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Conserved domains on  [gi|556394170|ref|WP_023304044|]
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MULTISPECIES: ParA family plasmid-partitioning AAA ATPase [Enterobacteriaceae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
2-205 7.37e-53

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 168.11  E-value: 7.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDlPHIPVTGATG-NIKAMLKEHEKSYDYV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDE-RPFPVVGLARpTLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNENIRGYLVLNMTPTNmfVNEANQAAEVLKD 160
Cdd:NF041546  80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIAR--TALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 556394170 161 YPeMRLANSRVCDRKAHRDAWAESMTIFETQ-NDKAQQEIEALVKE 205
Cdd:NF041546 158 YG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
2-205 7.37e-53

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 168.11  E-value: 7.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDlPHIPVTGATG-NIKAMLKEHEKSYDYV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDE-RPFPVVGLARpTLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNENIRGYLVLNMTPTNmfVNEANQAAEVLKD 160
Cdd:NF041546  80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIAR--TALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 556394170 161 YPeMRLANSRVCDRKAHRDAWAESMTIFETQ-NDKAQQEIEALVKE 205
Cdd:NF041546 158 YG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-208 2.28e-43

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 144.61  E-value: 2.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPHIPVTGATGNIKAMLKEHEKSYDYV 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNENIRGYLVLNMTPTNMFVNEANqAAEVLKD 160
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYRE-ARKALAG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 556394170 161 YpEMRLANSRVCDRKAHRDAWAESMTIFETQND-KAQQEIEALVKEVIL 208
Cdd:PHA02518 160 Y-GLPILRNGTTQRVAYADAAEAGGSVLELPEDdKAAEEIIQLVKELFR 207
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-159 2.44e-37

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: 126.12  E-value: 2.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYnnrpedlphipvtgatgnikamlkeheksYDYV 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-----------------------------YDYI 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNEN--IRGYLVLNMTPTNMfvNEANQAAEVL 158
Cdd:cd02042   52 LIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRT--KLAREVLEEL 129


                 .
gi 556394170 159 K 159
Cdd:cd02042  130 K 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-207 3.71e-27

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: 103.78  E-value: 3.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPH------------------------ 56
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPtlydlllddapledaivpteipgl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  57 --IP--------------VTGATGNIKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTC 120
Cdd:COG1192   82 dlIPanidlagaeielvsRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170 121 SVFTA-AKDFNENIR-GYLVLNMTPTNmfVNEANQAAEVLKDYPEMRLANSRVCDRKAHRDAWAESMTIFETQ-NDKAQQ 197
Cdd:COG1192  162 ETIEEvREDLNPKLEiLGILLTMVDPR--TRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDpKSKGAK 239

                        250
                 ....*....|
gi 556394170 198 EIEALVKEVI 207
Cdd:COG1192  240 AYRALAEELL 249
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-116 4.71e-18

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: 79.81  E-value: 4.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD-DQKSVLTWYNNRPE---------------DLPHIPVTGATGN 65
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDlRQRTFHRYFENRSAtadrtglslptpehlNLPDNDVAEVPDG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556394170   66 -------IKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVV 116
Cdd:pfam09140  82 eniddarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLL 139
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-89 5.06e-06

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 45.79  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD------------DQKSVLTWYN---------------NRPEDL 54
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglrnldlllglENRIVYTLVDvvegecrlqqalikdKRLKNL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 556394170   55 PHIPVTG-------ATGNIKAMLKEHEKSYDYVIADC-AGRDS 89
Cdd:TIGR01968  83 YLLPASQtrdkdavTPEQMKKLVNELKEEFDYVIIDCpAGIES 125
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2-83 1.56e-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: 37.74  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170     2 IIVLGSQkgGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPHIPVTGATGNIKAMLKEHEKS-YDYV 80
Cdd:smart00382   5 ILIVGPP--GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLkPDVL 82


                   ...
gi 556394170    81 IAD 83
Cdd:smart00382  83 ILD 85
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
2-205 7.37e-53

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 168.11  E-value: 7.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDlPHIPVTGATG-NIKAMLKEHEKSYDYV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDE-RPFPVVGLARpTLHRELPSLARDYDFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNENIRGYLVLNMTPTNmfVNEANQAAEVLKD 160
Cdd:NF041546  80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIAR--TALGREVAEALAE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 556394170 161 YPeMRLANSRVCDRKAHRDAWAESMTIFETQ-NDKAQQEIEALVKE 205
Cdd:NF041546 158 YG-LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-208 2.28e-43

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 144.61  E-value: 2.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPHIPVTGATGNIKAMLKEHEKSYDYV 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIPVVRMGKSIRADLPKVASGYDYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNENIRGYLVLNMTPTNMFVNEANqAAEVLKD 160
Cdd:PHA02518  81 VVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYRE-ARKALAG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 556394170 161 YpEMRLANSRVCDRKAHRDAWAESMTIFETQND-KAQQEIEALVKEVIL 208
Cdd:PHA02518 160 Y-GLPILRNGTTQRVAYADAAEAGGSVLELPEDdKAAEEIIQLVKELFR 207
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-159 2.44e-37

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: 126.12  E-value: 2.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYnnrpedlphipvtgatgnikamlkeheksYDYV 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-----------------------------YDYI 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  81 IADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTCSVFTAAKDFNEN--IRGYLVLNMTPTNMfvNEANQAAEVL 158
Cdd:cd02042   52 LIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRT--KLAREVLEEL 129


                 .
gi 556394170 159 K 159
Cdd:cd02042  130 K 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-207 3.71e-27

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: 103.78  E-value: 3.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPH------------------------ 56
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPtlydlllddapledaivpteipgl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  57 --IP--------------VTGATGNIKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVVPHTC 120
Cdd:COG1192   82 dlIPanidlagaeielvsRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170 121 SVFTA-AKDFNENIR-GYLVLNMTPTNmfVNEANQAAEVLKDYPEMRLANSRVCDRKAHRDAWAESMTIFETQ-NDKAQQ 197
Cdd:COG1192  162 ETIEEvREDLNPKLEiLGILLTMVDPR--TRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDpKSKGAK 239

                        250
                 ....*....|
gi 556394170 198 EIEALVKEVI 207
Cdd:COG1192  240 AYRALAEELL 249
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-116 4.71e-18

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: 79.81  E-value: 4.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD-DQKSVLTWYNNRPE---------------DLPHIPVTGATGN 65
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDlRQRTFHRYFENRSAtadrtglslptpehlNLPDNDVAEVPDG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556394170   66 -------IKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQMDLDVV 116
Cdd:pfam09140  82 eniddarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLL 139
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-162 2.05e-16

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: 74.69  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    3 IVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVL--------------TWYNNRPEDL--------PHIPVT 60
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsveglegdiapalqALAEGLKGRVnldpillkEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   61 G---------------------ATGNIKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQ---MDLDVV 116
Cdd:pfam01656  81 GldlipgnidlekfekellgprKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVilvEDAKRL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 556394170  117 PHTCS-VFTAAKDFNENIRGYlVLNM-TPTNMFVNEANQAAEVLKDYP 162
Cdd:pfam01656 161 GGVIAaLVGGYALLGLKIIGV-VLNKvDGDNHGKLLKEALEELLRGLP 207
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-38 4.24e-11

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: 59.82  E-value: 4.24e-11
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-114 4.72e-11

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: 59.13  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQ------------KSVLTWYN-----NRPED----------- 53
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgnatsglgidknNVEKTIYElligeCNIEEaiiktvienld 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556394170   54 -LP-HIPVTGATGN----------IKAMLKEHEKSYDYVIADCAGRDSAEMRSGLMAADVFISPLRPSQMDLD 114
Cdd:pfam13614  83 lIPsNIDLAGAEIEligienreniLKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALE 155
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-38 1.10e-09

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: 56.31  E-value: 1.10e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-145 1.19e-08

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: 53.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWY---NNRP-------------EDLPHIPVTG---- 61
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMlglENRPglsdvlageasleDVIQPTEVEGldvl 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  62 -------------ATGNIKAMLKEHEKSYDYVIADCA-GRDSAEMRSGLMAAD--VFISplRPSQMDLDVVPHTCSVFTA 125
Cdd:COG0489  174 pagplppnpsellASKRLKQLLEELRGRYDYVIIDTPpGLGVADATLLASLVDgvLLVV--RPGKTALDDVRKALEMLEK 251

                        170       180
                 ....*....|....*....|
gi 556394170 126 AkdfNENIRGyLVLNMTPTN 145
Cdd:COG0489  252 A---GVPVLG-VVLNMVCPK 267
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-39 1.95e-08

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: 50.51  E-value: 1.95e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADD 39
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-174 2.25e-07

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: 49.49  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD-------------DQKSVLTWYNNR----------PEDLPHIP 58
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRvslediivegPEGLDIIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  59 vtGATG-----NIKAM--------LKEHEKSYDYVIADCAGRDSAEMRSGLMAAD---VFISPLRPSQMDldvvPHTCSV 122
Cdd:cd02038   82 --GGSGmeelaNLDPEqkaklieeLSSLESNYDYLLIDTGAGISRNVLDFLLAADeviVVTTPEPTSITD----AYALIK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556394170 123 FTAAKDFNENIRgyLVLNMTPTnmfVNEANQAAEVLKdypemrlansRVCDR 174
Cdd:cd02038  156 VLSRRGGKKNFR--LIVNMARS---PKEGRATFERLK----------KVAKR 192
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-38 4.53e-07

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 48.90  E-value: 4.53e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:COG2894    4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 1-207 5.80e-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: 48.96  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   1 MIIVLGSqKGGVGKSTLAVSIAAYLM-SLGNRVIIVDAD----------DQKSVLTWYN--------------------- 48
Cdd:COG4963  104 VIAVVGA-KGGVGATTLAVNLAWALArESGRRVLLVDLDlqfgdvalylDLEPRRGLADalrnpdrldetlldraltrhs 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  49 ---------NRPEDLPHIPvTGATGNIKAMLKEHeksYDYVIADCAGRDSAEMRSGLMAADVFISPlrpsqMDLDVVphT 119
Cdd:COG4963  183 sglsvlaapADLERAEEVS-PEAVERLLDLLRRH---FDYVVVDLPRGLNPWTLAALEAADEVVLV-----TEPDLP--S 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170 120 CSVFTAAKDFNENIRG-----YLVLNMTPTNMFVNeANQAAEVLKDYPEMRLANsrvcDRKAHRDAWAESMTIFETQ-ND 193
Cdd:COG4963  252 LRNAKRLLDLLRELGLpddkvRLVLNRVPKRGEIS-AKDIEEALGLPVAAVLPN----DPKAVAEAANQGRPLAEVApKS 326

                        250
                 ....*....|....
gi 556394170 194 KAQQEIEALVKEVI 207
Cdd:COG4963  327 PLAKAIRKLAARLT 340
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-38 2.63e-06

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: 46.43  E-value: 2.63e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-38 2.79e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 46.31  E-value: 2.79e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 556394170   1 MIIVLgSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:COG3640    1 MKIAV-AGKGGVGKTTLSALLARYLAEKGKPVLAVDAD 37
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-38 3.20e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 46.57  E-value: 3.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-35 4.44e-06

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: 45.96  E-value: 4.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 556394170   2 IIVLGsqKGGVGKSTLAVSIAAYLMSLGNRVIIV 35
Cdd:cd02035    3 IFFGG--KGGVGKTTIAAATAVRLAEQGKRVLLV 34
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-89 5.06e-06

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 45.79  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD------------DQKSVLTWYN---------------NRPEDL 54
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglrnldlllglENRIVYTLVDvvegecrlqqalikdKRLKNL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 556394170   55 PHIPVTG-------ATGNIKAMLKEHEKSYDYVIADC-AGRDS 89
Cdd:TIGR01968  83 YLLPASQtrdkdavTPEQMKKLVNELKEEFDYVIIDCpAGIES 125
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 1-38 1.01e-05

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 44.72  E-value: 1.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 556394170    1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-39 3.08e-05

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: 43.45  E-value: 3.08e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 556394170   1 MIIVLgSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADD 39
Cdd:cd02034    1 MKIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 2-87 3.26e-05

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


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 43.13  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQkgGVGKSTLAVSIAAYLMSLGNRVIIVDAD-------DQKSVLTwynnrpeDLPHIPV----TGATGNI---K 67
Cdd:cd03115    3 ILLVGLQ--GSGKTTTLAKLARYYQEKGKKVLLIAADtfraaavEQLKTLA-------EKLGVPVfesyTGTDPASiaqE 73

                         90       100
                 ....*....|....*....|
gi 556394170  68 AMLKEHEKSYDYVIADCAGR 87
Cdd:cd03115   74 AVEKAKLEGYDVLLVDTAGR 93
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 16-207 3.80e-05

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: 42.95  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  16 TLAVSIAAYLMSLGNRVIIVDAD-------------DQKSVLTWYNNR----------------------PEDLPHIPvt 60
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADlglanldvllglePKATLADVLAGEadledaivqgpggldvlpggsgPAELAELD-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  61 gATGNIKAMLKEHEKSYDYVIADC-AGRdSAEMRSGLMAADVFISPLRPsqmDLDVVPHTCSVFTAAKDFNENIRGYLVL 139
Cdd:COG0455   79 -PEERLIRVLEELERFYDVVLVDTgAGI-SDSVLLFLAAADEVVVVTTP---EPTSITDAYALLKLLRRRLGVRRAGVVV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556394170 140 NMT-PTNMFVNEANQAAEVLKDYPEMRLansRV-----CDRKAHRdAWAESMTIFETQ-NDKAQQEIEALVKEVI 207
Cdd:COG0455  154 NRVrSEAEARDVFERLEQVAERFLGVRL---RVlgvipEDPAVRE-AVRRGRPLVLAApDSPAARAIRELAARLA 224
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 2-87 5.99e-05

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 42.14  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQkgGVGKSTLAVSIAAYLMSLGNRVIIVDAD-------DQksvLTWYNNRPEdlphIPVTGATGN-------IK 67
Cdd:pfam00448   3 ILLVGLQ--GSGKTTTIAKLAAYLKKKGKKVLLVAADtfraaaiEQ---LKQLAEKLG----VPVFGSKTGadpaavaFD 73

                          90       100
                  ....*....|....*....|
gi 556394170   68 AMLKEHEKSYDYVIADCAGR 87
Cdd:pfam00448  74 AVEKAKAENYDVVLVDTAGR 93
minD CHL00175
septum-site determining protein; Validated
 2-38 1.34e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 41.68  E-value: 1.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:CHL00175  17 IIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 2-205 1.83e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 41.58  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPE---------------DLPHIPVTGAT--- 63
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtdvganetlyaairyDDTRRPLRDVIrpt 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  64 ---------GNIKAMLKEHEK---------------------------SYDYVIADCAGRDSAEMRSGLMAADVFISPLR 107
Cdd:PRK13869 203 yfdglhlvpGNLELMEFEHTTpkalsdkgtrdglfftrvaqafdevadDYDVVVIDCPPQLGFLTLSGLCAATSMVITVH 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170 108 PSQMDLDVVPH----TCSVFTAAKDFNENIR----GYLVLNMTPTNMfvnEANQAAEVLKDYPEMRLANSRVCDRKAHRD 179
Cdd:PRK13869 283 PQMLDIASMSQfllmTRDLLGVVKEAGGNLQydfiRYLLTRYEPQDA---PQTKVAALLRNMFEDHVLTNPMVKSAAVSD 359

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 556394170 180 AWAESMTIFE--------TQNDKAQQ-------EIEALVKE 205
Cdd:PRK13869 360 AGLTKQTLYEigrenltrSTYDRAMEsldavnsEIEALIKM 400
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 2-114 1.90e-04

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


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 41.02  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRP-----EDLPHIPVTGATGNIKAMLKEHEKS 76
Cdd:pfam07015   3 LITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWRENALrkgtwDPACEIFNADELPLLEQAYEHAEGS 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 556394170   77 -YDYVIADCAGrDSAEMRSGLMA-ADVFISPLRPSQMDLD 114
Cdd:pfam07015  83 gFDYALADTHG-GSSELNNTIIAsSDLLLIPTMLTPLDID 121
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 2-47 2.65e-04

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 41.24  E-value: 2.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWY 47
Cdd:TIGR01005 555 LIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQM 600
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 11-38 3.15e-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: 39.93  E-value: 3.15e-04
                          10        20
                  ....*....|....*....|....*...
gi 556394170   11 GVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLD 31
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
2-114 4.42e-04

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 39.83  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWY-----NNRPEDLPHIPVTGATGNIKAMLKEHEKS 76
Cdd:PRK13849   3 LLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKenalrSNTWDPACEVYAADELPLLEAAYEDAELQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556394170  77 -YDYVIADCAGrDSAEMRSGLMA-ADVFISPLRPSQMDLD 114
Cdd:PRK13849  83 gFDYALADTHG-GSSELNNTIIAsSNLLLIPTMLTPLDID 121
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-38 4.73e-04

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: 40.03  E-value: 4.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 556394170    1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-85 5.18e-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: 39.48  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLT-------------WYNNRPEDLPHIPVTGATG---- 64
Cdd:cd05387   21 VIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHrllglpnepglseVLSGQASLEDVIQSTNIPNldvl 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556394170  65 ----------------NIKAMLKEHEKSYDYVIADCA 85
Cdd:cd05387  101 pagtvppnpsellsspRFAELLEELKEQYDYVIIDTP 137
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 2-57 1.42e-03

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 38.81  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLpHI 57
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL-HI 162
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 1-57 1.44e-03

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 38.84  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556394170   1 MIIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLpHI 57
Cdd:PHA02519 107 VVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL-HI 162
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2-83 1.56e-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: 37.74  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170     2 IIVLGSQkgGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVLTWYNNRPEDLPHIPVTGATGNIKAMLKEHEKS-YDYV 80
Cdd:smart00382   5 ILIVGPP--GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLkPDVL 82


                   ...
gi 556394170    81 IAD 83
Cdd:smart00382  83 ILD 85
PRK10818 PRK10818
septum site-determining protein MinD;
2-38 1.65e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 38.38  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:PRK10818   4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
2-35 1.66e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 38.26  E-value: 1.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 556394170   2 IIVLGsqKGGVGKSTLAVSIAAYLMSLGNRVIIV 35
Cdd:COG0003    6 IFFTG--KGGVGKTTVAAATALALAERGKRTLLV 37
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 9-38 2.29e-03

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 37.88  E-value: 2.29e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 556394170   9 KGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCD 37
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 2-87 2.51e-03

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


Pssm-ID: 349786  Cd Length: 193  Bit Score: 37.58  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   2 IIVLGSQkgGVGKSTLAVSIAAYLMSLGNRVIIVDAD-------DQKSVLT------WYnnrPEDLPHIPVTGATgniKA 68
Cdd:cd18539    3 ILLVGLQ--GSGKTTTAAKLALYLKKKGKKVLLVAADvyrpaaiEQLQTLGeqvgvpVF---ESGDGQSPVDIAK---RA 74

                         90
                 ....*....|....*....
gi 556394170  69 MLKEHEKSYDYVIADCAGR 87
Cdd:cd18539   75 LEKAKEEGFDVVIVDTAGR 93
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 2-38 3.00e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 37.36  E-value: 3.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGSQKGGVGKSTLAVSIAAYLmslgNRVIIVDAD 38
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCD 33
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 2-44 3.18e-03

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 37.03  E-value: 3.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 556394170    2 IIVLGSQKGGVGKSTLAVSIAAYLMSLGNRVIIVDADDQKSVL 44
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVM 61
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-38 3.31e-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: 37.76  E-value: 3.31e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 556394170    9 KGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 2-38 3.43e-03

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: 37.34  E-value: 3.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556394170   2 IIVLGsqKGGVGKSTLAVSIAAYLMSLGNRVIIVDAD 38
Cdd:cd02117    3 IVVYG--KGGIGKSTTASNLSAALAEGGKKVLHVGCD 37
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 4-152 7.58e-03

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 35.78  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170   4 VLGSqKGGVGKSTLAVSIAAYLMSLGNRVIIVDADdqksvltwynnrpedlphiPVTGATGNIKAM-------LKEHEKS 76
Cdd:cd05386    5 VLQG-KGGVGKSVIASLLAQYLIDKGQPVSCIDTD-------------------PVNKTFAGYKALnvqriniIDNDEII 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556394170  77 YDY--------------VIADCAGRDSAEMRSGLMAADVfisPLRPSQMDLDVVPHTcsVFTAAKDFNENIRGYLVLnmt 142
Cdd:cd05386   65 QSKfdqlveqflaedgtVVIDTGASTFLPLMNYLIDNDV---PDLLKDMGKEVVIHT--VINGGQALDDTINGLQTL--- 136

                        170
                 ....*....|
gi 556394170 143 pTNMFVNEAN 152
Cdd:cd05386  137 -LDQFKDNAK 145
 
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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