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Conserved domains on  [gi|89886027|ref|YP_516224|]
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ParA-like partition protein [Sodalis phage phiSG1]

Protein Classification

PHA02518 family protein( domain architecture ID 11476013)

PHA02518 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
1-214 2.69e-114

ParA-like protein; Provisional


:

Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 324.88  E-value: 2.69e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAQERNEGElPSISCVEMSGNIRAPLEEMRSRFDV 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE-PLIPVVRMGKSIRADLPKVASGYDY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNRLRVFSIITQAPTHPNQRYRidNARKLL 160
Cdd:PHA02518  80 VVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYR--EARKAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89886027  161 VDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAAEDAIQVFDELFRGIHE 214
Cdd:PHA02518 158 AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELFRGISG 211
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
1-214 2.69e-114

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 324.88  E-value: 2.69e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAQERNEGElPSISCVEMSGNIRAPLEEMRSRFDV 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE-PLIPVVRMGKSIRADLPKVASGYDY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNRLRVFSIITQAPTHPNQRYRidNARKLL 160
Cdd:PHA02518  80 VVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYR--EARKAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89886027  161 VDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAAEDAIQVFDELFRGIHE 214
Cdd:PHA02518 158 AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELFRGISG 211
ParA_partition NF041546
ParA family partition ATPase;
2-207 5.65e-36

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 125.36  E-value: 5.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAQERNEGELPSIscVEMSG-NIRAPLEEMRSRFDV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV--VGLARpTLHRELPSLARDYDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNRLRVFSIITQAPThpnqRYRI-DNARKL 159
Cdd:NF041546  79 VVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIA----RTALgREVAEA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 89886027  160 LVDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAAEDAIQVFDE 207
Cdd:NF041546 155 LAEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
1-160 1.50e-33

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: 116.87  E-value: 1.50e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAqernegelpsiscvemsgnirapleemrsrFDV 80
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL------------------------------YDY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNR--LRVFSIITQAPTHPNQRyriDNARK 158
Cdd:cd02042  51 ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLA---REVLE 127

                ..
gi 89886027 159 LL 160
Cdd:cd02042 128 EL 129
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
1-212 1.74e-24

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: 96.85  E-value: 1.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQ---------------KTTADWAQERNEGE----------- 54
Cdd:COG1192   2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQgnltsglgldpddldPTLYDLLLDDAPLEdaivpteipgl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  55 --LPS-----------ISCVEMSGNIRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMA 121
Cdd:COG1192  82 dlIPAnidlagaeielVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027 122 EIIETVQ-VFNNRLRVFSIItqaPT--HPNQRYRIDNARKLLVDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAA 198
Cdd:COG1192 162 ETIEEVReDLNPKLEILGIL---LTmvDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGA 238
                       250
                ....*....|....
gi 89886027 199 EDAIQVFDELFRGI 212
Cdd:COG1192 239 KAYRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
3-162 1.60e-15

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: 72.38  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     3 VTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQK--TTADWAQERNEGELPSISCVEMSGN-------------- 66
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPALQALAEGLKGRVnldpillkeksdeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    67 --------------------------IRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEM 120
Cdd:pfam01656  81 gldlipgnidlekfekellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 89886027   121 AEIIETVQ--VFNNRLRVFSIItqapthPNqRYRIDNARKLLVD 162
Cdd:pfam01656 161 GGVIAALVggYALLGLKIIGVV------LN-KVDGDNHGKLLKE 197
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
2-122 1.06e-06

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: 47.43  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADW---AQERNEG--EL--------------------- 55
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGtfkSQNKITGltNFlsgttdlsdaicdtnienldv 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89886027    56 -------PSISCVEMSGNIRAPLEEMRSRFDVVTVDCG--GA--DSKAMRSALAISDMAILPFRPKRRDLKVAPEMAE 122
Cdd:TIGR01007  99 itagpvpPNPTELLQSSNFKTLIETLRKRFDYIIIDTPpiGTvtDAAIIARACDASILVTDAGKIKKREVKKAKEQLE 176
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
1-214 2.69e-114

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 324.88  E-value: 2.69e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAQERNEGElPSISCVEMSGNIRAPLEEMRSRFDV 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE-PLIPVVRMGKSIRADLPKVASGYDY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNRLRVFSIITQAPTHPNQRYRidNARKLL 160
Cdd:PHA02518  80 VVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYR--EARKAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89886027  161 VDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAAEDAIQVFDELFRGIHE 214
Cdd:PHA02518 158 AGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLVKELFRGISG 211
ParA_partition NF041546
ParA family partition ATPase;
2-207 5.65e-36

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 125.36  E-value: 5.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAQERNEGELPSIscVEMSG-NIRAPLEEMRSRFDV 80
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV--VGLARpTLHRELPSLARDYDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNRLRVFSIITQAPThpnqRYRI-DNARKL 159
Cdd:NF041546  79 VVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIA----RTALgREVAEA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 89886027  160 LVDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAAEDAIQVFDE 207
Cdd:NF041546 155 LAEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAKE 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
1-160 1.50e-33

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: 116.87  E-value: 1.50e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADWAqernegelpsiscvemsgnirapleemrsrFDV 80
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL------------------------------YDY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  81 VTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQVFNNR--LRVFSIITQAPTHPNQRyriDNARK 158
Cdd:cd02042  51 ILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLA---REVLE 127

                ..
gi 89886027 159 LL 160
Cdd:cd02042 128 EL 129
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
1-212 1.74e-24

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: 96.85  E-value: 1.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQ---------------KTTADWAQERNEGE----------- 54
Cdd:COG1192   2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQgnltsglgldpddldPTLYDLLLDDAPLEdaivpteipgl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  55 --LPS-----------ISCVEMSGNIRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMA 121
Cdd:COG1192  82 dlIPAnidlagaeielVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027 122 EIIETVQ-VFNNRLRVFSIItqaPT--HPNQRYRIDNARKLLVDLGLNPLRSFTRNLNAWDDAEEAGCSVLEYQEDKKAA 198
Cdd:COG1192 162 ETIEEVReDLNPKLEILGIL---LTmvDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGA 238
                       250
                ....*....|....
gi 89886027 199 EDAIQVFDELFRGI 212
Cdd:COG1192 239 KAYRALAEELLERL 252
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
3-162 1.60e-15

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: 72.38  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     3 VTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQK--TTADWAQERNEGELPSISCVEMSGN-------------- 66
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSnnSSVEGLEGDIAPALQALAEGLKGRVnldpillkeksdeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    67 --------------------------IRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEM 120
Cdd:pfam01656  81 gldlipgnidlekfekellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 89886027   121 AEIIETVQ--VFNNRLRVFSIItqapthPNqRYRIDNARKLLVD 162
Cdd:pfam01656 161 GGVIAALVggYALLGLKIIGVV------LN-KVDGDNHGKLLKE 197
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
2-106 3.91e-11

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: 60.55  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTT--------ADWAqERNEGELPSISCVEMSGN------- 66
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTfhryfenrSATA-DRTGLSLPTPEHLNLPDNdvaevpd 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 89886027    67 --------IRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILP 106
Cdd:pfam09140  81 geniddarLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTP 128
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
9-129 3.46e-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: 52.50  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDAD-------------PQKTTADWAQERNEGE-------------LPSISCVE 62
Cdd:COG0489 101 KGGEGKSTVAANLALALAQSGKRVLLIDADlrgpslhrmlgleNRPGLSDVLAGEASLEdviqptevegldvLPAGPLPP 180
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89886027  63 ------MSGNIRAPLEEMRSRFDVVTVDC--GGADSKAmRSALAISDMAILPFRPKRRDLKVAPEMAEIIETVQV 129
Cdd:COG0489 181 npsellASKRLKQLLEELRGRYDYVIIDTppGLGVADA-TLLASLVDGVLLVVRPGKTALDDVRKALEMLEKAGV 254
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-128 5.73e-08

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: 50.66  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQ-KTTADWAQERNEGE-------------------------- 54
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgNATSGLGIDKNNVEktiyelligecnieeaiiktvienld 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    55 -LPS--------ISCVEMSGN---IRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAE 122
Cdd:pfam13614  83 lIPSnidlagaeIELIGIENReniLKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLN 162

                  ....*.
gi 89886027   123 IIETVQ 128
Cdd:pfam13614 163 TIKLVK 168
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-147 1.60e-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: 50.50  E-value: 1.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFLRQ-GKTVLLVDADPQKTTAD----------WAQ-----ERNEGE----------- 54
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVAlyldleprrgLADalrnpDRLDETlldraltrhss 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  55 ----LPSISCVEMSGNIRAP-----LEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVAPEMAEIIE 125
Cdd:COG4963 184 glsvLAAPADLERAEEVSPEaverlLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLLDLLR 263
                       170       180
                ....*....|....*....|..
gi 89886027 126 TVQVFNNRLRVfsIITQAPTHP 147
Cdd:COG4963 264 ELGLPDDKVRL--VLNRVPKRG 283
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
1-39 2.16e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 49.78  E-value: 2.16e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 89886027   1 MIVTVCNeKGGAGKSSVAQSLAVHFLRQGKTVLLVDADP 39
Cdd:COG3640   1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADP 38
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
2-122 1.06e-06

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: 47.43  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADW---AQERNEG--EL--------------------- 55
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGtfkSQNKITGltNFlsgttdlsdaicdtnienldv 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89886027    56 -------PSISCVEMSGNIRAPLEEMRSRFDVVTVDCG--GA--DSKAMRSALAISDMAILPFRPKRRDLKVAPEMAE 122
Cdd:TIGR01007  99 itagpvpPNPTELLQSSNFKTLIETLRKRFDYIIIDTPpiGTvtDAAIIARACDASILVTDAGKIKKREVKKAKEQLE 176
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
2-38 4.49e-06

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: 45.64  E-value: 4.49e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:cd05387  21 VIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD 57
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
1-38 6.12e-06

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: 43.57  E-value: 6.12e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 89886027   1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
2-38 7.33e-06

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: 45.18  E-value: 7.33e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:cd02037   2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
9-45 7.54e-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: 45.19  E-value: 7.54e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTAD 45
Cdd:cd02035   8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSD 44
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
2-38 8.52e-06

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: 45.14  E-value: 8.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:pfam10609   5 VIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
9-45 1.45e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 44.81  E-value: 1.45e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTAD 45
Cdd:COG0003  11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGD 47
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
2-105 2.21e-05

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: 43.71  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD-------------PQKTTADW----------AQERNEG----- 53
Cdd:cd02038   2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVlkgrvslediIVEGPEGldiip 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 89886027  54 ------ELPSISCVEMSGNIRApLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAIL 105
Cdd:cd02038  82 ggsgmeELANLDPEQKAKLIEE-LSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
1-129 4.16e-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: 43.18  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     1 MIVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD-------------PQKTT--------ADWAQERNEGE----- 54
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADitmanlelilgmeDKPVTlhdvlageADIKDAIYEGPfgvkv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    55 LPSISCVE--MSGNI---RAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAIlpfrpkrrdLKVAPEMAEIIETVQV 129
Cdd:TIGR01969  81 IPAGVSLEglRKADPdklEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELL---------LVVNPEISSITDALKT 151
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
2-144 4.81e-05

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 42.91  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADW---AQERNEGElpsiSCVEMSGNIRAPLEEMR--- 75
Cdd:PRK13849   3 LLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWkenALRSNTWD----PACEVYAADELPLLEAAyed 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89886027   76 ---SRFDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVA-PEMAEIIETVQVFNNRLRVFSIITQAP 144
Cdd:PRK13849  79 aelQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLDIDEAlSTYRYVIELLLSENLAIPTAILRQRVP 151
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
9-99 6.64e-05

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: 42.72  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADwAQERNEGELPS-----ISCVEMsgNIRAPLEEMRSRFDVVTV 83
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSD-SFNQKFGHEPTkvkenLSAMEI--DPNMELEEYWQEVQKYMN 85
                          90
                  ....*....|....*...
gi 89886027    84 DCGGAD--SKAMRSALAI 99
Cdd:pfam02374  86 ALLGLRmlEGILAEELAS 103
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
1-39 6.93e-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: 42.30  E-value: 6.93e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 89886027   1 MIVTVCNeKGGAGKSSVAQSLAVHFLRQGKTVLLVDADP 39
Cdd:cd02034   1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
5-39 1.75e-04

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: 40.40  E-value: 1.75e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 89886027   5 VCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADP 39
Cdd:cd05386   5 VLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
2-42 1.85e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 41.58  E-value: 1.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 89886027    2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKT 42
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQAS 163
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
9-65 2.38e-04

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: 40.96  E-value: 2.38e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89886027   9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADP-------------QKTTADWAQERNEGELPS---------ISCVEMSG 65
Cdd:cd02040   8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPkadstrlllggkaIPTVLDTLREKGEVEELEdvikegfngIKCVESGG 86
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
2-40 2.40e-04

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: 41.12  E-value: 2.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQ 40
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ 144
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
2-38 2.69e-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: 40.65  E-value: 2.69e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:cd02036   2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
9-212 4.09e-04

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 40.43  E-value: 4.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027   9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADP-------------QKTTADWAQERNEGEL-----------PSISCVEMS 64
Cdd:cd02117   8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPkhdstllltggkvPPTIDEMLTEDGTAEElrredllfsgfNGVDCVEAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  65 G----------NIRAPLEEMR------SRFDVVTVD------CGGAdskAMrsalaisdmailpfrPKRRDLK------V 116
Cdd:cd02117  88 GpepgvgcggrGIGTMLELLEehglldDDYDVVIFDvlgdvvCGGF---AA---------------PLRRGFAqkvvivV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027 117 APEMA------EIIETVQVF-NNRLRVFSIITQAPTHPNQRYRIDNARKLLVdlglnPLRSFTRNLNAWDDAEEAGCSVL 189
Cdd:cd02117 150 SEELMslyaanNIVKAVENYsKNGVRLAGLVANLRDPAGTEEIQAFAAAVGT-----KILAVIPRDPAVRRAELARVTVF 224
                       250       260
                ....*....|....*....|...
gi 89886027 190 EYQEDKKAAEDaiqvFDELFRGI 212
Cdd:cd02117 225 EHDPVSPAASE----FARLAAKI 243
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
2-40 4.86e-04

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 40.02  E-value: 4.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQ 40
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
9-39 5.53e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.46  E-value: 5.53e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 89886027     9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADP 39
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDP 41
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
2-163 6.03e-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: 39.48  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTADW---AQERNE-GELPSISCVEMSGNIRAPLEEMRSR 77
Cdd:pfam07015   3 LITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWrenALRKGTwDPACEIFNADELPLLEQAYEHAEGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027    78 -FDVVTVDCGGADSKAMRSALAISDMAILPFRPKRRDLKVA-PEMAEIIETVQVFNNRLRVFSIITQAPTHpnqryRIDN 155
Cdd:pfam07015  83 gFDYALADTHGGSSELNNTIIASSDLLLIPTMLTPLDIDEAlATYRYVIELLLTENLAIPTAILRQRVPVG-----RLTS 157

                  ....*...
gi 89886027   156 ARKLLVDL 163
Cdd:pfam07015 158 SQRFCSDM 165
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
21-109 9.81e-04

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: 39.10  E-value: 9.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  21 LAVHFLRQGKTVLLVDAD-------------PQKTTADWAQER-------NEGE-----LPSISCVEMSGNIRAP----- 70
Cdd:COG0455   6 LAAALARLGKRVLLVDADlglanldvllglePKATLADVLAGEadledaiVQGPggldvLPGGSGPAELAELDPEerlir 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 89886027  71 -LEEMRSRFDVVTVDCGGADSKAMRSALAISDMAILPFRP 109
Cdd:COG0455  86 vLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTP 125
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
2-105 1.02e-03

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 39.24  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027     2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDADP------------------------QKTTADWAQERNE----G 53
Cdd:TIGR03815  95 VVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADPwgggldlllgaedvpglrwpdlsqARGRLPAGALRDAlprrG 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 89886027    54 ELPSISC-----VEMS-GNIRAPLEEMRSRFDVVTVDCGGADSKAMRSALAISDMAIL 105
Cdd:TIGR03815 175 GLSVLSWgravgAALPpAAVRAVLDAARRGGDLVVVDLPRRLTPAAETALESADLVLV 232
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
11-87 2.44e-03

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: 37.35  E-value: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89886027  11 GAGKSSVAQSLAVHFLRQGKTVLLVDADPQKTTAdWAQERNEGELPSISCVE-MSGN-----IRAPLEEMRSR-FDVVTV 83
Cdd:cd03115  10 GSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAA-VEQLKTLAEKLGVPVFEsYTGTdpasiAQEAVEKAKLEgYDVLLV 88

                ....
gi 89886027  84 DCGG 87
Cdd:cd03115  89 DTAG 92
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-38 2.61e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 38.10  E-value: 2.61e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 89886027    2 IVTVCNEKGGAGKSSVAQSLAVHFLRQGKTVLLVDAD 38
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
9-39 3.62e-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: 3.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 89886027     9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADP 39
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
2-45 4.10e-03

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 37.26  E-value: 4.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFL-RQGKTVLLVDADPQKTTAD 45
Cdd:cd03111   2 VVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLPFGDLG 46
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
2-38 7.12e-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: 36.59  E-value: 7.12e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 89886027   2 IVTVCNEKGGAGKSSVAQSLAVHFlrqgKTVLLVDAD 38
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCD 33
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
9-54 9.52e-03

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 36.27  E-value: 9.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 89886027     9 KGGAGKSSVAQSLAVHFLRQGKTVLLVDADP-------------QKTTADWAQERNEGE 54
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPkadstrlllggklQPTVLDTAREKGYVE 66
 
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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