NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1799432010|gb|QHL61519|]
View 

polysaccharide biosynthesis tyrosine autokinase [Staphylococcus aureus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 23-226 4.11e-86

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member TIGR01007:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 204  Bit Score: 253.90  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  23 EKFRGIRSNIMFANPDsaVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPN-NEGLSSLL 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAE--IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 102 LNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVV 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1799432010 182 NSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSAS-YYAYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 23-226 4.11e-86

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: 253.90  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  23 EKFRGIRSNIMFANPDsaVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPN-NEGLSSLL 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAE--IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 102 LNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVV 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1799432010 182 NSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSAS-YYAYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 23-212 1.78e-85

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: 251.72  E-value: 1.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  23 EKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLL 102
Cdd:cd05387     1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 103 NWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVVN 182
Cdd:cd05387    81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1799432010 183 SENNNKDEVKKGKELIEATGAKLLGVVLNR 212
Cdd:cd05387   161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-226 8.59e-71

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: 217.75  E-value: 8.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  32 IMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWSTYQDSI 111
Cdd:COG0489    83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 112 ISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVVNSENNNKDEV 191
Cdd:COG0489   163 QPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDV 242

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1799432010 192 KKGKELIEATGAKLLGVVLNRMPKDKSASY--YAYYG 226
Cdd:COG0489   243 RKALEMLEKAGVPVLGVVLNMVCPKGERYYggGEEYG 279
PRK09841 PRK09841
tyrosine-protein kinase;
15-230 1.05e-38

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 141.97  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  15 EQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNN 94
Cdd:PRK09841  505 DNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  95 EGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFT 174
Cdd:PRK09841  585 HGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSV 664

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799432010 175 GNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSASY---YAYYGTDES 230
Cdd:PRK09841  665 GTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYsygYNYYGYSYS 723
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 44-160 1.69e-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: 68.76  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLS--SLLLNWSTYQDSIISTEIEDLDV 121
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTiyELLIGECNIEEAIIKTVIENLDL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1799432010 122 LTSGP---------IPPNPSELITSRAFANLYDtllmNYNFVIIDTPP 160
Cdd:pfam13614  84 IPSNIdlagaeielIGIENRENILKEALEPVKD----NYDYIIIDCPP 127
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 37-86 1.74e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.09  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1799432010  37 PDSAVQSIVITSEApGAGKSTIAANLAVAYAQAGYKTLIVDGDmrkPTQH 86
Cdd:NF041417  329 PQKDTRYLFFTGKG-GVGKSTIASTTATYLAEEGYETLIVTTD---PASH 374
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 23-226 4.11e-86

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: 253.90  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  23 EKFRGIRSNIMFANPDsaVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPN-NEGLSSLL 101
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAE--IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkITGLTNFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 102 LNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVV 181
Cdd:TIGR01007  79 SGTTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1799432010 182 NSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSAS-YYAYYG 226
Cdd:TIGR01007 159 DAGKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYgYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 23-212 1.78e-85

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: 251.72  E-value: 1.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  23 EKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLL 102
Cdd:cd05387     1 EAFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 103 NWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVVN 182
Cdd:cd05387    81 GQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVVR 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1799432010 183 SENNNKDEVKKGKELIEATGAKLLGVVLNR 212
Cdd:cd05387   161 AGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-226 8.59e-71

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: 217.75  E-value: 8.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  32 IMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWSTYQDSI 111
Cdd:COG0489    83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSDVLAGEASLEDVI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 112 ISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVYVVNSENNNKDEV 191
Cdd:COG0489   163 QPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDV 242

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1799432010 192 KKGKELIEATGAKLLGVVLNRMPKDKSASY--YAYYG 226
Cdd:COG0489   243 RKALEMLEKAGVPVLGVVLNMVCPKGERYYggGEEYG 279
EpsG TIGR03029
chain length determinant protein tyrosine kinase EpsG; The proteins in this family are ...
 11-211 1.15e-40

chain length determinant protein tyrosine kinase EpsG; The proteins in this family are homologs of the EpsG protein found in Methylobacillus strain 12S and are generally found in operons with other Eps homologs. The protein is believed to function as the protein tyrosine kinase component of the chain length regulator (along with the transmembrane component EpsF).


Pssm-ID: 132074 [Multi-domain]  Cd Length: 274  Bit Score: 140.00  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  11 LIVHEQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFN 90
Cdd:TIGR03029  73 LIAAYQPFSPQVEALRALRSQLMLRWFSEGRKALAVVSAKSGEGCSYIAANLAIVFSQLGEKTLLIDANLRDPVQHRNFK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  91 LPNNEGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLF 170
Cdd:TIGR03029 153 LSEQRGLSDILAGRSDLEVITHIPALENLSVLPAGAIPPNPQELLARPAFTDLLNKVMGDYDVVIVDTPSAEHSSDAQIV 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1799432010 171 SKFTGNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLN 211
Cdd:TIGR03029 233 ATRARGTLIVSRVNETRLHELTSLKEHLSGVGVRVVGAVLN 273
PRK09841 PRK09841
tyrosine-protein kinase;
15-230 1.05e-38

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 141.97  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  15 EQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNN 94
Cdd:PRK09841  505 DNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNE 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  95 EGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFT 174
Cdd:PRK09841  585 HGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSV 664

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799432010 175 GNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSASY---YAYYGTDES 230
Cdd:PRK09841  665 GTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYsygYNYYGYSYS 723
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
5-224 1.73e-38

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 141.06  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010   5 RRSTSSLIVHEQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPT 84
Cdd:PRK11519  490 RYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGY 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  85 QHYIFNLPNNEGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTV 164
Cdd:PRK11519  570 THELLGTNNVNGLSDILIGQGDITTAAKPTSIANFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAV 649

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 165 TDAQLFSKFTGNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKdKSASYYAY 224
Cdd:PRK11519  650 TDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFR-RASAYQDY 708
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 10-221 6.26e-35

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: 131.38  E-value: 6.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  10 SLIVHEQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIF 89
Cdd:TIGR01005 522 ARIVPDAPRSTFAEAFRNAKLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMF 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  90 NLPNNEGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPI---PPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTD 166
Cdd:TIGR01005 602 GKAPKPGLLDLLAGEASIEAGIHRDQRPGLAFIAAGGAshfPHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVAD 681

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1799432010 167 AQLFSKFTGNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSASY 221
Cdd:TIGR01005 682 AAAFAALADGILFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNALDMNELGKY 736
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 42-216 2.29e-21

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: 90.56  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLAVAYAQ-AGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWS----TYQDSIISTEI 116
Cdd:COG4963   103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLDLEPRRGLADALRNPDrldeTLLDRALTRHS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 117 EDLDVLtSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVNTVTDAQLFSKFTgNVVYVVNSENNNKDEVKKGKE 196
Cdd:COG4963   183 SGLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAAD-EVVLVTEPDLPSLRNAKRLLD 260

                         170       180
                  ....*....|....*....|..
gi 1799432010 197 LIEATGAKL--LGVVLNRMPKD 216
Cdd:COG4963   261 LLRELGLPDdkVRLVLNRVPKR 282
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 57-219 2.43e-18

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: 80.32  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  57 TIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWSTYQDSIISTEiEDLDVLTSGPIPPNPSELIT 136
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 137 SRAFANLYDTLLMNYNFVIIDTPPvNTVTDAQLFSKFTGNVVYVVNSEnnnKDEVKKGKELIE----ATGAKLLGVVLNR 212
Cdd:COG0455    80 EERLIRVLEELERFYDVVLVDTGA-GISDSVLLFLAAADEVVVVTTPE---PTSITDAYALLKllrrRLGVRRAGVVVNR 155


                  ....*..
gi 1799432010 213 MPKDKSA 219
Cdd:COG0455   156 VRSEAEA 162
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 42-160 2.37e-15

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: 72.58  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDmrkpTQH---YIFNLPNNE---GLSSLLLNWSTYQDSIISTE 115
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLD----PQGnltSGLGLDPDDldpTLYDLLLDDAPLEDAIVPTE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1799432010 116 IEDLDVltsgpIPPNPS------ELITSRA----FANLYDTLLMNYNFVIIDTPP 160
Cdd:COG1192    78 IPGLDL-----IPANIDlagaeiELVSRPGrelrLKRALAPLADDYDYILIDCPP 127
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 44-160 1.69e-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: 68.76  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLS--SLLLNWSTYQDSIISTEIEDLDV 121
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTiyELLIGECNIEEAIIKTVIENLDL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1799432010 122 LTSGP---------IPPNPSELITSRAFANLYDtllmNYNFVIIDTPP 160
Cdd:pfam13614  84 IPSNIdlagaeielIGIENRENILKEALEPVKD----NYDYIIIDCPP 127
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 44-212 4.35e-14

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: 68.91  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGD-------------MRKPTQHYIFN-LPNNEGLSSLLLN---WST 106
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnnssveglegDIAPALQALAEgLKGRVNLDPILLKeksDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 107 YQDSIIST-EIEDLDVLTSGPippnPSELITSRAFANLYDtllmNYNFVIIDTPP------VNTVTDAQLFSKFTGNVVY 179
Cdd:pfam01656  81 GLDLIPGNiDLEKFEKELLGP----RKEERLREALEALKE----DYDYVIIDGAPglgellRNALIAADYVIIPLEPEVI 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1799432010 180 VVNSennnkdeVKKGKELIEATGA-------KLLGVVLNR 212
Cdd:pfam01656 153 LVED-------AKRLGGVIAALVGgyallglKIIGVVLNK 185
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 42-212 2.52e-12

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: 61.29  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDmrkptqhyifnlpnneglsslllnwstyqdsiisteiedldv 121
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------ 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 122 ltsgpippnpselitsrafanlydtllmnyNFVIIDTPPVNTV------TDAQLFSKFTGNVVYVVNSENNNKDEVKKG- 194
Cdd:cd01983    39 ------------------------------DYVLIDGGGGLETglllgtIVALLALKKADEVIVVVDPELGSLLEAVKLl 88

                         170
                  ....*....|....*....
gi 1799432010 195 -KELIEATGAKLLGVVLNR 212
Cdd:cd01983    89 lALLLLGIGIRPDGIVLNK 107
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 42-160 2.09e-10

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: 58.73  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWSTYQDSIISTEiEDLDV 121
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLGDVLKGRVSLEDIIVEGP-EGLDI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1799432010 122 LTSGPIPPNPSELITSR--AFANLYDTLLMNYNFVIIDTPP 160
Cdd:cd02038    80 IPGGSGMEELANLDPEQkaKLIEELSSLESNYDYLLIDTGA 120
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 43-209 2.78e-10

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: 58.37  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  43 SIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGD--MRkptqhyifNL--------PNNEGLSSLLLNWSTYQDSII 112
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADigLR--------NLdlilglenRIVYTLVDVLEGECRLEQALI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 113 ST-EIEDLDVLtsgPIPPNPSEL-ITSRAFANLYDTLLMNYNFVIID-----------------------TPPVNTVTDA 167
Cdd:cd02036    74 KDkRWENLYLL---PASQTRDKDaLTPEKLEELVKELKDSFDFILIDspagiesgfinaiapadeaiivtNPEISSVRDA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1799432010 168 Q-----LFSKFTGNVVYVVNSENNnkDEVKKGKEL-----IEATGAKLLGVV 209
Cdd:cd02036   151 DrviglLESKGIVNIGLIVNRYRP--EMVKSGDMLsvediQEILGIPLLGVI 200
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 43-217 8.69e-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: 57.05  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  43 SIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLpnnEGLSSLLLNwstyqdsIISTEIEDLDVL 122
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGM---EDKPVTLHD-------VLAGEADIKDAI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 123 TSGP-----IPPNPS-ELITSRAFANLYDTL---LMNYNFVIIDTPPVNTVTDAQLFSKFTGNVVyVVNSENNNKDEVKK 193
Cdd:TIGR01969  72 YEGPfgvkvIPAGVSlEGLRKADPDKLEDVLkeiIDDTDFLLIDAPAGLERDAVTALAAADELLL-VVNPEISSITDALK 150

                         170       180
                  ....*....|....*....|....
gi 1799432010 194 GKELIEATGAKLLGVVLNRMPKDK 217
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVTRDK 174
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 44-211 2.13e-09

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: 55.59  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSlllnwstyQDSIISTEIEDLDVLT 123
Cdd:cd02037     3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQS--------EEGIVPVEVGGIKVMS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 124 SG-------PIP---PNPSELItsRAFanLYDTLLMNYNFVIIDTPPvNTvTDAQL----FSKFTGNVVYVVNSENNNKD 189
Cdd:cd02037    75 IGfllpeddAVIwrgPMKSGAI--KQF--LKDVDWGELDYLIIDLPP-GT-GDEHLslvqLIPIDGAVVVTTPQEVSLID 148

                         170       180
                  ....*....|....*....|..
gi 1799432010 190 eVKKGKELIEATGAKLLGVVLN 211
Cdd:cd02037   149 -VRKAIDMCKKLNIPVLGIVEN 169
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 44-159 4.47e-09

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: 55.15  E-value: 4.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNlpnneglsslllNWSTYQDsiiSTEIeDLDVLT 123
Cdd:pfam09140   3 IVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFE------------NRSATAD---RTGL-SLPTPE 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1799432010 124 SGPIPPNPSELIT------SRAFANLYDTLLMNYNFVIIDTP 159
Cdd:pfam09140  67 HLNLPDNDVAEVPdgenidDARLEEAFADLEARCDFIVIDTP 108
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 44-79 9.56e-09

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: 52.16  E-value: 9.56e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:cd02042     3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 44-222 4.73e-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: 52.07  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNL------PNNEGLSSLllnwSTYQDSIIS---- 113
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLegerpeQSDGGIIPV----EAHGIKVMSigfl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 114 TEIEDLDVLTSGPippnpseLITS--RAFanLYDTLLMNYNFVIIDTPPvNTvTDAQL----FSKFTGNVVyVVNSENNN 187
Cdd:pfam10609  82 LPDEDDAVIWRGP-------MKSGaiKQF--LTDVDWGELDYLIIDLPP-GT-GDEQLtlaqLLPLTGAVI-VTTPQDVA 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1799432010 188 KDEVKKGKELIEATGAKLLGVVLNrMpkdksaSYY 222
Cdd:pfam10609 150 LLDVRKAIDMFKKVNVPVLGVVEN-M------SYF 177
minD CHL00175
septum-site determining protein; Validated
 44-216 2.64e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 50.15  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMrkptqhyifnlpnneGLSS--LLLNwstYQDSIISTEIEDLDV 121
Cdd:CHL00175   18 IVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI---------------GLRNldLLLG---LENRVLYTAMDVLEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 122 ----------------LTSGPIPPNPSEL-ITSRAFANLYDTL-LMNYNFVIIDTPP------VNTVTDAQlfskftgNV 177
Cdd:CHL00175   80 ecrldqalirdkrwknLSLLAISKNRQRYnVTRKNMNMLVDSLkNRGYDYILIDCPAgidvgfINAIAPAQ-------EA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1799432010 178 VYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKD 216
Cdd:CHL00175  153 IVVTTPEITAIRDADRVAGLLEANGIYNVKLLVNRVRPD 191
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
42-217 2.57e-06

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 47.52  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLA---------VAY----AQAGYKTLIVDGD---MRKptqhyIFNLPNNEGLSSLLlnws 105
Cdd:COG0857     3 KSIYIASTEPGSGKTSVALGLAralqrkglrVGYfkpiGQSLVGGGERDEDvelIRE-----HLGLDLPYEDASPV---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 106 TYQDSIISTEIEDLDVLTsgpippnpsELITSRafanlYDTLLMNYNFVII---DTPPVNTVTDAQLFSKFTGN----VV 178
Cdd:COG0857    74 TLDEVETLLAEGDPDELL---------ERIVER-----YEALAAECDVVLVegsDPTGVGSPFELSLNARIAKNlgapVL 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1799432010 179 YVVNSENNN----KDEVKKGKELIEATGAKLLGVVLNRMPKDK 217
Cdd:COG0857   140 LVASGGGRTpeelVDALLLAADEFRGEGARVLGVIINRVPPEK 182
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
3-226 2.99e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010   3 NTRRSTSSLIVHEQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRK 82
Cdd:COG3206   461 RRRARLALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLLLLLDLLL 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  83 PTQHYIFNLPNNEGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFVIIDTPPVN 162
Cdd:COG3206   541 LLLLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLILDLVPLL 620

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799432010 163 TVTDAQLFSKFTGNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSASYYAYYG 226
Cdd:COG3206   621 AALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYY 684
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 43-209 6.50e-06

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 45.45  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  43 SIVITSEAPGAGKSTIAANLAVAYAQ-----------AGYKTLIVDGDMRkptqhyifnlpnNEGLSSLLLNWSTYQDSi 111
Cdd:pfam13481  34 GLGLLAGAPGTGKTTLALDLAAAVATgkpwlggprvpEQGKVLYVSAEGP------------ADELRRRLRAAGADLDL- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 112 isteIEDLDVLTSGPIPPNPSE----LITSRAFANLYDTLLMNYN--FVIIDTppvntvtdaqlFSKFTGnvvyvvNSEN 185
Cdd:pfam13481 101 ----PARLLFLSLVESLPLFFLdrggPLLDADVDALEAALEEVEDpdLVVIDP-----------LARALG------GDEN 159

                         170       180
                  ....*....|....*....|....*..
gi 1799432010 186 NNKDE---VKKGKELIEATGAKLLGVV 209
Cdd:pfam13481 160 SNSDVgrlVKALDRLARRTGATVLLVH 186
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 52-160 8.66e-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: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIV--D-----GDM-------RKPTQhyIF-NL------P------NNEGLSSLLLNW 104
Cdd:cd02035    10 GVGKTTIAAATAVRLAEQGKRVLLVstDpahslSDAfgqklggETPVK--GApNLwameidPeealeeYWEEVKELLAQY 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1799432010 105 STYQDSIISTEIEDLdvltsgpIPPNPSELITSRAFANLYDTllMNYNFVIIDTPP 160
Cdd:cd02035    88 LRLPGLDEVYAEELL-------SLPGMDEAAAFDELREYVES--GEYDVIVFDTAP 134
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1-226 9.07e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010   1 MTNTRRSTSSLIVHEQPKSPISEKFRGIRSNIMFANPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDM 80
Cdd:COG3206   454 PLKSKRERRRARLALLLLAAALAALLALLLALLLLLLLLLLLLLVSSSSGGGSSSTSSALAAASAAAAAAAALLLLLLLL 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  81 RKPT------QHYIFNLPNNEGLSSLLLNWSTYQDSIISTEIEDLDVLTSGPIPPNPSELITSRAFANLYDTLLMNYNFV 154
Cdd:COG3206   534 LLLDllllllLLLLLLLLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLPPPLLLPLLLLLLLLLLLLLLLLLLLLSDDLI 613

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799432010 155 IIDTPPVNTVTDAQLFSKFTGNVVYVVNSENNNKDEVKKGKELIEATGAKLLGVVLNRMPKDKSASYYAYYG 226
Cdd:COG3206   614 LDLVPLLAALLAAAVLAVLVVVLLLVVALVALARLALLAAALLLLLVLVVVGGVVLGGVVYGYYYYYYYYYY 685
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 21-160 1.76e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 45.05  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  21 ISEKFRGiRSNIMFA---NPDSAVQSIVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPTQHYIFNLPN---- 93
Cdd:PRK13869   99 LAGSTRG-RESIDFVphrRGSEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtdvg 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  94 -NEGLSSLLLNWST---YQDSIISTEIEDLDvLTSGPIPPNPSELITSRAF--------------ANLYDTLLMNYNFVI 155
Cdd:PRK13869  178 aNETLYAAIRYDDTrrpLRDVIRPTYFDGLH-LVPGNLELMEFEHTTPKALsdkgtrdglfftrvAQAFDEVADDYDVVV 256


                  ....*
gi 1799432010 156 IDTPP 160
Cdd:PRK13869  257 IDCPP 261
PHA02518 PHA02518
ParA-like protein; Provisional
 44-84 3.10e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 43.30  E-value: 3.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPT 84
Cdd:PHA02518    3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
52-76 9.06e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 42.50  E-value: 9.06e-05
                          10        20
                  ....*....|....*....|....*
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIV 76
Cdd:COG0003    13 GVGKTTVAAATALALAERGKRTLLV 37
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 44-90 9.10e-05

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: 42.37  E-value: 9.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYaqagYKTLIVDGDMRKPTQHYIFN 90
Cdd:cd03110     2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLG 44
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
44-84 1.11e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 42.34  E-value: 1.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGDMRKPT 84
Cdd:PRK11670  110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPS 150
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 51-79 1.28e-04

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 41.23  E-value: 1.28e-04
                          10        20
                  ....*....|....*....|....*....
gi 1799432010  51 PGAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:COG0529    25 SGSGKSTLANALERRLFERGRHVYLLDGD 53
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 52-76 2.78e-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: 2.78e-04
                          10        20
                  ....*....|....*....|....*
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIV 76
Cdd:cd02040    10 GIGKSTTASNLSAALAEMGKKVLHV 34
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 52-209 4.98e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 40.15  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIVD-----------------------GDMRKptqhYIFNLPNNEGLSSLLLNWSTyq 108
Cdd:COG3640    10 GVGKTTLSALLARYLAEKGKPVLAVDadpnanlaealgleveadlikplGEMRE----LIKERTGAPGGGMFKLNPKV-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 109 DSII---STEIEDLDVLTSGPI---------PPNpselitsrAFANLY-DTL-LMNYNFVIIDTP------------PVN 162
Cdd:COG3640    84 DDIPeeyLVEGDGVDLLVMGTIeeggsgcycPEN--------ALLRALlNHLvLGNYEYVVVDMEagiehlgrgtaeGVD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799432010 163 T---VTD--------AQLFSKFT-----GNVVYVVNSENNNKDEvkkgKELIEATGAKLLGVV 209
Cdd:COG3640   156 LllvVSEpsrrsietARRIKELAeelgiKKIYLVGNKVREEEDE----EFLRELLGLELLGFI 214
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 42-118 1.21e-03

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 38.89  E-value: 1.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799432010  42 QSIVITSEApGAGKSTIAANLAVAYAQAGYKTLIVDGDmrkptqhyifnlPNNEglSSLLLNWSTYQDSIISTEIED 118
Cdd:cd02117     1 ESIVVYGKG-GIGKSTTASNLSAALAEGGKKVLHVGCD------------PKHD--STLLLTGGKVPPTIDEMLTED 62
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 52-79 1.25e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 38.77  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|....*...
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:PRK03846   34 GSGKSTVAGALEEALHELGVSTYLLDGD 61
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
 52-79 1.43e-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: 38.86  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....*...
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:TIGR03815 104 GAGASTLAAALALAAARHGLRTLLVDAD 131
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 52-79 1.52e-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: 1.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:cd02034    10 GVGKTTIAALLIRYLAKKGGKVLAVDAD 37
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 37-86 1.74e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.09  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1799432010  37 PDSAVQSIVITSEApGAGKSTIAANLAVAYAQAGYKTLIVDGDmrkPTQH 86
Cdd:NF041417  329 PQKDTRYLFFTGKG-GVGKSTIASTTATYLAEEGYETLIVTTD---PASH 374
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 42-163 2.01e-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: 38.41  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  42 QSIVITSEAPGAGKSTIAANLAVAYAQ-AGYKTLIVDGDMRKPTQHYIFNLPNNEGLSSLLLNWS----TYQDSIISTEI 116
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLDrldrTLLDSAVTRHS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1799432010 117 EDLDVLTSgpippnPSELITSRAF-ANLYDTLL----MNYNFVIIDTPPVNT 163
Cdd:cd03111    81 SGLSLLPA------PQELEDLEALgAEQVDKLLqvlrAFYDHIIVDLGHFLD 126
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 51-79 3.12e-03

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 36.69  E-value: 3.12e-03
                          10        20
                  ....*....|....*....|....*....
gi 1799432010  51 PGAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:cd02027     8 SGSGKSTIARALEEKLFQRGRPVYVLDGD 36
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 52-79 4.65e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 36.54  E-value: 4.65e-03
                          10        20
                  ....*....|....*....|....*...
gi 1799432010  52 GAGKSTIAANLAVAYAQAGYKTLIVDGD 79
Cdd:PRK00889   14 GAGKTTIARALAEKLREAGYPVEVLDGD 41
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 44-185 4.83e-03

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 37.13  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010  44 IVITSEAPGAGKSTIAANLAVAYAQAGYKTLIVDGD------------MRKPTQHYIFNL-PNNEGLSSLLlnwstyqDS 110
Cdd:cd17869     6 ITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMErlqstdvffgasGRYLMSDHLYTLkSRKANLADKL-------ES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799432010 111 IISTEIEDLDVltsgpIPPNPSELITSRAFANLYDTLLMN------YNFVIIDTPPVNTVTDAQLFSKFTGNVVYVVNSE 184
Cdd:cd17869    79 CVKQHESGVYY-----FSPFKSALDILEIKKDDILHMITKlveahaYDYIIMDLSFEFSSTVCKLLQASHNNVVIALQDA 153


                  .
gi 1799432010 185 N 185
Cdd:cd17869   154 N 154
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH