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Conserved domains on  [gi|490732093|ref|WP_004594451|]
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MULTISPECIES: ParA family protein [Halobacteriales]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 13-287 2.56e-57

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: 184.29  E-value: 2.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAyDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:COG1192    5 AVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD-DLDPTLYDLLLDDAPLEDAIVPTEIpGLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  92 LPSSNELENVETRLKDERFADVKLRRnVVDPLiQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMI 171
Cdd:COG1192   84 IPANIDLAGAEIELVSRPGRELRLKR-ALAPL-ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 172 ERqISPIRQ--NIGLDILAVTPNMIRetmGQRNEHRTLVENLNREFGsfvpeyarvdpeifdalddsgrtiDSIPKPGIR 249
Cdd:COG1192  162 ET-IEEVREdlNPKLEILGILLTMVD---PRTRLSREVLEELREEFG------------------------DKVLDTVIP 213

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490732093 250 ERTAISRAFKQGMPVSEFDEDCDQIPNFDHLADLVEEH 287
Cdd:COG1192  214 RSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 13-287 2.56e-57

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: 184.29  E-value: 2.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAyDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:COG1192    5 AVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD-DLDPTLYDLLLDDAPLEDAIVPTEIpGLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  92 LPSSNELENVETRLKDERFADVKLRRnVVDPLiQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMI 171
Cdd:COG1192   84 IPANIDLAGAEIELVSRPGRELRLKR-ALAPL-ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 172 ERqISPIRQ--NIGLDILAVTPNMIRetmGQRNEHRTLVENLNREFGsfvpeyarvdpeifdalddsgrtiDSIPKPGIR 249
Cdd:COG1192  162 ET-IEEVREdlNPKLEILGILLTMVD---PRTRLSREVLEELREEFG------------------------DKVLDTVIP 213

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490732093 250 ERTAISRAFKQGMPVSEFDEDCDQIPNFDHLADLVEEH 287
Cdd:COG1192  214 RSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 13-172 1.27e-28

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: 107.67  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDaYDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:pfam13614   5 AIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDK-NNVEKTIYELLIGECNIEEAIIKTVIeNLDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   92 LPSSNELENVETRLkderfADVKLRRNVVDPLIQ---NGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:pfam13614  84 IPSNIDLAGAEIEL-----IGIENRENILKEALEpvkDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLS 158


                  ....
gi 490732093  169 KMIE 172
Cdd:pfam13614 159 QLLN 162
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 13-209 6.41e-22

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: 88.75  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLgyddaydrdanlgdalidgedpedllietdfgvhll 92
Cdd:cd02042    4 AVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL------------------------------------ 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  93 pssnelenvetrlkderfadvklrrnvvdpliqngYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIE 172
Cdd:cd02042   48 -----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490732093 173 RqISPIRQ--NIGLDILAVTPNMIRETMGQRNEHRTLVE 209
Cdd:cd02042   93 T-LEELKKqlNPPLLILGILLTRVDPRTKLAREVLEELK 130
PHA02518 PHA02518
ParA-like protein; Provisional
 18-280 1.57e-10

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 59.48  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDkdghmttqlgyddaydrdanlgdalidgedpedllietdfgvhllPSSNE 97
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLD---------------------------------------------PQGSS 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  98 LENVETRLKDER-FADVKLRRNVVDPLIQ--NGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIErq 174
Cdd:PHA02518  44 TDWAEAREEGEPlIPVVRMGKSIRADLPKvaSGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVE-- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 175 ispirqnigldilavtpnMIRETMGQRNEHRTlvenlnrefGSFVPEYA----RVDPEIFDALDDSGRtidSIPKPGIRE 250
Cdd:PHA02518 122 ------------------LIKARQEVTDGLPK---------FAFIISRAikntQLYREARKALAGYGL---PILRNGTTQ 171

                        250       260       270
                 ....*....|....*....|....*....|....
gi 490732093 251 RTAISRAFKQGMPVSEFDED----CDQIPNFDHL 280
Cdd:PHA02518 172 RVAYADAAEAGGSVLELPEDdkaaEEIIQLVKEL 205
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 18-194 7.36e-10

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


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 58.12  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLD-------LDKDGHMTTQLGYD--DAYDRDANLGDALIDGEDPEDLlietdfg 88
Cdd:TIGR01968  10 KGGVGKTTTTANLGTALARLGKKVVLIDadiglrnLDLLLGLENRIVYTlvDVVEGECRLQQALIKDKRLKNL------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   89 vHLLPSSnelenvETRLKDErfADVKLRRNVVDPLIQNgYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:TIGR01968  83 -YLLPAS------QTRDKDA--VTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDAD 152

                         170       180
                  ....*....|....*....|....*.
gi 490732093  169 KMIERQISPIRQNIGLDILAVTPNMI 194
Cdd:TIGR01968 153 RVIGLLEAKGIEKIHLIVNRLRPEMV 178
ParA_partition NF041546
ParA family partition ATPase;
18-270 2.11e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.02  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTtqlgydDAYDRDANlgdalidgedpedlliETDFGVHLLPSSNe 97
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------DWAAARED----------------ERPFPVVGLARPT- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  98 lenvetrlkderfadvkLRRNVvdPLIQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPragsinglnkmierqiSP 177
Cdd:NF041546  65 -----------------LHREL--PSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQP----------------SP 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 178 irqnigLDILAV--TPNMIRETMGQRNEHRT-LVenLNRefgsfVPEYARVDPEIFDALDDSGrtidsIP--KPGIRERT 252
Cdd:NF041546 110 ------YDLWASadTVDLIKEAREYTPGLKAaFV--LNR-----AIARTALGREVAEALAEYG-----LPvlKTRIGQRV 171

                        250
                 ....*....|....*...
gi 490732093 253 AISRAFKQGMPVSEFDED 270
Cdd:NF041546 172 AFAESAAEGLTVFEAEPD 189
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 18-76 3.20e-05

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: 45.26  E-value: 3.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMT----TQLGYDDAYDRDANLGDALIDGE 76
Cdd:NF041417 341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgTEVGHEPTKVGVENLYAARIDQE 403
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 13-287 2.56e-57

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: 184.29  E-value: 2.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAyDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:COG1192    5 AVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPD-DLDPTLYDLLLDDAPLEDAIVPTEIpGLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  92 LPSSNELENVETRLKDERFADVKLRRnVVDPLiQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMI 171
Cdd:COG1192   84 IPANIDLAGAEIELVSRPGRELRLKR-ALAPL-ADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 172 ERqISPIRQ--NIGLDILAVTPNMIRetmGQRNEHRTLVENLNREFGsfvpeyarvdpeifdalddsgrtiDSIPKPGIR 249
Cdd:COG1192  162 ET-IEEVREdlNPKLEILGILLTMVD---PRTRLSREVLEELREEFG------------------------DKVLDTVIP 213

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490732093 250 ERTAISRAFKQGMPVSEFDEDCDQIPNFDHLADLVEEH 287
Cdd:COG1192  214 RSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 13-172 1.27e-28

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: 107.67  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDaYDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:pfam13614   5 AIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDK-NNVEKTIYELLIGECNIEEAIIKTVIeNLDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   92 LPSSNELENVETRLkderfADVKLRRNVVDPLIQ---NGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:pfam13614  84 IPSNIDLAGAEIEL-----IGIENRENILKEALEpvkDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLS 158


                  ....
gi 490732093  169 KMIE 172
Cdd:pfam13614 159 QLLN 162
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 18-264 4.60e-26

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: 102.42  E-value: 4.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAYDRD-ANLGDALIDGEDPEDLLIETD---FGVHLLP 93
Cdd:pfam01656   7 KGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPAlQALAEGLKGRVNLDPILLKEKsdeGGLDLIP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   94 SSNELENVETRLKDERFAdVKLRRNVvdPLIQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIE- 172
Cdd:pfam01656  87 GNIDLEKFEKELLGPRKE-ERLREAL--EALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRLGGv 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  173 -RQISPIRQNIGLDILAVTPNMIREtmgqRNEHRTLVENLNRE-FGSFVpeyarvdpeifdalddsgrtIDSIPkpgirE 250
Cdd:pfam01656 164 iAALVGGYALLGLKIIGVVLNKVDG----DNHGKLLKEALEELlRGLPV--------------------LGVIP-----R 214

                         250
                  ....*....|....
gi 490732093  251 RTAISRAFKQGMPV 264
Cdd:pfam01656 215 DEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 13-209 6.41e-22

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: 88.75  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLgyddaydrdanlgdalidgedpedllietdfgvhll 92
Cdd:cd02042    4 AVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL------------------------------------ 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  93 pssnelenvetrlkderfadvklrrnvvdpliqngYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIE 172
Cdd:cd02042   48 -----------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490732093 173 RqISPIRQ--NIGLDILAVTPNMIRETMGQRNEHRTLVE 209
Cdd:cd02042   93 T-LEELKKqlNPPLLILGILLTRVDPRTKLAREVLEELK 130
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 25-260 1.89e-17

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: 79.16  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  25 TIALNIADRLAARGHETVLLDLDKD-GHMTTQLGYDDAYdrdaNLGDALIDGEDPEDLLIETDFGVHLLPSSNELENVET 103
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPKA----TLADVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 104 RLKDERFADV--KLRRNvvdpliqngYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIERqispIRQN 181
Cdd:COG0455   77 LDPEERLIRVleELERF---------YDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKL----LRRR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 182 IGLDILAVTPNMIRETMGQRNEHRTLVENLNREFGSFVPEYARV--DPEIFDALDDSGRTIDSIPKPgirertAISRAFK 259
Cdd:COG0455  144 LGVRRAGVVVNRVRSEAEARDVFERLEQVAERFLGVRLRVLGVIpeDPAVREAVRRGRPLVLAAPDS------PAARAIR 217


                 .
gi 490732093 260 Q 260
Cdd:COG0455  218 E 218
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 18-173 6.12e-13

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: 68.22  E-value: 6.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAAR-GHETVLLDLD-KDGHMTTQLGYDDAYdrdaNLGDAL-----IDGEDPEDLLIETDFGVH 90
Cdd:COG4963  111 KGGVGATTLAVNLAWALAREsGRRVLLVDLDlQFGDVALYLDLEPRR----GLADALrnpdrLDETLLDRALTRHSSGLS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  91 LLPSSNELENVEtRLKDERFADV--KLRRNvvdpliqngYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:COG4963  187 VLAAPADLERAE-EVSPEAVERLldLLRRH---------FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAK 256


                 ....*
gi 490732093 169 KMIER 173
Cdd:COG4963  257 RLLDL 261
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 13-164 2.29e-12

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: 64.90  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKD-GHMTTQLGYDDAYdrdaNLGDALIDGEDPEDLLIETDFGVHL 91
Cdd:cd02038    4 AVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGlANLDILLGLAPKK----TLGDVLKGRVSLEDIIVEGPEGLDI 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490732093  92 LPSSNELENVeTRLKDERFAdvKLRRNVVDplIQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSI 164
Cdd:cd02038   80 IPGGSGMEEL-ANLDPEQKA--KLIEELSS--LESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSI 147
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 18-154 5.06e-12

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: 64.82  E-value: 5.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLD-KDGHMTTQLGYDDaydrDANLGDALIDGEDPEDLLIETDF-GVHLLPSS 95
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADlRGPSLHRMLGLEN----RPGLSDVLAGEASLEDVIQPTEVeGLDVLPAG 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490732093  96 NELENVETRLKDERFADVkLRRnvvdplIQNGYDYVIIDAAGGrgkLSDNALIAVQRVI 154
Cdd:COG0489  177 PLPPNPSELLASKRLKQL-LEE------LRGRYDYVIIDTPPG---LGVADATLLASLV 225
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 18-196 5.63e-12

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: 64.15  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLD-----KDGHMTTQ--LGYD--DAYDRDANLGDALIDGEDPEdllietdfG 88
Cdd:cd02036    9 KGGVGKTTTTANLGVALAKLGKKVLLIDADiglrnLDLILGLEnrIVYTlvDVLEGECRLEQALIKDKRWE--------N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  89 VHLLPSSNELENVEtrLKDERFADvklrrnVVDPLIQNgYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:cd02036   81 LYLLPASQTRDKDA--LTPEKLEE------LVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDAD 151

                        170       180
                 ....*....|....*....|....*...
gi 490732093 169 KMIERQISPIRQNIGLDILAVTPNMIRE 196
Cdd:cd02036  152 RVIGLLESKGIVNIGLIVNRYRPEMVKS 179
PHA02518 PHA02518
ParA-like protein; Provisional
 18-280 1.57e-10

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 59.48  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDkdghmttqlgyddaydrdanlgdalidgedpedllietdfgvhllPSSNE 97
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLD---------------------------------------------PQGSS 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  98 LENVETRLKDER-FADVKLRRNVVDPLIQ--NGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLNKMIErq 174
Cdd:PHA02518  44 TDWAEAREEGEPlIPVVRMGKSIRADLPKvaSGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVE-- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 175 ispirqnigldilavtpnMIRETMGQRNEHRTlvenlnrefGSFVPEYA----RVDPEIFDALDDSGRtidSIPKPGIRE 250
Cdd:PHA02518 122 ------------------LIKARQEVTDGLPK---------FAFIISRAikntQLYREARKALAGYGL---PILRNGTTQ 171

                        250       260       270
                 ....*....|....*....|....*....|....
gi 490732093 251 RTAISRAFKQGMPVSEFDED----CDQIPNFDHL 280
Cdd:PHA02518 172 RVAYADAAEAGGSVLELPEDdkaaEEIIQLVKEL 205
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 18-194 7.36e-10

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


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 58.12  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLD-------LDKDGHMTTQLGYD--DAYDRDANLGDALIDGEDPEDLlietdfg 88
Cdd:TIGR01968  10 KGGVGKTTTTANLGTALARLGKKVVLIDadiglrnLDLLLGLENRIVYTlvDVVEGECRLQQALIKDKRLKNL------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   89 vHLLPSSnelenvETRLKDErfADVKLRRNVVDPLIQNgYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:TIGR01968  83 -YLLPAS------QTRDKDA--VTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDAD 152

                         170       180
                  ....*....|....*....|....*.
gi 490732093  169 KMIERQISPIRQNIGLDILAVTPNMI 194
Cdd:TIGR01968 153 RVIGLLEAKGIEKIHLIVNRLRPEMV 178
ParA_partition NF041546
ParA family partition ATPase;
18-270 2.11e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.02  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTtqlgydDAYDRDANlgdalidgedpedlliETDFGVHLLPSSNe 97
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL------DWAAARED----------------ERPFPVVGLARPT- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  98 lenvetrlkderfadvkLRRNVvdPLIQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPragsinglnkmierqiSP 177
Cdd:NF041546  65 -----------------LHREL--PSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQP----------------SP 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 178 irqnigLDILAV--TPNMIRETMGQRNEHRT-LVenLNRefgsfVPEYARVDPEIFDALDDSGrtidsIP--KPGIRERT 252
Cdd:NF041546 110 ------YDLWASadTVDLIKEAREYTPGLKAaFV--LNR-----AIARTALGREVAEALAEYG-----LPvlKTRIGQRV 171

                        250
                 ....*....|....*...
gi 490732093 253 AISRAFKQGMPVSEFDED 270
Cdd:NF041546 172 AFAESAAEGLTVFEAEPD 189
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 7-159 5.20e-09

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 56.53  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093    7 EGLPGAAVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAYDRDAN--LGDALIDGEDP---EDL 81
Cdd:TIGR03453 102 EHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDVGENetLYGAIRYDDERrpiSEI 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   82 LIETDF-GVHLLPSSNELENVETR----LKDERFADVKLRRNVVDPL--IQNGYDYVIIDAAGGRGKLSDNALIAVQRVI 154
Cdd:TIGR03453 182 IRKTYFpGLDLVPGNLELMEFEHEtpraLSRGQGGDTIFFARVGEALaeVEDDYDVVVIDCPPQLGFLTLSALCAATGVL 261


                  ....*
gi 490732093  155 IPLIP 159
Cdd:TIGR03453 262 ITVHP 266
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 20-136 7.71e-09

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: 54.11  E-value: 7.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  20 GVGKSTIALNIADRLAARGHETVLLDLD-KDGHMTTQLGYDDAYDrdanLGDALIDGEDPEDLLIETD-FGVHLLPSSNE 97
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADlRRPSLHRLLGLPNEPG----LSEVLSGQASLEDVIQSTNiPNLDVLPAGTV 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490732093  98 LENVETRLKDERFADV--KLRRNvvdpliqngYDYVIIDAA 136
Cdd:cd05387  106 PPNPSELLSSPRFAELleELKEQ---------YDYVIIDTP 137
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 18-209 5.14e-08

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: 52.67  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAAR-GHETVLLDLDkdghmtTQLGYDDAY---DRDANLGDALIDGEDPEDLLIET-----DFG 88
Cdd:cd03111    9 KGGVGASTLAVNLAQELAQRaKDKVLLIDLD------LPFGDLGLYlnlRPDYDLADVIQNLDRLDRTLLDSavtrhSSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  89 VHLLPSSNELENVEtrlkderfadvKLRRNVVDPLIQ---NGYDYVIIDAAGGRGKLSDNALIAVQRVI------IPLIP 159
Cdd:cd03111   83 LSLLPAPQELEDLE-----------ALGAEQVDKLLQvlrAFYDHIIVDLGHFLDEVTLAVLEAADEILlvtqqdLPSLR 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490732093 160 RAGSI---------NG------LNKMIER-QISP--IRQNIGLDILAVTPNMiRETMGQ-RNEHRTLVE 209
Cdd:cd03111  152 NARRLldslrelegSSdrlrlvLNRYDKKsEISPkdIEEALGLEVFATLPND-YKAVSEsANTGRPLVE 219
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 18-155 2.21e-07

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 50.83  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDkdghmttqLG---------------YD--DAYDRDANLGDALIDGEDPED 80
Cdd:COG2894   11 KGGVGKTTTTANLGTALALLGKKVVLIDAD--------IGlrnldlvmglenrivYDlvDVIEGECRLKQALIKDKRFEN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490732093  81 LlietdfgvHLLPSSNelenveTRLKDE-RFADVKlrrNVVDPLIQnGYDYVIIDA-AG-GRGKLsdNALIAVQRVII 155
Cdd:COG2894   83 L--------YLLPASQ------TRDKDAlTPEQMK---KLVEELKE-EFDYILIDSpAGiEQGFK--NAIAGADEAIV 140
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 7-171 3.00e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 51.21  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   7 EGLPGAAVSLLKGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAYDRDANLG-DALIDGEDPE----DL 81
Cdd:PRK13869 119 EHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETlYAAIRYDDTRrplrDV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  82 LIETDF-GVHLLPSSNELENVE----TRLKDERFADVKLRRNVVDPL--IQNGYDYVIIDAAGGRGKLSDNALIAVQRVI 154
Cdd:PRK13869 199 IRPTYFdGLHLVPGNLELMEFEhttpKALSDKGTRDGLFFTRVAQAFdeVADDYDVVVIDCPPQLGFLTLSGLCAATSMV 278

                        170
                 ....*....|....*..
gi 490732093 155 IPLIPRAGSINGLNKMI 171
Cdd:PRK13869 279 ITVHPQMLDIASMSQFL 295
PRK10818 PRK10818
septum site-determining protein MinD;
18-238 4.83e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 49.94  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLD-----KDGHMTTQ--LGYD--DAYDRDANLGDALIDGEDPEDLLIetdfg 88
Cdd:PRK10818  11 KGGVGKTTSSAAIATGLAQKGKKTVVIDFDiglrnLDLIMGCErrVVYDfvNVIQGDATLNQALIKDKRTENLYI----- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  89 vhlLPSSnelenvETRLKDERFADVKlrRNVVDPLIQNGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGSINGLN 168
Cdd:PRK10818  86 ---LPAS------QTRDKDALTREGV--AKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 169 KMI----------ERQISPIRQNigldILAVTPNMIRETMGQRNEHRTLVENLNREFGSFVPEYARV-------DPEIFD 231
Cdd:PRK10818 155 RILgilasksrraENGEEPIKEH----LLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVlrasnqgEPVILD 230


                 ....*..
gi 490732093 232 ALDDSGR 238
Cdd:PRK10818 231 IEADAGK 237
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 18-250 5.71e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 49.39  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAYDRDANLGD--ALI----------------DGED-P 78
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLIKPLGEmrELIkertgapgggmfklnpKVDDiP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  79 EDLLIETDfGVHLL----PSSNEL-----ENvetrlkderfadvKLRRNVVDPLIQNGYDYVIIDA-AG----GRGKLSD 144
Cdd:COG3640   88 EEYLVEGD-GVDLLvmgtIEEGGSgcycpEN-------------ALLRALLNHLVLGNYEYVVVDMeAGiehlGRGTAEG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093 145 -NALIAvqrVIIPlipragSINGLNKMieRQISPIRQNIGLDILAVTPNMIRETmgqrNEHRTLVENLNREFGSFVPEya 223
Cdd:COG3640  154 vDLLLV---VSEP------SRRSIETA--RRIKELAEELGIKKIYLVGNKVREE----EDEEFLRELLGLELLGFIPY-- 216

                        250       260
                 ....*....|....*....|....*..
gi 490732093 224 rvDPEIFDAlDDSGRTIDSIPKPGIRE 250
Cdd:COG3640  217 --DEEVREA-DLEGKPLLDLPDSPAVA 240
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 6-68 6.48e-07

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: 48.55  E-value: 6.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   6 FEGLPGAavsllkggvGKSTIALNIADRLAARGHETVLLDLD-------KDghmttqLGYDDAyDRDANL 68
Cdd:COG0529   21 FTGLSGS---------GKSTLANALERRLFERGRHVYLLDGDnvrhglnKD------LGFSKE-DRDENI 74
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 18-47 6.96e-07

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: 49.37  E-value: 6.96e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLDLD 47
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 13-165 7.73e-07

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: 48.59  E-value: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   13 AVSLLKGGVGKSTIALNIADRLAARGHETVLldLDKDGHMTTQLGYDDAYDRDANLGDALIDGEDPEDLLIETDF-GVHL 91
Cdd:TIGR01007  21 LITSVKPGEGKSTTSANIAIAFAQAGYKTLL--IDGDMRNSVMSGTFKSQNKITGLTNFLSGTTDLSDAICDTNIeNLDV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490732093   92 LPSSNELENVETRLKDERFadvklrRNVVDpLIQNGYDYVIIDAAgGRGKLSDNALIAVQRVIIPLIPRAGSIN 165
Cdd:TIGR01007  99 ITAGPVPPNPTELLQSSNF------KTLIE-TLRKRFDYIIIDTP-PIGTVTDAAIIARACDASILVTDAGKIK 164
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 18-50 2.22e-06

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 47.50  E-value: 2.22e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDG 50
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDADIYG 41
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 18-76 3.20e-05

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: 45.26  E-value: 3.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMT----TQLGYDDAYDRDANLGDALIDGE 76
Cdd:NF041417 341 KGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgTEVGHEPTKVGVENLYAARIDQE 403
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
13-47 4.86e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 44.26  E-value: 4.86e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490732093  13 AVSLLKGGVGKSTIALNIADRLAARGHETVLLDLD 47
Cdd:PRK11670 111 AVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 18-136 8.36e-05

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 43.92  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDdaydrDANLGDALIdgeDPEDLLieTDFGVHLLPSSNE 97
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGS-----LNNLQVSRI---DPKQET--ERYRQEVLATKGK 398

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 490732093   98 ------LENVETRLKD---ERFADVKLRRNVVDpliQNGYDYVIIDAA 136
Cdd:TIGR04291 399 eldedgKAYLEEDLRSpctEEIAVFQAFSRIIR---EAGDRFVVMDTA 443
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 18-78 1.44e-04

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: 42.49  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLldldkdghMTTqlgyddayDRDANLGDAL---IDGEDP 78
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLL--------VST--------DPAHSLSDAFgqkLGGETP 55
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 18-48 1.51e-04

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: 40.11  E-value: 1.51e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLDK 48
Cdd:cd01983    9 KGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 19-181 2.62e-04

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: 41.37  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  19 GGVGKSTIALNIADRLAARGHETVLLDLDKDGHMTTQLGYDDAYD----------RDANLGDALidgedpEDLLIETDFG 88
Cdd:cd17869   13 GGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLmsdhlytlksRKANLADKL------ESCVKQHESG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093  89 VHLLPSSNELENVETRLKDErfadvklrrnvVDPLIQ-----NGYDYVIIDAAGGRGKLSDNALIAVQRVIIPLIPRAGS 163
Cdd:cd17869   87 VYYFSPFKSALDILEIKKDD-----------ILHMITklveaHAYDYIIMDLSFEFSSTVCKLLQASHNNVVIALQDANS 155

                        170
                 ....*....|....*...
gi 490732093 164 INGLNKMIERQISPIRQN 181
Cdd:cd17869  156 SYKLNKFLRALEDLFQEN 173
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 18-157 4.15e-04

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: 40.90  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLDLD-KDGHMTTQLGyddayDRDANLGDALIDGEDPEDLLIEtDFGVHLLPssn 96
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLDlRQRTFHRYFE-----NRSATADRTGLSLPTPEHLNLP-DNDVAEVP--- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490732093   97 ELENVETRLKDERFADVKLRrnvvdpliqngYDYVIIDAAGGRGKLSDNALIAVQRVIIPL 157
Cdd:pfam09140  80 DGENIDDARLEEAFADLEAR-----------CDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
18-47 7.97e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.19  E-value: 7.97e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 490732093  18 KGGVGKSTIALNIADRLAARGHETVLLDLD 47
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTD 40
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 6-68 1.40e-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: 38.23  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   6 FEGLPGAavsllkggvGKSTIALNIADRLAARGHETVLLDLD-------KDghmttqLGYDDAyDRDANL 68
Cdd:cd02027    4 LTGLSGS---------GKSTIARALEEKLFQRGRPVYVLDGDnvrhglnKD------LGFSRE-DREENI 57
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 10-43 2.57e-03

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 38.67  E-value: 2.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 490732093  10 PGAAVsLLKG--GVGKSTIALNIADRLAARGHeTVL 43
Cdd:cd01121   81 PGSVV-LIGGdpGIGKSTLLLQVAARLAQRGG-KVL 114
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 6-68 3.60e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 37.69  E-value: 3.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490732093   6 FEGLPGAavsllkggvGKSTIALNIADRLAARGHETVLLDLDK-DGHMTTQLGYDDAyDRDANL 68
Cdd:PRK00889   9 FTGLSGA---------GKTTIARALAEKLREAGYPVEVLDGDAvRTNLSKGLGFSKE-DRDTNI 62
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 18-47 5.50e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 37.71  E-value: 5.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490732093   18 KGGVGKSTIALNIADRLAARGHETVLLDLD 47
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTD 38
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
9-134 8.43e-03

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 37.19  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490732093   9 LPGAAVSLL--KGGVGKSTIALNIADRLAARGhetvlldldkdghmttqlgydDAYDRDANLGDAL-IDGEDPEDLLIE- 84
Cdd:COG3598   10 LPEGGVTLLagPPGTGKSFLALQLAAAVAAGG---------------------PWLGRRVPPGKVLyLAAEDDRGELRRr 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490732093  85 -TDFGVHL-LPSSNELENVETRLKDERFADVKLRRNVVDPLIQNGYDYVIID 134
Cdd:COG3598   69 lKALGADLgLPFADLDGRLRLLSLAGDLDDTDDLEALERAIEEEGPDLVVID 120
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 6-68 9.57e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 37.22  E-value: 9.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490732093   6 FEGLPGAavsllkggvGKSTIALNIADRLAARGHETVLLDLDKDGH-MTTQLGYDDAyDRDANL 68
Cdd:PRK05506 465 FTGLSGS---------GKSTIANLVERRLHALGRHTYLLDGDNVRHgLNRDLGFSDA-DRVENI 518
 
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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