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Conserved domains on  [gi|972373122|ref|WP_059027022|]
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ParA family protein [Clostridioides difficile]

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 ...
 10-266 2.49e-41

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: 142.69  E-value: 2.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  10 FNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNENyinVD 87
Cdd:COG1192    7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDdAPLEDAIVPTEIPG---LD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  88 LIPSDIQMARFEQELSPLPAREKFLARwYMQNFntLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRGAE 167
Cdd:COG1192   83 LIPANIDLAGAEIELVSRPGRELRLKR-ALAPL--ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE-YLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122 168 LFKQLWDVDRTYFDKEDNIKSTVLVGFEKKKTQISDTFDSYLEGFNdmrDIMLDTYIRKNEFIEKALLKKLSLTDYtkiT 247
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFG---DKVLDTVIPRSVALAEAPSAGKPVFEY---D 232

                        250
                 ....*....|....*....
gi 972373122 248 KEHFSRQEFTNMLEELKRK 266
Cdd:COG1192  233 PKSKGAKAYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 10-266 2.49e-41

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: 142.69  E-value: 2.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  10 FNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNENyinVD 87
Cdd:COG1192    7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDdAPLEDAIVPTEIPG---LD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  88 LIPSDIQMARFEQELSPLPAREKFLARwYMQNFntLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRGAE 167
Cdd:COG1192   83 LIPANIDLAGAEIELVSRPGRELRLKR-ALAPL--ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE-YLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122 168 LFKQLWDVDRTYFDKEDNIKSTVLVGFEKKKTQISDTFDSYLEGFNdmrDIMLDTYIRKNEFIEKALLKKLSLTDYtkiT 247
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFG---DKVLDTVIPRSVALAEAPSAGKPVFEY---D 232

                        250
                 ....*....|....*....
gi 972373122 248 KEHFSRQEFTNMLEELKRK 266
Cdd:COG1192  233 PKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 4-169 4.82e-30

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: 110.75  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122    4 TKLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNE 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLgIDKNNVEKTIYELLIGeCNIEEAIIKTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   82 NyinVDLIPSDIQMARFEQELSPLPAREKFLARwYMQNFNtlSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnIS 161
Cdd:pfam13614  80 N---LDLIPSNIDLAGAEIELIGIENRENILKE-ALEPVK--DNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE-YY 152


                  ....*...
gi 972373122  162 SLRGAELF 169
Cdd:pfam13614 153 ALEGLSQL 160
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-179 2.60e-13

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: 65.25  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   5 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVyeinhndnttldilkgisandaivkspnenyi 84
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  85 nvdlipsdiqmarfeqelsplparekflarwymqnfntlseYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKNIsSLR 164
Cdd:cd02042   48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF-DLD 85

                        170
                 ....*....|....*.
gi 972373122 165 GA-ELFKQLWDVDRTY 179
Cdd:cd02042   86 GLaKLLDTLEELKKQL 101
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 13-195 3.30e-10

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 59.61  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  13 KGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQY---VYEIN-HNDNTTLDILKGiSANDAIVKSPNENYINVDL 88
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwVPDLHiHAEDTLLPFYLG-EKDDATYAIKPTCWPGLDI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  89 IPSDIQMARFEQELSP------LPAREKFLARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQdkniss 162
Cdd:PRK13705 194 IPSCLALHRIETELMGkfdegkLPTDPHLMLRLAIE--TVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP------ 265

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 972373122 163 lrgAELFK-----QLWDVDRtyfdkeDNIKSTVLVGFE 195
Cdd:PRK13705 266 ---AELFDytsalQFFDMLR------DLLKNVDLKGFE 294
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 11-155 3.95e-06

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: 47.28  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   11 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQ---YVYEINHNDNTTL-------DILKGISanDAIVKSpn 80
Cdd:TIGR03453 111 NFKGGSGKTTTAAHLAQYLAL-RGYRVLAIDLDPQASLSAlfgYQPEFDVGENETLygairydDERRPIS--EIIRKT-- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   81 eNYINVDLIPSDIQMARFEQElSPL------PAREKFLARWYMqnfnTLSE----YDYIICDLSPRYDLTAKNVLFLADS 150
Cdd:TIGR03453 186 -YFPGLDLVPGNLELMEFEHE-TPRalsrgqGGDTIFFARVGE----ALAEveddYDVVVIDCPPQLGFLTLSALCAATG 259


                  ....*
gi 972373122  151 IIIPI 155
Cdd:TIGR03453 260 VLITV 264
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 10-266 2.49e-41

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: 142.69  E-value: 2.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  10 FNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNENyinVD 87
Cdd:COG1192    7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDdAPLEDAIVPTEIPG---LD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  88 LIPSDIQMARFEQELSPLPAREKFLARwYMQNFntLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRGAE 167
Cdd:COG1192   83 LIPANIDLAGAEIELVSRPGRELRLKR-ALAPL--ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE-YLSLEGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122 168 LFKQLWDVDRTYFDKEDNIKSTVLVGFEKKKTQISDTFDSYLEGFNdmrDIMLDTYIRKNEFIEKALLKKLSLTDYtkiT 247
Cdd:COG1192  159 QLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFG---DKVLDTVIPRSVALAEAPSAGKPVFEY---D 232

                        250
                 ....*....|....*....
gi 972373122 248 KEHFSRQEFTNMLEELKRK 266
Cdd:COG1192  233 PKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 4-169 4.82e-30

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: 110.75  E-value: 4.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122    4 TKLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYV-YEINHNDNTTLDILKG-ISANDAIVKSPNE 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLgIDKNNVEKTIYELLIGeCNIEEAIIKTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   82 NyinVDLIPSDIQMARFEQELSPLPAREKFLARwYMQNFNtlSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnIS 161
Cdd:pfam13614  80 N---LDLIPSNIDLAGAEIELIGIENRENILKE-ALEPVK--DNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE-YY 152


                  ....*...
gi 972373122  162 SLRGAELF 169
Cdd:pfam13614 153 ALEGLSQL 160
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 11-191 2.14e-18

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: 81.24  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   11 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQY---VYEINHNDNTTLDILKG-ISANDAIVKsPNENYINV 86
Cdd:pfam01656   5 GTKGGVGKTTLAANLARALAR-RGLRVLLIDLDPQSNNSSVeglEGDIAPALQALAEGLKGrVNLDPILLK-EKSDEGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   87 DLIPSDIQMARFEQELSPLPAREKFLArwymqNFNTLSE-YDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKnISSLRG 165
Cdd:pfam01656  83 DLIPGNIDLEKFEKELLGPRKEERLRE-----ALEALKEdYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE-VILVED 156

                         170       180
                  ....*....|....*....|....*..
gi 972373122  166 AELFKQLW-DVDRTYFDKEDNIKSTVL 191
Cdd:pfam01656 157 AKRLGGVIaALVGGYALLGLKIIGVVL 183
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-179 2.60e-13

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: 65.25  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   5 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVyeinhndnttldilkgisandaivkspnenyi 84
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  85 nvdlipsdiqmarfeqelsplparekflarwymqnfntlseYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDKNIsSLR 164
Cdd:cd02042   48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF-DLD 85

                        170
                 ....*....|....*.
gi 972373122 165 GA-ELFKQLWDVDRTY 179
Cdd:cd02042   86 GLaKLLDTLEELKKQL 101
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 13-195 3.30e-10

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 59.61  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  13 KGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQY---VYEIN-HNDNTTLDILKGiSANDAIVKSPNENYINVDL 88
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwVPDLHiHAEDTLLPFYLG-EKDDATYAIKPTCWPGLDI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  89 IPSDIQMARFEQELSP------LPAREKFLARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQdkniss 162
Cdd:PRK13705 194 IPSCLALHRIETELMGkfdegkLPTDPHLMLRLAIE--TVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP------ 265

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 972373122 163 lrgAELFK-----QLWDVDRtyfdkeDNIKSTVLVGFE 195
Cdd:PRK13705 266 ---AELFDytsalQFFDMLR------DLLKNVDLKGFE 294
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 20-166 4.99e-10

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: 57.98  E-value: 4.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  20 TTSIMTAYELAKdKDKKILLWDLDVQ-ANLTQYvyeINHNDNTTL-DILKG-ISANDAIVKSPNenyiNVDLIPSDIQMA 96
Cdd:COG0455    1 TVAVNLAAALAR-LGKRVLLVDADLGlANLDVL---LGLEPKATLaDVLAGeADLEDAIVQGPG----GLDVLPGGSGPA 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972373122  97 RFEqELSPlparekflARWYMQNFNTLSE-YDYIICDLSPryDLTAKNVLFL--ADSIIIPIQDkNISSLRGA 166
Cdd:COG0455   73 ELA-ELDP--------EERLIRVLEELERfYDVVLVDTGA--GISDSVLLFLaaADEVVVVTTP-EPTSITDA 133
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 3-154 9.31e-10

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 58.48  E-value: 9.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   3 NTKLLTYFNIKGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQANLTQ---YVYEIN-HNDNTTLDILKGISANDAIVKS 78
Cdd:PHA02519 105 NPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMyhgYVPDLHiHADDTLLPFYLGERDNAEYAIK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  79 PNeNYINVDLIPSDIQMARFEQELSPLPAREKF------LARWYMQnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSII 152
Cdd:PHA02519 185 PT-CWPGLDIIPSCLALHRIETDLMQYHDAGKLphpphlMLRAAIE--SVWDNYDIIVIDSAPNLGTGTINVVCAADVIV 261


                 ..
gi 972373122 153 IP 154
Cdd:PHA02519 262 VA 263
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 13-153 9.59e-08

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: 51.42  E-value: 9.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  13 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANLtqyvyEI---NHNDNTTLDILKG-ISANDAIVKSPNenyiNVD 87
Cdd:cd02038    9 KGGVGKTNVSANLALALSK-LGKRVLLLDADLgLANL-----DIllgLAPKKTLGDVLKGrVSLEDIIVEGPE----GLD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972373122  88 LIPSDIQMarfeQELSPLPA--REKFLarwymQNFNTL-SEYDYIICDLSPRydlTAKNVLFL---ADSIII 153
Cdd:cd02038   79 IIPGGSGM----EELANLDPeqKAKLI-----EELSSLeSNYDYLLIDTGAG---ISRNVLDFllaADEVIV 138
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 5-172 1.01e-07

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: 52.04  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   5 KLLTYFNIKGGIYKTTTSIMTAYELAKDKDKKILLWDLDVQA-NLTQYVyeiNHNDNTTL-DILKGISAND------AIV 76
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFgDVALYL---DLEPRRGLaDALRNPDRLDetlldrALT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  77 KSPNenyiNVDLIPSDIQMARFEqELSPLPARE--KFLARwymqnfntlsEYDYIICDLSPRYDLTAKNVLFLADSIIIP 154
Cdd:COG4963  180 RHSS----GLSVLAAPADLERAE-EVSPEAVERllDLLRR----------HFDYVVVDLPRGLNPWTLAALEAADEVVLV 244

                        170       180
                 ....*....|....*....|..
gi 972373122 155 IqDKNISSLRGA----ELFKQL 172
Cdd:COG4963  245 T-EPDLPSLRNAkrllDLLREL 265
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 11-155 3.95e-06

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: 47.28  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   11 NIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQ---YVYEINHNDNTTL-------DILKGISanDAIVKSpn 80
Cdd:TIGR03453 111 NFKGGSGKTTTAAHLAQYLAL-RGYRVLAIDLDPQASLSAlfgYQPEFDVGENETLygairydDERRPIS--EIIRKT-- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   81 eNYINVDLIPSDIQMARFEQElSPL------PAREKFLARWYMqnfnTLSE----YDYIICDLSPRYDLTAKNVLFLADS 150
Cdd:TIGR03453 186 -YFPGLDLVPGNLELMEFEHE-TPRalsrgqGGDTIFFARVGE----ALAEveddYDVVVIDCPPQLGFLTLSALCAATG 259


                  ....*
gi 972373122  151 IIIPI 155
Cdd:TIGR03453 260 VLITV 264
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-263 1.74e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 45.44  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   5 KLLTYFNIKGGIYKTTTSIMTAYELAKdKDKKILLWDLDVQANLTQYVYEINHND---NTTLdiLKGISANDAivKSPNE 81
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLAL-QGYRVLAVDLDPQASLSALLGVLPETDvgaNETL--YAAIRYDDT--RRPLR 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  82 NYI------NVDLIPSDIQMARFE----QELSPLPAREKFLARWYMQNFNTLSE-YDYIICDLSPRYDLTAKNVLFLADS 150
Cdd:PRK13869 197 DVIrptyfdGLHLVPGNLELMEFEhttpKALSDKGTRDGLFFTRVAQAFDEVADdYDVVVIDCPPQLGFLTLSGLCAATS 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122 151 IIIPI--QDKNISSLRGAELF-KQLWDVDRtyfDKEDNIK----STVLVGFEKK---KTQISDTfdsylegfndMRDiML 220
Cdd:PRK13869 277 MVITVhpQMLDIASMSQFLLMtRDLLGVVK---EAGGNLQydfiRYLLTRYEPQdapQTKVAAL----------LRN-MF 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 972373122 221 DTYIRKNEFIEKALLKKLSLTDYT--KITKEHFSRQEFTNMLEEL 263
Cdd:PRK13869 343 EDHVLTNPMVKSAAVSDAGLTKQTlyEIGRENLTRSTYDRAMESL 387
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 13-135 4.36e-05

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: 44.02  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  13 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANLTQYvYEInHNDNTTLDILKG-ISANDAIVKSPNENyinVDLIP 90
Cdd:COG0489  101 KGGEGKSTVAANLALALAQ-SGKRVLLIDADLrGPSLHRM-LGL-ENRPGLSDVLAGeASLEDVIQPTEVEG---LDVLP 174

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 972373122  91 SDiQMARFEQELSPLPAREKFLARWymqnfntLSEYDYIICDLSP 135
Cdd:COG0489  175 AG-PLPPNPSELLASKRLKQLLEEL-------RGRYDYVIIDTPP 211
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 13-166 1.41e-04

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: 42.19  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  13 KGGIYKTTTSIMTAYELAKdKDKKILLWDLDV-QANltqyvyeinhndnttLDILKGIsandaivkspnENYINVDLIPS 91
Cdd:cd02036    9 KGGVGKTTTTANLGVALAK-LGKKVLLIDADIgLRN---------------LDLILGL-----------ENRIVYTLVDV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  92 DIQMARFEQ---------ELSPLPA---REKFLARwyMQNFNTL-----SEYDYIICDLSPRYDLTAKNVLFLADSIIIp 154
Cdd:cd02036   62 LEGECRLEQalikdkrweNLYLLPAsqtRDKDALT--PEKLEELvkelkDSFDFILIDSPAGIESGFINAIAPADEAII- 138

                        170
                 ....*....|..
gi 972373122 155 IQDKNISSLRGA 166
Cdd:cd02036  139 VTNPEISSVRDA 150
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 4-175 4.48e-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: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   4 TKLLTYFNIKGGIYKTTTSIMTAYELAkDKDKKILLWDLD------------VQANLTQYVYEINHNDNTTLDILkgisa 71
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLA-EKGKKTLYLNMErlqstdvffgasGRYLMSDHLYTLKSRKANLADKL----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  72 nDAIVKSPNE--NYINVDLIPSDIQMARFEQElsplpareKFLArwymQNFNTLSEYDYIICDLSPRYDLTAKNVLFLAD 149
Cdd:cd17869   77 -ESCVKQHESgvYYFSPFKSALDILEIKKDDI--------LHMI----TKLVEAHAYDYIIMDLSFEFSSTVCKLLQASH 143

                        170       180
                 ....*....|....*....|....*.
gi 972373122 150 SIIIPIQDKNISSLRGAELFKQLWDV 175
Cdd:cd17869  144 NNVVIALQDANSSYKLNKFLRALEDL 169
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 18-153 4.88e-04

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: 40.25  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122  18 KTTTSIMTAYELAKDkDKKILLWDLDV-QANLTQYVYEinHNDNTTLDILKGISANDAIVKSPNENyiNVDLIPSdiqmA 96
Cdd:cd05387   33 KSTVAANLAVALAQS-GKRVLLIDADLrRPSLHRLLGL--PNEPGLSEVLSGQASLEDVIQSTNIP--NLDVLPA----G 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 972373122  97 RFEQELSPLPAREKFLARwymqnFNTLSE-YDYIICDLSPrydltaknVLFLADSIII 153
Cdd:cd05387  104 TVPPNPSELLSSPRFAEL-----LEELKEqYDYVIIDTPP--------VLAVADALIL 148
PHA02518 PHA02518
ParA-like protein; Provisional
 5-158 5.41e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.22  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122   5 KLLTYFNIKGGIYKTTTSIMTAYELAKDkDKKILLWDLDVQANLTQYVYEINHNDnttldilkgisandaivkspnenyi 84
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHAD-GHKVLLVDLDPQGSSTDWAEAREEGE------------------------- 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972373122  85 nvDLIPSdIQMARfeQELSPLParekflarwymqnfNTLSEYDYIICDLSPRYDLTAKNVLFLADSIIIPIQDK 158
Cdd:PHA02518  55 --PLIPV-VRMGK--SIRADLP--------------KVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPS 109
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-135 1.80e-03

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: 39.30  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972373122    9 YFNIKGGIYKTTTSIMTAYELAkDKDKKILLWDLDVQANLTQYVYEINHNDNTTLDILKGISANDAIVKSPNENYIN--V 86
Cdd:TIGR04291   7 FFTGKGGVGKTSIACATAINLA-DQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYRAriV 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 972373122   87 D----LIPSDIqMARFEQELS-----PLPAREKFLArwYMQNFNTLSEYDYIICDLSP 135
Cdd:TIGR04291  86 DpvrgVLPDDV-VSSIEEQLSgacttEIAAFDEFTG--LLTDAELTQDFDHIIFDTAP 140
 
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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