIVLKEGRVLAEG 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-188 |
3.51e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ----ADRsqlakH 87
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEdgEF-LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppKDR-----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 88 VGLMFQNPddqIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL-LALqISEP 164
Cdd:COG3839 77 IAMVFQSY---ALYPhmTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALgRAL-VREP 152
|
170 180
....*....|....*....|....
gi 2539771384 165 ATLLLDEPFASLDllsqARLAAQL 188
Cdd:COG3839 153 KVFLLDEPLSNLD----AKLRVEM 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-218 |
4.20e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.94 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 20 VTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQnpdd 97
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIvALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 98 qiifptvaeelafsltargetrqaarqqareflarrgleawagravseLSQGQRQQVCLLALQISEPATLLLDEPFASLD 177
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2539771384 178 LLSQARLAA---QLEDSGHQILVSTHLLEHV-YGFERVLWLEQGR 218
Cdd:cd00267 113 PASRERLLEllrELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
41-223 |
4.49e-27 |
|
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: 103.82 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPddQIIFPTVAEELAFSLTARGETR 119
Cdd:cd03245 32 KVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLDPADLRRNIGYVPQDV--TLFYGTLRDNITLGAPLADDER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 --QAARQQ-AREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED--SG 192
Cdd:cd03245 110 ilRAAELAgVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGD 189
|
170 180 190
....*....|....*....|....*....|....
gi 2539771384 193 HQILVSTH---LLEHVygfERVLWLEQGRVRADG 223
Cdd:cd03245 190 KTLIIITHrpsLLDLV---DRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-228 |
6.57e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI------GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-----DRS 82
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGRALFDVNLTIedgsytAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 83 QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQI 161
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 162 SEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTlfkKLHQSGMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-229 |
7.41e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 103.35 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQnpdDQIIFP 102
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIfGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQ---FDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 --TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL-LALqISEPATLLLDEPFASLDLL 179
Cdd:cd03263 89 elTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLaIAL-IGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 180 SQARLAAQLEDSGHQ--ILVSTHLLEHVygfE----RVLWLEQGRVRADGPGREIC 229
Cdd:cd03263 168 SRRAIWDLILEVRKGrsIILTTHSMDEA---EalcdRIAIMSDGKLRCIGSPQELK 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-231 |
1.41e-26 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 107.64 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 12 SHSIRLDAVTLV--RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKH 87
Cdd:TIGR03375 461 QGEIEFRNVSFAypGQETPALDNVSLTIRPgEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDiRQIDPADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 88 VGLMFQNPddQIIFPTVAEELAFSLTARGETR--QAARQQAREFLARR---GLEawagRAVSE----LSQGQRQQVCLLA 158
Cdd:TIGR03375 541 IGYVPQDP--RLFYGTLRDNIALGAPYADDEEilRAAELAGVTEFVRRhpdGLD----MQIGErgrsLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 159 LQISEPATLLLDEPFASLDLLSQARLAAQLED--SGHQILVSTH---LLEHVygfERVLWLEQGRVRADGPGREICEA 231
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRwlAGKTLVLVTHrtsLLDLV---DRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-223 |
2.32e-26 |
|
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: 102.20 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADRSQLAKHVGLMFQNPD-- 96
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklSRRLRKIRRKEIQMVFQDPMss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 -DqiifP--TVAEELAFSLTARGETRQAARQQAREFLARRGL---EAWAGRAVSELSQGQRQQVCL-LALqISEPATLLL 169
Cdd:cd03257 95 lN----PrmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIaRAL-ALNPKLLIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 170 DEPFASLDLLSQARLAAQL----EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-224 |
2.48e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 9 TVSSHSIRLDAVTLV-RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLA 85
Cdd:COG1132 334 PPVRGEIEFENVSFSyPGDRPVLKDISLTIPPgETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 86 KHVGLMFQNPddqIIFP-TVAEELAFS-LTA-RGETRQAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLL-A 158
Cdd:COG1132 414 RQIGVVPQDT---FLFSgTIRENIRYGrPDAtDEEVEEAAKAaQAHEFIEAlpDGYDTVVGERGVNLSGGQRQRIAIArA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 159 LqISEPATLLLDEPFASLDLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVRADGP 224
Cdd:COG1132 491 L-LKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-228 |
2.58e-26 |
|
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: 102.81 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 16 RLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKH-VGLMF 92
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERgEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDiTGLPPHRIARLgIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPDdqiIFP--TVAE---------------ELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQV- 154
Cdd:COG0411 86 QNPR---LFPelTVLEnvlvaaharlgrgllAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLe 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 155 --CLLAlqiSEPATLLLDEPFASLDLLSQARLAAQL----EDSGHQILvsthLLEHVYGF-----ERVLWLEQGRVRADG 223
Cdd:COG0411 163 iaRALA---TEPKLLLLDEPAAGLNPEETEELAELIrrlrDERGITIL----LIEHDMDLvmglaDRIVVLDFGRVIAEG 235
|
....*
gi 2539771384 224 PGREI 228
Cdd:COG0411 236 TPAEV 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-228 |
2.86e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.20 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI------GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHG---CDTQADRSQL 84
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEKKALDNVNIEIedgefvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 85 AKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL--EAWAGRAVSELSQGQRQQVCLLALQIS 162
Cdd:PRK13637 82 RKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 163 EPATLLLDEPFASLDLLSQARLAAQLEDSgHQ------ILVStHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKEL-HKeynmtiILVS-HSMEDVAKLaDRIIVMNKGKCELQGTPREV 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-189 |
4.54e-26 |
|
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: 101.54 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQ 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEfFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NpddQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:cd03300 80 N---YALFPhlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170
....*....|....*...
gi 2539771384 172 PFASLDLlsQARLAAQLE 189
Cdd:cd03300 157 PLGALDL--KLRKDMQLE 172
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-228 |
7.94e-26 |
|
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: 100.72 E-value: 7.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGL-----DQPKQGRVVVHG---CDTQADRSQLA 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEItALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 86 KHVGLMFQNPDdqiIFP-TVAEELAFSLTARGE-TRQAARQQAREFLARRGLEAWAGR--AVSELSQGQRQQVCL---LA 158
Cdd:cd03260 81 RRVGMVFQKPN---PFPgSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLaraLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 159 LqisEPATLLLDEPFASLDLLSQAR---LAAQLEDSgHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:cd03260 158 N---EPEVLLLDEPTSALDPISTAKieeLIAELKKE-YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-228 |
7.99e-26 |
|
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: 100.73 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV----RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQL---A 85
Cdd:cd03258 2 IELKNVSKVfgdtGGKVTALKDVSLSVPKGEIfGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDlTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 86 KHVGLMFQNpddqiiF-----PTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---L 157
Cdd:cd03258 82 RRIGMIFQH------FnllssRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIaraL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 158 AlqiSEPATLLLDEPFASLD---------LLSQarLAAQLedsGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGRE 227
Cdd:cd03258 156 A---NNPKVLLCDEATSALDpettqsilaLLRD--INREL---GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
.
gi 2539771384 228 I 228
Cdd:cd03258 228 V 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-228 |
1.28e-25 |
|
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: 100.49 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMF 92
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGElVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNpddQIIFP--TVAEELAFSLTARGETR----QAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALQIsEPA 165
Cdd:cd03296 81 QH---YALFRhmTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALArALAV-EPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 166 TLLLDEPFASLDLLSQARLAAQLEDSGHQILVSTHLLEHVYG-----FERVLWLEQGRVRADGPGREI 228
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEealevADRVVVMNKGRIEQVGTPDEV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-177 |
3.02e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 98.71 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRIG-LVGDNGAGKSSLFRLISG-LDQP--KQGRVVVHGCDTqADRSQLAKHVG 89
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILtLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRL-TALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQnpdDQIIFP--TVAEELAFSLtARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATL 167
Cdd:COG4136 80 ILFQ---DDLLFPhlSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|
gi 2539771384 168 LLDEPFASLD 177
Cdd:COG4136 156 LLDEPFSKLD 165
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-218 |
3.55e-25 |
|
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: 97.45 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRT--VFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGL 90
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPgEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 MFQNPddqIIFP-TVAEELafsltargetrqaarqqareflarrgleawagravseLSQGQRQQVCLL-ALqISEPATLL 168
Cdd:cd03228 81 VPQDP---FLFSgTIRENI-------------------------------------LSGGQRQRIAIArAL-LRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 169 LDEPFASLDLLSQARLAAQLEDS--GHQILVSTHLLEHVYGFERVLWLEQGR 218
Cdd:cd03228 120 LDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-218 |
4.14e-25 |
|
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: 97.64 E-value: 4.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKH---VGL 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIvALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 MFQNPddqIIFP--TVAEELAFSltargetrqaarqqareflarrgleawagravseLSQGQRQQVCLLALQISEPATLL 168
Cdd:cd03229 81 VFQDF---ALFPhlTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 169 LDEPFASLDLLSQARLAAQLED----SGHQILVSTHLLEHVYGF-ERVLWLEQGR 218
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-225 |
4.90e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 29 VFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ-ADRSQLA--KHVGLMFQNPDDQIIFPTV 104
Cdd:PRK13638 16 VLKGLNLDFSLSPVtGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLAlrQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 105 AEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARL 184
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2539771384 185 AA---QLEDSGHQILVSTHLLEHVYGFERVLW-LEQGRVRADG-PG 225
Cdd:PRK13638 176 IAiirRIVAQGNHVIISSHDIDLIYEISDAVYvLRQGQILTHGaPG 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-228 |
6.56e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRIG-LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGC---DTQADRSQLAKHVGLMFQnpddQI- 99
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVvIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGMVFQ----QFy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFP--TVAEELAFS-LTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALQIsEPATLLLDEPFAS 175
Cdd:PRK09493 88 LFPhlTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIArALAV-KPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 176 LD-LLSQA--RLAAQLEDSGHQILVSTHLLehvyGF-----ERVLWLEQGRVRADGPGREI 228
Cdd:PRK09493 167 LDpELRHEvlKVMQDLAEEGMTMVIVTHEI----GFaekvaSRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-223 |
1.39e-24 |
|
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: 97.18 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEmRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSqlAKHVGLMFQ 93
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGE-ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvTAAPPA--DRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 npdDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:cd03298 78 ---ENNLFAhlTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 172 PFASLDLLSQARLAAQLEDSGHQ-----ILVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAEtkmtvLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-228 |
1.50e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEmRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqADRSQLAKH---VGLM 91
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIAAGE-RVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----QDLTALPPAerpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQnpdDQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLL 169
Cdd:COG3840 77 FQ---ENNLFPhlTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 170 DEPFASLD---------LLSQARLAAQLedsghQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:COG3840 154 DEPFSALDpalrqemldLVDELCRERGL-----TVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-228 |
2.04e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.16 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAA 122
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlSEETVWDVRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LALQisePATLLLDEPFASLDLLSQARLAA---QLEDSGHQIL 196
Cdd:PRK13635 118 VERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIagvLALQ---PDIIILDEATSMLDPRGRREVLEtvrQLKEQKGITV 194
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 197 VS-THLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13635 195 LSiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-244 |
4.42e-24 |
|
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: 96.60 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVR-GSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT-QADRSQLAKHVGLM 91
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEfLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQnpddQI-IFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLE--AWAGRAVSELSQGQRQQVCLLALQISEPAT 166
Cdd:cd03295 81 IQ----QIgLFPhmTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 167 LLLDEPFASLDLLSQARLAAQL----EDSGHQILVSTH-LLEHVYGFERVLWLEQGRVRADGPGREICEAYAED-VRERA 240
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHdIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDfVAEFV 236
|
....
gi 2539771384 241 AAER 244
Cdd:cd03295 237 GADR 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-228 |
4.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLD-----LQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS----- 82
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKKGLDnisfeLEEGSfVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 83 QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQI 161
Cdd:PRK13641 82 KLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 162 SEPATLLLDEPFASLDLLSQARLAAQLED---SGHQILVSTHLLEHVYGF-ERVLWLEQGR-VRADGPgREI 228
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDyqkAGHTVILVTHNMDDVAEYaDDVLVLEHGKlIKHASP-KEI 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-220 |
5.14e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 17 LDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadrsqlAKHVGLMFQNP 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 ---DDQIIFPTVA-----------------EELAFS---------LTARGETRQA--ARQQAREFLARRGL-EAWAGRAV 143
Cdd:COG0488 71 pldDDLTVLDTVLdgdaelraleaeleeleAKLAEPdedlerlaeLQEEFEALGGweAEARAEEILSGLGFpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 144 SELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQILVSTH---LLEHVYGfeRVLWLEQGRVR 220
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHdryFLDRVAT--RILELDRGKLT 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-228 |
1.08e-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: 95.33 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGS-RTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS----QLAKH 87
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINpgEF-VALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 88 VGLMFQNPddQIIFP-TVAEE-----LAFSLTARGETRQ---AARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLA 158
Cdd:cd03256 80 IGMIFQQF--NLIERlSVLENvlsgrLGRRSTWRSLFGLfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 159 LQISEPATLLLDEPFASLD-LLSQ------ARLAAQLEDSghqILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:cd03256 158 ALMQQPKLILADEPVASLDpASSRqvmdllKRINREEGIT---VIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-228 |
1.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEgltLDLQEMR---IGLVGDNGAGKSSLFRLISGLDQPKQGRV-----VVHGCDTQADRSQLAKHVGLMFQNPD 96
Cdd:PRK13643 18 ASRALFD---IDLEVKKgsyTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 DQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL--EAWAgRAVSELSQGQRQQVCLLALQISEPATLLLDEPFA 174
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLadEFWE-KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 175 SLD---LLSQARLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13643 174 GLDpkaRIEMMQLFESIHQSGQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDV 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-216 |
3.14e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.33 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 19 AVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLakHVGLMF---Q 93
Cdd:PRK13538 6 NLACERDERILFSGLSFTLNagEL-VQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY--HQDLLYlghQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPddqiIFP--TVAEELAFSLTARGETRQAARQQArefLARRGLeawAGR---AVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK13538 83 PG----IKTelTALENLRFYQRLHGPGDDEALWEA---LAQVGL---AGFedvPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 169 LDEPFASLD----LLSQARLAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQ 216
Cdd:PRK13538 153 LDEPFTAIDkqgvARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-188 |
3.37e-23 |
|
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: 93.47 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQ 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADgEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NpddQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:cd03301 80 N---YALYPhmTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170
....*....|....*..
gi 2539771384 172 PFASLDllsqARLAAQL 188
Cdd:cd03301 157 PLSNLD----AKLRVQM 169
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-231 |
3.40e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 95.64 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQNpddQIIFP--TVAEELAFSLTARGETRQA 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRHINMVFQS---YALFPhmTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQILVSTHL 201
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2539771384 202 LEH-----VYGFERVLWLEQGRVRADGPGREICEA 231
Cdd:TIGR01187 157 VTHdqeeaMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
44-228 |
3.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAA 122
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlTEENVWDIRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE------PFASLDLLSQARlaAQLEDSGHQIL 196
Cdd:PRK13650 118 KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEatsmldPEGRLELIKTIK--GIRDDYQMTVI 195
|
170 180 190
....*....|....*....|....*....|..
gi 2539771384 197 VSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13650 196 SITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-219 |
4.30e-23 |
|
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: 92.98 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLA---KHVGLMFQNPDdqiI 100
Cdd:cd03262 11 GDFHVLKGIDLTVKKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVGMVFQQFN---L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 101 FP--TVAEELAFSL-TARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LALQisePATLLLDEPFA 174
Cdd:cd03262 88 FPhlTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIaraLAMN---PKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 175 SLD------LLSQARlaaQLEDSGHQILVSTHLLehvyGF-----ERVLWLEQGRV 219
Cdd:cd03262 165 ALDpelvgeVLDVMK---DLAEEGMTMVVVTHEM----GFarevaDRVIFMDDGRI 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
44-228 |
4.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.29 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADR-SQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAA 122
Cdd:PRK13632 40 ILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LALqisEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQIL 196
Cdd:PRK13632 120 KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIasvLAL---NPEIIIFDESTSMLDPKGKREIKKimvDLRKTRKKTL 196
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 197 VS-THLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13632 197 ISiTHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-228 |
1.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS---QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQ 120
Cdd:PRK13636 37 ILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPED 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 121 AARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQAR----LAAQLEDSGHQIL 196
Cdd:PRK13636 117 EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEimklLVEMQKELGLTII 196
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 197 VSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13636 197 IATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-223 |
1.21e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.89 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLaKHVGLMFQ 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIyGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPddqIIFPTVAEELAFSLTARGETRQAARQQarEFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:cd03268 80 AP---GFYPNLTARENLRLLARLLGIRKKRID--EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 174 ASLD---LLSQARLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03268 155 NGLDpdgIKELRELILSLRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
42-228 |
4.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.07 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS--QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETR 119
Cdd:PRK13633 39 LVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 QAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED----SGHQI 195
Cdd:PRK13633 119 EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnkkYGITI 198
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 196 LVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13633 199 ILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
44-219 |
6.83e-22 |
|
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: 90.16 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQ----LAKHVGLMFQnpdDQIIFP--TVAEELAFSLTARGE 117
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVFQ---DFRLLPdrNVYENVAFALEVTGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDS---GHQ 194
Cdd:cd03292 109 PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkaGTT 188
|
170 180
....*....|....*....|....*.
gi 2539771384 195 ILVSTHLLEHVYGFE-RVLWLEQGRV 219
Cdd:cd03292 189 VVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-238 |
7.51e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 90.29 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQA---DRSQLakhvGLMFQnPDDQI 99
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIvGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLpmhKRARL----GIGYL-PQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLD 177
Cdd:cd03218 86 IFRklTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 178 LLSQA---RLAAQLEDSGHQILVSTH----LLEHVygfERVLWLEQGRVRADGPGREICEayAEDVRE 238
Cdd:cd03218 166 PIAVQdiqKIIKILKDRGIGVLITDHnvreTLSIT---DRAYIIYEGKVLAEGTPEEIAA--NELVRK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-212 |
1.09e-21 |
|
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: 93.12 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 5 SPSETVSSHSIRLDAVTLV-RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADR 81
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAyPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 82 SQLAKHVGLMFQNPddqIIFP-TVAEELAFSL--TARGETRQAARQQ-AREFLA--RRGLEAWAGRAVSELSQGQRQQVC 155
Cdd:TIGR02857 392 DSWRDQIAWVPQHP---FLFAgTIAENIRLARpdASDAEIREALERAgLDEFVAalPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 156 LLALQISEPATLLLDEPFASLDLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVL 212
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAlaQGRTVLLVTHRLALAALADRIV 527
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
44-228 |
1.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.63 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGL---DQPKQGRVVVHGCDTQADRS-QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETR 119
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVwDIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 QAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQAR---LAAQL-EDSGHQI 195
Cdd:PRK13640 118 PEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQilkLIRKLkKKNNLTV 197
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 196 LVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13640 198 ISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-227 |
1.46e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.15 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNpddqiifP-- 102
Cdd:COG1101 19 KRALDGLNLTIEEGDfVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKLPEYKRAKYIGRVFQD-------Pmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 ------TVAEELAFSLtARGETR-------QAARQQAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATL 167
Cdd:COG1101 92 gtapsmTIEENLALAY-RRGKRRglrrgltKKRRELFRELLATlgLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 168 LLDEPFASLDllsqARLAAQLED------SGHQI--LVSTHLLEHV--YGfERVLWLEQGRVRADGPGRE 227
Cdd:COG1101 171 LLDEHTAALD----PKTAALVLEltekivEENNLttLMVTHNMEQAldYG-NRLIMMHEGRIILDVSGEE 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
42-223 |
2.33e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 88.75 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRsqlaKHVGLMFQNPDDQIIFPTVAEELAFSLTAR--GETR 119
Cdd:TIGR03771 9 LGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW----RHIGYVPQRHEFAWDFPISVAHTVMSGRTGhiGWLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 QAARQQ---AREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLA---AQLEDSGH 193
Cdd:TIGR03771 85 RPCVADfaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTelfIELAGAGT 164
|
170 180 190
....*....|....*....|....*....|.
gi 2539771384 194 QILVSTH-LLEHVYGFERVLwLEQGRVRADG 223
Cdd:TIGR03771 165 AILMTTHdLAQAMATCDRVV-LLNGRVIADG 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
15-230 |
2.71e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.16 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQlaKHVGLMF 92
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEfLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDiTHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNpddQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLD 170
Cdd:PRK09452 93 QS---YALFPhmTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 171 EPFASLDLlsQARLAAQLEDSGHQ-------ILVsTHLLEHVYGF-ERVLWLEQGRVRADGPGREICE 230
Cdd:PRK09452 170 ESLSALDY--KLRKQMQNELKALQrklgitfVFV-THDQEEALTMsDRIVVMRDGRIEQDGTPREIYE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-183 |
4.83e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqadrSQLA---KHV 88
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPsgQM-VALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHardRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNpddQIIFP--TVAEELAFSLTA--RGE--TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALQI 161
Cdd:PRK10851 77 GFVFQH---YALFRhmTVFDNIAFGLTVlpRRErpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALArALAV 153
|
170 180
....*....|....*....|..
gi 2539771384 162 sEPATLLLDEPFASLDllSQAR 183
Cdd:PRK10851 154 -EPQILLLDEPFGALD--AQVR 172
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1-228 |
7.21e-21 |
|
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: 90.87 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 1 MPQPSPSETVSshsirLDAVTLV--RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD- 76
Cdd:TIGR01842 308 MPLPEPEGHLS-----VENVTIVppGGKKPTLRGISFSLQAGEAlAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADl 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 77 TQADRSQLAKHVGLMfqnPDDQIIFP-TVAEELA-FSLTARGET-RQAAR-QQAREFLAR--RGLEAWAGRAVSELSQGQ 150
Cdd:TIGR01842 383 KQWDRETFGKHIGYL---PQDVELFPgTVAENIArFGENADPEKiIEAAKlAGVHELILRlpDGYDTVIGPGGATLSGGQ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 151 RQQVCLLALQISEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTH---LLEHVygfERVLWLEQGRVRADGP 224
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANaikALKARGITVVVITHrpsLLGCV---DKILVLQDGRIARFGE 536
|
....
gi 2539771384 225 GREI 228
Cdd:TIGR01842 537 RDEV 540
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
42-238 |
9.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 9.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS-QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQ 120
Cdd:PRK13642 36 VSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 121 AARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA---RLAAQLEDSGHQILV 197
Cdd:PRK13642 116 EMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQeimRVIHEIKEKYQLTVL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2539771384 198 S-THLLEHVYGFERVLWLEQGRVRADGPGREICeAYAEDVRE 238
Cdd:PRK13642 196 SiTHDLDEAASSDRILVMKAGEIIKEAAPSELF-ATSEDMVE 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-223 |
1.28e-20 |
|
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: 86.82 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqADRSQLAKHVGLmfqNPDdqiifP 102
Cdd:cd03220 32 VGEFWALKDVSFEVPRgERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGGGF---NPE-----L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQvclLALQIS---EPATLLLDEPFASLD-- 177
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR---LAFAIAtalEPDILLIDEVLAVGDaa 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2539771384 178 --LLSQARLAAQLEDSGHQILVStHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03220 177 fqEKCQRRLRELLKQGKTVILVS-HDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-228 |
2.36e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGlmf 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLvGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 qnpddqiifpTVAEE--LAFSLTAR-----------------GETRQAARQQArefLARRGLEAWAGRAVSELSQGQRQQ 153
Cdd:PRK09536 81 ----------SVPQDtsLSFEFDVRqvvemgrtphrsrfdtwTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 154 VCLLALQISEPATLLLDEPFASLDLLSQAR---LAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-219 |
2.45e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 12 SHSIRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLA---K 86
Cdd:PRK10419 10 SHHYAHGGLSGKHQHQTVLNNVSLSLKSGEtVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKLNRAQRKafrR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 87 HVGLMFQ------NPDdQIIFPTVAEELAfSLTARGETRQAARqqAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLAL 159
Cdd:PRK10419 90 DIQMVFQdsisavNPR-KTVREIIREPLR-HLLSLDKAERLAR--ASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 160 QISEPATLLLDEPFASLDLLSQARLAAQLED----SGHQILVSTHLLEHVYGF-ERVLWLEQGRV 219
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFcQRVMVMDNGQI 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
42-223 |
2.56e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.23 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQA 121
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPAR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL----EDSGHQILV 197
Cdd:cd03267 130 FKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeynRERGTTVLL 209
|
170 180
....*....|....*....|....*..
gi 2539771384 198 STHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03267 210 TSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-228 |
2.78e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTL-DLQEM-----RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQ----- 83
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALyDVNVSipsgsYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQIS 162
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 163 EPATLLLDEPFASLDLLSQARLA---AQLEDSGHQ--ILVsTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMemfYKLHKEKGLttVLV-THSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-220 |
3.02e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQ-EMRIGLVGDNGAGKSSLFRLISGLDQPKQGRV-----VVHGCDTQaDRSQLakhv 88
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDrGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetVKIGYFDQ-HQEEL---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 glmfqNPDDqiifpTVAEELafsltaRGETRQAARQQAREFLAR---RGLEAWagRAVSELSQGQRQQVCLLALQISEPA 165
Cdd:COG0488 391 -----DPDK-----TVLDEL------RDGAPGGTEQEVRGYLGRflfSGDDAF--KPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 166 TLLLDEPFASLDLLSQARLAAQLED-SGHQILVS--THLLEHVygFERVLWLEQGRVR 220
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDfPGTVLLVShdRYFLDRV--ATRILEFEDGGVR 508
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
44-228 |
4.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHG-CDTQADRSQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAA 122
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA---RLAAQLEDSGHQILVS- 198
Cdd:PRK13648 120 HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQnllDLVRKVKSEHNITIISi 199
|
170 180 190
....*....|....*....|....*....|
gi 2539771384 199 THLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK13648 200 THDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-228 |
6.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 12 SHSIRLDAVTLVRGSRTVFEGLTLDLQEMRIG------LVGDNGAGKSSLFRLISGLDQPKQGRVVV------HGCDTQA 79
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALNNTSLTFKknkvtcVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 80 DRSQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLA 158
Cdd:PRK13645 84 EVKRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 159 LQISEPATLLLDEPFASLDLLSQARLAAQLE----DSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFEI 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-228 |
9.05e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.13 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMF 92
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPDDQIIFpTVAEELAFS--------LTARGEtrqAARQQAREFLarrGLEAWAGRAVSELSQGQRQQVcLLALQISEp 164
Cdd:COG4604 82 QENHINSRL-TVRELVAFGrfpyskgrLTAEDR---EIIDEAIAYL---DLEDLADRYLDELSGGQRQRA-FIAMVLAQ- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 165 AT--LLLDEPFASLD------LLSQARLAAqlEDSGHQILVSTHLLEH--VYGfERVLWLEQGRVRADGPGREI 228
Cdd:COG4604 153 DTdyVLLDEPLNNLDmkhsvqMMKLLRRLA--DELGKTVVIVLHDINFasCYA-DHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-201 |
9.58e-20 |
|
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: 84.08 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 18 DAVTLVRGSRTVFEGL--TLDLQEMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQNP 95
Cdd:cd03231 4 DELTCERDGRALFSGLsfTLAAGEA-LQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 DDQIIFpTVAEELAFSltargeTRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFAS 175
Cdd:cd03231 83 GIKTTL-SVLENLRFW------HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 2539771384 176 LDLLSQARLAAQLE---DSGHQILVSTHL 201
Cdd:cd03231 156 LDKAGVARFAEAMAghcARGGMVVLTTHQ 184
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-200 |
1.15e-19 |
|
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: 83.56 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 17 LDAVTLVRGSRTVFEGLTLDLQ--EMRIgLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQN 94
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNagEALQ-VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDDQIIFpTVAEELAFsltaRGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFA 174
Cdd:TIGR01189 82 PGLKPEL-SALENLHF----WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 2539771384 175 SLDLLSQARLAAQLEDSGHQ---ILVSTH 200
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARggiVLLTTH 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-214 |
1.33e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadrsqlAKHVGLMFQNPDDQIIFP- 102
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLtAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSLPl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 TVAEELAFSLTAR----GETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDL 178
Cdd:NF040873 73 TVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2539771384 179 LSQARLA---AQLEDSGHQILVSTHLLEHVYGFERVLWL 214
Cdd:NF040873 153 ESRERIIallAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-177 |
2.62e-19 |
|
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: 83.64 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV----RGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK-- 86
Cdd:COG4181 9 IELRGLTKTvgtgAGELTILKGISLEVEAGEsVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 87 --HVGLMFQNpddqiiFPTVAeelafSLTA----------RGetRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQV 154
Cdd:COG4181 89 arHVGFVFQS------FQLLP-----TLTAlenvmlplelAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180
....*....|....*....|...
gi 2539771384 155 CLLALQISEPATLLLDEPFASLD 177
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLD 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-228 |
2.86e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.91 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLM 91
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKItALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPiSMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQnpddQIIFP---TVAEELAFS----LTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEP 164
Cdd:PRK11231 82 PQ----HHLTPegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 165 ATLLLDEPFASLDLLSQA---RLAAQLEDSGHQILVSTHLLEHV--YGFERVLwLEQGRVRADGPGREI 228
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVelmRLMRELNTQGKTVVTVLHDLNQAsrYCDHLVV-LANGHVMAQGTPEEV 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-240 |
3.24e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadR--SQLAKHVGLmfqNPDDqii 100
Cdd:COG1134 36 REEFWALKDVSFEVERgESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RvsALLELGAGF---HPEL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 101 fpTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQvclLALQIS---EPATLLLDEPFASLD 177
Cdd:COG1134 104 --TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRAR---LAFAVAtavDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 178 LL----SQARLAAQLEDSGHQILVStHLLEHVYGF-ERVLWLEQGRVRADGPGREICEAYAEDVRERA 240
Cdd:COG1134 179 AAfqkkCLARIRELRESGRTVIFVS-HSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAAYEALLAGRE 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
42-228 |
4.10e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.92 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQnpDDQIIFPTVAEELAFSLTA--RGET 118
Cdd:cd03252 31 VGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQ--ENVLFNRSIRDNIALADPGmsMERV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 119 RQAAR-QQAREFLA--RRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED--SGH 193
Cdd:cd03252 109 IEAAKlAGAHDFISelPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDicAGR 188
|
170 180 190
....*....|....*....|....*....|....*
gi 2539771384 194 QILVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:cd03252 189 TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-219 |
5.09e-19 |
|
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: 81.11 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRG--SRTVFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVG 89
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEpgES-LAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADiSQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQnpDDQIIFPTVAEELafsltargetrqaarqqareflarrgleawagravseLSQGQRQQVCLLALQISEPATLLL 169
Cdd:cd03246 80 YLPQ--DDELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 170 DEPFASLDLLSQARLAAQLED---SGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAlkaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
33-242 |
5.35e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMRIGLvGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ---ADRsqlakhvGLMFQNpDDQIIFPTVAEELA 109
Cdd:PRK11248 22 LTLESGELLVVL-GPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAER-------GVVFQN-EGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 110 FSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL- 188
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLl 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 189 ---EDSGHQILVSTHLLEhvygfERVLWLEQGRVRADGPGReICEAYAEDVRERAAA 242
Cdd:PRK11248 173 klwQETGKQVLLITHDIE-----EAVFMATELVLLSPGPGR-VVERLPLNFARRFVA 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
27-228 |
5.90e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS---------QLAKHVGLMFQNPD 96
Cdd:PRK11264 16 QTVLHGIDLEVKPGEvVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 dqiIFP--TVAEE-LAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:PRK11264 96 ---LFPhrTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 174 ASLD------LLSQARlaaQLEDSGHQILVSTHLLehvyGF-----ERVLWLEQGRVRADGPGREI 228
Cdd:PRK11264 173 SALDpelvgeVLNTIR---QLAQEKRTMVIVTHEM----SFardvaDRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-227 |
6.35e-19 |
|
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: 82.27 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPddqIIFP-T 103
Cdd:cd03254 16 KPVLKDINFSIKPgETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSLRSMIGVVLQDT---FLFSgT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 104 VAEELAFS-LTARGETRQAARQQAR--EFLARR--GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDL 178
Cdd:cd03254 93 IMENIRLGrPNATDEEVIEAAKEAGahDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 179 LSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGRE 227
Cdd:cd03254 173 ETEKLIQEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-222 |
9.73e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 9.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 17 LDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVhgcdTQADRSQLAKHVGLMFQnp 95
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQfVAVVGRSGCGKSTLLRLLAGLETPSAGELLA----GTAPLAEAREDTRLMFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 dDQIIFP--TVAEELAFSLtaRGETRQAARQQarefLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:PRK11247 89 -DARLLPwkKVIDNVGLGL--KGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 174 ASLDLLSQARLAAQLE----DSGHQILVSTH-LLEHVYGFERVLWLEQGRVRAD 222
Cdd:PRK11247 162 GALDALTRIEMQDLIEslwqQHGFTVLLVTHdVSEAVAMADRVLLIEEGKIGLD 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-177 |
1.98e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.82 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLV----RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLA--- 85
Cdd:COG1135 2 IELENLSKTfptkGGPVTALDDVSLTIEKGEIfGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSERELRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 86 KHVGLMFQNpddqiiFP-----TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---L 157
Cdd:COG1135 82 RKIGMIFQH------FNllssrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIaraL 155
|
170 180
....*....|....*....|
gi 2539771384 158 AlqiSEPATLLLDEPFASLD 177
Cdd:COG1135 156 A---NNPKVLLCDEATSALD 172
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-223 |
2.01e-18 |
|
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: 80.88 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQNP--DDQIif 101
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIfGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLsvDDEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 pTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQ 181
Cdd:cd03265 89 -TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2539771384 182 A----RLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:cd03265 168 AhvweYIEKLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEG 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
43-177 |
2.37e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.54 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK---HVGLMFQNpddqiiF-----PTVAEELAFSLT 113
Cdd:PRK11153 35 GVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTALSEKELRKarrQIGMIFQH------FnllssRTVFDNVALPLE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 114 ARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCL---LAlqiSEPATLLLDEPFASLD 177
Cdd:PRK11153 109 LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIaraLA---SNPKVLLCDEATSALD 172
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-248 |
2.74e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD--TQADRSQLAKHVGLM 91
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAgCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmaDARHRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 92 FQ----NpddqiIFPT--VAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqISEP 164
Cdd:NF033858 82 PQglgkN-----LYPTlsVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCcAL-IHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 165 ATLLLDEPFASLDLLSQAR---LAAQL--EDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEAYAEDVRER 239
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQfweLIDRIraERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEA 235
|
250
....*....|....*
gi 2539771384 240 A------AAERGRHA 248
Cdd:NF033858 236 AfiallpEEKRRGHQ 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-228 |
3.67e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 28 TVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRV----VVHGCDTQADRS-------------QLAKHVG 89
Cdd:PRK13631 40 VALNNISYTFEKNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 169 LDEPFASLDLLSQARLAAQLEDS---GHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEI 263
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-200 |
7.26e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 7.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 20 VTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKH-VG-LMFQNPd 96
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEaLVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLGhRNAMKP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 dqiiFPTVAEELAFSLTARGetrqAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASL 176
Cdd:PRK13539 87 ----ALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 2539771384 177 DLLSQARLAAQLE---DSGHQILVSTH 200
Cdd:PRK13539 159 DAAAVALFAELIRahlAQGGIVIAATH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-219 |
7.39e-18 |
|
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: 79.44 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHG-CDTQADRSQLAKHVGLMFQNPddQIIF 101
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVtALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkPISQYEHKYLHSKVSLVGQEP--VLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 PTVAEELAFSLTARGETRQAARQQ---AREFLARRGLEAW--AGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASL 176
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQkahAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2539771384 177 DLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:cd03248 182 DAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
44-189 |
1.42e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.65 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQNpddQIIFP--TVAEELAFSLTARGETRQA 121
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQS---YALFPhmTVEQNIAFGLKQDKLPKAE 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDllSQARLAAQLE 189
Cdd:PRK11607 126 IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD--KKLRDRMQLE 191
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-224 |
2.14e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.92 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQ-EMRIGLVGDNGAGKSS----LFRLIsgldQPKQGRVVVHGCDTQA-DRSQLAKHVGLMFQNPddq 98
Cdd:cd03244 15 NLPPVLKNISFSIKpGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKiGLHDLRSRISIIPQDP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 99 IIFP-TVAEELA-FSLTARGETRQAARQ-QAREFLARR--GLEAwagrAVSE----LSQGQRQQVCLL-ALqISEPATLL 168
Cdd:cd03244 88 VLFSgTIRSNLDpFGEYSDEELWQALERvGLKEFVESLpgGLDT----VVEEggenLSVGQRQLLCLArAL-LRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 169 LDEPFASLDLLSQARLAAQL--EDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGP 224
Cdd:cd03244 163 LDEATASVDPETDALIQKTIreAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-228 |
3.20e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLdQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPDDQIIFPtVAEELAFSLtaRGETR 119
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPlSDWSAAELARHRAYLSQQQSPPFAMP-VFQYLALHQ--PAGAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 QAARQQAREFLARR-GLEAWAGRAVSELSQGQRQQVCLLA--LQIS-----EPATLLLDEPFASLDLLSQA---RLAAQL 188
Cdd:COG4138 100 SEAVEQLLAQLAEAlGLEDKLSRPLTQLSGGEWQRVRLAAvlLQVWptinpEGQLLLLDEPMNSLDVAQQAaldRLLREL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 189 EDSGHQILVSTHLLEHVYGFERVLW-LEQGRVRADGPGREI 228
Cdd:COG4138 180 CQQGITVVMSSHDLNHTLRHADRVWlLKQGKLVASGETAEV 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-231 |
3.30e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 9 TVSSHSIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS-QLAK 86
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 87 HVGLMFQN---PDDQiifpTVAEelafsLTARGE-------TRQaaRQQAREFLAR----RGLEAWAGRAVSELSQGQRQ 152
Cdd:PRK10253 82 RIGLLAQNattPGDI----TVQE-----LVARGRyphqplfTRW--RKEDEEAVTKamqaTGITHLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 153 QVCLLALQISEPATLLLDEPFASLD---------LLSQAR------LAAQLEDSGHQILVSTHLLEhvygfervlwLEQG 217
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDishqidlleLLSELNrekgytLAAVLHDLNQACRYASHLIA----------LREG 220
|
250
....*....|....
gi 2539771384 218 RVRADGPGREICEA 231
Cdd:PRK10253 221 KIVAQGAPKEIVTA 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-177 |
3.61e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 12 SHSIRLDAVTLVRGSRTVFEGLTLDL-QEMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGL 90
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIkQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 MFQNpddQIIFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK11432 83 VFQS---YALFPhmSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
....*....
gi 2539771384 169 LDEPFASLD 177
Cdd:PRK11432 160 FDEPLSNLD 168
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-228 |
6.30e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ-----------ADRSQLA---KHVG 89
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDvISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRllrTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 169 LDEPFASLD--LLSQA-RLAAQLEDSGHQILVSTHLLE---HVYgfERVLWLEQGRVRADGPGREI 228
Cdd:PRK10619 176 FDEPTSALDpeLVGEVlRIMQQLAEEGKTMVVVTHEMGfarHVS--SHVIFLHQGKIEEEGAPEQL 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-219 |
8.55e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdTQADRSQ--------- 83
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGEtLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG--NHFDFSKtpsdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAKHVGLMFQNPDdqiIFP--TVAEELAFS-LTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQ 160
Cdd:PRK11124 80 LRRNVGMVFQQYN---LWPhlTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 161 ISEPATLLLDEPFASLDllsqARLAAQ-------LEDSG-HQILVsTHLLEHVYGF-ERVLWLEQGRV 219
Cdd:PRK11124 157 MMEPQVLLFDEPTAALD----PEITAQivsiireLAETGiTQVIV-THEVEVARKTaSRVVYMENGHI 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-224 |
9.17e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 10 VSSHSIRLDAVTLV-RGSRTVFEGLTLDLQEMRIG-LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT-QADRSQLAK 86
Cdd:PRK15056 2 MQQAGIVVNDVTVTwRNGHTALRDASFTVPGGSIAaLVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 87 HVGlmfQNPDDQIIFPTVAEELAfsLTAR----GETRQAA---RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLAL 159
Cdd:PRK15056 82 YVP---QSEEVDWSFPVLVEDVV--MMGRyghmGWLRRAKkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 160 QISEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGP 224
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISllrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
41-225 |
9.80e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.05 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQlaKHVGLMFQNPDdqiIFP--TVAEELAFSLTArGE 117
Cdd:TIGR01277 26 IVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShTGLAPYQ--RPVSMLFQENN---LFAhlTVRQNIGLGLHP-GL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAREFLARR-GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLD-LLSQARLA--AQLEDSGH 193
Cdd:TIGR01277 100 KLNAEQQEKVVDAAQQvGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpLLREEMLAlvKQLCSERQ 179
|
170 180 190
....*....|....*....|....*....|....
gi 2539771384 194 Q--ILVSTHLLEHVYGFERVLWLEQGRVRADGPG 225
Cdd:TIGR01277 180 RtlLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
41-223 |
1.22e-16 |
|
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: 76.12 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGLMFQnpdDQIIFP-TVAEELAFSLT--ARG 116
Cdd:cd03251 30 TVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ---DVFLFNdTVAENIAYGRPgaTRE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 117 ETRQAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED--S 191
Cdd:cd03251 107 EVEEAARAaNAHEFIMElpEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmK 186
|
170 180 190
....*....|....*....|....*....|..
gi 2539771384 192 GHQILVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:cd03251 187 NRTTFVIAHRLSTIENADRIVVLEDGKIVERG 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-218 |
1.34e-16 |
|
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: 74.02 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEM-RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadrsqlakhvglmfq 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 npddqiifptvAEELAFsltargetrqaarqqareflarrgleawagraVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:cd03221 62 -----------TVKIGY--------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2539771384 174 ASLDLLSQARLAAQLEDSGHQILVSTH---LLEHVygFERVLWLEQGR 218
Cdd:cd03221 99 NHLDLESIEALEEALKEYPGTVILVSHdryFLDQV--ATKIIELEDGK 144
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-228 |
1.58e-16 |
|
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: 75.55 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQnPDDQIIFP- 102
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIvALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV-PEGRRIFPe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 -TVAEELAFSLTARGETRQAARQQA--------REFLARRGleawagravSELSQGQRQQVCL-LALqISEPATLLLDEP 172
Cdd:cd03224 90 lTVEENLLLGAYARRRAKRKARLERvyelfprlKERRKQLA---------GTLSGGEQQMLAIaRAL-MSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 173 FASL-----DLLSQArlAAQLEDSGHQILVS----THLLEHVygfERVLWLEQGRVRADGPGREI 228
Cdd:cd03224 160 SEGLapkivEEIFEA--IRELRDEGVTILLVeqnaRFALEIA---DRAYVLERGRVVLEGTAAEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
39-222 |
1.78e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 39 EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADRSQLAKH-VGLMFQN----PDdqiiFpTVAEELA 109
Cdd:PRK11629 36 EM-MAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklSSAAKAELRNQkLGFIYQFhhllPD----F-TALENVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 110 FSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLE 189
Cdd:PRK11629 110 MPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLG 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 2539771384 190 D----SGHQILVSTHLLEHVYGFERVLWLEQGRVRAD 222
Cdd:PRK11629 190 ElnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-238 |
2.29e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 5 SPSETVSSHSIRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQAdRSQ 83
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGEcFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAK-HVGLM--FQNPDDQIifpTVAEEL-AFSLTARGETRQ--AARQQAREFlARrgLEAWAGRAVSELSQGQRQQVCLL 157
Cdd:PRK13536 111 LARaRIGVVpqFDNLDLEF---TVRENLlVFGRYFGMSTREieAVIPSLLEF-AR--LESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 158 ALQISEPATLLLDEPFASLD----LLSQARLAAQLEdSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGP-------- 224
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDpharHLIWERLRSLLA-RGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRphalideh 263
|
250
....*....|....*
gi 2539771384 225 -GREICEAYAEDVRE 238
Cdd:PRK13536 264 iGCQVIEIYGGDPHE 278
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
44-228 |
3.10e-16 |
|
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: 75.06 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqADRSQLAKHVGLMFQNpddQIIFP--TVAEELAFSLTARGETRQA 121
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQN---YALFPhmTVYKNIAYGLKKRKVDKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQ----ILV 197
Cdd:cd03299 106 IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfgvtVLH 185
|
170 180 190
....*....|....*....|....*....|..
gi 2539771384 198 STHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:cd03299 186 VTHDFEEAWALaDKVAIMLNGKLIQVGKPEEV 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-227 |
3.32e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 29 VFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK----HVGLMFQNPDdqiIF 101
Cdd:PRK10535 23 VLKGISLDIYagEM-VAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAQlrreHFGFIFQRYH---LL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 P--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLL 179
Cdd:PRK10535 99 ShlTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 180 SQARLAA---QLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGRE 227
Cdd:PRK10535 179 SGEEVMAilhQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-230 |
4.06e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPddQIIF 101
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVvALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEP--VLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 PTVAEELAFSLT--ARGETRQAARQQ-AREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASL 176
Cdd:TIGR00958 569 GSVRENIAYGLTdtPDEEIMAAAKAAnAHDFIMEfpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 177 DLLSQARLAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICE 230
Cdd:TIGR00958 649 DAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
41-177 |
9.79e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 9.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQlaKHVGLMFQnpdDQIIFP--TVAEELAFSLTARGE 117
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSR--RPVSMLFQ---ENNLFShlTVAQNIGLGLNPGLK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLD 177
Cdd:PRK10771 102 LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-219 |
1.21e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQ--EMRIgLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQ----LAKHVGLMFQnpDDQ 98
Cdd:PRK10908 13 GGRQALQGVTFHMRpgEMAF-LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQ--DHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 99 IIFP-TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLD 177
Cdd:PRK10908 90 LLMDrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2539771384 178 -LLSQA--RLAAQLEDSGHQILVSTHLLEHVYGFE-RVLWLEQGRV 219
Cdd:PRK10908 170 dALSEGilRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-237 |
1.54e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLdQPKQGRVVVHG-CDTQADRSQLAKHVGLMFQNPDDQIIFPtVAEELAFSLTARgeTRQAA 122
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqPLEAWSAAELARHRAYLSQQQTPPFAMP-VFQYLTLHQPDK--TRTEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQQAREFLARR-GLEAWAGRAVSELSQGQRQQVCLLA--LQISePAT------LLLDEPFASLDLLSQA---RLAAQLED 190
Cdd:PRK03695 103 VASALNEVAEAlGLDDKLGRSVNQLSGGEWQRVRLAAvvLQVW-PDInpagqlLLLDEPMNSLDVAQQAaldRLLSELCQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 191 SGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI------CEAYAEDVR 237
Cdd:PRK03695 182 QGIAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRDEVltpenlAQVFGVNFR 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
46-224 |
1.93e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 46 GDNGAGKSSLFRLISGLDQPKQGRVVVHGcDTQADRSQ---LA---KHVGLMFQnpdDQIIFP--TVAEELAFSLTargE 117
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAEKgicLPpekRRIGYVFQ---DARLFPhyKVRGNLRYGMA---K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAREFLarrGLEAWAGRAVSELSQGQRQQVCL-LALqISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQ-- 194
Cdd:PRK11144 104 SMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIgRAL-LTAPELLLMDEPLASLDLPRKRELLPYLERLAREin 179
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 195 --ILVSTHLLEHVYGF-ERVLWLEQGRVRADGP 224
Cdd:PRK11144 180 ipILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
42-228 |
3.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADR---------------------SQLAKHVGLMFQNPD 96
Cdd:PRK13651 36 IAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkKKTKEkekvleklviqktrfkkikkiKEIRRRVGVVFQFAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 DQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFAS 175
Cdd:PRK13651 116 YQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAG 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 176 LD---LLSQARLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13651 196 LDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWtKRTIFFKDGKIIKDGDTYDI 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
41-219 |
4.36e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLdQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPddQIIFPTVAEELAFSLTARGETR 119
Cdd:PRK11174 378 RIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIElRELDPESWRKHLSWVGQNP--QLPHGTLRDNVLLGNPDASDEQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 --QAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLS-QARLAAQLEDSGH 193
Cdd:PRK11174 455 lqQALENaWVSEFLPLlpQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeQLVMQALNAASRR 534
|
170 180
....*....|....*....|....*...
gi 2539771384 194 Q--ILVsTHLLEHVYGFERVLWLEQGRV 219
Cdd:PRK11174 535 QttLMV-THQLEDLAQWDQIWVMQDGQI 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-230 |
7.24e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 8 ETVSSHSIRLDavtlvRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQAD------ 80
Cdd:TIGR03269 283 RNVSKRYISVD-----RGVVKAVDNVSLEVKEGEIfGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDmtkpgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 81 --RSQLAKHVGLMFQNPDdqiIFP--TVAEEL--AFSLTARGETrqaARQQAREFLARRGLEAWAGRAV-----SELSQG 149
Cdd:TIGR03269 358 dgRGRAKRYIGILHQEYD---LYPhrTVLDNLteAIGLELPDEL---ARMKAVITLKMVGFDEEKAEEIldkypDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 150 QRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL----EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGP 224
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGD 511
|
....*.
gi 2539771384 225 GREICE 230
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
42-220 |
7.47e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQAD---RSQL-AKHVGLMFQNpddQIIFPTVAEELAFSLTA-- 114
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDeeaRAKLrAKHVGFVFQS---FMLIPTLNALENVELPAll 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 115 RGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL----ED 190
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnRE 195
|
170 180 190
....*....|....*....|....*....|
gi 2539771384 191 SGHQILVSTHLLEHVYGFERVLWLEQGRVR 220
Cdd:PRK10584 196 HGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-182 |
1.01e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 72.01 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 31 EGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPK---QGRVVVHGCD-TQADRSQL----AKHVGLMFQNP------ 95
Cdd:COG0444 22 DGVSFDVRRGETlGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDlLKLSEKELrkirGREIQMIFQDPmtslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 ----DDQIifptvAEELafsLTARGETRQAARQQAREFLARRGLEAWAGRAVS---ELSQGQRQQVCL-LALqISEPATL 167
Cdd:COG0444 102 vmtvGDQI-----AEPL---RIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIaRAL-ALEPKLL 172
|
170
....*....|....*
gi 2539771384 168 LLDEPFASLDLLSQA 182
Cdd:COG0444 173 IADEPTTALDVTIQA 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-231 |
1.57e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcDTQADRSQLAK-HVGLM--FQNPDDQIi 100
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGEcFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARqRVGVVpqFDNLDPDF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 101 fpTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDllS 180
Cdd:PRK13537 96 --TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD--P 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 181 QAR-----LAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEA 231
Cdd:PRK13537 172 QARhlmweRLRSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIES 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-239 |
1.90e-14 |
|
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: 70.40 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 16 RLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRS-QLAKH-VGLMf 92
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIvALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLgIGYV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 qnPDDQIIFP--TVAEELAFSLTARGETRQAARQQAREF-----LARRgLEAWAGRavseLSQGQRQQVCL-LALqISEP 164
Cdd:COG0410 84 --PEGRRIFPslTVEENLLLGAYARRDRAEVRADLERVYelfprLKER-RRQRAGT----LSGGEQQMLAIgRAL-MSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 165 ATLLLDEPFASLdllsQARLAAQLED-------SGHQILvsthLLEHVYGF-----ERVLWLEQGRVRADGPGREIceAY 232
Cdd:COG0410 156 KLLLLDEPSLGL----APLIVEEIFEiirrlnrEGVTIL----LVEQNARFaleiaDRAYVLERGRIVLEGTAAEL--LA 225
|
....*..
gi 2539771384 233 AEDVRER 239
Cdd:COG0410 226 DPEVREA 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-238 |
4.49e-14 |
|
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: 70.99 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQ--PKQGRVVVH------------------ 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVlGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 74 -----------------GCDtQADRSQLAKHVGLMFQNP-----DDqiifpTVAEELAFSLTARGETRQAARQQAREFLA 131
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLS-DKLRRRIRKRIAIMLQRTfalygDD-----TVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 132 RRGLEAWAGRAVSELSQGQRQQVcLLALQIS-EPATLLLDEPFASLD-----LLSQARLAAqLEDSGHQILVSTHLLEHV 205
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRV-VLARQLAkEPFLFLADEPTGTLDpqtakLVHNALEEA-VKASGISMVLTSHWPEVI 232
|
250 260 270
....*....|....*....|....*....|....
gi 2539771384 206 YGF-ERVLWLEQGRVRADGPGREICEAYAEDVRE 238
Cdd:TIGR03269 233 EDLsDKAIWLENGEIKEEGTPDEVVAVFMEGVSE 266
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
41-231 |
5.45e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 70.90 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQ-LAKHVGLMFQnpdDQIIF-PTVAEELAFSLTA---R 115
Cdd:TIGR02203 360 TVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQ---DVVLFnDTIANNIAYGRTEqadR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 116 GETRQAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED-- 190
Cdd:TIGR02203 437 AEIERALAAaYAQDFVDKlpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlm 516
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 191 SGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEA 231
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-223 |
5.89e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.20 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMfqnPDDQIIFP--T 103
Cdd:TIGR01257 943 RPAVDRLNITFYENQItAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC---PQHNILFHhlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 104 VAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQAR 183
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2539771384 184 LAAQLED--SGHQILVSTHLLEH--VYGfERVLWLEQGRVRADG 223
Cdd:TIGR01257 1100 IWDLLLKyrSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSG 1142
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
41-219 |
1.10e-13 |
|
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: 67.82 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGLMFQNPddqiifptvaeeLAFSLTARGETR 119
Cdd:cd03369 36 KIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDP------------TLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 120 QAARQQAREFLArrGLEAWAGRavSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL--EDSGHQILV 197
Cdd:cd03369 104 PFDEYSDEEIYG--ALRVSEGG--LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIreEFTNSTILT 179
|
170 180
....*....|....*....|..
gi 2539771384 198 STHLLEHVYGFERVLWLEQGRV 219
Cdd:cd03369 180 IAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-228 |
1.58e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGL----DQPK-QGRVVVHGCDT-QADRSQLAKHVGLMFQNPD- 96
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTItALMGPSGSGKSTLLRVFNRLielyPEARvSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 97 --DQIIFPTVAeeLAFSLTARGETRQAARQQAREFL--------ARRGLEAWAGRavseLSQGQRQQVCLLALQISEPAT 166
Cdd:PRK14247 94 ipNLSIFENVA--LGLKLNRLVKSKKELQERVRWALekaqlwdeVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 167 LLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESlflELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-238 |
1.78e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.75 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQAD----RSQLAkhVGLMFQNPDdqi 99
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIvGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkRARLG--IGYLPQEAS--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQV----CLlalqISEPATLLLDEPF 173
Cdd:COG1137 89 IFRklTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVeiarAL----ATNPKFILLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 174 ASLDLLSQA---RLAAQLEDSGHQILVSTH-------LLEHVYgfervlWLEQGRVRADGPGREIceAYAEDVRE 238
Cdd:COG1137 165 AGVDPIAVAdiqKIIRHLKERGIGVLITDHnvretlgICDRAY------IISEGKVLAEGTPEEI--LNNPLVRK 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-202 |
1.92e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.31 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNPddQIIFP 102
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPvSSLDQDEVRRRVSVCAQDA--HLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 TVAEELAFsltARGEtrqAARQQAREFLARRGLEAWA-----------GRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:TIGR02868 424 TVRENLRL---ARPD---ATDEELWAALERVGLADWLralpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 172 PFASLDLLSQARLAAQL--EDSGHQILVSTHLL 202
Cdd:TIGR02868 498 PTEHLDAETADELLEDLlaALSGRTVVLITHHL 530
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-203 |
2.86e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQ--PK---QGRVVVHGCDT---QADRSQLAKHVGLMFQNP 95
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEItALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 DDqiiFP-TVAEELAFSLTARGETRQAARQQAREfLARRGLEAWA-------GRAVSeLSQGQRQQVCLLALQISEPATL 167
Cdd:PRK14239 96 NP---FPmSIYENVVYGLRLKGIKDKQVLDEAVE-KSLKGASIWDevkdrlhDSALG-LSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2539771384 168 LLDEPFASLDLLSQARLAAQLEDSGHQ--ILVSTHLLE 203
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDytMLLVTRSMQ 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-219 |
2.94e-13 |
|
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: 65.53 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadrsqlakhvglmfq 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVhALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 npddqiifptvaEELAFSltargeTRQAARqqareflaRRGLEawagrAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:cd03216 62 ------------KEVSFA------SPRDAR--------RAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2539771384 174 ASLDLLSQARL---AAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRV 219
Cdd:cd03216 111 AALTPAEVERLfkvIRRLRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-228 |
5.05e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 32 GLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLM--FQNPDdqiIFP--TVAE 106
Cdd:PRK11300 23 NVNLEVREQEIvSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrtFQHVR---LFRemTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 107 ELA---------------FSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:PRK11300 100 NLLvaqhqqlktglfsglLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 172 PFASL-----DLLSQarLAAQLEDSgHQilVSTHLLEH----VYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK11300 180 PAAGLnpketKELDE--LIAELRNE-HN--VTVLLIEHdmklVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
42-219 |
8.46e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVGLMFQNP---------DDQIIFPTVAEElafs 111
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAglfnrsiedNIRVGRPDATDE---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 ltargETRQAA-RQQAREFLARR--GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL 188
Cdd:PRK13657 440 -----EMRAAAeRAQAHDFIERKpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
170 180 190
....*....|....*....|....*....|...
gi 2539771384 189 ED--SGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:PRK13657 515 DElmKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
33-223 |
1.03e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.80 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMrIGLVGDNGAGKSSLFRLISGL---DQPKQGRVVVHGCDTQADrSQLAK-------HVGLMFQ--NPDDQIi 100
Cdd:PRK09984 25 LNIHHGEM-VALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQRE-GRLARdirksraNTGYIFQqfNLVNRL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 101 fpTVAEELAfsLTARGET----------RQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLD 170
Cdd:PRK09984 102 --SVLENVL--IGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 171 EPFASLDLLSQARLAAQLED----SGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDinqnDGITVVVTLHQVDYALRYcERIVALRQGHVFYDG 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
44-235 |
1.12e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQAD-RSQLAKHVGLMFQNpddQIIFP--TVAEELAFSLTARG 116
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakiSDAElREVRRKKIAMVFQS---FALMPhmTVLDNTAFGMELAG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 117 ETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLE--DSGHQ 194
Cdd:PRK10070 136 INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVklQAKHQ 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2539771384 195 ---ILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEAYAED 235
Cdd:PRK10070 216 rtiVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
43-177 |
1.76e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKH--VGLMFQNPDdqiIFP--TVAEELAFS--LTARG 116
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAagIAIIHQELN---LVPnlSVAENIFLGrePRRGG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 117 ETRQAA-RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL-ALqISEPATLLLDEPFASLD 177
Cdd:COG1129 111 LIDWRAmRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIArAL-SRDARVLILDEPTASLT 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-206 |
1.81e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ--ADRSQLAKHVGLMFQN----PDdqiifPTVAEELAF-SLTAR 115
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQElhlvPE-----MTVAENLYLgQLPHK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 116 GE--TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVcLLALQISEPATLL-LDEPFASL-----DLLsqARLAAQ 187
Cdd:PRK11288 109 GGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV-EIAKALARNARVIaFDEPTSSLsareiEQL--FRVIRE 185
|
170
....*....|....*....
gi 2539771384 188 LEDSGHQILVSTHLLEHVY 206
Cdd:PRK11288 186 LRAEGRVILYVSHRMEEIF 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-244 |
1.84e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 31 EGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMF----Qnpddqiifptv 104
Cdd:COG4586 39 DDISFTIEpgEI-VGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFgqrsQ----------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 105 aeeLAFSLTARgET-----------RQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:COG4586 107 ---LWWDLPAI-DSfrllkaiyripDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 174 ASLDLLSQAR----LAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPgreiceayAEDVRERAAAER 244
Cdd:COG4586 183 IGLDVVSKEAirefLKEYNRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGS--------LEELKERFGPYK 250
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-219 |
1.94e-12 |
|
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: 64.60 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQP---KQGRVVVHGCdtQADRSQLAKHVGLMFQNpDDQI 99
Cdd:cd03234 17 NKYARILNDVSLHVESGQVmAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ--PRKPDQFQKCVAYVRQD-DILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFPTVAEELAFSLTARG--ETRQAARQQAREFLARR--GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFAS 175
Cdd:cd03234 94 PGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRdlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 176 LDLLSQ---ARLAAQLEDSGHQILVSTH-----LLEHvygFERVLWLEQGRV 219
Cdd:cd03234 174 LDSFTAlnlVSTLSQLARRNRIVILTIHqprsdLFRL---FDRILLLSSGEI 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-219 |
2.71e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 34 TLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQ--LAKHVGLMFQNPddqIIFP--TVAEEL 108
Cdd:COG3845 25 SLTVRPGEIhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaIALGIGMVHQHF---MLVPnlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 109 AFSLTARGET---RQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQV----CLLAlqisEPATLLLDEPFASL----- 176
Cdd:COG3845 102 VLGLEPTKGGrldRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVeilkALYR----GARILILDEPTAVLtpqea 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2539771384 177 -DLLSQARlaaQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRV 219
Cdd:COG3845 178 dELFEILR---RLAAEGKSIIFITHKLREVMAIaDRVTVLRRGKV 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-194 |
3.21e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 1 MPQPSPSETvsshSIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA 79
Cdd:PRK10575 2 QEYTNHSDT----TFALRNVSFRVPGRTLLHPLSLTFPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 80 DRSQL-AKHVGLMFQN-PDDQIIfpTVAEELAFSL----TARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQ 153
Cdd:PRK10575 78 WSSKAfARKVAYLPQQlPAAEGM--TVRELVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 154 VCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQ 194
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-227 |
3.93e-12 |
|
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: 63.71 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 24 RGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT-QADRSQLAKHVGLMFQNPddqIIF 101
Cdd:cd03249 13 RPDVPILKGLSLTIPPgKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGLVSQEP---VLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 102 P-TVAEELAFSLTARG--ETRQAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFAS 175
Cdd:cd03249 90 DgTIAENIRYGKPDATdeEVEEAAKKaNIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 176 LDLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGRE 227
Cdd:cd03249 170 LDAESEKLVQEALDRamKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
41-234 |
4.30e-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: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMfqnPDDQIIF-PTVAEELAF-SLTARGE 117
Cdd:cd03253 29 KVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSLRRAIGVV---PQDTVLFnDTIGYNIRYgRPDATDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAR--EFLAR-----------RGLeawagravsELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARL 184
Cdd:cd03253 106 EVIEAAKAAQihDKIMRfpdgydtivgeRGL---------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 185 AAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICE---AYAE 234
Cdd:cd03253 177 QAALRDvsKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAkggLYAE 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-200 |
4.44e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 19 AVTLVRGSRTVFEGLTLDLQEMRIGLV-GDNGAGKSSLFRLISGLDQPKQGRVVVHGcdTQADRSQLAKHVGLMFQNPDD 97
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQIDG--KTATRGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 98 QIIFPTVaEELAFSLTARGetrQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLD 177
Cdd:PRK13543 94 KADLSTL-ENLHFLCGLHG---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*..
gi 2539771384 178 L----LSQARLAAQLEdSGHQILVSTH 200
Cdd:PRK13543 170 LegitLVNRMISAHLR-GGGAALVTTH 195
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-200 |
4.50e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQ----NPddqiiFPTVAE----ELAFSLTAR 115
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHrsgiNP-----YLTLREnclyDIHFSPGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 116 GETrqaarqqarEFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED---SG 192
Cdd:PRK13540 107 GIT---------ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEhraKG 177
|
....*...
gi 2539771384 193 HQILVSTH 200
Cdd:PRK13540 178 GAVLLTSH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-200 |
6.43e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.65 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFR-------LISGLDqpKQGRVVVHG---CDTQADRSQ 83
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQItAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGknlYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAKHVGLMFQNPDDqiiFP-TVAEELAFSLTARG-----------ETRQAAR-QQAREFLARRGLEawagravseLSQGQ 150
Cdd:PRK14243 89 VRRRIGMVFQKPNP---FPkSIYDNIAYGARINGykgdmdelverSLRQAALwDEVKDKLKQSGLS---------LSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 151 RQQVCL---LALQisePATLLLDEPFASLDLLSQARLAAQLEDSGHQ--ILVSTH 200
Cdd:PRK14243 157 QQRLCIaraIAVQ---PEVILMDEPCSALDPISTLRIEELMHELKEQytIIIVTH 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-228 |
6.95e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVhgcdTQADRSQLAKH------VGLMfqnPDDQI 99
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIvGLLGPNGAGKTTTFYMVVGIVPRDAGNIII----DDEDISLLPLHararrgIGYL---PQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFP--TVAEELAFSLTARGETRQAARQ-QAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASL 176
Cdd:PRK10895 89 IFRrlSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 177 DLLSQ---ARLAAQLEDSGHQILVSTH-LLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK10895 169 DPISVidiKRIIEHLRDSGLGVLITDHnVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
42-182 |
7.84e-12 |
|
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: 64.32 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLdQPKQGRVVVHGCD-TQADRSQLA---KHVGLMFQNPD---------DQIIfptvAEEL 108
Cdd:COG4172 315 LGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDlDGLSRRALRplrRRMQVVFQDPFgslsprmtvGQII----AEGL 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 109 AfsLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCL---LALqisEPATLLLDEPFASLDLLSQA 182
Cdd:COG4172 390 R--VHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIaraLIL---EPKLLVLDEPTSALDVSVQA 462
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-239 |
8.81e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMRI-GLVGDNGAGKSSLF----RLISGLDQPKQ--GRVVVHGCDT-QADRSQLAKHVGLMFQNPDDq 98
Cdd:PRK14246 23 KAILKDITIKIPNNSIfGIMGPSGSGKSTLLkvlnRLIEIYDSKIKvdGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 99 iiFP--TVAEELAFSLTARG-ETRQAARQQAREFLARRGLeaWA------GRAVSELSQGQRQQVCLLALQISEPATLLL 169
Cdd:PRK14246 102 --FPhlSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGL--WKevydrlNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 170 DEPFASLDLLSQA---RLAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEAYAEDVRER 239
Cdd:PRK14246 178 DEPTSMIDIVNSQaieKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
29-177 |
1.63e-11 |
|
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: 62.07 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 29 VFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHvglmfqnpddQII------- 100
Cdd:COG4778 26 VLDGVSFSVAAGEcVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPR----------EILalrrrti 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 101 -----F----PTV-AEEL-AFSLTARGETRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:COG4778 96 gyvsqFlrviPRVsALDVvAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
....*....
gi 2539771384 169 LDEPFASLD 177
Cdd:COG4778 176 LDEPTASLD 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-218 |
2.61e-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: 63.03 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 23 VRGSRTVFEGLTLD-LQEMRIGLVGDNGAGKSSLFRLISGLDQPKQGR--------------------------VVVHGC 75
Cdd:TIGR03719 14 VPPKKEILKDISLSfFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgikvgylpqepqldptktvreNVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 76 DTQADRSQLAKHVGLMFQNPDDQiiFPTVAEELAfSLTARGETRQA---ARQQAREFLARRgLEAWAGRaVSELSQGQRQ 152
Cdd:TIGR03719 94 AEIKDALDRFNEISAKYAEPDAD--FDKLAAEQA-ELQEIIDAADAwdlDSQLEIAMDALR-CPPWDAD-VTKLSGGERR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 153 QVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQILVSTH---LLEHVYGFerVLWLEQGR 218
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHdryFLDNVAGW--ILELDRGR 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-182 |
4.74e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.52 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 22 LVRGSRTV--FEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT----QADRSQLAKHVGLMFQN 94
Cdd:PRK11308 21 LFKPERLVkaLDGVSFTLERGKtLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 P-----DDQIIFPTVAEELAFSLTArgeTRQAARQQAREFLARRGLEA-WAGRAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK11308 101 PygslnPRKKVGQILEEPLLINTSL---SAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170
....*....|....
gi 2539771384 169 LDEPFASLDLLSQA 182
Cdd:PRK11308 178 ADEPVSALDVSVQA 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-228 |
5.56e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFE-----GLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA---DR--S 82
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYEhqaihDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKyiR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 83 QLAKHVGLMFQNPDDQIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGLEawagRAVSELSQ-----GQRQQVCLL 157
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS----RDVMSQSPfqmsgGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 158 ALQISEPATLLLDEPFASLDLLSQARLAA-----QLEDSGHQILVsTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRllkslQTDENKTIILV-SHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-177 |
7.27e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ----ADRSqlakhV 88
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEfVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvppAERG-----V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNpddQIIFP--TVAEELAFSL----TARGETRQAArQQAREFLArrgLEAWAGRAVSELSQGQRQQVCLLALQIS 162
Cdd:PRK11000 78 GMVFQS---YALYPhlSVAENMSFGLklagAKKEEINQRV-NQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170
....*....|....*
gi 2539771384 163 EPATLLLDEPFASLD 177
Cdd:PRK11000 151 EPSVFLLDEPLSNLD 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-217 |
7.75e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.36 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 3 QPSPSETVSSHSIRLDAVTLVRGS-RTVFEGLTLDLQ--EmRIGLVGDNGAGKSSLFRLISGLDQPKQGRVvvhgcdtqa 79
Cdd:COG4178 351 AASRIETSEDGALALEDLTLRTPDgRPLLEDLSLSLKpgE-RLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 80 drsQLAKHVGLMF--QNP-------DDQIIFPtvAEELAFSltargetrqaaRQQAREFLARRGLEAWAGRAVSE----- 145
Cdd:COG4178 421 ---ARPAGARVLFlpQRPylplgtlREALLYP--ATAEAFS-----------DAELREALEAVGLGHLAERLDEEadwdq 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 146 -LSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLEDSGHQI-LVS-TH---LLEHvygFERVLWLEQG 217
Cdd:COG4178 485 vLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTtVISvGHrstLAAF---HDRVLELTGD 559
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-224 |
8.10e-11 |
|
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: 59.46 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPK--QGRVVVHGCDTQA----DRSQLAkhVGLMFQNPDD 97
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVhALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDlppeERARLG--IFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 98 qiiFPTVAEElafsltargetrqaarqqarEFLarrgleawagRAVSE-LSQGQRQQVCLLALQISEPATLLLDEPFASL 176
Cdd:cd03217 89 ---IPGVKNA--------------------DFL----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 177 DLLSQ---ARLAAQLEDSGHQILVSTH---LLEHVYGfERVLWLEQGRVRADGP 224
Cdd:cd03217 136 DIDALrlvAEVINKLREEGKSVLIITHyqrLLDYIKP-DRVHVLYDGRIVKSGD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-215 |
1.56e-10 |
|
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: 60.72 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVhgcdtqADRSQLAkHVGLMFQNPDDQiifPT 103
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIvGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLA-YVDQSRDALDPN---KT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 104 VAEELAFSLTargETRQAARQ-QAREFLAR---RGLEawAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLL 179
Cdd:TIGR03719 403 VWEEISGGLD---IIKLGKREiPSRAYVGRfnfKGSD--QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2539771384 180 SQARLAAQLEDSGHQILVSTH-------LLEHVYGFE---RVLWLE 215
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHdrwfldrIATHILAFEgdsHVEWFE 523
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-183 |
1.56e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 18 DAVTLvrgsrTVFEGLTLdlqemriGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADRSQLAKHVGLMFQ 93
Cdd:PRK15079 38 DGVTL-----RLYEGETL-------GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgmKDDEWRAVRSDIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPDDQI-----IFPTVAEELafsLTARGE-TRQAARQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLALQISEPAT 166
Cdd:PRK15079 106 DPLASLnprmtIGEIIAEPL---RTYHPKlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKL 182
|
170
....*....|....*..
gi 2539771384 167 LLLDEPFASLDLLSQAR 183
Cdd:PRK15079 183 IICDEPVSALDVSIQAQ 199
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-177 |
1.81e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRIGLV-GDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMF 92
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPddqIIF-PTVAEELAFSLTARGETRQaaRQQAREFLARRGL-EAWAGRAVSELSQGQRQQVCLLA-LQISePATLLL 169
Cdd:PRK10247 88 QTP---TLFgDTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRnLQFM-PKVLLL 161
|
....*...
gi 2539771384 170 DEPFASLD 177
Cdd:PRK10247 162 DEITSALD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-228 |
2.02e-10 |
|
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: 60.08 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQE-MRIGLVGDNGAGKS----SLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAK----HVGLMFQ- 93
Cdd:COG4172 21 GTVEAVKGVSFDIAAgETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDlLGLSERELRRirgnRIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 -----NPddqiiFPTVAEELAFSLTA-RGETRQAARQQAREFLARRGLEAWAGRAVS---ELSQGQRQQVCL-LALqISE 163
Cdd:COG4172 101 pmtslNP-----LHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIaMAL-ANE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 164 PATLLLDEPFASLDLLSQAR---LAAQL-EDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQildLLKDLqRELGMALLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTAEL 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
42-219 |
2.11e-10 |
|
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: 58.33 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGL--DQPKQGRVVVHGcdTQADRSQLAKHVGLMFQnpdDQIIFP--TVAEELAFSLTARGe 117
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING--RPLDKRSFRKIIGYVPQ---DDILHPtlTVRETLMFAAKLRG- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 trqaarqqareflarrgleawagravseLSQGQRQQVCL-LALqISEPATLLLDEP------FASLDLLSQARlaaQLED 190
Cdd:cd03213 112 ----------------------------LSGGERKRVSIaLEL-VSNPSLLFLDEPtsgldsSSALQVMSLLR---RLAD 159
|
170 180 190
....*....|....*....|....*....|.
gi 2539771384 191 SGHQILVSTHLL--EHVYGFERVLWLEQGRV 219
Cdd:cd03213 160 TGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-186 |
3.55e-10 |
|
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: 58.57 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcDTQADRSQLAKhvglmfqnPDdqiiFPTVAEELAFSLTARGETRQa 121
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQYIK--------AD----YEGTVRDLLSSITKDFYTHP- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 122 arQQAREFLARRGLEAWAGRAVSELSQGQRQQVClLALQISEPATL-LLDEPFASLDllSQARLAA 186
Cdd:cd03237 94 --YFKTEIAKPLQIEQILDREVPELSGGELQRVA-IAACLSKDADIyLLDEPSAYLD--VEQRLMA 154
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-228 |
4.95e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISG-LDQPK-------QGRVVVHGCDTQA-DRSQL 84
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVtALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAiDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 85 AKHVGLMFQNPddQIIFPTVAEELAF-----SLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQ--RQQVCLL 157
Cdd:PRK13547 82 ARLRAVLPQAA--QPAFAFSAREIVLlgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGElaRVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 158 ALQI-------SEPATLLLDEPFASLDLLSQARLAAQLEDSGHQILVSTHLLEHVYGF-----ERVLWLEQGRVRADGPG 225
Cdd:PRK13547 160 LAQLwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaarhaDRIAMLADGAIVAHGAP 239
|
...
gi 2539771384 226 REI 228
Cdd:PRK13547 240 ADV 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-206 |
5.49e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLmFQNPDDQIIFP--TVAEELAFSLTARGETRQA 121
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI-YLVPQEPLLFPnlSVKENILFGLPKRQASMQK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGravsELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQ---LEDSGHQILVS 198
Cdd:PRK15439 121 MKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRireLLAQGVGIVFI 196
|
....*...
gi 2539771384 199 THLLEHVY 206
Cdd:PRK15439 197 SHKLPEIR 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-231 |
8.05e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 31 EGLTLDLQEM--------RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTqadrSQLAKHvGLMFQ---NPDDQI 99
Cdd:TIGR00957 1296 EDLDLVLRHInvtihggeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLH-DLRFKitiIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 100 IFP-TVAEEL-AFSLTARGETRQAAR-QQAREFLARR--GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFA 174
Cdd:TIGR00957 1371 LFSgSLRMNLdPFSQYSDEEVWWALElAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 175 SLDL----LSQARLAAQLEDSghQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEA 231
Cdd:TIGR00957 1451 AVDLetdnLIQSTIRTQFEDC--TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-200 |
8.42e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRIGL-VGDNGAGKSSLFRLISG--LDQPKQGRVVVhgcdtqadrsqlakhvgl 90
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLiVGASGSGKSTLLRLLAGalKGTPVAGCVDV------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 mfqnPDDQIifptvAEELAF--SLTARGETRQAArqqarEFLARRGL-EAWAGRA-VSELSQGQRQQVcLLALQISE-PA 165
Cdd:COG2401 92 ----PDNQF-----GREASLidAIGRKGDFKDAV-----ELLNAVGLsDAVLWLRrFKELSTGQKFRF-RLALLLAErPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2539771384 166 TLLLDEPFASLDLLSQARLAAQLED----SGHQILVSTH 200
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKlarrAGITLVVATH 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-228 |
9.85e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED---SGHQ 194
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmvrDGAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 2539771384 195 ILVSTHLLEHVYGFERVLW-LEQGRVRADGPGREI 228
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTvIDRGRVIADGKVDEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-219 |
1.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 29 VFEGLTLDLQEM-RIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT-QADRSQLAKHVGLMFQNPddqIIFPTVae 106
Cdd:PLN03130 1254 VLHGLSFEISPSeKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIsKFGLMDLRKVLGIIPQAP---VLFSGT-- 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 107 eLAFSLTARGETRQA------ARQQAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDL 178
Cdd:PLN03130 1329 -VRFNLDPFNEHNDAdlweslERAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2539771384 179 LSQARLAAQL--EDSGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:PLN03130 1408 RTDALIQKTIreEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-239 |
1.82e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDL-QEMRIGLVGDNGAGKSSLFRLISGL-----DQPKQGRVVVHGCDT---QADRSQLAKHVGLMFQNP 95
Cdd:PRK14267 15 GSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIyspDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 DDqiiFP--TVAEELAFSLTARGETRQAARQQAREFLARRGLEAWA------GRAVSELSQGQRQQVCLLALQISEPATL 167
Cdd:PRK14267 95 NP---FPhlTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDevkdrlNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 168 LLDEPFASLDLLSQAR---LAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICEAYAEDVRER 239
Cdd:PRK14267 172 LMDEPTANIDPVGTAKieeLLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-202 |
1.99e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVvvhgcdtqadrsQLAKHVGLMFq 93
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPgSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------GLAKGIKLGY- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 NPDDQIIFpTVAEELAFSLTARgETRQAARQQAREFLARRGLEawaGRAVSE----LSQGQRQQVCLLALQISEPATLLL 169
Cdd:PRK10636 380 FAQHQLEF-LRADESPLQHLAR-LAPQELEQKLRDYLGGFGFQ---GDKVTEetrrFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*.
gi 2539771384 170 DEPFASLDL-LSQARLAAQLEDSGHQILVS--THLL 202
Cdd:PRK10636 455 DEPTNHLDLdMRQALTEALIDFEGALVVVShdRHLL 490
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-237 |
2.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 5 SPSETVSSHSIRLDAVTLVRG--SRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQP-----KQGRVVVHGCD 76
Cdd:PRK14271 10 SGAADVDAAAPAMAAVNLTLGfaGKTVLDQVSMGFPARAVtSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 77 --TQADRSQLAKHVGLMFQNPDD---QIIFPTVAEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQR 151
Cdd:PRK14271 90 ifNYRDVLEFRRRVGMLFQRPNPfpmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 152 QQVCLLALQISEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREI 228
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEfirSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
250
....*....|.
gi 2539771384 229 CEA--YAEDVR 237
Cdd:PRK14271 250 FSSpkHAETAR 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-205 |
2.40e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD----TQADRSQLAkhVG 89
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIhALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynklDHKLAAQLG--IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNPD--DQIifpTVAEELafsLTARGETRQA----------ARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLL 157
Cdd:PRK09700 84 IIYQELSviDEL---TVLENL---YIGRHLTKKVcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 158 ALQISEPATLLLDEPFASLDLLSQARLAA---QLEDSGHQILVSTHLLEHV 205
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLimnQLRKEGTAIVYISHKLAEI 208
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
42-234 |
2.65e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADR-SQLAKHVGLMFQNPddQIIFPTVAEELAFSLT---ARGE 117
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQVALVSQNV--HLFNDTIANNIAYARTeqySREQ 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 118 TRQAARQ-QAREFLAR--RGLEAWAGRAVSELSQGQRQQVCLL-ALQISEPaTLLLDEPFASLDLLSQARLAAQLED--S 191
Cdd:PRK11176 450 IEEAARMaYAMDFINKmdNGLDTVIGENGVLLSGGQRQRIAIArALLRDSP-ILILDEATSALDTESERAIQAALDElqK 528
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2539771384 192 GHQILVSTHLLEHVYGFERVLWLEQGRVRADGPGREICE---AYAE 234
Cdd:PRK11176 529 NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAqngVYAQ 574
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-187 |
3.79e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRT-VFEGLTLDLQ--EMrIGLVGDNGAGKSSLFRLISGLDQPKQG------RVVvhgcdTQ---ADR 81
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVAdgEF-IVLVGPSGCGKSTLLRMVAGLERITSGeiwiggRVV-----NElepADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 82 SqlakhVGLMFQNpddQIIFP--TVAEELAFSL----TARGETRQAARQQAR-----EFLARRGleawagravSELSQGQ 150
Cdd:PRK11650 77 D-----IAMVFQN---YALYPhmSVRENMAYGLkirgMPKAEIEERVAEAARilelePLLDRKP---------RELSGGQ 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 2539771384 151 RQQVCLLALQISEPATLLLDEPFASLDllsqARLAAQ 187
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD----AKLRVQ 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-219 |
4.30e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 6 PSETVSSHSIRLDAVTLVR--GSRTVFEGLTLDLQ-EMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADR 81
Cdd:PLN03232 1226 VSGWPSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSpSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvAKFGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 82 SQLAKHVGLMFQNPddqIIFptvAEELAFSLTARGETRQAA------RQQAREFLARR--GLEAWAGRAVSELSQGQRQQ 153
Cdd:PLN03232 1306 TDLRRVLSIIPQSP---VLF---SGTVRFNIDPFSEHNDADlwealeRAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQL 1379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 154 VCLLALQISEPATLLLDEPFASLDLLSQARLAAQL--EDSGHQILVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIreEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-236 |
6.13e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPK--QGRVVVHGcdtQADRSQLAKHVGLMFQnpdDQIIFP- 102
Cdd:PLN03211 81 RTILNGVTGMASPGEIlAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN---RKPTKQILKRTGFVTQ---DDILYPh 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 103 -TVAEELAF--------SLTARGETRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPF 173
Cdd:PLN03211 155 lTVRETLVFcsllrlpkSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 174 ASLDLLSQARLA---AQLEDSGHQILVSTHL-LEHVYG-FERVLWLEQGRVRADGPGREiCEAYAEDV 236
Cdd:PLN03211 235 SGLDATAAYRLVltlGSLAQKGKTIVTSMHQpSSRVYQmFDSVLVLSEGRCLFFGKGSD-AMAYFESV 301
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
30-237 |
6.99e-09 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 55.39 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 30 FEGLTLDLQEMRIGLVGDNGAGKSSLFRLISG-LDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQNPDDQI----IFPTV 104
Cdd:COG3593 14 IKDLSIELSDDLTVLVGENNSGKSSILEALRLlLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLlrllLKEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 105 AEELAFSLTARGETRQAARQQAREFLARRGLEAWAGRAV----------------------------SELSQGQRQQVCL 156
Cdd:COG3593 94 KEELEEALEELNEELKEALKALNELLSEYLKELLDGLDLelelsldeledllkslslriedgkelplDRLGSGFQRLILL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 157 LALQI-------SEPATLLLDEPFASLDLLSQARLAAQLED---SGHQILVSTH---LLEHVyGFERVLWLEqgRVRADG 223
Cdd:COG3593 174 ALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKElseKPNQVIITTHsphLLSEV-PLENIRRLR--RDSGGT 250
|
250
....*....|....
gi 2539771384 224 PGREICEAYAEDVR 237
Cdd:COG3593 251 TSTKLIDLDDEDLR 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-205 |
9.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPK-----QGRVVVHGCDTQADR---SQL 84
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVtAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRvnlNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 85 AKHVGLMFQNPDdqiIFP-TVAEELAFSLTARGETRQAARQQAREFlARRGLEAW------AGRAVSELSQGQRQQVCLL 157
Cdd:PRK14258 87 RRQVSMVHPKPN---LFPmSVYDNVAYGVKIVGWRPKLEIDDIVES-ALKDADLWdeikhkIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 158 ALQISEPATLLLDEPFASLD---------LLSQARLAAQLedsghQILVSTHLLEHV 205
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasmkvesLIQSLRLRSEL-----TMVIVSHNLHQV 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-204 |
2.07e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 20 VTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQL---AKHVGLMFQN 94
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKItAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLytvRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 pddQIIFP--TVAEELAFSLtaRGETRQAA---RQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLL 169
Cdd:PRK11831 93 ---GALFTdmNVFDNVAYPL--REHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2539771384 170 DEPFASLDLLSQARLAAQLEDSGHQILVSTHLLEH 204
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
42-235 |
2.15e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSS----LFRLIsgldqPKQGRVVVHGCDTQA-DRSQL---AKHVGLMFQNPDDQIiFP--TVAEELAFS 111
Cdd:PRK15134 315 LGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNlNRRQLlpvRHRIQVVFQDPNSSL-NPrlNVLQIIEEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 LTARGETRQAARQQAR--EFLARRGLEAWA-GRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQL 188
Cdd:PRK15134 389 LRVHQPTLSAAQREQQviAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2539771384 189 E--DSGHQI--LVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEAYAED 235
Cdd:PRK15134 469 KslQQKHQLayLFISHDLHVVRALcHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-192 |
3.44e-08 |
|
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: 51.39 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGS-RTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDtqadrsqlakhvGLMF 92
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPgDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------DLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 --QNP-------DDQIIFPtvaeelafsltargetrqaarqqareflarrgleaWAgravSELSQGQRQQVCLLALQISE 163
Cdd:cd03223 69 lpQRPylplgtlREQLIYP-----------------------------------WD----DVLSGGEQQRLAFARLLLHK 109
|
170 180
....*....|....*....|....*....
gi 2539771384 164 PATLLLDEPFASLDLLSQARLAAQLEDSG 192
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELG 138
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-72 |
4.96e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 4.96e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVV 72
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIvGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
42-234 |
5.10e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.13 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSL-----FRLISGLDqpKQGRVVVHGcdTQADRSQLAKHVGLMFQnpdDQIIFP--TVAEELAFSLTA 114
Cdd:TIGR00955 54 LAVMGSSGAGKTTLmnalaFRSPKGVK--GSGSVLLNG--MPIDAKEMRAISAYVQQ---DDLFIPtlTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 115 RGETRQAA---RQQAREFLARRGLEAWA-------GRaVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARL 184
Cdd:TIGR00955 127 RMPRRVTKkekRERVDEVLQALGLRKCAntrigvpGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2539771384 185 AA---QLEDSGHQILVSTHL-LEHVYG-FERVLWLEQGRVRADGPGREICEAYAE 234
Cdd:TIGR00955 206 VQvlkGLAQKGKTIICTIHQpSSELFElFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
42-219 |
6.81e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQAdRSQL---AKHVGLMFQNPDDQIIFP--TVAEELAFS----- 111
Cdd:PRK09700 292 LGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-RSPLdavKKGMAYITESRRDNGFFPnfSIAQNMAISrslkd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 ---------LTARGETRQAarQQAREFLARRGleAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA 182
Cdd:PRK09700 371 ggykgamglFHEVDEQRTA--ENQRELLALKC--HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKA 446
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 183 ---RLAAQLEDSGHQIL-VSTHLLEHVYGFERVLWLEQGRV 219
Cdd:PRK09700 447 eiyKVMRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
42-244 |
6.93e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqaDRSQLAKHVGLMFQnpddqiifPTVAEELAFSLTARGETRQA 121
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ--------LTGIENIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQvclLALQIS---EPATLLLDEPFASLD-LLSQARLAA--QLEDSGHQI 195
Cdd:PRK13546 120 IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAK---LGFSINitvNPDILVIDEALSVGDqTFAQKCLDKiyEFKEQNKTI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 196 LVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREIC---EAYAEDVRERAAAER 244
Cdd:PRK13546 197 FFVSHNLGQVRQFcTKIAWIEGGKLKDYGELDDVLpkyEAFLNDFKKKSKAEQ 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-178 |
1.30e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 2 PQPSPSETVSSHSirlDAVTLVRGSRTVFEGLT--LDLqEMRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA 79
Cdd:PLN03073 500 PDDRPGPPIISFS---DASFGYPGGPLLFKNLNfgIDL-DSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 80 DRSQlaKHV-GL-MFQNPDDQII--FPTVAEelafsltargetrqaarQQAREFLARRGLEA-WAGRAVSELSQGQRQQV 154
Cdd:PLN03073 576 VFSQ--HHVdGLdLSSNPLLYMMrcFPGVPE-----------------QKLRAHLGSFGVTGnLALQPMYTLSGGQKSRV 636
|
170 180
....*....|....*....|....
gi 2539771384 155 CLLALQISEPATLLLDEPFASLDL 178
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDL 660
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-194 |
1.57e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFegltldlqemriglVGDNGAGKSSLFRLISGLDQPKQGRvvvhgCDTQADR------SQLAKHV 88
Cdd:PRK10938 19 LQLPSLTLNAGDSWAF--------------VGANGSGKSALARALAGELPLLSGE-----RQSQFSHitrlsfEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 89 GLMFQNPDDQIIFPtvaEELAFSLTAR----GETRQAAR--QQAREFlarrGLEAWAGRAVSELSQGQRQQVCLLALQIS 162
Cdd:PRK10938 80 SDEWQRNNTDMLSP---GEDDTGRTTAeiiqDEVKDPARceQLAQQF----GITALLDRRFKYLSTGETRKTLLCQALMS 152
|
170 180 190
....*....|....*....|....*....|..
gi 2539771384 163 EPATLLLDEPFASLDLLSQARLAAQLEDSGHQ 194
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-222 |
4.14e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFqNPDD---QIIFP--TVAEELAFS----- 111
Cdd:PRK11288 282 VGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIML-CPEDrkaEGIIPvhSVADNINISarrhh 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 ------LTARGETRQAARQQAREFLARRGLEawagRAVSELSQGQRQQVcLLALQISEP-ATLLLDEPFASLDLLSQA-- 182
Cdd:PRK11288 361 lragclINNRWEAENADRFIRSLNIKTPSRE----QLIMNLSGGNQQKA-ILGRWLSEDmKVILLDEPTRGIDVGAKHei 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2539771384 183 -RLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRAD 222
Cdd:PRK11288 436 yNVIYELAAQGVAVLFVSSDLPEVLGVaDRIVVMREGRIAGE 477
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-184 |
4.23e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVvvhgcdtqadRSQLAKHVGLMfq 93
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKIlTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 94 nPDDQIIFPTVAEELAFSLTARGETRQA------ARQQAREFLArrgleawagRAVSELSQGQRQQVCLLALQISEPATL 167
Cdd:PRK09544 73 -PQKLYLDTTLPLTVNRFLRLRPGTKKEdilpalKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQLL 142
|
170
....*....|....*..
gi 2539771384 168 LLDEPFASLDLLSQARL 184
Cdd:PRK09544 143 VLDEPTQGVDVNGQVAL 159
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-242 |
5.74e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 16 RLDAVTLVrgSRTVFEGLTLdlqemriGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQN 94
Cdd:PRK15112 25 TVEAVKPL--SFTLREGQTL-------AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlHFGDYSYRSQRIRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDDQI-IFPTVAEELAFSLTARGETRQAARQQA-REFLARRGLEA-WAGRAVSELSQGQRQQVCLLALQISEPATLLLDE 171
Cdd:PRK15112 96 PSTSLnPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 172 PFASLDLLSQAR-----LAAQLEDSGHQILVSTHL--LEHVYgfERVLWLEQGRVRADGPGREICEAYAEDVRERAAA 242
Cdd:PRK15112 176 ALASLDMSMRSQlinlmLELQEKQGISYIYVTQHLgmMKHIS--DQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
42-218 |
5.85e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVhgcdtqadrSQLAKhVGLMFQNPddqiifptvaeELAFSLTARGETRQA 121
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARP---------APGIK-VGYLPQEP-----------QLDPEKTVRENVEEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQ----QAR----------------EFLARRG-----LEAWAG--------RA------------VSELSQGQRQQVCL 156
Cdd:PRK11819 95 VAEvkaaLDRfneiyaayaepdadfdALAAEQGelqeiIDAADAwdldsqleIAmdalrcppwdakVTKLSGGERRRVAL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 157 LALQISEPATLLLDEPFASLDLLSQARLAAQLED-SGHQILVsTH---LLEHVYGFerVLWLEQGR 218
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDyPGTVVAV-THdryFLDNVAGW--ILELDRGR 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
43-203 |
8.25e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGL--MFQNPDDQIifpTVAEELAFSLTARGETRQ 120
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYcpQFDAIDDLL---TGREHLYLYARLRGVPAE 2045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 121 AARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDllSQAR-----LAAQLEDSGHQI 195
Cdd:TIGR01257 2046 EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD--PQARrmlwnTIVSIIREGRAV 2123
|
....*...
gi 2539771384 196 LVSTHLLE 203
Cdd:TIGR01257 2124 VLTSHSME 2131
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
41-217 |
2.11e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSL----FRLISGLDqpkqGRVVVHGCDT-----QADRSQLAkhvgLMFQNPddqIIFptvAEELAFS 111
Cdd:cd03288 49 KVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDIsklplHTLRSRLS----IILQDP---ILF---SGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 LTARGETRQAARQQAREFLARR--------GLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQAR 183
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKnmvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 2539771384 184 LAAQLEDSGHQILVST--HLLEHVYGFERVLWLEQG 217
Cdd:cd03288 195 LQKVVMTAFADRTVVTiaHRVSTILDADLVLVLSRG 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-236 |
2.40e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 1 MPQpspseTVSSHSIRLDAvtlvrgSRTVFEGLTLDLQEMRI-GLVGDNGAGKS-----SLFRLISGLDQpKQGRVVVHG 74
Cdd:PRK10418 1 MPQ-----QIELRNIALQA------AQPLVHGVSLTLQRGRVlALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 75 cDTQADRSQLAKHVGLMFQNPDDQI-IFPTVAEELAFSLTARGetRQAARQQAREFLARRGLEAwAGRAVS----ELSQG 149
Cdd:PRK10418 69 -KPVAPCALRGRKIATIMQNPRSAFnPLHTMHTHARETCLALG--KPADDATLTAALEAVGLEN-AARVLKlypfEMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 150 QRQQVCL-LALqISEPATLLLDEPFASLDLLSQAR----LAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADG 223
Cdd:PRK10418 145 MLQRMMIaLAL-LCEAPFIIADEPTTDLDVVAQARildlLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
250
....*....|...
gi 2539771384 224 PGREICEAYAEDV 236
Cdd:PRK10418 224 DVETLFNAPKHAV 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-190 |
2.53e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 27 RTVFEGLTLDLQEMR-IGLVGDNGAGKS----SLFRLisgLDQPK----QGRVVVHG-----CDTQADRSQLAKHVGLMF 92
Cdd:PRK15134 22 RTVVNDVSLQIEAGEtLALVGESGSGKSvtalSILRL---LPSPPvvypSGDIRFHGesllhASEQTLRGVRGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 QNPDDQI-IFPTVAEELAFSLTA-RGETRQAARQQAREFLARRGLEAWAGRAVS---ELSQGQRQQVCLLALQISEPATL 167
Cdd:PRK15134 99 QEPMVSLnPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELL 178
|
170 180
....*....|....*....|...
gi 2539771384 168 LLDEPFASLDLLSQARLAAQLED 190
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRE 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
33-205 |
2.66e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.59 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMRiGLVGDNGAGKSSLFRLISGLDQPK----QGRVVVHGCD----TQADRSQL-AKHVGLMFQNP-------- 95
Cdd:COG4170 28 LTLNEGEIR-GLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDllklSPRERRKIiGREIAMIFQEPsscldpsa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 --DDQIIFPTVAEELAFSLTARgetRQAARQQAREFLARRG-------LEAWAgravSELSQGQRQQVcLLALQI-SEPA 165
Cdd:COG4170 107 kiGDQLIEAIPSWTFKGKWWQR---FKWRKKRAIELLHRVGikdhkdiMNSYP----HELTEGECQKV-MIAMAIaNQPR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2539771384 166 TLLLDEPFASLDLLSQA---RLAAQL-EDSGHQILVSTHLLEHV 205
Cdd:COG4170 179 LLIADEPTNAMESTTQAqifRLLARLnQLQGTSILLISHDLESI 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-202 |
6.41e-06 |
|
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: 46.21 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRvvvHGCDTQADR-------SQLAKHVGLMFQNPDDQIIFPTVAEELAFSLTA 114
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEildefrgSELQNYFTKLLEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 115 R-GE--TRQAARQQAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDL---LSQARLAAQL 188
Cdd:cd03236 106 KvGEllKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIREL 185
|
170
....*....|....
gi 2539771384 189 EDSGHQILVSTHLL 202
Cdd:cd03236 186 AEDDNYVLVVEHDL 199
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-243 |
6.59e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMrIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMFQNpddqiifptvaeelaFS 111
Cdd:PRK10522 344 LTIKRGEL-LFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYRKLFSAVFTD---------------FH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 LTAR---GETRQAARQQAREFLARRG----LEAWAGRAVS-ELSQGQRQQVCLLALQISEPATLLLDEPFASLDllSQAR 183
Cdd:PRK10522 408 LFDQllgPEGKPANPALVEKWLERLKmahkLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQD--PHFR 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539771384 184 ------LAAQLEDSGHQILVSTHLLEHVYGFERVLWLEQGrvradgpgrEICEAYAEDvRERAAAE 243
Cdd:PRK10522 486 refyqvLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG---------QLSELTGEE-RDAASRD 541
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-205 |
7.19e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 46 GDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQNPDDQiifpTVAEELAF--SLTARGETRQAAR 123
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEM----TVFENLKFwsEIYNSAETLYAAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 124 QQAReflarrgLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASL-----DLLSQarLAAQLEDSGHQILVS 198
Cdd:PRK13541 109 HYFK-------LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLskenrDLLNN--LIVMKANSGGIVLLS 179
|
....*..
gi 2539771384 199 THLLEHV 205
Cdd:PRK13541 180 SHLESSI 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-247 |
7.29e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.55 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 23 VRG--SRTVFEGLTLDLQEMRI----GLVGdngAGKSSLFRLISGLDQPKQGRVVVHG--CDTQADRSQLAKHVGLMfqn 94
Cdd:COG1129 259 VEGlsVGGVVRDVSFSVRAGEIlgiaGLVG---AGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYV--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDD---QIIFP--TVAEELAFSLTARGET-----RQAARQQAREFLAR-----RGLEAwagrAVSELSQGQRQQVCL--- 156
Cdd:COG1129 333 PEDrkgEGLVLdlSIRENITLASLDRLSRgglldRRRERALAEEYIKRlriktPSPEQ----PVGNLSGGNQQKVVLakw 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 157 LAlqiSEPATLLLDEPFASLDLLSQA---RLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEay 232
Cdd:COG1129 409 LA---TDPKVLILDEPTRGIDVGAKAeiyRLIRELAAEGKAVIVISSELPELLGLsDRILVMREGRIVGELDREEATE-- 483
|
250
....*....|....*
gi 2539771384 233 aEDVRERAAAERGRH 247
Cdd:COG1129 484 -EAIMAAATGGAAAA 497
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
144-200 |
1.66e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 1.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539771384 144 SELSQGQRQQVCLLALQIS---EPATLLLDEPFASLDLLSQARLA---AQLEDSGHQILVSTH 200
Cdd:pfam13304 235 FELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLellKELSRNGAQLILTTH 297
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-217 |
1.86e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. 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: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.85 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVvvhgcdtqadrsqlaKHVGLMFQNPDDQIIFP-TVAEELAFSLTaRGETRQ 120
Cdd:cd03291 66 LAITGSTGSGKTSLLMLILGELEPSEGKI---------------KHSGRISFSSQFSWIMPgTIKENIIFGVS-YDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 121 AARQQAREFlaRRGLEAWA-------GRAVSELSQGQRQQVClLALQISEPATL-LLDEPFASLDLLSQARL----AAQL 188
Cdd:cd03291 130 KSVVKACQL--EEDITKFPekdntvlGEGGITLSGGQRARIS-LARAVYKDADLyLLDSPFGYLDVFTEKEIfescVCKL 206
|
170 180
....*....|....*....|....*....
gi 2539771384 189 EDSGHQILVsTHLLEHVYGFERVLWLEQG 217
Cdd:cd03291 207 MANKTRILV-TSKMEHLKKADKILILHEG 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
44-205 |
2.04e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.24 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISGLDQPKQGRV-----VVHGCDTQADRSQLAKHVGLMFQNPddQIIFPTVAEELAFSLTARGET 118
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKP--WLLNATVEENITFGSPFNKQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 119 RQAARQ----QAREFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDL-----LSQARLAAQLE 189
Cdd:cd03290 110 YKAVTDacslQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQ 189
|
170
....*....|....*.
gi 2539771384 190 DSGHQILVSTHLLEHV 205
Cdd:cd03290 190 DDKRTLVLVTHKLQYL 205
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-223 |
2.25e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.20 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 14 SIRLDAV--TLVRGSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQLAKHVG 89
Cdd:PRK11160 338 SLTLNNVsfTYPDQPQPVLKGLSLQIKAgEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 90 LMFQNPDdqiIFP-TVAEELAFSL-TARGETRQAARQQAR-EFLA--RRGLEAWAGRAVSELSQGQRQQVCLLALQISEP 164
Cdd:PRK11160 418 VVSQRVH---LFSaTLRDNLLLAApNASDEALIEVLQQVGlEKLLedDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539771384 165 ATLLLDEPFASLDLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVRADG 223
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
42-230 |
2.74e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHG--CDTQADRS--QLAKHVGLMFQNP-----DDQIIFPTVAEELAFSL 112
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKlqALRRDIQFIFQDPyasldPRQTVGDSIMEPLRVHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 113 TARGEtrqAARQQAREFLARRGLE---AWagRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLE 189
Cdd:PRK10261 433 LLPGK---AAAARVAWLLERVGLLpehAW--RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2539771384 190 DSGHQILVSTHLLEHVYGF-----ERVLWLEQGRVRADGPGREICE 230
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVverisHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
42-219 |
3.54e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQ---------ADRSQLAK-HVGLMFQNPddqiifptvAEELAFS 111
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseAERRRLLRtEWGFVHQHP---------RDGLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 112 LTAR---GETRQAA--------RQQAREFLARrgLEAWAGR---AVSELSQGQRQQvcllaLQI-----SEPATLLLDEP 172
Cdd:PRK11701 106 VSAGgniGERLMAVgarhygdiRATAGDWLER--VEIDAARiddLPTTFSGGMQQR-----LQIarnlvTHPRLVFMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 173 FASLDLLSQARLAAQL----EDSGHQILVSTH------LLEHvygfeRVLWLEQGRV 219
Cdd:PRK11701 179 TGGLDVSVQARLLDLLrglvRELGLAVVIVTHdlavarLLAH-----RLLVMKQGRV 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-177 |
3.93e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 7 SETVSSHSIRLDAVTLV-RGSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQA-DRSQ 83
Cdd:PRK10790 333 DRPLQSGRIDIDNVSFAyRDDNLVLQNINLSVPSRGfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 84 LAKHVGLMFQNPddqiifPTVAEELAFSLTARGETRQAARQQAREF-----LARR---GLEAWAGRAVSELSQGQRQQVC 155
Cdd:PRK10790 413 LRQGVAMVQQDP------VVLADTFLANVTLGRDISEEQVWQALETvqlaeLARSlpdGLYTPLGEQGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 2539771384 156 LLALQISEPATLLLDEPFASLD 177
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
42-238 |
6.49e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVvvhgcDTQADRSQLAKHVGLmfqnpDDQIifpTVAEELAFSLTARGETRQA 121
Cdd:PRK13545 53 VGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGL-----NGQL---TGIENIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 ARQQAREFLARRGLEAWAGRAVSELSQGQRQQvclLALQIS---EPATLLLDEPFASLDLLSQARLAAQL---EDSGHQI 195
Cdd:PRK13545 120 IKEIIPEIIEFADIGKFIYQPVKTYSSGMKSR---LGFAISvhiNPDILVIDEALSVGDQTFTKKCLDKMnefKEQGKTI 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2539771384 196 LVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREICEAYAEDVRE 238
Cdd:PRK13545 197 FFISHSLSQVKSFcTKALWLHYGQVKEYGDIKEVVDHYDEFLKK 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
42-231 |
6.88e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGL-DQPkqGRVVV-----HGCDTQA----DRSQL-AKHVGLMFQNPDDQIiFP--TVAEEL 108
Cdd:PRK11022 36 VGIVGESGSGKSVSSLAIMGLiDYP--GRVMAeklefNGQDLQRisekERRNLvGAEVAMIFQDPMTSL-NPcyTVGFQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 109 AFSL-TARGETRQAARQQAREFLARRGLEAWAGRA---VSELSQGQRQQVcLLALQIS-EPATLLLDEPFASLDLLSQAR 183
Cdd:PRK11022 113 MEAIkVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRV-MIAMAIAcRPKLLIADEPTTALDVTIQAQ 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 184 -----LAAQLEDSGHQILVsTHLLEHVY-GFERVLWLEQGRVRADGPGREICEA 231
Cdd:PRK11022 192 iiellLELQQKENMALVLI-THDLALVAeAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
142-247 |
1.08e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 142 AVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA---RLAAQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQG 217
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQQGVAIIVISSELPEVLGLsDRVLVMHEG 481
|
90 100 110
....*....|....*....|....*....|
gi 2539771384 218 RVRADGPGREICEayaEDVREraAAERGRH 247
Cdd:PRK13549 482 KLKGDLINHNLTQ---EQVME--AALRSEH 506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
111-222 |
1.36e-04 |
|
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: 42.50 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 111 SLTARGETRQAARQQA-REFLARRGLEAWA-GRAVSELSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQA---RLA 185
Cdd:TIGR02633 367 SFCFKMRIDAAAELQIiGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYeiyKLI 446
|
90 100 110
....*....|....*....|....*....|....*...
gi 2539771384 186 AQLEDSGHQILVSTHLLEHVYGF-ERVLWLEQGRVRAD 222
Cdd:TIGR02633 447 NQLAQEGVAIIVVSSELAEVLGLsDRVLVIGEGKLKGD 484
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-177 |
1.54e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 41 RIGLVGDNGAGKSSLFRLISG-------------------LDQ--PK--QGRV---VVHGCDTQADR----SQLAKHVGl 90
Cdd:PRK11147 31 RVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarLQQdpPRnvEGTVydfVAEGIEEQAEYlkryHDISHLVE- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 91 mfQNPDDQIIfptvaEELAfSLTARGETRQAARQQAR--EFLARRGLEAWAgrAVSELSQGQRQQVCLLALQISEPATLL 168
Cdd:PRK11147 110 --TDPSEKNL-----NELA-KLQEQLDHHNLWQLENRinEVLAQLGLDPDA--ALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 2539771384 169 LDEPFASLD 177
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
15-219 |
1.93e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.40 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCD-TQADRSQLAKHVGLMF 92
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIvTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 qnPDDQIIFP--TVAEELAFSltargeTRQAARQQAREFLAR------RGLEAWAGRAvSELSQGQRQQVCLLALQISEP 164
Cdd:PRK11614 86 --PEGRRVFSrmTVEENLAMG------GFFAERDQFQERIKWvyelfpRLHERRIQRA-GTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 165 ATLLLDEP---FASLDLLSQARLAAQLEDSGHQI-LVSTHLLEHVYGFERVLWLEQGRV 219
Cdd:PRK11614 157 RLLLLDEPslgLAPIIIQQIFDTIEQLREQGMTIfLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
146-220 |
2.27e-04 |
|
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: 41.38 E-value: 2.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 146 LSQGQRQQVCLLALQISEPATLLLDEPFASLDLLSQARLAAQLED--SGHQILVSTHLLEHVYGFERVLWLEQGRVR 220
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
42-231 |
2.39e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKS----SLFRLI--SG--------LDQPKQGRVVVHGCDTQAD-RSQLAKHVGLMFQNPDDQI--IFPtV 104
Cdd:PRK10261 45 LAIVGESGSGKSvtalALMRLLeqAGglvqcdkmLLRRRSRQVIELSEQSAAQmRHVRGADMAMIFQEPMTSLnpVFT-V 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 105 AEELAFSLTA-RGETRQAARQQAREFLARRGL---EAWAGRAVSELSQGQRQQVcLLALQIS-EPATLLLDEPFASLDLL 179
Cdd:PRK10261 124 GEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRV-MIAMALScRPAVLIADEPTTALDVT 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2539771384 180 SQARLAAQLEDSGHQILVSTHLLEHVYGF-----ERVLWLEQGRVRADGPGREICEA 231
Cdd:PRK10261 203 IQAQILQLIKVLQKEMSMGVIFITHDMGVvaeiaDRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-205 |
2.49e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMRI-GLVGDNGAGKSSLFRLISGldQPK----QGRVVVHG---CDTQAD-RSQLAkhVGLMFQNP 95
Cdd:CHL00131 18 NENEILKGLNLSINKGEIhAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGesiLDLEPEeRAHLG--IFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 96 ddqIIFPTVAEE--LAFSLTARGETRQAARQQAREF-------LARRGLEA-WAGRAVSE-LSQGQRQQVCLLALQISEP 164
Cdd:CHL00131 94 ---IEIPGVSNAdfLRLAYNSKRKFQGLPELDPLEFleiinekLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2539771384 165 ATLLLDEPFASLD---LLSQARLAAQLEDSGHQILVSTH---LLEHV 205
Cdd:CHL00131 171 ELAILDETDSGLDidaLKIIAEGINKLMTSENSIILITHyqrLLDYI 217
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
144-215 |
3.50e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539771384 144 SELSQGQRQQVCLLA--LQISEPATLLLDEPFASLDLLSQARLAAQLEDSG--HQILVSTH---LLEHVyGFERVLWLE 215
Cdd:COG4637 257 RELSDGTLRFLALLAalLSPRPPPLLCIEEPENGLHPDLLPALAELLREASerTQVIVTTHspaLLDAL-EPEEVLVLE 334
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-228 |
5.24e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.48 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 25 GSRTVFEGLTLDLQEMR-IGLVGDNGAGKSSLFRLISGLDQPK---------QGRVVVHGCDTQADRSQlAKHVGLMFQN 94
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGEtLGIVGESGSGKSQTAFALMGLLAANgriggsatfNGREILNLPEKELNKLR-AEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 95 PDDQI-IFPTVAEELAFSLTA-RGETRQAARQQAREFL-------ARRGLEAWAgravSELSQGQRQQVCLLALQISEPA 165
Cdd:PRK09473 106 PMTSLnPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLdavkmpeARKRMKMYP----HEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539771384 166 TLLLDEPFASLDLLSQARLAAQLEDSGHQ----ILVSTHLLEHVYGF-ERVLWLEQGRVRADGPGREI 228
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREfntaIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
42-218 |
9.71e-04 |
|
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: 38.99 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGcdtqadrsqlakHVGLMFQNPddQIIFPTVAEELAFsltarGETRQA 121
Cdd:cd03250 34 VAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEP--WIQNGTIRENILF-----GKPFDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 122 AR-QQAREFLA-RRGLEAWAG--------RAVSeLSQGQRQQVCLlALQI-SEPATLLLDEPFASLDllsqARLAAQLED 190
Cdd:cd03250 95 ERyEKVIKACAlEPDLEILPDgdlteigeKGIN-LSGGQKQRISL-ARAVySDADIYLLDDPLSAVD----AHVGRHIFE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2539771384 191 S---GH------QILVsTHLLEHVYGFERVLWLEQGR 218
Cdd:cd03250 169 NcilGLllnnktRILV-THQLQLLPHADQIVVLDNGR 204
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-203 |
1.10e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 33 LTLDLQEMRiGLVGDNGAGKSSLFRLISGLDQPK----QGRVVVHGCD----TQADRSQLAKH-VGLMFQNPDdQIIFPT 103
Cdd:PRK15093 28 MTLTEGEIR-GLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDllrlSPRERRKLVGHnVSMIFQEPQ-SCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 104 --VAEELAFSL---TARGETRQAARQQAR---EFLARRGLEAWAGRAVS---ELSQGQRQQVCLLALQISEPATLLLDEP 172
Cdd:PRK15093 106 erVGRQLMQNIpgwTYKGRWWQRFGWRKRraiELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEP 185
|
170 180 190
....*....|....*....|....*....|....*
gi 2539771384 173 FASLDLLSQA---RLAAQL-EDSGHQILVSTHLLE 203
Cdd:PRK15093 186 TNAMEPTTQAqifRLLTRLnQNNNTTILLISHDLQ 220
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
43-203 |
1.45e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISgldqpkqgrVVVHGcDTQADRSQLAKHvglMFQNPDDQIIfptvaeELAFSLTARGETRQAA 122
Cdd:cd03279 32 LICGPTGAGKSTILDAIT---------YALYG-KTPRYGRQENLR---SVFAPGEDTA------EVSFTFQLGGKKYRVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 123 RQ-----------------QAREFLArrgleawagRAVSELSQGQRQQVCL-LALQISEPA---------TLLLDEPFAS 175
Cdd:cd03279 93 RSrgldydqftrivllpqgEFDRFLA---------RPVSTLSGGETFLASLsLALALSEVLqnrggarleALFIDEGFGT 163
|
170 180 190
....*....|....*....|....*....|.
gi 2539771384 176 LDLLSQARLAAQLE---DSGHQILVSTHLLE 203
Cdd:cd03279 164 LDPEALEAVATALElirTENRMVGVISHVEE 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-109 |
2.27e-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: 37.35 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 42 IGLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDT--QADRSQLAKHVGLMFQNPDDQIIFPTVAEELA 109
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDilEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
44-217 |
2.38e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 44 LVGDNGAGKSSLFRLISgldqpkqGRVVVhGCDTQADR--------SQLAKHVGLMFQNpDDQIIFPTVAEELAFSLTAR 115
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLA-------ERVTT-GVITGGDRlvngrpldSSFQRSIGYVQQQ-DLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 116 gETRQAARQQAREFLAR----RGLEAWA----GRAVSELSQGQRQQVCLLALQISEPATLL-LDEPFASLDllSQA---- 182
Cdd:TIGR00956 865 -QPKSVSKSEKMEYVEEviklLEMESYAdavvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD--SQTawsi 941
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2539771384 183 -RLAAQLEDSGHQILVSTH-----LLEHvygFERVLWLEQG 217
Cdd:TIGR00956 942 cKLMRKLADHGQAILCTIHqpsaiLFEE---FDRLLLLQKG 979
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-171 |
2.82e-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: 38.58 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 15 IRLDAVTLVRGSRTVF-EGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRvvvhgcdtqadRSQLAKhvGLMF 92
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLiESLSFEVPSgNNLLICGPNGCGKSSLFRILGELWPVYGGR-----------LTKPAK--GKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 93 ---QNP-------DDQIIFPTVAEElafsLTARGETRQAARQ-----QAREFLARR-GLEA---WAgravSELSQGQRQQ 153
Cdd:TIGR00954 519 yvpQRPymtlgtlRDQIIYPDSSED----MKRRGLSDKDLEQildnvQLTHILEREgGWSAvqdWM----DVLSGGEKQR 590
|
170
....*....|....*...
gi 2539771384 154 VCLLALQISEPATLLLDE 171
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDE 608
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
43-172 |
3.34e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.57 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539771384 43 GLVGDNGAGKSSLFRLISGLDQPKQGRVVVHGCDTQADRSQLAKHVGLMFQnpddqiifptvaeelAFSLTARGETRQ-- 120
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQ---------------AFSLYGELTVRQnl 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539771384 121 ----------AARQQAR--EFLARRGLEAWAGRAVSELSQGQRQQVCLLALQISEPATLLLDEP 172
Cdd:NF033858 361 elharlfhlpAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-70 |
4.18e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 4.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2539771384 25 GSRTVFEGLTLDLQE-MRIGLVGDNGAGKSSLFRLISGLDQPKQGRV 70
Cdd:PRK15064 330 DNGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| |
