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Conserved domains on  [gi|971760194|ref|YP_009213499|]
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ParA-like partition protein [Rhodobacter phage RcRhea]

Protein Classification

ParA family protein( domain architecture ID 10114212)

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, and to BcsQ, an essential component of the cellulose biosynthesis apparatus

CATH:  3.40.50.300
Gene Ontology:  GO:0005524
PubMed:  28373206|22672910|17161598|2149583
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-156 1.72e-20

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: 82.97  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWAlrrdemgtdpeiqvqkyrdagkavkdaegWDL 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL-----------------------------YDY 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  81 MILDGPAHAERSGLVMARAADLVLVPTGYSVDDLDPQIRVAFDLESAGV----DPDRIKLAFCRVNGSAKADQSARDFVQ 156
Cdd:cd02042   51 ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKqlnpPLLILGILLTRVDPRTKLAREVLEELK 130
 
Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-156 1.72e-20

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: 82.97  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWAlrrdemgtdpeiqvqkyrdagkavkdaegWDL 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL-----------------------------YDY 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  81 MILDGPAHAERSGLVMARAADLVLVPTGYSVDDLDPQIRVAFDLESAGV----DPDRIKLAFCRVNGSAKADQSARDFVQ 156
Cdd:cd02042   51 ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKqlnpPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
2-201 2.50e-19

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 81.83  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWALRRDEMGTDPEIQVQKYRDAGKAVKDAEGWDLM 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-QGSALDWAAAREDERPFPVVGLARPTLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  82 ILDGPAHAERSGLVMARAADLVLVPTGYSVDDLDPQIRVAFDLESAGVDPDRIKLAFCrVNGSAKADQSARDfVQRA--- 158
Cdd:NF041546  80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFV-LNRAIARTALGRE-VAEAlae 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 971760194 159 -GLKALQGAIRElpciRLAHAA----GRTAAETGHKAVDA-ESKALAAE 201
Cdd:NF041546 158 yGLPVLKTRIGQ----RVAFAEsaaeGLTVFEAEPDGKAArEIRALAKE 202
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 3.94e-13

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: 66.04  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWaLRRDEMGTDP---------------------- 58
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDP-QGNLTSG-LGLDPDDLDPtlydlllddapledaivpteip 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  59 --------------EIQVQKYRDAGKAVKDA-----EGWDLMILDGPAHaeRSGLVMA--RAADLVLVPT---GYSVDDL 114
Cdd:COG1192   80 gldlipanidlagaEIELVSRPGRELRLKRAlaplaDDYDYILIDCPPS--LGLLTLNalAAADSVLIPVqpeYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194 115 DpQIRVAFDLESAGVDPDRIKLA--FCRVNGSAKADQSARDFVQRA-GLKALQGAIRELPCIRLAHAAGRTAAETGHKAV 191
Cdd:COG1192  158 A-QLLETIEEVREDLNPKLEILGilLTMVDPRTRLSREVLEELREEfGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236

                        250
                 ....*....|....*.
gi 971760194 192 DAES-KALAAEVSRIL 206
Cdd:COG1192  237 GAKAyRALAEELLERL 252
PHA02518 PHA02518
ParA-like protein; Provisional
 1-107 6.21e-13

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 64.87  E-value: 6.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWALRRDEmgTDPEIQVQKYrdaGKAV-----KDA 75
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDP-QGSSTDWAEAREE--GEPLIPVVRM---GKSIradlpKVA 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 971760194  76 EGWDLMILDGPAHAERSGLVMARAADLVLVPT 107
Cdd:PHA02518  75 SGYDYVVVDGAPQDSELARAALRIADMVLIPV 106
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-138 2.73e-08

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 52.35  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194    3 LALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDP--------------AQGTSTKWALRRDEMGTDPEI-------- 60
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPqsnnssveglegdiAPALQALAEGLKGRVNLDPILlkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   61 ---------------QVQKYRDAGKAVKDA-----EGWDLMILDGPAHAERSGLVMARAADLVLVPTG---YSVDDLDPQ 117
Cdd:pfam01656  81 gldlipgnidlekfeKELLGPRKEERLREAlealkEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEpevILVEDAKRL 160

                         170       180
                  ....*....|....*....|.
gi 971760194  118 IRVAFDLEsAGVDPDRIKLAF 138
Cdd:pfam01656 161 GGVIAALV-GGYALLGLKIIG 180
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-66 1.16e-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: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971760194    9 KGGVGKSTLARVLAAEFTGAGWRVKIGDLDPAQGTSTKWALRRDEMGT---DPEIQVQKYR 66
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVsriDPKQETERYR 389
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 11-92 7.29e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.81  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194    11 GVGKSTLARVLAAEFTGAGWRVKIGDLDPAQGTSTKWALRRDEMGTDPEIQVQKYRDAGKAVKDAEGWDLMILDGPAHAE 90
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLL 91


                   ..
gi 971760194    91 RS 92
Cdd:smart00382  92 DA 93
 
Name Accession Description Interval E-value
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-156 1.72e-20

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: 82.97  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWAlrrdemgtdpeiqvqkyrdagkavkdaegWDL 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL-----------------------------YDY 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  81 MILDGPAHAERSGLVMARAADLVLVPTGYSVDDLDPQIRVAFDLESAGV----DPDRIKLAFCRVNGSAKADQSARDFVQ 156
Cdd:cd02042   51 ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKqlnpPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
2-201 2.50e-19

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 81.83  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWALRRDEMGTDPEIQVQKYRDAGKAVKDAEGWDLM 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-QGSALDWAAAREDERPFPVVGLARPTLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  82 ILDGPAHAERSGLVMARAADLVLVPTGYSVDDLDPQIRVAFDLESAGVDPDRIKLAFCrVNGSAKADQSARDfVQRA--- 158
Cdd:NF041546  80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFV-LNRAIARTALGRE-VAEAlae 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 971760194 159 -GLKALQGAIRElpciRLAHAA----GRTAAETGHKAVDA-ESKALAAE 201
Cdd:NF041546 158 yGLPVLKTRIGQ----RVAFAEsaaeGLTVFEAEPDGKAArEIRALAKE 202
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-206 3.94e-13

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: 66.04  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWaLRRDEMGTDP---------------------- 58
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDP-QGNLTSG-LGLDPDDLDPtlydlllddapledaivpteip 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194  59 --------------EIQVQKYRDAGKAVKDA-----EGWDLMILDGPAHaeRSGLVMA--RAADLVLVPT---GYSVDDL 114
Cdd:COG1192   80 gldlipanidlagaEIELVSRPGRELRLKRAlaplaDDYDYILIDCPPS--LGLLTLNalAAADSVLIPVqpeYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194 115 DpQIRVAFDLESAGVDPDRIKLA--FCRVNGSAKADQSARDFVQRA-GLKALQGAIRELPCIRLAHAAGRTAAETGHKAV 191
Cdd:COG1192  158 A-QLLETIEEVREDLNPKLEILGilLTMVDPRTRLSREVLEELREEfGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236

                        250
                 ....*....|....*.
gi 971760194 192 DAES-KALAAEVSRIL 206
Cdd:COG1192  237 GAKAyRALAEELLERL 252
PHA02518 PHA02518
ParA-like protein; Provisional
 1-107 6.21e-13

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 64.87  E-value: 6.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTSTKWALRRDEmgTDPEIQVQKYrdaGKAV-----KDA 75
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDP-QGSSTDWAEAREE--GEPLIPVVRM---GKSIradlpKVA 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 971760194  76 EGWDLMILDGPAHAERSGLVMARAADLVLVPT 107
Cdd:PHA02518  75 SGYDYVVVDGAPQDSELARAALRIADMVLIPV 106
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-138 2.73e-08

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 52.35  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194    3 LALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDP--------------AQGTSTKWALRRDEMGTDPEI-------- 60
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPqsnnssveglegdiAPALQALAEGLKGRVNLDPILlkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194   61 ---------------QVQKYRDAGKAVKDA-----EGWDLMILDGPAHAERSGLVMARAADLVLVPTG---YSVDDLDPQ 117
Cdd:pfam01656  81 gldlipgnidlekfeKELLGPRKEERLREAlealkEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEpevILVEDAKRL 160

                         170       180
                  ....*....|....*....|.
gi 971760194  118 IRVAFDLEsAGVDPDRIKLAF 138
Cdd:pfam01656 161 GGVIAALV-GGYALLGLKIIG 180
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-45 1.82e-06

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: 46.42  E-value: 1.82e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 971760194    2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPaQGTST 45
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP-QGNAT 45
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-38 1.94e-05

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: 44.03  E-value: 1.94e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 971760194   2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLD 38
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 11-42 1.77e-04

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 40.70  E-value: 1.77e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 971760194   11 GVGKSTLARVLAAEFTGAGWRVKIGDLDPAQG 42
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDVGQS 35
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-38 2.03e-04

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 40.90  E-value: 2.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 971760194    2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLD 38
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-39 8.17e-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: 39.22  E-value: 8.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 971760194   1 MILAlVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDP 39
Cdd:cd02034    1 MKIA-VAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-66 1.16e-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: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971760194    9 KGGVGKSTLARVLAAEFTGAGWRVKIGDLDPAQGTSTKWALRRDEMGT---DPEIQVQKYR 66
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVsriDPKQETERYR 389
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-38 1.60e-03

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 37.03  E-value: 1.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 971760194   1 MILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLD 38
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-115 2.60e-03

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: 37.82  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194    2 ILALVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPAQGTSTK-------WALRR-------DEMGTDPEIQVQKYRD 67
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRyfenrsaTADRTglslptpEHLNLPDNDVAEVPDG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 971760194   68 AG-------KAVKDAE-GWDLMILDGPAHAERSGLVMARAADLVLVPTGYSVDDLD 115
Cdd:pfam09140  82 ENiddarleEAFADLEaRCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFD 137
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-42 2.86e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 37.84  E-value: 2.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 971760194   1 MILAlVSQKGGVGKSTLARVLAAEFTGAGWRVKIGDLDPAQG 42
Cdd:COG3640    1 MKIA-VAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-38 4.61e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 37.33  E-value: 4.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 971760194   2 ILALVSQKGGVGKST----LARVLAAEftgaGWRVKIGDLD 38
Cdd:PRK11670 109 IIAVSSGKGGVGKSStavnLALALAAE----GAKVGILDAD 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 11-92 7.29e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.81  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971760194    11 GVGKSTLARVLAAEFTGAGWRVKIGDLDPAQGTSTKWALRRDEMGTDPEIQVQKYRDAGKAVKDAEGWDLMILDGPAHAE 90
Cdd:smart00382  12 GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLL 91


                   ..
gi 971760194    91 RS 92
Cdd:smart00382  92 DA 93
 
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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