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Conserved domains on  [gi|380002990|gb|AFD28175|]
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ATPase involved in plasmide/chromosome partitioning, ParA/Soj-like protein (plasmid) [Deinococcus gobiensis I-0]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-245 9.08e-71

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: 217.42  E-value: 9.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIEIDQTIYPVAVDGAPLPA---PVQVHG 77
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDaivPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  78 LSLIPAHVDLASAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGQLaTLGAL-AADRLIVPMPTRQKGLDALPG 156
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLL-TLNALaAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 157 LNRAMGMYHR-LRPELRVALYVPTMHDARRLHDREVLEQLRGYLNP--MSEPVPQREAVwLDSTTAGQPVGVYAPRSPVH 233
Cdd:COG1192  160 LLETIEEVREdLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDkvLDTVIPRSVAL-AEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|..
gi 380002990 234 ADVIRLTSAIAQ 245
Cdd:COG1192  239 KAYRALAEELLE 250
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-245 9.08e-71

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: 217.42  E-value: 9.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIEIDQTIYPVAVDGAPLPA---PVQVHG 77
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDaivPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  78 LSLIPAHVDLASAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGQLaTLGAL-AADRLIVPMPTRQKGLDALPG 156
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLL-TLNALaAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 157 LNRAMGMYHR-LRPELRVALYVPTMHDARRLHDREVLEQLRGYLNP--MSEPVPQREAVwLDSTTAGQPVGVYAPRSPVH 233
Cdd:COG1192  160 LLETIEEVREdLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDkvLDTVIPRSVAL-AEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|..
gi 380002990 234 ADVIRLTSAIAQ 245
Cdd:COG1192  239 KAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-157 1.97e-37

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: 129.63  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIEIDQTIYPVAVDGAPLPA---PVQVHG 77
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEaiiKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   78 LSLIPAHVDLASAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGqLATLGAL-AADRLIVPMPTRQKGLDALPG 156
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLG-LLTINALtASDSVLIPVQCEYYALEGLSQ 159


                  .
gi 380002990  157 L 157
Cdd:pfam13614 160 L 160
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-196 1.34e-31

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: 113.02  E-value: 1.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   3 TLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLgvggieidqtiypvavdgaplpapvqvhglslip 82
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  83 ahvdlasaeaqmlgqvgsilflkqaltavadqYDVVLIDSPPSLGQLATLGALAADRLIVPMPTRQKGLDALPGLNRAMG 162
Cdd:cd02042   48 --------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLE 95

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380002990 163 MYHR-LRPELRVALYVPTMHDARRLHDREVLEQLR 196
Cdd:cd02042   96 ELKKqLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-145 2.97e-22

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: 94.27  E-value: 2.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGiEID----QTIY-PVAVDGAPLPAPVQVH-- 76
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQP-EFDvgenETLYgAIRYDDERRPISEIIRkt 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   77 ---GLSLIPAHVDL-----ASAEAQMLGQVGSILF---LKQALTAVADQYDVVLIDSPPSLGQLaTLGAL-AADRLIVPM 144
Cdd:TIGR03453 186 yfpGLDLVPGNLELmefehETPRALSRGQGGDTIFfarVGEALAEVEDDYDVVVIDCPPQLGFL-TLSALcAATGVLITV 264


                  .
gi 380002990  145 P 145
Cdd:TIGR03453 265 H 265
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 4-142 6.70e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 87.81  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGV---GGIEIDQTIY-PVAVDGAPLP-----APVQ 74
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpeTDVGANETLYaAIRYDDTRRPlrdviRPTY 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380002990  75 VHGLSLIPAHVDL-----ASAEAQMLGQVGSILF---LKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIV 142
Cdd:PRK13869 204 FDGLHLVPGNLELmefehTTPKALSDKGTRDGLFftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
ParA_partition NF041546
ParA family partition ATPase;
3-231 2.19e-15

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 72.20  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   3 TLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWlgvggieidqtiYPVAVDGAPLPApvqvhglslip 82
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDW------------AAAREDERPFPV----------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  83 ahVDLASAEaqmlgqvgsilfLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVpmPTRQKGLD-----ALPGL 157
Cdd:NF041546  58 --VGLARPT------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI--PVQPSPYDlwasaDTVDL 121

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380002990 158 NRAMGMYhrlRPELRVALyVPTMHDARRLHDREVLEQLRGYLNP-MSEPVPQREAvWLDSTTAGQPVGVYAPRSP 231
Cdd:NF041546 122 IKEAREY---TPGLKAAF-VLNRAIARTALGREVAEALAEYGLPvLKTRIGQRVA-FAESAAEGLTVFEAEPDGK 191
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-245 9.08e-71

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: 217.42  E-value: 9.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIEIDQTIYPVAVDGAPLPA---PVQVHG 77
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDaivPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  78 LSLIPAHVDLASAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGQLaTLGAL-AADRLIVPMPTRQKGLDALPG 156
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLL-TLNALaAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 157 LNRAMGMYHR-LRPELRVALYVPTMHDARRLHDREVLEQLRGYLNP--MSEPVPQREAVwLDSTTAGQPVGVYAPRSPVH 233
Cdd:COG1192  160 LLETIEEVREdLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDkvLDTVIPRSVAL-AEAPSAGKPVFEYDPKSKGA 238

                        250
                 ....*....|..
gi 380002990 234 ADVIRLTSAIAQ 245
Cdd:COG1192  239 KAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-157 1.97e-37

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: 129.63  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIEIDQTIYPVAVDGAPLPA---PVQVHG 77
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEaiiKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   78 LSLIPAHVDLASAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGqLATLGAL-AADRLIVPMPTRQKGLDALPG 156
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLG-LLTINALtASDSVLIPVQCEYYALEGLSQ 159


                  .
gi 380002990  157 L 157
Cdd:pfam13614 160 L 160
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-196 1.34e-31

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: 113.02  E-value: 1.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   3 TLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLgvggieidqtiypvavdgaplpapvqvhglslip 82
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  83 ahvdlasaeaqmlgqvgsilflkqaltavadqYDVVLIDSPPSLGQLATLGALAADRLIVPMPTRQKGLDALPGLNRAMG 162
Cdd:cd02042   48 --------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLE 95

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380002990 163 MYHR-LRPELRVALYVPTMHDARRLHDREVLEQLR 196
Cdd:cd02042   96 ELKKqLNPPLLILGILLTRVDPRTKLAREVLEELK 130
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-212 8.29e-30

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: 111.28  E-value: 8.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVgGIEIDQTIYPVA--------VDGAPLPAPVQV 75
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGL-EGDIAPALQALAeglkgrvnLDPILLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   76 HGLSLIPAHVDLASAEaQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPMPTRQK---GLD 152
Cdd:pfam01656  80 GGLDLIPGNIDLEKFE-KELLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVIlveDAK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380002990  153 ALPGLNRAMGMYHRLRpELRVALYVPTMHDARRLHDRE---VLEQLRGylNPMSEPVPQREAV 212
Cdd:pfam01656 159 RLGGVIAALVGGYALL-GLKIIGVVLNKVDGDNHGKLLkeaLEELLRG--LPVLGVIPRDEAV 218
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-145 2.97e-22

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: 94.27  E-value: 2.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGiEID----QTIY-PVAVDGAPLPAPVQVH-- 76
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQP-EFDvgenETLYgAIRYDDERRPISEIIRkt 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   77 ---GLSLIPAHVDL-----ASAEAQMLGQVGSILF---LKQALTAVADQYDVVLIDSPPSLGQLaTLGAL-AADRLIVPM 144
Cdd:TIGR03453 186 yfpGLDLVPGNLELmefehETPRALSRGQGGDTIFfarVGEALAEVEDDYDVVVIDCPPQLGFL-TLSALcAATGVLITV 264


                  .
gi 380002990  145 P 145
Cdd:TIGR03453 265 H 265
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 4-142 6.70e-20

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 87.81  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGV---GGIEIDQTIY-PVAVDGAPLP-----APVQ 74
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlpeTDVGANETLYaAIRYDDTRRPlrdviRPTY 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380002990  75 VHGLSLIPAHVDL-----ASAEAQMLGQVGSILF---LKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIV 142
Cdd:PRK13869 204 FDGLHLVPGNLELmefehTTPKALSDKGTRDGLFftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 2-145 6.37e-16

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 76.17  E-value: 6.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   2 ITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLID-LDPQANLT---GWLGVGGIEIDQTIYPVAV----DGAPLPAPV 73
Cdd:PRK13705 107 PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASmyhGWVPDLHIHAEDTLLPFYLgekdDATYAIKPT 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  74 QVHGLSLIPAHVDLASAEAQMLGQ-------VGSILFLKQALTAVADQYDVVLIDSPPSLGqLATLG-ALAADRLIVPMP 145
Cdd:PRK13705 187 CWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLG-IGTINvVCAADVLIVPTP 265
ParA_partition NF041546
ParA family partition ATPase;
3-231 2.19e-15

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 72.20  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   3 TLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWlgvggieidqtiYPVAVDGAPLPApvqvhglslip 82
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDW------------AAAREDERPFPV----------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  83 ahVDLASAEaqmlgqvgsilfLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVpmPTRQKGLD-----ALPGL 157
Cdd:NF041546  58 --VGLARPT------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI--PVQPSPYDlwasaDTVDL 121

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380002990 158 NRAMGMYhrlRPELRVALyVPTMHDARRLHDREVLEQLRGYLNP-MSEPVPQREAvWLDSTTAGQPVGVYAPRSP 231
Cdd:NF041546 122 IKEAREY---TPGLKAAF-VLNRAIARTALGREVAEALAEYGLPvLKTRIGQRVA-FAESAAEGLTVFEAEPDGK 191
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 22-246 4.74e-15

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: 71.84  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  22 VGYELAHGGQRVLLIDLDPQ-ANLTGWLGV-----------GGIEIDQTIYPVAvdgaplpapvqvHGLSLIPAHVDLAS 89
Cdd:COG0455    6 LAAALARLGKRVLLVDADLGlANLDVLLGLepkatladvlaGEADLEDAIVQGP------------GGLDVLPGGSGPAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  90 AEAqmlgqVGSILFLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPMPtrqkglDALPGLNRAMGMYHRLRP 169
Cdd:COG0455   74 LAE-----LDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTT------PEPTSITDAYALLKLLRR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 170 ELRVALY------VPTMHDARRLHDReVLEQLRGYLNPMSEP---VPQREAVWlDSTTAGQPVGVYAPRSPVHADVIRLT 240
Cdd:COG0455  143 RLGVRRAgvvvnrVRSEAEARDVFER-LEQVAERFLGVRLRVlgvIPEDPAVR-EAVRRGRPLVLAAPDSPAARAIRELA 220


                 ....*.
gi 380002990 241 SAIAQA 246
Cdd:COG0455  221 ARLAGW 226
PHA02518 PHA02518
ParA-like protein; Provisional
 4-239 8.27e-14

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 68.34  E-value: 8.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   4 LTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWlgvggieidqtiypvavdgaplpAPVQVHGLSLIPA 83
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW-----------------------AEAREEGEPLIPV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  84 hvdlasaeAQMLGQVgsilflKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPMPTRQKGLDALPGLNRAMGM 163
Cdd:PHA02518  60 --------VRMGKSI------RADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKA 125

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380002990 164 YHRLRPELRVALYVPT--MHDARRlhDREVLEQLRGY-LNPMSEPVPQREAvWLDSTTAGQPVGVYAPRSPVHADVIRL 239
Cdd:PHA02518 126 RQEVTDGLPKFAFIISraIKNTQL--YREARKALAGYgLPILRNGTTQRVA-YADAAEAGGSVLELPEDDKAAEEIIQL 201
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 2-145 2.27e-12

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 65.80  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   2 ITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLID-LDPQANLT---GWLGVGGIEIDQTIYPVAV---DGAPLP-APV 73
Cdd:PHA02519 107 VVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASmyhGYVPDLHIHADDTLLPFYLgerDNAEYAiKPT 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380002990  74 QVHGLSLIPAHVDLASAEAQMLG-------QVGSILFLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPMP 145
Cdd:PHA02519 187 CWPGLDIIPSCLALHRIETDLMQyhdagklPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATP 265
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 11-142 3.78e-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: 61.74  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDP-QANLTGWLGVGGieiDQTIYPVAVDGAPLPA---PVQVHGLSLIPAHVD 86
Cdd:COG0489  102 GGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLEN---RPGLSDVLAGEASLEDviqPTEVEGLDVLPAGPL 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 380002990  87 LASAEAQMLGQVgsilfLKQALTAVADQYDVVLIDSPPSLG--QLATLGALAADRLIV 142
Cdd:COG0489  179 PPNPSELLASKR-----LKQLLEELRGRYDYVIIDTPPGLGvaDATLLASLVDGVLLV 231
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-235 1.14e-09

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: 56.97  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    1 MITLTVFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVgGIEIDQTIYPVAVDGAPLPAPVQ--VHGL 78
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGM-DWSVRDGWARALLNGADWAAAAYrsPDGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   79 SLIP-AHVDLASAEAQMLGQVGSILFLKQALTAVADqyDVVLIDSPPSLGQLATLGALAADRLIVPMPTRQKGLDALPgl 157
Cdd:TIGR03371  80 LFLPyGDLSADEREAYQAHDAGWLARLLQQLDLAAR--DWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLH-- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380002990  158 nRAMGMYHRLRPELRVALYVPTMHDARRLHDREVLEQLRGYLNPMSEPVP-QREAVWLDSTTAGQPVGVYAPRSPVHAD 235
Cdd:TIGR03371 156 -QLALALFAGSGPRDGPRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFViHRDEAVSEALARGTPVLNYAPHSQAAHD 233
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-247 1.22e-09

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: 57.82  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   3 TLTVFNHAGGAGKTSLARDVGYELAH-GGQRVLLIDLDPQA-NLTGWLGvggIEIDQTIY-----PVAVDGAPLPAPVQV 75
Cdd:COG4963  104 VIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFgDVALYLD---LEPRRGLAdalrnPDRLDETLLDRALTR 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  76 H--GLSLIPAHVDLASAEAQMLGQVGSILflkqalTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPMptrqkGLD- 152
Cdd:COG4963  181 HssGLSVLAAPADLERAEEVSPEAVERLL------DLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVT-----EPDl 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 153 -ALPGLNRAMGMYHRLRPELRVALYVPTMHDARRLHDREVLEQLRGYlnPMSEPVPQREAVWLDSTTAGQPVGVYAPRSP 231
Cdd:COG4963  250 pSLRNAKRLLDLLRELGLPDDKVRLVLNRVPKRGEISAKDIEEALGL--PVAAVLPNDPKAVAEAANQGRPLAEVAPKSP 327

                        250
                 ....*....|....*.
gi 380002990 232 VHADVIRLTSAIAQAA 247
Cdd:COG4963  328 LAKAIRKLAARLTGRP 343
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 11-146 2.96e-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: 55.65  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDpqanltgwLGVGGIEI------DQTIYPVAVDGAPL-PAPVQV-HGLSLIP 82
Cdd:cd02038   10 GGVGKTNVSANLALALSKLGKRVLLLDAD--------LGLANLDIllglapKKTLGDVLKGRVSLeDIIVEGpEGLDIIP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  83 A---HVDLASAEAQMLGQvgsilfLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIV---PMPT 146
Cdd:cd02038   82 GgsgMEELANLDPEQKAK------LIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVvttPEPT 145
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 5-240 2.43e-08

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: 53.05  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   5 TVFNHAGGAGKTSLARDVGYELAH-GGQRVLLIDLD-PQANLTGWLGvggIEIDQTIYPVA-----VDGAPLPAPVQVH- 76
Cdd:cd03111    4 AVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDlPFGDLGLYLN---LRPDYDLADVIqnldrLDRTLLDSAVTRHs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  77 -GLSLIPAHVDLASAEAQMLGQVGSILflkQALTAvadQYDVVLIDSPPSLGQLATLGALAADRLIVPMptrQKGLDALP 155
Cdd:cd03111   81 sGLSLLPAPQELEDLEALGAEQVDKLL---QVLRA---FYDHIIVDLGHFLDEVTLAVLEAADEILLVT---QQDLPSLR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 156 GLNRAMGMYHRLRP-ELRVALYVpTMHDARRLHDREVLEQLRGylNPMSEPVPQREAVWLDSTTAGQPVGVYAPRSPVHA 234
Cdd:cd03111  152 NARRLLDSLRELEGsSDRLRLVL-NRYDKKSEISPKDIEEALG--LEVFATLPNDYKAVSESANTGRPLVEVAPRSALVR 228


                 ....*.
gi 380002990 235 DVIRLT 240
Cdd:cd03111  229 ALQDLA 234
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 11-231 5.97e-08

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: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLD-PQANLTGWLGV-------------GGIEIDQTIYpvavdgaplpAPVQVH 76
Cdd:cd02036   10 GGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLenrivytlvdvleGECRLEQALI----------KDKRWE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  77 GLSLIPAHVDLASAEAQMLGqvgsilfLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIV---PMPTRQKGLDA 153
Cdd:cd02036   80 NLYLLPASQTRDKDALTPEK-------LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIvtnPEISSVRDADR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380002990 154 LPGLNRAMGMYHrlrPELRVALYVPTMHDARRLHDREVLEQLRGYlnPMSEPVPQREAVwLDSTTAGQPVGVYAPRSP 231
Cdd:cd02036  153 VIGLLESKGIVN---IGLIVNRYRPEMVKSGDMLSVEDIQEILGI--PLLGVIPEDPEV-IVATNRGEPLVLYKPNSL 224
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 12-127 1.92e-07

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: 49.88  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  12 GAGKTSLARDVGYELAHGGQRVLLIDLD-------------PQANLTGWLgVGGIEIDQTIYPvavDGAPlpapvqvhGL 78
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADlrrpslhrllglpNEPGLSEVL-SGQASLEDVIQS---TNIP--------NL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 380002990  79 SLIPAhvdlasaeaqmlGQV---GSILF----LKQALTAVADQYDVVLIDSPPSLG 127
Cdd:cd05387   98 DVLPA------------GTVppnPSELLssprFAELLEELKEQYDYVIIDTPPVLA 141
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 8-144 5.27e-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: 49.37  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990    8 NHAGGAGKTSLARDVGYELAHGGQRVLLIDLDP-QANLTGWLGVGGIEIDQTiypvavdgaplpapvqvhGLSL-IPAHV 85
Cdd:pfam09140   7 NEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRT------------------GLSLpTPEHL 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380002990   86 DLASAEAQMLGQVGSILF--LKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIVPM 144
Cdd:pfam09140  69 NLPDNDVAEVPDGENIDDarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 11-230 9.19e-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: 42.36  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   11 GGAGKTSLARDVGYELAHGGQRVLLIDLDPqANLTGWLGVGGIEIDQTIYPVAVDGAPLPAPVQ--VHGLSLIPAHVDLA 88
Cdd:pfam06564  11 GGVGTTSILAALAWALQRLGERVLLIDLSP-DNLLRLHFNVPFEHRQGWARAELDGADWRDAALeyTPGLDLLPFGRLSV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   89 SAEAQMLGQVGSILFLKQALTAVADQYDVVLIDSPPSLGQLATLGALAADRLIV---PMPTRQKGLDALPGLNRAMGMYH 165
Cdd:pfam06564  90 EEQENLQQLQPDPGAWCRRLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLvvnPDANCHVLLHQQPLPDADHLLIN 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380002990  166 RLRPELRValyvptmhdARRLHdrEVLEQLRGYLNPMsepVPQREAVWLDSTTAGQPVGVYAPRS 230
Cdd:pfam06564 170 DFRPASQL---------QQDLL--QLWRQSQRRLLPL---VIHRDEALAEALAAKQPLGEYRPDS 220
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 11-50 1.08e-04

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: 42.30  E-value: 1.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGV 50
Cdd:cd02034    9 GGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGV 48
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
11-163 2.20e-04

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.73  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVggiEIDQTIYPVAVDGaplpapvqVHGLSL---------I 81
Cdd:COG0003   12 GGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGT---ELGNEPTEVAVPN--------LYALEIdpeaeleeyW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  82 PAHVDLASA--EAQMLGQVGSIL------FLKQALTAVA--DQYDVVLIDSPPSLGQLATLGA---LAA--DRLivpMPT 146
Cdd:COG0003   81 ERVRAPLRGllPSAGVDELAESLpgteelAALDELLELLeeGEYDVIVVDTAPTGHTLRLLSLpelLGWwlDRL---LKL 157

                        170
                 ....*....|....*..
gi 380002990 147 RQKGLDALPGLNRAMGM 163
Cdd:COG0003  158 RRKASGLGRPLAGILGL 174
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 6-250 2.69e-04

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: 41.20  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990   6 VFNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTGWLGVGGIE--IDQTIYPVAVDGAPLPAPVQVHGLSlipa 83
Cdd:cd02117    4 VVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPptIDEMLTEDGTAEELRREDLLFSGFN---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  84 HVDLASAEAQMLGQ------VGSILFLKQALTAVADQYDVVLIDsppSLGQLATLG-------ALAADRLIVPmptrQKG 150
Cdd:cd02117   80 GVDCVEAGGPEPGVgcggrgIGTMLELLEEHGLLDDDYDVVIFD---VLGDVVCGGfaaplrrGFAQKVVIVV----SEE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990 151 LDALPGLNR---AMGMYHRLRpeLRVALYVPTMHDARRlhdREVLEQLRGYLN-PMSEPVPQREAVwLDSTTAGQPVGVY 226
Cdd:cd02117  153 LMSLYAANNivkAVENYSKNG--VRLAGLVANLRDPAG---TEEIQAFAAAVGtKILAVIPRDPAV-RRAELARVTVFEH 226

                        250       260
                 ....*....|....*....|....
gi 380002990 227 APRSPVHADVIRLTSAIAQAAGLR 250
Cdd:cd02117  227 DPVSPAASEFARLAAKIADAVPPV 250
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-50 3.03e-04

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 40.92  E-value: 3.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 380002990  11 GGAGKTS----LARdvgyELAHGGQRVLLIDLDPQANLTGWLGV 50
Cdd:COG3640    9 GGVGKTTlsalLAR----YLAEKGKPVLAVDADPNANLAEALGL 48
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 7-63 7.31e-04

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.46  E-value: 7.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 380002990    7 FNHAGGAGKTSLARDVGYELAHGGQRVLLIDLDPQANLTgwlGVGGIEIDQTIYPVA 63
Cdd:TIGR04291   8 FTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVG---QVFGQTIGNKITAIA 61
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
14-142 1.23e-03

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 39.75  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  14 GKTSLARDVGYELAHGGQRVLLIDLD-------------PQANLTGWLgVGGIEIDQTIYPVAVDgaplpapvqvhGLSL 80
Cdd:PRK11519 539 GKTFVCANLAAVISQTNKRVLLIDCDmrkgythellgtnNVNGLSDIL-IGQGDITTAAKPTSIA-----------NFDL 606

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380002990  81 IP-AHVDLASAEAQMLGQVGSilFLKQAltavADQYDVVLIDSPPSLG--QLATLGALAADRLIV 142
Cdd:PRK11519 607 IPrGQVPPNPSELLMSERFAE--LVNWA----SKNYDLVLIDTPPILAvtDAAIVGRHVGTTLMV 665
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 11-142 1.82e-03

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: 38.64  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDpqanLTG-----WLGVGGIEIDQtiypvavdGAPLPAPVQVHGLSLIpahv 85
Cdd:cd02037   10 GGVGKSTVAVNLALALAKKGYKVGLLDAD----IYGpsiprLLGVEGKPLHQ--------SEEGIVPVEVGGIKVM---- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380002990  86 dlaSAeAQMLGQVGSILF--------LKQALTAVA-DQYDVVLIDSPPSLG--QLATLGALAADRLIV 142
Cdd:cd02037   74 ---SI-GFLLPEDDAVIWrgpmksgaIKQFLKDVDwGELDYLIIDLPPGTGdeHLSLVQLIPIDGAVV 137
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-44 2.13e-03

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: 38.64  E-value: 2.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 380002990  11 GGAGKTSLARDVGYELAHGGQRVLLIDLDPQANL 44
Cdd:cd02035    9 GGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL 42
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-44 2.57e-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: 38.48  E-value: 2.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 380002990   11 GGAGKTSLARDVGYELAHGGQRVLLIDLDPQANL 44
Cdd:pfam02374  10 GGVGKTTVSAATAVQLSELGKKVLLISTDPAHSL 43
 
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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