|
Name |
Accession |
Description |
Interval |
E-value |
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
49-406 |
6.13e-69 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 223.32 E-value: 6.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 49 RRLSLREIADSIGVSHSTVNRVAANMMGPDAAggtespksTGRTGYR-YSLAEAVALRKAIAELPeiRKKAKLDRRRGAG 127
Cdd:TIGR03453 32 RKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPE--------TLSNGRRsYTLEQINELRRHLAQRG--REARRYLPHRRGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 128 EPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVEDTL---LPYFEgSETSLDY 204
Cdd:TIGR03453 102 EHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDVGENETLygaIRYDD-ERRPISE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 205 CIRKTEIPTLDVIPSNVGLASADLVLPsrQRDMRQAGDLSWFYMKVlAEGIATIEKDYDVILIDCPPSMSYLTTVATQAC 284
Cdd:TIGR03453 181 IIRKTYFPGLDLVPGNLELMEFEHETP--RALSRGQGGDTIFFARV-GEALAEVEDDYDVVVIDCPPQLGFLTLSALCAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 285 DALLVPMRPSMPDFASSAQFIRMFGGFQREVDEVVGNAKeFDWIQVLITLGENNNAS-AEMEAIIRKAYGDLVMGEKFPY 363
Cdd:TIGR03453 258 TGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLS-YDFMRYLVTRYEPNDGPqAQMVAFLRSLFGDHVLTNPMLK 336
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499664877 364 LTAVARAAKAMRTIYDVARADTDTRQLSKAMNIVNQLCQSIEA 406
Cdd:TIGR03453 337 STAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEG 379
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
135-408 |
4.86e-62 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 201.24 E-value: 4.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 135 IMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHP-DIELSVEDTLLpyfegSETSLDYCIRKTEIPT 213
Cdd:COG1192 6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPdDLDPTLYDLLL-----DDAPLEDAIVPTEIPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 214 LDVIPSNVGLASADLVLPSRQRDMRqagdlswfymkVLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMRP 293
Cdd:COG1192 81 LDLIPANIDLAGAEIELVSRPGREL-----------RLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 294 SMPDFASSAQFIRMFGGFQREVDevvgnaKEFDWIQVLIT-LGENNNASAEMEAIIRKAYGDLVMGEKFPYLTAVARAAK 372
Cdd:COG1192 150 EYLSLEGLAQLLETIEEVREDLN------PKLEILGILLTmVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPS 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 499664877 373 AMRTIYDVARAdtdtrqlSKAMNIVNQLCQSIEARL 408
Cdd:COG1192 224 AGKPVFEYDPK-------SKGAKAYRALAEELLERL 252
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
49-406 |
5.35e-51 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 177.17 E-value: 5.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 49 RRLSLREIADSIGVSHSTVNRVAANMMGPdaaggteSPKSTGRTGYRYSLAEAVALRKAIAELPEIRKKAKLDRRRGAGE 128
Cdd:PRK13869 47 RKFTSGEAARLMKISDSTLRKMTLAGEGP-------QPELASNGRRFYTLGQINEIRQMLAGSTRGRESIDFVPHRRGSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 129 PCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVEDTLLPYFEGSET--SLDYCI 206
Cdd:PRK13869 120 HLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTrrPLRDVI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 207 RKTEIPTLDVIPSNVGLASADLVLPSRQRDmRQAGDlSWFYMKVlAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDA 286
Cdd:PRK13869 200 RPTYFDGLHLVPGNLELMEFEHTTPKALSD-KGTRD-GLFFTRV-AQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 287 LLVPMRPSMPDFASSAQFIRMFGGFQREVDEVVGNAKeFDWIQVLITLGENNNA-SAEMEAIIRKAYGDLVMGEKFPYLT 365
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQ-YDFIRYLLTRYEPQDApQTKVAALLRNMFEDHVLTNPMVKSA 355
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499664877 366 AVARAAKAMRTIYDVARADTDTRQLSKAMNIVNQLCQSIEA 406
Cdd:PRK13869 356 AVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEA 396
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
135-377 |
2.33e-38 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 138.25 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 135 IMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVED--TLLPyfegSETSLDYCIRKTEIP 212
Cdd:pfam01656 3 IAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQAlaEGLK----GRVNLDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 213 T--LDVIPSNVGLASADLVLPSRQRDMRqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVP 290
Cdd:pfam01656 79 EggLDLIPGNIDLEKFEKELLGPRKEER------------LREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 291 MRPSMPDFASSAQFIRMFGGFQREVdevvgNAKEFDWIQVLITL-GENNNASAEMEAIIRKAYGDLVMGEkFPYLTAVAR 369
Cdd:pfam01656 147 LEPEVILVEDAKRLGGVIAALVGGY-----ALLGLKIIGVVLNKvDGDNHGKLLKEALEELLRGLPVLGV-IPRDEAVAE 220
|
....*...
gi 499664877 370 AAKAMRTI 377
Cdd:pfam01656 221 APARGLPV 228
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
132-349 |
3.95e-27 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 104.93 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFgihpdielsvedtllpyfegsetsldycirktei 211
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 ptldvipsnvglasadlvlpsrqrdmrqagdlswfymkvlaegiatiekdYDVILIDCPPSMSYLTTVATQACDALLVPM 291
Cdd:cd02042 48 --------------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPV 77
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499664877 292 RPSMPDFASSAQFIRMFGGFQREvdevvgNAKEFDWIQVLIT-LGENNNASAEMEAIIR 349
Cdd:cd02042 78 QPSPFDLDGLAKLLDTLEELKKQ------LNPPLLILGILLTrVDPRTKLAREVLEELK 130
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
132-307 |
1.13e-17 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 81.06 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFgihpdiELSVEDTLLPYfegsetsldycirktei 211
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWA------AAREDERPFPV----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 ptldvipsnVGLASADLvlpsrQRDmrqagdlswfymkvlaegIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPM 291
Cdd:NF041546 58 ---------VGLARPTL-----HRE------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105
|
170
....*....|....*.
gi 499664877 292 RPSMPDFASSAQFIRM 307
Cdd:NF041546 106 QPSPYDLWASADTVDL 121
|
|
| ArsA_halo |
NF041417 |
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
139-178 |
8.26e-06 |
|
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.
Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 47.95 E-value: 8.26e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFG 178
Cdd:NF041417 341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFG 380
|
|
| ArsA_halo |
NF041417 |
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
139-178 |
6.90e-05 |
|
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.
Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 45.26 E-value: 6.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFG 178
Cdd:NF041417 20 KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
49-406 |
6.13e-69 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 223.32 E-value: 6.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 49 RRLSLREIADSIGVSHSTVNRVAANMMGPDAAggtespksTGRTGYR-YSLAEAVALRKAIAELPeiRKKAKLDRRRGAG 127
Cdd:TIGR03453 32 RKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPE--------TLSNGRRsYTLEQINELRRHLAQRG--REARRYLPHRRGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 128 EPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVEDTL---LPYFEgSETSLDY 204
Cdd:TIGR03453 102 EHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDVGENETLygaIRYDD-ERRPISE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 205 CIRKTEIPTLDVIPSNVGLASADLVLPsrQRDMRQAGDLSWFYMKVlAEGIATIEKDYDVILIDCPPSMSYLTTVATQAC 284
Cdd:TIGR03453 181 IIRKTYFPGLDLVPGNLELMEFEHETP--RALSRGQGGDTIFFARV-GEALAEVEDDYDVVVIDCPPQLGFLTLSALCAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 285 DALLVPMRPSMPDFASSAQFIRMFGGFQREVDEVVGNAKeFDWIQVLITLGENNNAS-AEMEAIIRKAYGDLVMGEKFPY 363
Cdd:TIGR03453 258 TGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLS-YDFMRYLVTRYEPNDGPqAQMVAFLRSLFGDHVLTNPMLK 336
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499664877 364 LTAVARAAKAMRTIYDVARADTDTRQLSKAMNIVNQLCQSIEA 406
Cdd:TIGR03453 337 STAISDAGLTKQTLYEVERSQFTRSTYDRAMESLDAVNAEIEG 379
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
135-408 |
4.86e-62 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 201.24 E-value: 4.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 135 IMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHP-DIELSVEDTLLpyfegSETSLDYCIRKTEIPT 213
Cdd:COG1192 6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPdDLDPTLYDLLL-----DDAPLEDAIVPTEIPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 214 LDVIPSNVGLASADLVLPSRQRDMRqagdlswfymkVLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMRP 293
Cdd:COG1192 81 LDLIPANIDLAGAEIELVSRPGREL-----------RLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 294 SMPDFASSAQFIRMFGGFQREVDevvgnaKEFDWIQVLIT-LGENNNASAEMEAIIRKAYGDLVMGEKFPYLTAVARAAK 372
Cdd:COG1192 150 EYLSLEGLAQLLETIEEVREDLN------PKLEILGILLTmVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPS 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 499664877 373 AMRTIYDVARAdtdtrqlSKAMNIVNQLCQSIEARL 408
Cdd:COG1192 224 AGKPVFEYDPK-------SKGAKAYRALAEELLERL 252
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
49-406 |
5.35e-51 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 177.17 E-value: 5.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 49 RRLSLREIADSIGVSHSTVNRVAANMMGPdaaggteSPKSTGRTGYRYSLAEAVALRKAIAELPEIRKKAKLDRRRGAGE 128
Cdd:PRK13869 47 RKFTSGEAARLMKISDSTLRKMTLAGEGP-------QPELASNGRRFYTLGQINEIRQMLAGSTRGRESIDFVPHRRGSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 129 PCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVEDTLLPYFEGSET--SLDYCI 206
Cdd:PRK13869 120 HLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTrrPLRDVI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 207 RKTEIPTLDVIPSNVGLASADLVLPSRQRDmRQAGDlSWFYMKVlAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDA 286
Cdd:PRK13869 200 RPTYFDGLHLVPGNLELMEFEHTTPKALSD-KGTRD-GLFFTRV-AQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 287 LLVPMRPSMPDFASSAQFIRMFGGFQREVDEVVGNAKeFDWIQVLITLGENNNA-SAEMEAIIRKAYGDLVMGEKFPYLT 365
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQ-YDFIRYLLTRYEPQDApQTKVAALLRNMFEDHVLTNPMVKSA 355
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499664877 366 AVARAAKAMRTIYDVARADTDTRQLSKAMNIVNQLCQSIEA 406
Cdd:PRK13869 356 AVSDAGLTKQTLYEIGRENLTRSTYDRAMESLDAVNSEIEA 396
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
26-412 |
2.07e-46 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 164.38 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 26 GQMVMRAKDFSHPSKLSPEQGE-SRRLSLREIADSIGVSHSTVNRV--AANMMGPDAA--GGTESpkstgRTGYryslae 100
Cdd:PRK13705 14 GHEMTKAIAIAQFNDDSPEARKiTRRWRIGEAADLVGVSSQAIRDAekAGRLPHPDMEmrGRVEQ-----RVGY------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 101 avalrkAIAELPEIRKKAKLDRRRGAGEPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVID-TDPQATLSTLFGI 179
Cdd:PRK13705 83 ------TIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 180 HPDIELSVEDTLLPYFEGSETSLDYCIRKTEIPTLDVIPSNVGLASADLVLPSRQrdmrQAGDLSWFYMKVLAEGIATIE 259
Cdd:PRK13705 157 VPDLHIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKF----DEGKLPTDPHLMLRLAIETVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 260 KDYDVILIDCPPSMSYLTTVATQACDALLVPMRPSMPDFASSAQFIRMFGGFQREVDEvvgNAKEFDwIQVLITLGENNN 339
Cdd:PRK13705 233 HDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDL---KGFEPD-VRILLTKYSNSN 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664877 340 ASAE--MEAIIRKAYGDLVMGEKFPYLTAVARAAKAMRTIYD-VARADTDTRQLSKAMNIVNQLCQSIEARLLLTR 412
Cdd:PRK13705 309 GSQSpwMEEQIRDAWGSMVLKNVVRETDEVGKGQIRMRTVFEqAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPR 384
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
26-412 |
1.70e-40 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 148.62 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 26 GQMVMRAKDFSHPSKLSPEQGE-SRRLSLREIADSIGVSHSTVNRV--AANMMGPDAAGGTESPKstgRTGYryslaeav 102
Cdd:PHA02519 14 GQEMTQAIAIAQFGDDSPEARAiTRRWGITEVADLIGVTPQAIRDAekSGRLPPPDFETRGRVER---RAGY-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 103 alrkAIAELPEIRKKAKLDRRRGAGEPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVID-TDPQATLSTLFGIHP 181
Cdd:PHA02519 83 ----TIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 182 DIELSVEDTLLPYFEGSETSLDYCIRKTEIPTLDVIPSNVGLASadlvLPSRQRDMRQAGDLSWFYMKVLAEGIATIEKD 261
Cdd:PHA02519 159 DLHIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHR----IETDLMQYHDAGKLPHPPHLMLRAAIESVWDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 262 YDVILIDCPPSMSYLTTVATQACDALLVPMRPSMPDFASSAQFIRMFGGFQREVDevVGNAKEFdwIQVLITLGENNNAS 341
Cdd:PHA02519 235 YDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVD--LGGFEPV--VRLLLTKYSLTVGN 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664877 342 AE--MEAIIRKAYGDLVMGEKFPYLTAVARAAKAMRTIYDVARADTDT-RQLSKAMNIVNQLCQSIEARLLLTR 412
Cdd:PHA02519 311 QSrwMEEQIRNTWGSMVLRQVVRVTDEVGKGQIKMRTVFEQAANQRSTlNAWRNAVAIWEPVCAEIFNDLIKPR 384
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
135-377 |
2.33e-38 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 138.25 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 135 IMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIELSVED--TLLPyfegSETSLDYCIRKTEIP 212
Cdd:pfam01656 3 IAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQAlaEGLK----GRVNLDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 213 T--LDVIPSNVGLASADLVLPSRQRDMRqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVP 290
Cdd:pfam01656 79 EggLDLIPGNIDLEKFEKELLGPRKEER------------LREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 291 MRPSMPDFASSAQFIRMFGGFQREVdevvgNAKEFDWIQVLITL-GENNNASAEMEAIIRKAYGDLVMGEkFPYLTAVAR 369
Cdd:pfam01656 147 LEPEVILVEDAKRLGGVIAALVGGY-----ALLGLKIIGVVLNKvDGDNHGKLLKEALEELLRGLPVLGV-IPRDEAVAE 220
|
....*...
gi 499664877 370 AAKAMRTI 377
Cdd:pfam01656 221 APARGLPV 228
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
135-294 |
5.99e-34 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 125.00 E-value: 5.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 135 IMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPD-IELSVEDTLLpyfegSETSLDYCIRKTEIPT 213
Cdd:pfam13614 6 IANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNnVEKTIYELLI-----GECNIEEAIIKTVIEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 214 LDVIPSNVGLASADLVLpsRQRDMRQagdlswfymKVLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMRP 293
Cdd:pfam13614 81 LDLIPSNIDLAGAEIEL--IGIENRE---------NILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQC 149
|
.
gi 499664877 294 S 294
Cdd:pfam13614 150 E 150
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
132-349 |
3.95e-27 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 104.93 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFgihpdielsvedtllpyfegsetsldycirktei 211
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 ptldvipsnvglasadlvlpsrqrdmrqagdlswfymkvlaegiatiekdYDVILIDCPPSMSYLTTVATQACDALLVPM 291
Cdd:cd02042 48 --------------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPV 77
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499664877 292 RPSMPDFASSAQFIRMFGGFQREvdevvgNAKEFDWIQVLIT-LGENNNASAEMEAIIR 349
Cdd:cd02042 78 QPSPFDLDGLAKLLDTLEELKKQ------LNPPLLILGILLTrVDPRTKLAREVLEELK 130
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
132-307 |
1.13e-17 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 81.06 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFgihpdiELSVEDTLLPYfegsetsldycirktei 211
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWA------AAREDERPFPV----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 ptldvipsnVGLASADLvlpsrQRDmrqagdlswfymkvlaegIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPM 291
Cdd:NF041546 58 ---------VGLARPTL-----HRE------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105
|
170
....*....|....*.
gi 499664877 292 RPSMPDFASSAQFIRM 307
Cdd:NF041546 106 QPSPYDLWASADTVDL 121
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
146-307 |
4.99e-17 |
|
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440223 [Multi-domain] Cd Length: 230 Bit Score: 79.93 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 146 TTTAHAGAYLSLHGYRTLVIDTDPQ-ATLSTLFGIHPDIelsvedTLLPYFEGsETSLDYCIRKTEiPTLDVIPSNVGLA 224
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPKA------TLADVLAG-EADLEDAIVQGP-GGLDVLPGGSGPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 225 SADLVLPSRQrdmrqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMRPSMPDFASSAQF 304
Cdd:COG0455 73 ELAELDPEER----------------LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYAL 136
|
...
gi 499664877 305 IRM 307
Cdd:COG0455 137 LKL 139
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
97-321 |
3.68e-16 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 78.30 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 97 SLAEAVALRKAIAELPEIRKKAKLDRRRGAGEPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDP-QATLST 175
Cdd:COG0489 59 LLLLLLLLLGLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 176 LFGIHPDIELSveDTLLpyfegSETSLDYCIRKTEIPTLDVIPSNVGLASADLVLPSRQrdMRQAgdlswfymkvlaegI 255
Cdd:COG0489 139 MLGLENRPGLS--DVLA-----GEASLEDVIQPTEVEGLDVLPAGPLPPNPSELLASKR--LKQL--------------L 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664877 256 ATIEKDYDVILIDCPPSMSYL-TTVATQACDALLVPMRPSMPDFASSAQFIRMFGGFQREVDEVVGN 321
Cdd:COG0489 196 EELRGRYDYVIIDTPPGLGVAdATLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLN 262
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
124-289 |
4.53e-14 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 70.29 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 124 RGAGEPCVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDP-QATLSTLFGIHPdiELSVEDTLLpyfegSETSL 202
Cdd:cd05387 13 AGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPN--EPGLSEVLS-----GQASL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 203 DYCIRKTEIPTLDVIPSNVGLASADLVLPSRQrdmrqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYL-TTVAT 281
Cdd:cd05387 86 EDVIQSTNIPNLDVLPAGTVPPNPSELLSSPR----------------FAELLEELKEQYDYVIIDTPPVLAVAdALILA 149
|
....*...
gi 499664877 282 QACDALLV 289
Cdd:cd05387 150 PLVDGVLL 157
|
|
| cellulose_yhjQ |
TIGR03371 |
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ... |
132-293 |
5.07e-10 |
|
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274549 [Multi-domain] Cd Length: 246 Bit Score: 59.67 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGihpdIELSVEDTLLPYFEGSETSLDYCIRktei 211
Cdd:TIGR03371 3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFG----MDWSVRDGWARALLNGADWAAAAYR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 ptldvipsnvGLASADLV----LPSRQRDMRQAGDLSWfymkvLAEGIATIEKD-YDVILIDCPPSMSYLTTVATQACDA 286
Cdd:TIGR03371 75 ----------SPDGVLFLpygdLSADEREAYQAHDAGW-----LARLLQQLDLAaRDWVLIDLPRGPSPITRQALAAADL 139
|
....*..
gi 499664877 287 LLVPMRP 293
Cdd:TIGR03371 140 VLVVVNA 146
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
139-289 |
2.87e-09 |
|
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.
Pssm-ID: 349758 [Multi-domain] Cd Length: 230 Bit Score: 57.19 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTD-PQATLSTLFGIHPdielsvEDTLLPYFEGSETSLDYCIRKTEipTLDVI 217
Cdd:cd02038 9 KGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAP------KKTLGDVLKGRVSLEDIIVEGPE--GLDII 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664877 218 PSNVGLAS-ADlvLPSRQRDMrqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALLV 289
Cdd:cd02038 81 PGGSGMEElAN--LDPEQKAK-------------LIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
139-271 |
1.77e-07 |
|
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.
Pssm-ID: 349755 [Multi-domain] Cd Length: 250 Bit Score: 52.12 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFG--IHPD-----------IELSVEDTLLPYFEGsetsldyc 205
Cdd:cd02035 8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGqkLGGEtpvkgapnlwaMEIDPEEALEEYWEE-------- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664877 206 IRKTEIPTLDVIPSNVGLASADLVLPSrqrdMRQAGDLSWFyMKVLAEGiatiekDYDVILIDCPP 271
Cdd:cd02035 80 VKELLAQYLRLPGLDEVYAEELLSLPG----MDEAAAFDEL-REYVESG------EYDVIVFDTAP 134
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
130-270 |
1.95e-07 |
|
septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.
Pssm-ID: 349756 [Multi-domain] Cd Length: 236 Bit Score: 51.82 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 130 CVTLGimnfKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDpqATLSTLfgihpDIELSVED----TLLPYFEGSETSLDYC 205
Cdd:cd02036 4 VITSG----KGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGLRNL-----DLILGLENrivyTLVDVLEGECRLEQAL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664877 206 IRKTEIPTLDVIPSNVglasadlvlpSRQRDMrqagdlswFYMKVLAEGIATIEKDYDVILIDCP 270
Cdd:cd02036 73 IKDKRWENLYLLPASQ----------TRDKDA--------LTPEKLEELVKELKDSFDFILIDSP 119
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
130-270 |
2.94e-07 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 51.69 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 130 CVTLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTD-PQATLSTLFGihpdIELSVEDTLLPYFEGsETSLDYC-IR 207
Cdd:CHL00175 15 SRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLG----LENRVLYTAMDVLEG-ECRLDQAlIR 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664877 208 KTEIPTLDVIPsnvglasadlVLPSRQRDmrqagDLSWFYMKVLAEGIAtiEKDYDVILIDCP 270
Cdd:CHL00175 90 DKRWKNLSLLA----------ISKNRQRY-----NVTRKNMNMLVDSLK--NRGYDYILIDCP 135
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
133-289 |
7.22e-07 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 49.74 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 133 LGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQ-ATLSTLFGIHPDIelsvedTLLPYFEGSETSLDYCIRKTEI 211
Cdd:TIGR01007 20 LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRnSVMSGTFKSQNKI------TGLTNFLSGTTDLSDAICDTNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 212 PTLDVIPSN-VGLASADLVLPSRQRDMrqagdlswfymkvlaegIATIEKDYDVILIDCPP-SMSYLTTVATQACDA-LL 288
Cdd:TIGR01007 94 ENLDVITAGpVPPNPTELLQSSNFKTL-----------------IETLRKRFDYIIIDTPPiGTVTDAAIIARACDAsIL 156
|
.
gi 499664877 289 V 289
Cdd:TIGR01007 157 V 157
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
70-318 |
3.51e-06 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 48.96 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 70 VAANMMGPDAAGGTESPKSTGRTGYRYSLAEAVALRKAIAELPEIRKKAKLDRRRGAGEP--CVTLGIMNFKGGVAKSTT 147
Cdd:COG4963 40 VAVASGGAAAAAAAYLSAPTPNLILLEALSESAALLADVLPLSPDELRAALARLLDPGAArrGRVIAVVGAKGGVGATTL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 148 TAHAGAYLS-LHGYRTLVIDTDPQA-TLSTLFGIHPDI-------------ELSVEDTLLPYFEGsetsldycirkteip 212
Cdd:COG4963 120 AVNLAWALArESGRRVLLVDLDLQFgDVALYLDLEPRRgladalrnpdrldETLLDRALTRHSSG--------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 213 tLDVIPSNVGLASADLVlpsrqrDMRQAGDLswfyMKVLAEGiatiekdYDVILIDCPPSMSYLTTVATQACDALLVPMR 292
Cdd:COG4963 185 -LSVLAAPADLERAEEV------SPEAVERL----LDLLRRH-------FDYVVVDLPRGLNPWTLAALEAADEVVLVTE 246
|
250 260
....*....|....*....|....*.
gi 499664877 293 PSMPDFASSAQFIRMFGGFQREVDEV 318
Cdd:COG4963 247 PDLPSLRNAKRLLDLLRELGLPDDKV 272
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
133-297 |
4.00e-06 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 47.54 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 133 LGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQAtlstlfgihpdielsvedtllpyfegseTSLDYCIRKTEip 212
Cdd:PHA02518 3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQG----------------------------SSTDWAEAREE-- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 213 TLDVIPSnVGLAsadlvlPSRQRDMRQagdlswfymkvlaegiatIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMR 292
Cdd:PHA02518 53 GEPLIPV-VRMG------KSIRADLPK------------------VASGYDYVVVDGAPQDSELARAALRIADMVLIPVQ 107
|
....*
gi 499664877 293 PSMPD 297
Cdd:PHA02518 108 PSPFD 112
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
139-272 |
5.81e-06 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 47.89 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGihpdIELSVEdtllpyfegsetsldycIRKTEIPTLDVIP 218
Cdd:COG0003 11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLG----TELGNE-----------------PTEVAVPNLYALE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664877 219 SNVgLASADLVLPSRQRDMRQAgdLSWFYMKVLAEG------IATIEK--------DYDVILIDCPPS 272
Cdd:COG0003 70 IDP-EAELEEYWERVRAPLRGL--LPSAGVDELAESlpgteeLAALDEllelleegEYDVIVVDTAPT 134
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
139-192 |
5.82e-06 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 47.73 E-value: 5.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFgihpDIELSVEDTLL 192
Cdd:pfam02374 9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSF----NQKFGHEPTKV 58
|
|
| ArsA_halo |
NF041417 |
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
139-178 |
8.26e-06 |
|
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.
Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 47.95 E-value: 8.26e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFG 178
Cdd:NF041417 341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFG 380
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
139-185 |
8.60e-06 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 46.70 E-value: 8.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIHPDIEL 185
Cdd:COG3640 8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADL 54
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
139-294 |
2.57e-05 |
|
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.
Pssm-ID: 349754 [Multi-domain] Cd Length: 249 Bit Score: 45.38 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFGIH-PDIELSVEDTLLPYFEGSETSLDYCIRKTEiPTLDVI 217
Cdd:cd02034 8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEvEKLPLIKTIGDIRERTGAKKGEPPEGMSLN-PYVDDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 218 PSN--VGLASADLVLPSRQRDmrqAGDLSWFYMKVLAEGI--ATIEKDYDVILIDCPPSMSYLTTVATQACDALLVPMRP 293
Cdd:cd02034 87 IKEiiVEPDGIDLLVMGRPEG---GGSGCYCPVNALLRELlrHLALKNYEYVVIDMEAGIEHLSRGTIRAVDLLIIVIEP 163
|
.
gi 499664877 294 S 294
Cdd:cd02034 164 S 164
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
132-168 |
5.71e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 42.03 E-value: 5.71e-05
10 20 30
....*....|....*....|....*....|....*..
gi 499664877 132 TLGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTD 168
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| CBP_BcsQ |
pfam06564 |
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ... |
133-295 |
5.87e-05 |
|
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.
Pssm-ID: 429004 [Multi-domain] Cd Length: 234 Bit Score: 44.29 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 133 LGIMNFKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPqatlSTLFGIHPDIELSVED----TLLPYFEGSETSLDYCirk 208
Cdd:pfam06564 4 LALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP----DNLLRLHFNVPFEHRQgwarAELDGADWRDAALEYT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 209 teiPTLDVIPsnVGLASADLVLpsrQRDMRQAGDLSWfymkvlAEGIATIEKDYDVILIDCPPSMSYLTTVATQACDALL 288
Cdd:pfam06564 77 ---PGLDLLP--FGRLSVEEQE---NLQQLQPDPGAW------CRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSL 142
|
....*..
gi 499664877 289 VPMRPSM 295
Cdd:pfam06564 143 LVVNPDA 149
|
|
| ArsA_halo |
NF041417 |
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ... |
139-178 |
6.90e-05 |
|
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.
Pssm-ID: 469308 [Multi-domain] Cd Length: 617 Bit Score: 45.26 E-value: 6.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLSTLFG 178
Cdd:NF041417 20 KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
141-271 |
8.55e-04 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 41.68 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 141 GVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATLS-TLFGIHPDIELSveDTLLpyfegSETSLDYCIRKTEIPTLDVIP- 218
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYThELLGTNNVNGLS--DILI-----GQGDITTAAKPTSIANFDLIPr 609
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499664877 219 SNVGLASADLVLPSRqrdmrqagdlswfymkvLAEGIATIEKDYDVILIDCPP 271
Cdd:PRK11519 610 GQVPPNPSELLMSER-----------------FAELVNWASKNYDLVLIDTPP 645
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
139-193 |
1.88e-03 |
|
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.
Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 39.74 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTD---PqaTLSTLFGIHPDIELSVEDTLLP 193
Cdd:pfam10609 12 KGGVGKSTVAVNLALALARLGYKVGLLDADiygP--SIPRMLGLEGERPEQSDGGIIP 67
|
|
| Sigma54_DBD |
pfam04552 |
Sigma-54, DNA binding domain; This DNA binding domain is based on peptide fragmentation data. ... |
24-73 |
2.36e-03 |
|
Sigma-54, DNA binding domain; This DNA binding domain is based on peptide fragmentation data. This domain is proximal to DNA in the promoter/holoenzyme complex. Furthermore this region contains a putative helix-turn-helix motif. At the C-terminus, there is a highly conserved region known as the RpoN box and is the signature of the sigma-54 proteins.
Pssm-ID: 428004 [Multi-domain] Cd Length: 159 Bit Score: 38.40 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499664877 24 RIGQM-VMRAKDFShpsklspEQGES--RRLSLREIADSIGVSHSTVNRVAAN 73
Cdd:pfam04552 26 KVAREiVRRQKAFL-------EHGPEalRPLTLREVADALGMHESTVSRATAN 71
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
139-171 |
3.73e-03 |
|
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.
Pssm-ID: 349759 Cd Length: 265 Bit Score: 39.03 E-value: 3.73e-03
10 20 30
....*....|....*....|....*....|...
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQA 171
Cdd:cd02040 8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKA 40
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
128-178 |
3.97e-03 |
|
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction
Pssm-ID: 349761 Cd Length: 266 Bit Score: 38.89 E-value: 3.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499664877 128 EPCVTLGimnfKGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQA-TLSTLFG 178
Cdd:cd02117 1 ESIVVYG----KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHdSTLLLTG 48
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
139-191 |
4.08e-03 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 38.96 E-value: 4.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499664877 139 KGGVAKSTTTAHAGAYLSLHGYRTLVIDTDPQATlSTLFGIHPDIELSVEDTL 191
Cdd:pfam00142 8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD-STRLLLGGKLQPTVLDTA 59
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
141-280 |
5.61e-03 |
|
exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273391 [Multi-domain] Cd Length: 764 Bit Score: 38.93 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664877 141 GVAKSTTTAHAGAYLSLHGYRTLVIDTD-PQATLSTLFGihPDIELSVEDTLLpyfegSETSLDYCIRKTEIPTLDVIPS 219
Cdd:TIGR01005 564 DEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFG--KAPKPGLLDLLA-----GEASIEAGIHRDQRPGLAFIAA 636
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664877 220 NVGL----ASADLVLPSRqrdmrqagdlswfymkvLAEGIATIEKDYDVILIDCPPSMSYLTTVA 280
Cdd:TIGR01005 637 GGAShfphNPNELLANPA-----------------MAELIDNARNAFDLVLVDLAALAAVADAAA 684
|
|
| |
