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Conserved domains on  [gi|1928004363|gb|QOW37889|]
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tyrosine-protein kinase [Leuconostoc mesenteroides]

Protein Classification

CpsD/CapB family tyrosine-protein kinase( domain architecture ID 12941857)

CpsD/CapB family tyrosine-protein kinase is an autophosphorylating protein-tyrosine kinase that may be involved in the regulation of capsular polysaccharide biosynthesis

CATH:  3.40.50.300
EC:  2.7.10.2
Gene Ontology:  GO:0005524|GO:0004715|GO:0004713
PubMed:  22889913|19525115
SCOP:  4003987

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 38-230 7.08e-76

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: 228.22  E-value: 7.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  38 EQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNkNASGLTNY 117
Cdd:cd05387     1 EAFRTLRTNLLFA-GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLP-NEPGLSEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 118 LGDSEkEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAI 197
Cdd:cd05387    79 LSGQA-SLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLL 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1928004363 198 VVNGGKTTKGALQRTHDILKIAEAPVLGFIYND 230
Cdd:cd05387   158 VVRAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
 
Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 38-230 7.08e-76

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: 228.22  E-value: 7.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  38 EQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNkNASGLTNY 117
Cdd:cd05387     1 EAFRTLRTNLLFA-GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLP-NEPGLSEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 118 LGDSEkEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAI 197
Cdd:cd05387    79 LSGQA-SLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLL 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1928004363 198 VVNGGKTTKGALQRTHDILKIAEAPVLGFIYND 230
Cdd:cd05387   158 VVRAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 40-238 6.01e-65

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: 203.88  E-value: 6.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  40 FRTLRTNIEFASVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLnKNASGLTNYLG 119
Cdd:COG0489    75 LALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGL-ENRPGLSDVLA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 120 DsEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAIVV 199
Cdd:COG0489   154 G-EASLEDVIQPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVV 232

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1928004363 200 NGGKTTKGALQRTHDILKIAEAPVLGFIYNDQSRKKKGS 238
Cdd:COG0489   233 RPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERY 271
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 38-238 3.75e-60

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: 188.80  E-value: 3.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  38 EQFRTLRTNIEFAsvaKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKNASGLTNY 117
Cdd:TIGR01007   1 EYYNAIRTNIQFS---GAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 118 LgDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAI 197
Cdd:TIGR01007  78 L-SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASIL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1928004363 198 VVNGGKTTKGALQRTHDILKIAEAPVLGFIYN--DQSRKKKGS 238
Cdd:TIGR01007 157 VTDAGKIKKREVKKAKEQLEQAGSNFLGVVLNkvDISVSKYGY 199
PRK09841 PRK09841
tyrosine-protein kinase;
32-230 4.72e-33

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 126.95  E-value: 4.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  32 PKNPVSEQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLnKNA 111
Cdd:PRK09841  507 PADSAVEAVRALRTSLHFA-MMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTV-SNE 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 112 SGLTNYLgDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSK 191
Cdd:PRK09841  585 HGLSEYL-AGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRS 663

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1928004363 192 MDGVAIVVNGGKTTKGALQRTHDILKIAEAPVLGFIYND 230
Cdd:PRK09841  664 VGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNG 702
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 70-180 4.57e-14

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: 68.38  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlrrPTVAVTF--GLNKNASGLTNY-LGDSEKEVGSIIHRTAMDNLNVMPSG--- 143
Cdd:pfam13614  14 GKTTTSVNLAAALAKKGKKVLLIDLD---PQGNATSglGIDKNNVEKTIYeLLIGECNIEEAIIKTVIENLDLIPSNidl 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1928004363 144 ---PIppnpaELLG----SGRMTNLITQLKTHYDMIIFDVPPFL 180
Cdd:pfam13614  91 agaEI-----ELIGienrENILKEALEPVKDNYDYIIIDCPPSL 129
 
Name Accession Description Interval E-value
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 38-230 7.08e-76

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: 228.22  E-value: 7.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  38 EQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNkNASGLTNY 117
Cdd:cd05387     1 EAFRTLRTNLLFA-GSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLP-NEPGLSEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 118 LGDSEkEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAI 197
Cdd:cd05387    79 LSGQA-SLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLL 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1928004363 198 VVNGGKTTKGALQRTHDILKIAEAPVLGFIYND 230
Cdd:cd05387   158 VVRAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 40-238 6.01e-65

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: 203.88  E-value: 6.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  40 FRTLRTNIEFASVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLnKNASGLTNYLG 119
Cdd:COG0489    75 LALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGL-ENRPGLSDVLA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 120 DsEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAIVV 199
Cdd:COG0489   154 G-EASLEDVIQPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVV 232

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1928004363 200 NGGKTTKGALQRTHDILKIAEAPVLGFIYNDQSRKKKGS 238
Cdd:COG0489   233 RPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERY 271
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 38-238 3.75e-60

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: 188.80  E-value: 3.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  38 EQFRTLRTNIEFAsvaKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKNASGLTNY 117
Cdd:TIGR01007   1 EYYNAIRTNIQFS---GAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 118 LgDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSKMDGVAI 197
Cdd:TIGR01007  78 L-SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASIL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1928004363 198 VVNGGKTTKGALQRTHDILKIAEAPVLGFIYN--DQSRKKKGS 238
Cdd:TIGR01007 157 VTDAGKIKKREVKKAKEQLEQAGSNFLGVVLNkvDISVSKYGY 199
pepcterm_TyrKin TIGR03018
exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are ...
 26-229 9.25e-50

exopolysaccharide/PEP-CTERM locus tyrosine autokinase; Members of this protein family are related to a known protein-tyrosine autokinase and to numerous homologs from exopolysaccharide biosynthesis region proteins, many of which are designated as chain length determinants. Most members of this family contain a short region, immediately C-terminal to the region modeled here, with an abundance of Tyr residues. These C-terminal tyrosine residues are likely to be autophosphorylation sites. Some members of this family are fusion proteins.


Pssm-ID: 274392 [Multi-domain]  Cd Length: 207  Bit Score: 162.47  E-value: 9.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  26 LITAAEPKNPVSEQFRTLRT---NIEFASVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQ-QGKNVLLVDADLRRPTV 101
Cdd:TIGR03018   1 LITPNSPRSRIAEEFRKIKRpllANAFSAATKKNNNLIMVTSSLPGEGKSFTAINLAISLAQeYDKTVLLIDADLRRPSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 102 AVTFGLnKNASGLTNYLGDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYD--MIIFDVPPF 179
Cdd:TIGR03018  81 HRTLGL-EAEPGLSDCLLDPVLDLADVLVPTNIGRLSLLPAGRRHPNPTELLASQRMRSLLHELARRYPdrIIIIDTPPL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1928004363 180 LMVTDAQVLMSKMDGVAIVVNGGKTTKGALQRTHDILKiaEAPVLGFIYN 229
Cdd:TIGR03018 160 LVFSEARALARLVGQIVLVVEEGRTTQEAVKEALSALE--SCKVLGVVLN 207
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 31-229 2.91e-34

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: 130.23  E-value: 2.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  31 EPKNPVSEQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKN 110
Cdd:TIGR01005 528 APRSTFAEAFRNAKLACDFA-LADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPK 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 111 ASGLTNYLGDSEKEVGsiIHRTAMDNLNVMPSGPI---PPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQV 187
Cdd:TIGR01005 607 PGLLDLLAGEASIEAG--IHRDQRPGLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAA 684

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1928004363 188 LMSKMDGVAIVVNGGKTTKGALQRTHDILKIAEAPVLGFIYN 229
Cdd:TIGR01005 685 FAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFN 726
PRK09841 PRK09841
tyrosine-protein kinase;
32-230 4.72e-33

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 126.95  E-value: 4.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  32 PKNPVSEQFRTLRTNIEFAsVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLnKNA 111
Cdd:PRK09841  507 PADSAVEAVRALRTSLHFA-MMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTV-SNE 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 112 SGLTNYLgDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSK 191
Cdd:PRK09841  585 HGLSEYL-AGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRS 663

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1928004363 192 MDGVAIVVNGGKTTKGALQRTHDILKIAEAPVLGFIYND 230
Cdd:PRK09841  664 VGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNG 702
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
26-188 7.66e-32

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 123.34  E-value: 7.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  26 LITAAEPKNPVSEQFRTLRTNIEFASV-AKGEIktLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVT 104
Cdd:PRK11519  496 LLAVGNPTDLAIEAIRSLRTSLHFAMMqAQNNV--LMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHEL 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 105 FGLNkNASGLTNYLGdSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVTD 184
Cdd:PRK11519  574 LGTN-NVNGLSDILI-GQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTD 651


                  ....
gi 1928004363 185 AQVL 188
Cdd:PRK11519  652 AAIV 655
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 73-232 2.18e-21

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: 89.18  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  73 TVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKNASgLTNYLGDsEKEVGSIIHRTAmDNLNVMPSGPIPPNPAEL 152
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKAT-LADVLAG-EADLEDAIVQGP-GGLDVLPGGSGPAELAEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 153 LGSGRMTNLITQLKTHYDMIIFDVPP--------FLMVTDAQVL------------------MSKMDGVA---IVVNGGK 203
Cdd:COG0455    78 DPEERLIRVLEELERFYDVVLVDTGAgisdsvllFLAAADEVVVvttpeptsitdayallklLRRRLGVRragVVVNRVR 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1928004363 204 TTKGALQRTHDILKIAEA------PVLGFIYNDQS 232
Cdd:COG0455   158 SEAEARDVFERLEQVAERflgvrlRVLGVIPEDPA 192
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 17-230 8.81e-17

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: 78.62  E-value: 8.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  17 VETMTEGARLITAAEPKNPVsEQFRTLRTNIEFASVAKGeiKTLLISSALPSEGKSTVTANLAVAYAQQ-GKNVLLVDAD 95
Cdd:COG4963    65 LEALSESAALLADVLPLSPD-ELRAALARLLDPGAARRG--RVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  96 LRRPTVAVTFGLNkNASGLTNYLGDSEKEVGSIIHRTAM---DNLNVMpSGPIPPNPAELLGSGRMTNLITQLKTHYDMI 172
Cdd:COG4963   142 LQFGDVALYLDLE-PRRGLADALRNPDRLDETLLDRALTrhsSGLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYV 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 173 IFDVPPFL---------------MVTDAQV---------------LMSKMDGVAIVVNggKTTKGALQRTHDILKIAEAP 222
Cdd:COG4963   220 VVDLPRGLnpwtlaaleaadevvLVTEPDLpslrnakrlldllreLGLPDDKVRLVLN--RVPKRGEISAKDIEEALGLP 297


                  ....*...
gi 1928004363 223 VLGFIYND 230
Cdd:COG4963   298 VAAVLPND 305
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 70-180 1.45e-16

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: 76.44  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlrrP--TVAVTFGLNKNASGLTNY--LGDsEKEVGSIIHRTAMDNLNVMPSGP- 144
Cdd:COG1192    14 GKTTTAVNLAAALARRGKRVLLIDLD---PqgNLTSGLGLDPDDLDPTLYdlLLD-DAPLEDAIVPTEIPGLDLIPANId 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1928004363 145 ---IPPNPAELLGSG-RMTNLITQLKTHYDMIIFDVPPFL 180
Cdd:COG1192    90 lagAEIELVSRPGRElRLKRALAPLADDYDYILIDCPPSL 129
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 70-180 4.57e-14

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: 68.38  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlrrPTVAVTF--GLNKNASGLTNY-LGDSEKEVGSIIHRTAMDNLNVMPSG--- 143
Cdd:pfam13614  14 GKTTTSVNLAAALAKKGKKVLLIDLD---PQGNATSglGIDKNNVEKTIYeLLIGECNIEEAIIKTVIENLDLIPSNidl 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1928004363 144 ---PIppnpaELLG----SGRMTNLITQLKTHYDMIIFDVPPFL 180
Cdd:pfam13614  91 agaEI-----ELIGienrENILKEALEPVKDNYDYIIIDCPPSL 129
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 70-225 3.58e-11

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: 61.21  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKNASGL-TNYLGD-SEKEVGSII--HRTAMDNLNVMPSGP- 144
Cdd:pfam01656  11 GKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqALAEGLkGRVNLDPILlkEKSDEGGLDLIPGNId 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 145 ---IPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLmvtdaqvlmskmdgvaivvngGKTTKGALQRTHDILKIAEA 221
Cdd:pfam01656  91 lekFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGL---------------------GELLRNALIAADYVIIPLEP 149


                  ....
gi 1928004363 222 PVLG 225
Cdd:pfam01656 150 EVIL 153
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 70-229 4.17e-10

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: 57.90  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNknasglTNYLGDSEK-----EVgsiihrtamDNLNVMPSGP 144
Cdd:cd02037    13 GKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVE------GKPLHQSEEgivpvEV---------GGIKVMSIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 145 I-PPNPAELLGSGRMTNLITQL--KTHY---DMIIFDVPPFLmvTDAQVLMS---KMDGvAIVVnggkTT--KGALQ--- 210
Cdd:cd02037    78 LlPEDDAVIWRGPMKSGAIKQFlkDVDWgelDYLIIDLPPGT--GDEHLSLVqliPIDG-AVVV----TTpqEVSLIdvr 150

                         170
                  ....*....|....*....
gi 1928004363 211 RTHDILKIAEAPVLGFIYN 229
Cdd:cd02037   151 KAIDMCKKLNIPVLGIVEN 169
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 58-235 9.75e-10

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: 57.43  E-value: 9.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  58 KTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKNASGLTNYLGdSEKEVGSIIHRTAMDnL 137
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLA-GEADIKDAIYEGPFG-V 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363 138 NVMPSGpIPPNPAELLGSGRMTNLITQLKTHYDMIIFDVPPFLMVtDAQVLMSKMDGVAIVVNGGKTTKGALQRTHDILK 217
Cdd:TIGR01969  79 KVIPAG-VSLEGLRKADPDKLEDVLKEIIDDTDFLLIDAPAGLER-DAVTALAAADELLLVVNPEISSITDALKTKIVAE 156

                         170
                  ....*....|....*...
gi 1928004363 218 IAEAPVLGFIYNDQSRKK 235
Cdd:TIGR01969 157 KLGTAILGVVLNRVTRDK 174
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 70-200 1.37e-08

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 53.75  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGL-NKNASGLTNYLGDSEKEVGSIIHRTAMDNLNVMPSGPIPPN 148
Cdd:cd02036    13 GKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLeNRIVYTLVDVLEGECRLEQALIKDKRWENLYLLPASQTRDK 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1928004363 149 PAelLGSGRMTNLITQLKTHYDMIIFDVPPFLMvTDAQVLMSKMDGVAIVVN 200
Cdd:cd02036    93 DA--LTPEKLEELVKELKDSFDFILIDSPAGIE-SGFINAIAPADEAIIVTN 141
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 70-110 1.99e-08

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: 53.61  E-value: 1.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLNKN 110
Cdd:pfam10609  16 GKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGE 56
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 70-178 6.51e-08

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 51.80  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFGLnKNASGLTNYLGDsEKEVGSIIHRTAmDNLNVMPSGPIPPNP 149
Cdd:cd02038    13 GKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGL-APKKTLGDVLKG-RVSLEDIIVEGP-EGLDIIPGGSGMEEL 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1928004363 150 AElLGSGRMTNLITQLKT---HYDMIIFDVPP 178
Cdd:cd02038    90 AN-LDPEQKAKLIEELSSlesNYDYLLIDTGA 120
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 70-95 1.70e-07

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: 49.08  E-value: 1.70e-07
                          10        20
                  ....*....|....*....|....*.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDAD 95
Cdd:cd02042    13 GKTTLAVNLAAALALRGKRVLLIDLD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 70-176 5.55e-06

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: 46.59  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlrrP----TVAVTFGLNKN-ASGLTNYLGDSEKEVGSIIHRTAMDNLNVMPS-G 143
Cdd:cd02117    12 GKSTTASNLSAALAEGGKKVLHVGCD---PkhdsTLLLTGGKVPPtIDEMLTEDGTAEELRREDLLFSGFNGVDCVEAgG 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1928004363 144 PIPPNPAELLGSGRMTNLITQLKTH---YDMIIFDV 176
Cdd:cd02117    89 PEPGVGCGGRGIGTMLELLEEHGLLdddYDVVIFDV 124
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 58-95 6.32e-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: 43.96  E-value: 6.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1928004363  58 KTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDAD 95
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 61-199 2.72e-05

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: 44.19  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  61 LISSALPSEGKSTVTANLAVAYAQQGK-NVLLVDADLRRPTVAVTFGLNkNASGLTNYLGDSEK----EVGSIIHRTAmD 135
Cdd:cd03111     4 AVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNLR-PDYDLADVIQNLDRldrtLLDSAVTRHS-S 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928004363 136 NLNVMPSgpippnPAEL-----LGSGRMTNLITQLKTHYDMIIFDVPPFLMVTDAQVLMSkMDGVAIVV 199
Cdd:cd03111    82 GLSLLPA------PQELedleaLGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEA-ADEILLVT 143
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 13-180 1.05e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 43.13  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  13 DGLSVETMTEGARLITAAEpknpVSEQFRTL------RTNIEFASVAKG--EIKTLLISSALPSEGKSTVTANLAVAYAQ 84
Cdd:PRK13869   73 EGPQPELASNGRRFYTLGQ----INEIRQMLagstrgRESIDFVPHRRGseHLQVIAVTNFKGGSGKTTTSAHLAQYLAL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  85 QGKNVLLVDADLRRPTVAV-------TFGLNKNASGLTNYlGDSEKEVGSIIHRTAMDNLNVMPsGPIP------PNPAE 151
Cdd:PRK13869  149 QGYRVLAVDLDPQASLSALlgvlpetDVGANETLYAAIRY-DDTRRPLRDVIRPTYFDGLHLVP-GNLElmefehTTPKA 226

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1928004363 152 LLGSG--------RMTNLITQLKTHYDMIIFDVPPFL 180
Cdd:PRK13869  227 LSDKGtrdglfftRVAQAFDEVADDYDVVVIDCPPQL 263
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 70-95 1.07e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.46  E-value: 1.07e-04
                          10        20
                  ....*....|....*....|....*.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDAD 95
Cdd:COG3640    12 GKTTLSALLARYLAEKGKPVLAVDAD 37
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
1-101 1.70e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 42.34  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363   1 MSF-FNKGRAVGKDGLSVETMtegaRLITAAEPKNPVSEQFRTLRTNIEFASVaKGEIKTLLISSALPSEGKSTVTANLA 79
Cdd:PRK11670   55 MPFvWNSAFEELKEQCSAELL----RITGAKAIDWKLSHNIATLKRVNNQPGV-NGVKNIIAVSSGKGGVGKSSTAVNLA 129

                          90       100
                  ....*....|....*....|..
gi 1928004363  80 VAYAQQGKNVLLVDADLRRPTV 101
Cdd:PRK11670  130 LALAAEGAKVGILDADIYGPSI 151
PHA02518 PHA02518
ParA-like protein; Provisional
 70-100 3.42e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.60  E-value: 3.42e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRPT 100
Cdd:PHA02518   13 GKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
minD CHL00175
septum-site determining protein; Validated
 54-96 6.55e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.14  E-value: 6.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1928004363  54 KGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVDADL 96
Cdd:CHL00175   12 ATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI 54
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 70-95 1.04e-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: 39.42  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDAD 95
Cdd:cd02040    12 GKSTTASNLSAALAEMGKKVLHVGCD 37
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 29-106 1.16e-03

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 39.43  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1928004363  29 AAEPKNPVSEQFRTLRTNIeFASVAKGEIktllissalpseGKSTVTANLAVAYAQQGKNVLLVDADLRRPTVAVTFG 106
Cdd:cd02033    15 AIEPSLEIPTGPPTKETQI-IAIYGKGGI------------GKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFG 79
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
14-246 1.42e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  14 GLSVETMTEGARLITAAEPKNPVSEQFRTLRTNIEFASVAKGEIKTLLISSALPSEGKSTVTANLAVAYAQQGKNVLLVD 93
Cdd:COG3206   449 LGPLPPLKSKRERRRARLALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLL 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928004363  94 ADLRRPTVAVTFGLNKNASGLTNYLGDSEKEVGSIIHRTAMDNLNVMPSGPIPPNPAELLGSGRMTNLITQLKTHYDMII 173
Cdd:COG3206   529 LLLLLLLLDLLLLLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLL 608

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1928004363 174 FDVPPFLMVTDAQVLMSKMDGVAIVVNGGKTTKGALQRTHDILKIAEAPVLGFIYNDQSRKKKGSAGYGYGYG 246
Cdd:COG3206   609 SDDLILDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYY 681
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 70-127 1.45e-03

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: 38.83  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlRRPTVAVTFGLNKNASGLTNYLGDSEKEVGS 127
Cdd:cd02034    12 GKTTIAALLIRYLAKKGGKVLAVDAD-PNSNLAETLGVEVEKLPLIKTIGDIRERTGA 68
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
70-140 1.98e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 38.65  E-value: 1.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADlrrPtvavtfglnknASGLTNYLGdseKEVGSIIHRTAMDNLNVM 140
Cdd:COG0003    15 GKTTVAAATALALAERGKRTLLVSTD---P-----------AHSLGDVLG---TELGNEPTEVAVPNLYAL 68
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 70-99 2.26e-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: 37.96  E-value: 2.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLVDADLRRP 99
Cdd:cd18539    12 GKTTTAAKLALYLKKKGKKVLLVAADVYRP 41
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 70-106 4.27e-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: 37.75  E-value: 4.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1928004363  70 GKSTVTANLAVAYaqqgKNVLLVDADLRRPTVAVTFG 106
Cdd:cd03110    12 GKTTITANLAVLL----YNVILVDCDVDAPNLHLLLG 44
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 70-92 5.06e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 37.49  E-value: 5.06e-03
                          10        20
                  ....*....|....*....|...
gi 1928004363  70 GKSTVTANLAVAYAQQGKNVLLV 92
Cdd:cd02035    12 GKTTIAAATAVRLAEQGKRVLLV 34
 
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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