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Conserved domains on  [gi|435048952|gb|ELM38499|]
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putative plasmid partition protein A [Salmonella enterica subsp. enterica serovar Enteritidis str. CDC_2010K_1747]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02518 super family cl33680
ParA-like protein; Provisional
3-216 1.89e-21

ParA-like protein; Provisional


The actual alignment was detected with superfamily member PHA02518:

Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 87.98  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLseIPYFECYTDIPAMARKLAARFD 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 435048952 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
3-216 1.89e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 87.98  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLseIPYFECYTDIPAMARKLAARFD 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 435048952 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
ParA_partition NF041546
ParA family partition ATPase;
4-215 3.68e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 84.14  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLS--EIPYFECYTDIPAMARklaaRF 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELPSLAR----DY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  82 DYVFVDTPGMKSPAFVKALSCADILFTFIEPgAGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 435048952 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-164 1.61e-16

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: 72.96  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIkdfieerktndrlseipyfecytdipamarkLAARFD 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSP-FDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126

                 ...
gi 435048952 162 RQL 164
Cdd:cd02042  127 EEL 129
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
3-215 2.03e-16

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: 75.28  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG---------------SIKDFIEERKTNDRL---SEIPYF 64
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  65 ECytdIPA--------------------MARKLAA---RFDYVFVDTPGMKSPAFVKALSCADILFTFIEPGAGiEINTL 121
Cdd:COG1192   82 DL---IPAnidlagaeielvsrpgrelrLKRALAPladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL-SLEGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNGGMGVHEYD 198
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232
                        250
                 ....*....|....*..
gi 435048952 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192  233 --PKSKGAKAYRALAEE 247
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-147 1.92e-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: 52.73  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952    5 ITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGS---------------------------IKDFI-EERKTND 56
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILlKEKSDEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   57 RLSEIP-------------YFECYTDIPAMARKLAARFDYVFVDTPGmkSPAF--VKALSCADILFTFIEPGAgIEINTL 121
Cdd:pfam01656  81 GLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEPEV-ILVEDA 157
                         170       180
                  ....*....|....*....|....*...
gi 435048952  122 GRLVFDIKTAQAGVNPS--MKAWIVLNK 147
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNK 185
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
3-216 1.89e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 87.98  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLseIPYFECYTDIPAMARKLAARFD 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 435048952 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
ParA_partition NF041546
ParA family partition ATPase;
4-215 3.68e-20

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 84.14  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFIEERKTNDRLS--EIPYFECYTDIPAMARklaaRF 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELPSLAR----DY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  82 DYVFVDTPGMKSPAFVKALSCADILFTFIEPgAGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 435048952 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNGGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-164 1.61e-16

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: 72.96  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIkdfieerktndrlseipyfecytdipamarkLAARFD 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  83 YVFVDTPGMKSPAFVKALSCADILFTFIEPGAgIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSP-FDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126

                 ...
gi 435048952 162 RQL 164
Cdd:cd02042  127 EEL 129
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
3-215 2.03e-16

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: 75.28  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG---------------SIKDFIEERKTNDRL---SEIPYF 64
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  65 ECytdIPA--------------------MARKLAA---RFDYVFVDTPGMKSPAFVKALSCADILFTFIEPGAGiEINTL 121
Cdd:COG1192   82 DL---IPAnidlagaeielvsrpgrelrLKRALAPladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYL-SLEGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNGGMGVHEYD 198
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232
                        250
                 ....*....|....*..
gi 435048952 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192  233 --PKSKGAKAYRALAEE 247
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-147 1.92e-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: 52.73  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952    5 ITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGS---------------------------IKDFI-EERKTND 56
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILlKEKSDEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   57 RLSEIP-------------YFECYTDIPAMARKLAARFDYVFVDTPGmkSPAF--VKALSCADILFTFIEPGAgIEINTL 121
Cdd:pfam01656  81 GLDLIPgnidlekfekellGPRKEERLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEPEV-ILVEDA 157
                         170       180
                  ....*....|....*....|....*...
gi 435048952  122 GRLVFDIKTAQAGVNPS--MKAWIVLNK 147
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNK 185
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
4-187 2.06e-07

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 50.15  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952    4 IITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDS-QGSIKDFIEERKTNDRLSEI----PYFECYTDIP------- 71
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRTGLslptPEHLNLPDNDvaevpdg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   72 ---------AMARKLAARFDYVFVDTPGMKSPAFVKALSCADILFTFIEpGAGIEINTLGRL---VFDIKtaqagvNPSM 139
Cdd:pfam09140  82 eniddarleEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLN-DSFVDFDLLGQVdpeTFKVK------RPSF 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 435048952  140 KAWIVLnkcstnpsdsEASELRRQLNDDP-DWLpVPRQRIYMRTAHKKA 187
Cdd:pfam09140 155 YAEMVW----------EARKKRAKADRAPmDWI-VLRNRLGTLEARNKR 192
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
3-114 1.53e-06

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: 47.18  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETD-------------SQGSIKDFIEERKT-NDRLSEIPY----- 63
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSlEDIIVEGPEgldii 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 435048952  64 -----FECYTDIPAMARK--------LAARFDYVFVDTPGMKSPAFVKALSCAD--ILFTFIEPGA 114
Cdd:cd02038   81 pggsgMEELANLDPEQKAklieelssLESNYDYLLIDTGAGISRNVLDFLLAADevIVVTTPEPTS 146
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-172 3.13e-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: 47.03  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   2 GKIITVAGHKGGIGKSTVLCSLCV---------CVII-----KGKTACFLETDSQGSIKDFIEERKTNDR---------- 57
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWalaresgrrVLLVdldlqFGDVALYLDLEPRRGLADALRNPDRLDEtlldraltrh 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952  58 ------LSEIPYFECYTDIPAMA-----RKLAARFDYVFVDTPGMKSPAFVKALSCADILFTFIEPgagiEINTLGRLVF 126
Cdd:COG4963  182 ssglsvLAAPADLERAEEVSPEAverllDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP----DLPSLRNAKR 257
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 435048952 127 DIKT-AQAGVNPSmKAWIVLNKCSTNPsDSEASELRRQLNDDPDW-LP 172
Cdd:COG4963  258 LLDLlRELGLPDD-KVRLVLNRVPKRG-EISAKDIEEALGLPVAAvLP 303
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
3-90 1.08e-04

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 41.59  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGgIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKdfIEERKTNDRLSEIPYFECYT-----DIpAMARKL 77
Cdd:cd03115    1 NVILLVGLQG-SGKTTTLAKLARYYQEKGKKVLLIAADTFRAAA--VEQLKTLAEKLGVPVFESYTgtdpaSI-AQEAVE 76
                         90
                 ....*....|....*.
gi 435048952  78 AAR---FDYVFVDTPG 90
Cdd:cd03115   77 KAKlegYDVLLVDTAG 92
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
3-93 2.82e-04

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 40.63  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952    3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSI---KDFIEERKTNDRLSEI------PYFEcytdiPAM 73
Cdd:pfam07015   2 QLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLtkwRENALRKGTWDPACEIfnadelPLLE-----QAY 76
                          90       100
                  ....*....|....*....|
gi 435048952   74 ARKLAARFDYVFVDTPGMKS 93
Cdd:pfam07015  77 EHAEGSGFDYALADTHGGSS 96
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
2-75 7.20e-04

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 39.26  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   2 GKIITVAGHKGgIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIK--------DFIEERKTNDRLSEIPYFECYTDIPAM 73
Cdd:cd01393    1 GKITEIYGPPG-SGKTQLALQLAANALLLGGGVVWIDTEGAFPPSrlvqileaSPSSELELAEALSRLLYFRPPDTLAHL 79

                 ..
gi 435048952  74 AR 75
Cdd:cd01393   80 LA 81
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
3-93 1.57e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 38.28  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435048952   3 KIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSI---KDFIEERKTNDRLSEI------PYFEcytdiPAM 73
Cdd:PRK13849   2 KLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLtrwKENALRSNTWDPACEVyaadelPLLE-----AAY 76
                         90       100
                 ....*....|....*....|
gi 435048952  74 ARKLAARFDYVFVDTPGMKS 93
Cdd:PRK13849  77 EDAELQGFDYALADTHGGSS 96
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
3-67 6.20e-03

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: 36.94  E-value: 6.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435048952    3 KIITVAGhKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQGSIKDFI------EERKTNDRLS--EI-PYFECY 67
Cdd:pfam02374   2 RWIFFGG-KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFnqkfghEPTKVKENLSamEIdPNMELE 74
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-43 8.76e-03

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: 35.64  E-value: 8.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 435048952    2 GKIITVAGHKGGIGKSTVLCSLCVCVIIKGKTACFLETDSQG 43
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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