|
Name |
Accession |
Description |
Interval |
E-value |
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
21-417 |
5.96e-102 |
|
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: 307.81 E-value: 5.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 21 FAPVARPVPRITVQAFCDTPDVAGTLDMAASDRRMARAHTKVHTGGITAAAEFYRSAPTPNLIVVESRLSREELLAhldd 100
Cdd:COG4963 1 DLVALRPLPRISIQAFCESAALAALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSESAALLA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 101 laevcdagtkvlvighsndvvtyrellkrgvseyLIAPVDVMTVIAAIADIyREDGESKLGHVFAFVGAKGGVGSSTIAH 180
Cdd:COG4963 77 ----------------------------------DVLPLSPDELRAALARL-LDPGAARRGRVIAVVGAKGGVGATTLAV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 181 NVAWTMARAFGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDRLLTKCEEHLSILAAPATLDKTYDFE 260
Cdd:COG4963 122 NLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 261 EDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLKQARPNDTPPKLILNKvgV 340
Cdd:COG4963 202 PEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDKVRLVLNR--V 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103969155 341 PRQPEIKVDDFGAALQLAPTAAIPFDPLLFGTAANNGQMIAEASAKSSINDTFAEIAQIITGRMELKHGRKSGLSLA 417
Cdd:COG4963 280 PKRGEISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGGKLLK 356
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
163-397 |
2.74e-80 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 247.96 E-value: 2.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 163 VFAFVGAKGGVGSSTIAHNVAWTMARAFGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDRLLTKCEE 242
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSAVTRHSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 243 HLSILAAPATLDKTYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLK 322
Cdd:cd03111 82 GLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLDSLR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2103969155 323 QARPNDTPPKLILNKVGVPrqPEIKVDDFGAALQLAPTAAIPFDPLLFGTAANNGQMIAEASAKSSINDTFAEIA 397
Cdd:cd03111 162 ELEGSSDRLRLVLNRYDKK--SEISPKDIEEALGLEVFATLPNDYKAVSESANTGRPLVEVAPRSALVRALQDLA 234
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
164-342 |
2.73e-08 |
|
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: 54.27 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 164 FAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLD-----LAFGTVALDFNQDpPQGMADAVFGSDRLDEVLLDRllT 238
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDpqsnnSSVEGLEGDIAPA-LQALAEGLKGRVNLDPILLKE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 239 KCEEHLSILAAPATLDKTYDFEEDSFDH-----VLDIVQSNVPTVVLDLPhmwTSW---TRKLLLAADDVIVTATPDLAN 310
Cdd:pfam01656 77 SDEGGLDLIPGNIDLEKFEKELLGPRKEerlreALEALKEDYDYVIIDGA---PGLgelLRNALIAADYVIIPLEPEVIL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2103969155 311 LRNAKNLVDLL-----KQARPNDTPPKLILNKVGVPR 342
Cdd:pfam01656 154 VEDAKRLGGVIaalvgGYALLGLKIIGVVLNKVDGDN 190
|
|
| CpaE_hom_Actino |
TIGR03815 |
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ... |
62-309 |
5.90e-06 |
|
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.
Pssm-ID: 274798 [Multi-domain] Cd Length: 322 Bit Score: 48.10 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 62 VHTGGITAAAEFYRSAPtpnLIVVESRLSREELLAHLDDLAEVcdagtkVLVIGHSNDVVTYRELLKRGVSEYLIAPVDV 141
Cdd:TIGR03815 5 DVAADPEAARRAWARAP---LVLVDADMAEACAAAGLPRRRRV------VLVGGGEPGGALWRAAAAVGAEHVAVLPEAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 142 MTVIAAIADIYREDGESklGHVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFNQDPPQGM--A 219
Cdd:TIGR03815 76 GWLVELLADLDQSPPAR--GVVVAVIGGRGGAGASTLAAALALAAARH-GLRTLLVDADPWGGGLDLLLGAEDVPGLrwP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 220 DAVFGSDRLD-EVLLDRLLTKceEHLSILAAPATldKTYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAAD 298
Cdd:TIGR03815 153 DLSQARGRLPaGALRDALPRR--GGLSVLSWGRA--VGAALPPAAVRAVLDAARRGGDLVVVDLPRRLTPAAETALESAD 228
|
250
....*....|.
gi 2103969155 299 DVIVTATPDLA 309
Cdd:TIGR03815 229 LVLVVVPADVR 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
21-417 |
5.96e-102 |
|
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: 307.81 E-value: 5.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 21 FAPVARPVPRITVQAFCDTPDVAGTLDMAASDRRMARAHTKVHTGGITAAAEFYRSAPTPNLIVVESRLSREELLAhldd 100
Cdd:COG4963 1 DLVALRPLPRISIQAFCESAALAALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSESAALLA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 101 laevcdagtkvlvighsndvvtyrellkrgvseyLIAPVDVMTVIAAIADIyREDGESKLGHVFAFVGAKGGVGSSTIAH 180
Cdd:COG4963 77 ----------------------------------DVLPLSPDELRAALARL-LDPGAARRGRVIAVVGAKGGVGATTLAV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 181 NVAWTMARAFGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDRLLTKCEEHLSILAAPATLDKTYDFE 260
Cdd:COG4963 122 NLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDRLDETLLDRALTRHSSGLSVLAAPADLERAEEVS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 261 EDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLKQARPNDTPPKLILNKvgV 340
Cdd:COG4963 202 PEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDKVRLVLNR--V 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103969155 341 PRQPEIKVDDFGAALQLAPTAAIPFDPLLFGTAANNGQMIAEASAKSSINDTFAEIAQIITGRMELKHGRKSGLSLA 417
Cdd:COG4963 280 PKRGEISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGGKLLK 356
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
163-397 |
2.74e-80 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 247.96 E-value: 2.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 163 VFAFVGAKGGVGSSTIAHNVAWTMARAFGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDRLLTKCEE 242
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDRLDRTLLDSAVTRHSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 243 HLSILAAPATLDKTYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLK 322
Cdd:cd03111 82 GLSLLPAPQELEDLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLLDSLR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2103969155 323 QARPNDTPPKLILNKVGVPrqPEIKVDDFGAALQLAPTAAIPFDPLLFGTAANNGQMIAEASAKSSINDTFAEIA 397
Cdd:cd03111 162 ELEGSSDRLRLVLNRYDKK--SEISPKDIEEALGLEVFATLPNDYKAVSESANTGRPLVEVAPRSALVRALQDLA 234
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
177-403 |
4.82e-19 |
|
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: 85.71 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 177 TIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDrlltkCEEHLSILAAPATLDKT 256
Cdd:COG0455 1 TVAVNLAAALARL-GKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQ-----GPGGLDVLPGGSGPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 257 YDF-EEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLKQARPNDtPPKLIL 335
Cdd:COG0455 75 AELdPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVR-RAGVVV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103969155 336 NKVGVPRQPEIKVDDFGAALQ------LAPTAAIPFDPLLfGTAANNGQMIAEASAKSSINDTFAEIAQIITGR 403
Cdd:COG0455 154 NRVRSEAEARDVFERLEQVAErflgvrLRVLGVIPEDPAV-REAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
163-369 |
1.07e-17 |
|
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: 81.85 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 163 VFAFVGAKGGVGSSTIAHNVAWTMARaFGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLdrlltKCEE 242
Cdd:cd02038 2 IIAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIV-----EGPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 243 HLSILAAPATLDKTYDFEEDSFDHVLDIVQ---SNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVD 319
Cdd:cd02038 76 GLDIIPGGSGMEELANLDPEQKAKLIEELSsleSNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2103969155 320 LLKQARPNdTPPKLILNKVGVPRQPE------IKVDD--FGAALQLAptAAIPFDPLL 369
Cdd:cd02038 156 VLSRRGGK-KNFRLIVNMARSPKEGRatferlKKVAKrfLDINLDFV--GFIPYDQSV 210
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
170-398 |
3.08e-14 |
|
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: 71.85 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 170 KGGVGSSTIAHNVAWTMARaFGSDVLL--ADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDrllTKCEEHLSIL 247
Cdd:cd02036 9 KGGVGKTTTTANLGVALAK-LGKKVLLidADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIK---DKRWENLYLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 248 AAPATLDKtYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLLKQARPn 327
Cdd:cd02036 85 PASQTRDK-DALTPEKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLESKGI- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103969155 328 dTPPKLILNKVG---VPRQPEIKVDDFGAALQLAPTAAIPFDPLLFgTAANNGQMIAEASAKSSINDTFAEIAQ 398
Cdd:cd02036 163 -VNIGLIVNRYRpemVKSGDMLSVEDIQEILGIPLLGVIPEDPEVI-VATNRGEPLVLYKPNSLAAKAFENIAR 234
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
135-325 |
8.37e-11 |
|
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: 62.51 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 135 LIAPVDVMTVIAAIADIYREDGESKLGHVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFNQDP 214
Cdd:COG0489 66 LLGLLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQS-GKRVLLIDADLRGPSLHRMLGLEN 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 215 PQGMADAVFGSDRLDEVLLDRLLtkceEHLSILAAPATLDKTYD-FEEDSFDHVLDIVQSNVPTVVLDLPHMwTSWTRKL 293
Cdd:COG0489 145 RPGLSDVLAGEASLEDVIQPTEV----EGLDVLPAGPLPPNPSElLASKRLKQLLEELRGRYDYVIIDTPPG-LGVADAT 219
|
170 180 190
....*....|....*....|....*....|....
gi 2103969155 294 LLA--ADDVIVTATPDLANLRNAKNLVDLLKQAR 325
Cdd:COG0489 220 LLAslVDGVLLVVRPGKTALDDVRKALEMLEKAG 253
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
162-335 |
9.38e-11 |
|
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: 61.80 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 162 HVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDlafgtvaldfnqdpPQGMADAVFGSDR-----------LDE 230
Cdd:COG1192 2 KVIAVANQKGGVGKTTTAVNLAAALARR-GKRVLLIDLD--------------PQGNLTSGLGLDPddldptlydllLDD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 231 VLLDRLLTKCE-EHLSILaaPATLD--------KTYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAADDVI 301
Cdd:COG1192 67 APLEDAIVPTEiPGLDLI--PANIDlagaeielVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVL 144
|
170 180 190
....*....|....*....|....*....|....
gi 2103969155 302 VTATPDLANLRNAKNLVDLLKQARPNDTPPKLIL 335
Cdd:COG1192 145 IPVQPEYLSLEGLAQLLETIEEVREDLNPKLEIL 178
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
156-327 |
1.51e-10 |
|
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: 60.28 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 156 GESKLGHVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFNQDPPQGMADAVFGSDRLDEVLLDR 235
Cdd:cd05387 14 GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQS-GKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLSGQASLEDVIQST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 236 LLtkceEHLSILAA------PATLdktydFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSwTRKLLLA--ADDVIVTATPD 307
Cdd:cd05387 93 NI----PNLDVLPAgtvppnPSEL-----LSSPRFAELLEELKEQYDYVIIDTPPVLAV-ADALILAplVDGVLLVVRAG 162
|
170 180
....*....|....*....|
gi 2103969155 308 LANLRNAKNLVDLLKQARPN 327
Cdd:cd05387 163 KTRRREVKEALERLEQAGAK 182
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
162-335 |
2.98e-09 |
|
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: 54.85 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 162 HVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDlafgtvaldfnqdpPQGmadavfgsdrldevlldrlltkce 241
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALR-GKRVLLIDLD--------------PQG------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 242 eHLSILAapatldktYDFeedsfdhvldivqsnvptVVLDLPHMWTSWTRKLLLAADDVIVTATPDLANLRNAKNLVDLL 321
Cdd:cd02042 42 -SLTSWL--------YDY------------------ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTL 94
|
170
....*....|....
gi 2103969155 322 KQARPNDTPPKLIL 335
Cdd:cd02042 95 EELKKQLNPPLLIL 108
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
164-342 |
2.73e-08 |
|
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: 54.27 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 164 FAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLD-----LAFGTVALDFNQDpPQGMADAVFGSDRLDEVLLDRllT 238
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDpqsnnSSVEGLEGDIAPA-LQALAEGLKGRVNLDPILLKE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 239 KCEEHLSILAAPATLDKTYDFEEDSFDH-----VLDIVQSNVPTVVLDLPhmwTSW---TRKLLLAADDVIVTATPDLAN 310
Cdd:pfam01656 77 SDEGGLDLIPGNIDLEKFEKELLGPRKEerlreALEALKEDYDYVIIDGA---PGLgelLRNALIAADYVIIPLEPEVIL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2103969155 311 LRNAKNLVDLL-----KQARPNDTPPKLILNKVGVPR 342
Cdd:pfam01656 154 VEDAKRLGGVIaalvgGYALLGLKIIGVVLNKVDGDN 190
|
|
| CpaE_hom_Actino |
TIGR03815 |
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ... |
62-309 |
5.90e-06 |
|
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.
Pssm-ID: 274798 [Multi-domain] Cd Length: 322 Bit Score: 48.10 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 62 VHTGGITAAAEFYRSAPtpnLIVVESRLSREELLAHLDDLAEVcdagtkVLVIGHSNDVVTYRELLKRGVSEYLIAPVDV 141
Cdd:TIGR03815 5 DVAADPEAARRAWARAP---LVLVDADMAEACAAAGLPRRRRV------VLVGGGEPGGALWRAAAAVGAEHVAVLPEAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 142 MTVIAAIADIYREDGESklGHVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFNQDPPQGM--A 219
Cdd:TIGR03815 76 GWLVELLADLDQSPPAR--GVVVAVIGGRGGAGASTLAAALALAAARH-GLRTLLVDADPWGGGLDLLLGAEDVPGLrwP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 220 DAVFGSDRLD-EVLLDRLLTKceEHLSILAAPATldKTYDFEEDSFDHVLDIVQSNVPTVVLDLPHMWTSWTRKLLLAAD 298
Cdd:TIGR03815 153 DLSQARGRLPaGALRDALPRR--GGLSVLSWGRA--VGAALPPAAVRAVLDAARRGGDLVVVDLPRRLTPAAETALESAD 228
|
250
....*....|.
gi 2103969155 299 DVIVTATPDLA 309
Cdd:TIGR03815 229 LVLVVVPADVR 239
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
162-201 |
1.14e-04 |
|
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.
Pssm-ID: 349757 [Multi-domain] Cd Length: 213 Bit Score: 43.26 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2103969155 162 HVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDL 201
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKK-GYKVGLLDADI 39
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
163-283 |
1.17e-04 |
|
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: 43.19 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 163 VFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDLAFGTVALDFN-QDPPQGMADAVFGSDRLDEVLLDrllTKCE 241
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQA-GYKTLLIDGDMRNSVMSGTFKsQNKITGLTNFLSGTTDLSDAICD---TNIE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2103969155 242 EHLSILAAPATLDKTYDFEEDSFDHVLDIVQSNVPTVVLDLP 283
Cdd:TIGR01007 95 NLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTP 136
|
|
| TadZ-like |
cd17869 |
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ... |
161-320 |
9.20e-04 |
|
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349778 [Multi-domain] Cd Length: 219 Bit Score: 40.60 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 161 GHVFAFVGAKGGVGSSTIAHNVAWTMArAFGSDVLLADLDlAFGTVALDFNQDPPQGMADAVFG---SDRLDEVLLDRLL 237
Cdd:cd17869 3 TSVITFHSPCGGSGKSTVAAACAYTLA-EKGKKTLYLNME-RLQSTDVFFGASGRYLMSDHLYTlksRKANLADKLESCV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103969155 238 TKCEEHLSILAAPATLDKTYDFEEDSFDHVLDIVQ--SNVPTVVLDLPHMWTSWTRKLLLAADDVIVTATPD-LANLRNA 314
Cdd:cd17869 81 KQHESGVYYFSPFKSALDILEIKKDDILHMITKLVeaHAYDYIIMDLSFEFSSTVCKLLQASHNNVVIALQDaNSSYKLN 160
|
....*.
gi 2103969155 315 KNLVDL 320
Cdd:cd17869 161 KFLRAL 166
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
162-201 |
2.99e-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: 38.97 E-value: 2.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2103969155 162 HVFAFVGAKGGVGSSTIAHNVAWTMARAfGSDVLLADLDL 201
Cdd:pfam10609 4 HVIAVASGKGGVGKSTVAVNLALALARL-GYKVGLLDADI 42
|
|
| |
