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Conserved domains on  [gi|490212002|ref|WP_004110398|]
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MULTISPECIES: ParA family protein [Gardnerella]

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 ...
 25-275 9.07e-115

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: 330.28  E-value: 9.07e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANALDNTVYTALFDSsVDVHDVIRHTETE 104
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDD-APLEDAIVPTEIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 105 NIDIIPANIDLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVAL 184
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 185 LMQSIEKVQSRINPNLKVFGVLVTMY-TRTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAK 263
Cdd:COG1192  160 LLETIEEVREDLNPKLEILGILLTMVdPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAK 239

                        250
                 ....*....|..
gi 490212002 264 EYREVARELIAK 275
Cdd:COG1192  240 AYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 25-275 9.07e-115

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: 330.28  E-value: 9.07e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANALDNTVYTALFDSsVDVHDVIRHTETE 104
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDD-APLEDAIVPTEIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 105 NIDIIPANIDLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVAL 184
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 185 LMQSIEKVQSRINPNLKVFGVLVTMY-TRTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAK 263
Cdd:COG1192  160 LLETIEEVREDLNPKLEILGILLTMVdPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAK 239

                        250
                 ....*....|..
gi 490212002 264 EYREVARELIAK 275
Cdd:COG1192  240 AYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 25-202 1.53e-80

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: 240.56  E-value: 1.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANALDNTVYTALFDSSvDVHDVIRHTETE 104
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGEC-NIEEAIIKTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  105 NIDIIPANIDLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVAL 184
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQ 159

                         170
                  ....*....|....*...
gi 490212002  185 LMQSIEKVQSRINPNLKV 202
Cdd:pfam13614 160 LLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 26-223 2.06e-40

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: 136.52  E-value: 2.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLginanaldntvytalfdssvdvhdvirhteten 105
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 106 idiipanidlsaaevqlvtevgreqilagvlrkvrdeYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALL 185
Cdd:cd02042   48 -------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKL 90

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490212002 186 MQSIEKVQSRINPNLKVFGVLVTMY-TRTLHSEEVLQRI 223
Cdd:cd02042   91 LDTLEELKKQLNPPLLILGILLTRVdPRTKLAREVLEEL 129
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 27-171 1.85e-29

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: 114.69  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINAN---ALDNTVYTAL-FDSS-VDVHDVIRHT 101
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEfdvGENETLYGAIrYDDErRPISEIIRKT 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490212002  102 ETENIDIIPANIDLSAAEVQ----LVTEVGREQI----LAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIP 171
Cdd:TIGR03453 186 YFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLIT 263
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 26-245 5.54e-25

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 102.83  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINAN---ALDNTVYTAL-FDSS-VDVHDVIRH 100
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtdvGANETLYAAIrYDDTrRPLRDVIRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 101 TETENIDIIPANIDLSAAE----VQLVTEVGREQI----LAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVII-- 170
Cdd:PRK13869 202 TYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVItv 281

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490212002 171 -PLAAEFFALRGVALLMQSIEKVQSRINPNLK--VFGVLVTMYT-RTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDS 245
Cdd:PRK13869 282 hPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQydFIRYLLTRYEpQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDA 360
ParA_partition NF041546
ParA family partition ATPase;
27-271 5.39e-23

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 93.39  E-value: 5.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAAtvgLGINANALDNTVYTalfdssvdvhdvirhteteni 106
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA---LDWAAAREDERPFP--------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 107 diipanidlsaaevqlVTEVGREQiLAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALLM 186
Cdd:NF041546  57 ----------------VVGLARPT-LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 187 QSIEKVQsRINPNLKVFGVLVTMYTRTLHSEEVLQRIyEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAKEYR 266
Cdd:NF041546 120 DLIKEAR-EYTPGLKAAFVLNRAIARTALGREVAEAL-AEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIR 197


                 ....*
gi 490212002 267 EVARE 271
Cdd:NF041546 198 ALAKE 202
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 25-275 9.07e-115

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: 330.28  E-value: 9.07e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANALDNTVYTALFDSsVDVHDVIRHTETE 104
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDD-APLEDAIVPTEIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 105 NIDIIPANIDLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVAL 184
Cdd:COG1192   80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 185 LMQSIEKVQSRINPNLKVFGVLVTMY-TRTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAK 263
Cdd:COG1192  160 LLETIEEVREDLNPKLEILGILLTMVdPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAK 239

                        250
                 ....*....|..
gi 490212002 264 EYREVARELIAK 275
Cdd:COG1192  240 AYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 25-202 1.53e-80

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: 240.56  E-value: 1.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANALDNTVYTALFDSSvDVHDVIRHTETE 104
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGEC-NIEEAIIKTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  105 NIDIIPANIDLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVAL 184
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQ 159

                         170
                  ....*....|....*...
gi 490212002  185 LMQSIEKVQSRINPNLKV 202
Cdd:pfam13614 160 LLNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 28-245 8.16e-49

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: 161.36  E-value: 8.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   28 IAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAAT--VGLGINANALDNTVYTALFdSSVDVHDVI--RHTET 103
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLK-GRVNLDPILlkEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  104 ENIDIIPANIDLSAAEVQLVTEVGREQILAgVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVA 183
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELLGPRKEERLRE-ALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490212002  184 LLMQSIEKVQSRINP-NLKVFGVLVTMYTRTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDS 245
Cdd:pfam01656 159 RLGGVIAALVGGYALlGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRDEAVAEA 221
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 26-223 2.06e-40

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: 136.52  E-value: 2.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLginanaldntvytalfdssvdvhdvirhteten 105
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 106 idiipanidlsaaevqlvtevgreqilagvlrkvrdeYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALL 185
Cdd:cd02042   48 -------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKL 90

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490212002 186 MQSIEKVQSRINPNLKVFGVLVTMY-TRTLHSEEVLQRI 223
Cdd:cd02042   91 LDTLEELKKQLNPPLLILGILLTRVdPRTKLAREVLEEL 129
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 27-171 1.85e-29

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: 114.69  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINAN---ALDNTVYTAL-FDSS-VDVHDVIRHT 101
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEfdvGENETLYGAIrYDDErRPISEIIRKT 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490212002  102 ETENIDIIPANIDLSAAEVQ----LVTEVGREQI----LAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIP 171
Cdd:TIGR03453 186 YFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGVLIT 263
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 41-279 3.24e-29

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: 110.75  E-value: 3.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  41 TSSINIAGALSQYGRRVLIVDFDPQGA-ATVGLGINANAldnTVYTALfDSSVDVHDVIRHTEtENIDIIPANIDLSAAE 119
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLAnLDVLLGLEPKA---TLADVL-AGEADLEDAIVQGP-GGLDVLPGGSGPAELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 120 vqlvtEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALLMQSIEKVQSRinpn 199
Cdd:COG0455   76 -----ELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGV---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 200 lKVFGVLVTMYTRTLHSEEVLQRIyEAFQDRVLHS------VISRSIKLPDSTVAAVPITIFAPEHKTAKEYREVARELI 273
Cdd:COG0455  147 -RRAGVVVNRVRSEAEARDVFERL-EQVAERFLGVrlrvlgVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLA 224


                 ....*.
gi 490212002 274 AKGVVA 279
Cdd:COG0455  225 GWPVPE 230
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 26-245 5.54e-25

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 102.83  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINAN---ALDNTVYTAL-FDSS-VDVHDVIRH 100
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtdvGANETLYAAIrYDDTrRPLRDVIRP 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 101 TETENIDIIPANIDLSAAE----VQLVTEVGREQI----LAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVII-- 170
Cdd:PRK13869 202 TYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVItv 281

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490212002 171 -PLAAEFFALRGVALLMQSIEKVQSRINPNLK--VFGVLVTMYT-RTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDS 245
Cdd:PRK13869 282 hPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQydFIRYLLTRYEpQDAPQTKVAALLRNMFEDHVLTNPMVKSAAVSDA 360
ParA_partition NF041546
ParA family partition ATPase;
27-271 5.39e-23

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 93.39  E-value: 5.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAAtvgLGINANALDNTVYTalfdssvdvhdvirhteteni 106
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSA---LDWAAAREDERPFP--------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 107 diipanidlsaaevqlVTEVGREQiLAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALLM 186
Cdd:NF041546  57 ----------------VVGLARPT-LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 187 QSIEKVQsRINPNLKVFGVLVTMYTRTLHSEEVLQRIyEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAKEYR 266
Cdd:NF041546 120 DLIKEAR-EYTPGLKAAFVLNRAIARTALGREVAEAL-AEYGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIR 197


                 ....*
gi 490212002 267 EVARE 271
Cdd:NF041546 198 ALAKE 202
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 23-279 1.76e-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: 92.48  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  23 GPARIIAMCNQKGGVGKTTSSINIAGALSQ-YGRRVLIVDFDPQ-GAATVGLGINAnalDNTVYTALFD-SSVDVHDVIR 99
Cdd:COG4963  100 RRGRVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQfGDVALYLDLEP---RRGLADALRNpDRLDETLLDR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 100 --HTETENIDIIPANIDLSAAEvqlvtEVGREQILAgVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFF 177
Cdd:COG4963  177 alTRHSSGLSVLAAPADLERAE-----EVSPEAVER-LLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLP 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 178 ALRGVALLMQSIEkvqsRINPNLKVFGVLVTMYTRtlHSEEVLQRIYEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAP 257
Cdd:COG4963  251 SLRNAKRLLDLLR----ELGLPDDKVRLVLNRVPK--RGEISAKDIEEALGLPVAAVLPNDPKAVAEAANQGRPLAEVAP 324

                        250       260
                 ....*....|....*....|..
gi 490212002 258 EHKTAKEYREVARELIAKGVVA 279
Cdd:COG4963  325 KSPLAKAIRKLAARLTGRPAAA 346
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 26-272 2.60e-20

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: 86.87  E-value: 2.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpqgaatVGLginAN-----ALDNTVytalfdsSVDVHDV--- 97
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD------IGL---RNldlilGLENRI-------VYTLVDVleg 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  98 --------IRHTETENIDIIPANIDLSAaevqlvTEVGREQiLAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVI 169
Cdd:cd02036   65 ecrleqalIKDKRWENLYLLPASQTRDK------DALTPEK-LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAI 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 170 IPLAAEFFALRG---VALLMQSIEKvqsrinpnlKVFGVLVTMYTRTLHSEEV---LQRIYEAFQDRVLhSVISRSIKLP 243
Cdd:cd02036  138 IVTNPEISSVRDadrVIGLLESKGI---------VNIGLIVNRYRPEMVKSGDmlsVEDIQEILGIPLL-GVIPEDPEVI 207

                        250       260
                 ....*....|....*....|....*....
gi 490212002 244 DSTVAAVPITIFAPEHKTAKEYREVAREL 272
Cdd:cd02036  208 VATNRGEPLVLYKPNSLAAKAFENIARRL 236
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 27-236 1.37e-19

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 87.34  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVD-FDPQGAATV------GLGINANaldNTVYTALFDSSVDVHDVIR 99
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMyhgwvpDLHIHAE---DTLLPFYLGEKDDATYAIK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 100 HTETENIDIIPANIDLSAAEVQLVTE-------VGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPL 172
Cdd:PRK13705 185 PTCWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPT 264

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490212002 173 AAEFF----ALRGVALLMQSIEKVQSR-INPNLKvfgVLVTMYTRTLHSEE--VLQRIYEAFQDRVLHSVI 236
Cdd:PRK13705 265 PAELFdytsALQFFDMLRDLLKNVDLKgFEPDVR---ILLTKYSNSNGSQSpwMEEQIRDAWGSMVLKNVV 332
PHA02518 PHA02518
ParA-like protein; Provisional
 26-272 2.16e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 84.13  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGaatvglginanaldntvytalfdSSVDVHDVIRHTEten 105
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQG-----------------------SSTDWAEAREEGE--- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 106 iDIIPanidlsaaevqlVTEVGREqiLAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALL 185
Cdd:PHA02518  55 -PLIP------------VVRMGKS--IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDL 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 186 MQSIEKVQSrINPNLKVFGVLVTMYTRTLHSEEVLQRIYEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTAKEY 265
Cdd:PHA02518 120 VELIKARQE-VTDGLPKFAFIISRAIKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEI 198


                 ....*..
gi 490212002 266 REVAREL 272
Cdd:PHA02518 199 IQLVKEL 205
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 26-273 6.51e-19

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: 83.63  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpQGAATVGLGINANALDNTVYTALFDSSvDVHDVIRHTETeN 105
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD-ITMANLELILGMEDKPVTLHDVLAGEA-DIKDAIYEGPF-G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  106 IDIIPANIDLSAaevqlvTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRGVALL 185
Cdd:TIGR01969  78 VKVIPAGVSLEG------LRKADPDKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  186 MQSIEKVqsrinpNLKVFGVLVTMYTRT---LHSEEVlqriyEAFQDRVLHSVISRSIKLPDSTVAAVPITIFAPEHKTA 262
Cdd:TIGR01969 152 KIVAEKL------GTAILGVVLNRVTRDkteLGREEI-----ETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAA 220

                         250
                  ....*....|.
gi 490212002  263 KEYREVARELI 273
Cdd:TIGR01969 221 QAFMELAAELA 231
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 27-236 7.97e-19

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 85.06  E-value: 7.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVD-FDPQGAATV------GLGINAnalDNTVYTALFDSSVDVHDVIR 99
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMyhgyvpDLHIHA---DDTLLPFYLGERDNAEYAIK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 100 HTETENIDIIPANIDLSAAEVQLVTEVGREQI-------LAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPL 172
Cdd:PHA02519 185 PTCWPGLDIIPSCLALHRIETDLMQYHDAGKLphpphlmLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVAT 264

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490212002 173 AAEFF----ALRGVALLMQSIEKVQ-SRINPNLKvfgVLVTMYTRTL--HSEEVLQRIYEAFQDRVLHSVI 236
Cdd:PHA02519 265 PAELFdyvsVLQFFTMLLDLLATVDlGGFEPVVR---LLLTKYSLTVgnQSRWMEEQIRNTWGSMVLRQVV 332
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 27-275 1.07e-16

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


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 77.39  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGA--------ATVGLGINANALDNTVYTALFDSSVDVHDVI 98
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLlrlhfgmdWSVRDGWARALLNGADWAAAAYRSPDGVLFL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   99 RHTEtenidiipanIDLSAAEVQLVTEVGreqILAGVLRKV-RDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFF 177
Cdd:TIGR03371  83 PYGD----------LSADEREAYQAHDAG---WLARLLQQLdLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  178 AlrgVALLMQSIEKVQSRINPNLKVfGVLVTMY--TRTLHS--EEVLQRIYEafqDRVLHSVISRSIKLPDSTVAAVPIT 253
Cdd:TIGR03371 150 C---YATLHQLALALFAGSGPRDGP-RFLINQFdpARQLSRdvRAVLRQTLG---SRLLPFVIHRDEAVSEALARGTPVL 222

                         250       260
                  ....*....|....*....|..
gi 490212002  254 IFAPEHKTAKEYREVARELIAK 275
Cdd:TIGR03371 223 NYAPHSQAAHDIRTLAGWLLSK 244
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 24-209 1.49e-16

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: 77.53  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  24 PARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFD---PQGAATVGLGINANALDntvytaLFDSSVDVHDVIRH 100
Cdd:COG0489   91 LLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENRPGLSD------VLAGEASLEDVIQP 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 101 TETENIDIIPANIDLSAAEVQLVTEVgreqiLAGVLRKVRDEYDVIIVDCQPslGLLTVNALTAA---DGVIIPLAAEFF 177
Cdd:COG0489  165 TEVEGLDVLPAGPLPPNPSELLASKR-----LKQLLEELRGRYDYVIIDTPP--GLGVADATLLAslvDGVLLVVRPGKT 237

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490212002 178 ALRGVALLMQSIEKVqsrinpNLKVFGVLVTM 209
Cdd:COG0489  238 ALDDVRKALEMLEKA------GVPVLGVVLNM 263
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 26-262 6.24e-16

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: 74.91  E-value: 6.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpQGAATV----GLGINANALDntvytaLFDSSVDVHDVIRHT 101
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD-LGLANLdillGLAPKKTLGD------VLKGRVSLEDIIVEG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 102 eTENIDIIPANIDLSaaEVQLVTEVGREQILaGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFFALRG 181
Cdd:cd02038   74 -PEGLDIIPGGSGME--ELANLDPEQKAKLI-EELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 182 VALLMQSIEKVQSRINpnlkvFGVLVTMyTRTLHSE----EVLQRIYEAFQDRVLHSV--ISRSIKLPDSTVAAVPITIF 255
Cdd:cd02038  150 AYALIKVLSRRGGKKN-----FRLIVNM-ARSPKEGratfERLKKVAKRFLDINLDFVgfIPYDQSVRRAVRSQKPFVLL 223


                 ....*..
gi 490212002 256 APEHKTA 262
Cdd:cd02038  224 FPNSKAS 230
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 19-196 1.49e-15

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: 72.99  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  19 LTSHGPARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDP-QGAATVGLGINAnalDNTVYTALFDSSvDVHDV 97
Cdd:cd05387   13 AGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPN---EPGLSEVLSGQA-SLEDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  98 IRHTETENIDIIPANidlsaAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNAL-TAADGVIIPLAAEF 176
Cdd:cd05387   89 IQSTNIPNLDVLPAG-----TVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDGVLLVVRAGK 163

                        170       180
                 ....*....|....*....|
gi 490212002 177 FALRGVALLMQSIEKVQSRI 196
Cdd:cd05387  164 TRRREVKEALERLEQAGAKV 183
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 26-198 9.32e-14

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: 68.84  E-value: 9.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQY-GRRVLIVDFD-PQGAATVGLGINA--------NALDNTVYTALFDSSVdvh 95
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDlPFGDLGLYLNLRPdydladviQNLDRLDRTLLDSAVT--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  96 dviRHTETenIDIIPANIDLSAAEvqlvtEVGREQILAgVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAE 175
Cdd:cd03111   78 ---RHSSG--LSLLPAPQELEDLE-----ALGAEQVDK-LLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQD 146

                        170       180
                 ....*....|....*....|...
gi 490212002 176 FFALRGVALLMQSIEKVQSRINP 198
Cdd:cd03111  147 LPSLRNARRLLDSLRELEGSSDR 169
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 25-170 1.34e-13

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 68.93  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpqgaatVGL-------GinanaLDN-TVYTAlfdssVDV-- 94
Cdd:COG2894    2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD------IGLrnldlvmG-----LENrIVYDL-----VDVie 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  95 ------HDVIRHTETENIDIIPA--NIDLSAaevqlVTEvgrEQILAgVLRKVRDEYDVIIVDCqPS---LGLLtvNALT 163
Cdd:COG2894   66 gecrlkQALIKDKRFENLYLLPAsqTRDKDA-----LTP---EQMKK-LVEELKEEFDYILIDS-PAgieQGFK--NAIA 133


                 ....*..
gi 490212002 164 AADGVII 170
Cdd:COG2894  134 GADEAIV 140
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 25-277 5.70e-13

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: 66.98  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpqgaatVGLGiNAN---ALDN-TVYTAlfdssVDV------ 94
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD------IGLR-NLDlllGLENrIVYTL-----VDVvegecr 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   95 --HDVIRHTETENIDIIPanidlsAAEVQLVTEVGREQILAgVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADGVIIPL 172
Cdd:TIGR01968  69 lqQALIKDKRLKNLYLLP------ASQTRDKDAVTPEQMKK-LVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  173 AAEFFALRG----VALL-MQSIEKVQ---SRINPNLKVFGVLVTMytrtlhsEEVLQRIYEAfqdrvLHSVISRSIKLPD 244
Cdd:TIGR01968 142 TPEVSAVRDadrvIGLLeAKGIEKIHlivNRLRPEMVKKGDMLSV-------DDVLEILSIP-----LIGVIPEDEAIIV 209

                         250       260       270
                  ....*....|....*....|....*....|...
gi 490212002  245 STVAAVPItIFAPEHKTAKEYREVARELIAKGV 277
Cdd:TIGR01968 210 STNKGEPV-VLNDKSRAGKAFENIARRILGEEV 241
PRK10818 PRK10818
septum site-determining protein MinD;
25-180 4.72e-11

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 61.88  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  25 ARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpqgaatVGL-------GINANALDNTVYTALFDSSVDvHDV 97
Cdd:PRK10818   2 ARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD------IGLrnldlimGCERRVVYDFVNVIQGDATLN-QAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  98 IRHTETENIDIIPANidlSAAEVQLVTEVGREQILAGVLRKvrdEYDVIIVDCQPSLGLLTVNALTAADGVIIPLAAEFF 177
Cdd:PRK10818  75 IKDKRTENLYILPAS---QTRDKDALTREGVAKVLDDLKAM---DFEFIVCDSPAGIETGALMALYFADEAIITTNPEVS 148


                 ...
gi 490212002 178 ALR 180
Cdd:PRK10818 149 SVR 151
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 26-196 1.32e-09

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: 56.68  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGaaTVGLGINANALDNTVYTALFDSSVDVHDVIRHTETEN 105
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN--SVMSGTFKSQNKITGLTNFLSGTTDLSDAICDTNIEN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  106 IDIIPA-----NidlsaaevqlVTEVGREQILAGVLRKVRDEYDVIIVDCQPsLGLLTVNALTA--ADGVIIPLAAEFFA 178
Cdd:TIGR01007  96 LDVITAgpvppN----------PTELLQSSNFKTLIETLRKRFDYIIIDTPP-IGTVTDAAIIAraCDASILVTDAGKIK 164

                         170
                  ....*....|....*...
gi 490212002  179 LRGVALLMQSIEKVQSRI 196
Cdd:TIGR01007 165 KREVKKAKEQLEQAGSNF 182
minD CHL00175
septum-site determining protein; Validated
 20-180 4.50e-09

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 55.93  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  20 TSHGPARIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDpqgaatVGLGiNAN---ALDNTV-YTALfdssvDVH 95
Cdd:CHL00175  10 KSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD------IGLR-NLDlllGLENRVlYTAM-----DVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  96 D--------VIRHTETENIDIipanidLSAAEVQLVTEVGREQILAGVLRKVRDEYDVIIVDCQPSLGLLTVNALTAADG 167
Cdd:CHL00175  78 EgecrldqaLIRDKRWKNLSL------LAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQE 151

                        170
                 ....*....|...
gi 490212002 168 VIIPLAAEFFALR 180
Cdd:CHL00175 152 AIVVTTPEITAIR 164
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
24-236 1.57e-08

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 54.44  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  24 PARIIaMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPqgAATVGlginaNALDntvytalfdssVDVHDVIRHTET 103
Cdd:COG0003    2 MTRII-FFTGKGGVGKTTVAAATALALAERGKRTLLVSTDP--AHSLG-----DVLG-----------TELGNEPTEVAV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 104 ENIDIipANID-------------------LSAAEVQLVTEV--GREQILAgvLRKVRD-----EYDVIIVDCQPS---L 154
Cdd:COG0003   63 PNLYA--LEIDpeaeleeywervraplrglLPSAGVDELAESlpGTEELAA--LDELLElleegEYDVIVVDTAPTghtL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 155 GLLTV-NALTAADGVIIPLaaeffaLRGVALLMQSIEKVQSriNPNLKVFGVLVTMYTRtlhseevLQRIYEAFQDRVLH 233
Cdd:COG0003  139 RLLSLpELLGWWLDRLLKL------RRKASGLGRPLAGILG--LPDDPVLEGLEELRER-------LERLRELLRDPERT 203


                 ...
gi 490212002 234 SVI 236
Cdd:COG0003  204 SFR 206
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 34-158 2.05e-08

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: 53.67  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPqgAATVG--LGINanaLDNTVYTALFD----SSVDVHDVIRhtetENID 107
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDP--AHSLSdaFGQK---LGGETPVKGAPnlwaMEIDPEEALE----EYWE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490212002 108 IIPANIDLSAAEVQLVTEVGREQ-ILAG-----VLRKVRD-----EYDVIIVDCQP---SLGLLT 158
Cdd:cd02035   79 EVKELLAQYLRLPGLDEVYAEELlSLPGmdeaaAFDELREyvesgEYDVIVFDTAPtghTLRLLS 143
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 34-203 9.02e-07

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: 49.27  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDP----QGAATVGLGINANALDNTVYTALFDSSVDVHdvirhtETENIDII 109
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPahslSDSFNQKFGHEPTKVKENLSAMEIDPNMELE------EYWQEVQK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  110 PANIDLSAAEVQLVTEV------GREQILA--GVLRKVR-DEYDVIIVDCQP---SLGLLT--------VNALTAADGVI 169
Cdd:pfam02374  83 YMNALLGLRMLEGILAEelaslpGIDEAASfdEFKKYMDeGEYDVVVFDTAPtghTLRLLSlptvlgwyLEKIVKLKNQI 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 490212002  170 IPLAAEFFALRGVAL--LMQSIEKVQSRINPNLKVF 203
Cdd:pfam02374 163 GPLAKPFLGMGGVSIpeALESLEETKERIERAREIL 198
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 26-63 1.73e-06

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 45.88  E-value: 1.73e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFD 63
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 26-63 5.12e-06

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 46.68  E-value: 5.12e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 490212002   26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFD 63
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 34-72 9.25e-06

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 45.82  E-value: 9.25e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGL 72
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
27-63 9.47e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 46.19  E-value: 9.47e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490212002  27 IIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFD 63
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
26-273 1.28e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.51  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002   26 RIIAMCNqKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGL--GINANALDNTVYTALFDSSVDVHDVIrHTET 103
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLlgGKLQPTVLDTAREKGYVEDVEVEDVV-YKGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  104 ENIDIipanIDLSAAEVQlVTEVGREQILAGVLRK---VRDEYDVIIVDCqpsLGLLTVNALTA------ADGVIIPLAA 174
Cdd:pfam00142  79 GGVKC----VESGGPEPG-VGCAGRGVITAINLLEelgAYDDLDFVLYDV---LGDVVCGGFAMpiregkAQEIYIVTSN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  175 EFFALRGVALLMQSIEKVQSRINPNLkvfGVLVTMYTRTLHSEEVLQRIYEAFQDRVLHsVISRSIKLPDSTVAAVPITI 254
Cdd:pfam00142 151 EMMALYAANNIAKGIQKYAKSGGVRL---GGIICNSRKVDDERELIDAFAEELGTQVLH-FVPRDNIVRKAELRKQTVIE 226

                         250
                  ....*....|....*....
gi 490212002  255 FAPEHKTAKEYREVARELI 273
Cdd:pfam00142 227 YAPDSEQAQEYRELARKIL 245
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 27-151 2.00e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 44.77  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  27 IIAMCNqKGGVGKTTSSINIAGALSQYGRRVLIVDFDPqgaatvglgiNAN---ALDNTVYTALFDSSVDVHDVIRH-TE 102
Cdd:COG3640    2 KIAVAG-KGGVGKTTLSALLARYLAEKGKPVLAVDADP----------NANlaeALGLEVEADLIKPLGEMRELIKErTG 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 103 TENIDIIPANIDLSAAEVQLVTEVGR---------EQ-----------ILAGVLRK-VRDEYDVIIVDCQ 151
Cdd:COG3640   71 APGGGMFKLNPKVDDIPEEYLVEGDGvdllvmgtiEEggsgcycpenaLLRALLNHlVLGNYEYVVVDME 140
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 34-73 2.28e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 44.76  E-value: 2.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLG 73
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 34-95 3.19e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.18  E-value: 3.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLginANALDNTVYTALfdSSVDVH 95
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTL---TGKLVPTVIDIL--EEVDFH 66
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 34-64 5.55e-05

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: 43.66  E-value: 5.55e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDP 64
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
PRK09841 PRK09841
tyrosine-protein kinase;
26-193 7.12e-05

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 44.13  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGaatvglGINANALDNTVYTAL---FDSSVDVHDVIRHTE 102
Cdd:PRK09841 532 NILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRR------GYSHNLFTVSNEHGLseyLAGKDELNKVIQHFG 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002 103 TENIDIIP-ANIDLSAAEVqLVTEVGREqilagVLRKVRDEYDVIIVDCQPSLGLltVNALTAADGVIIPLAAEFFALRG 181
Cdd:PRK09841 606 KGGFDVITrGQVPPNPSEL-LMRDRMRQ-----LLEWANDHYDLVIVDTPPMLAV--SDAAVVGRSVGTSLLVARFGLNT 677

                        170
                 ....*....|..
gi 490212002 182 VALLMQSIEKVQ 193
Cdd:PRK09841 678 AKEVSLSMQRLE 689
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 34-149 7.30e-05

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 43.44  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLginANALDNTVYTALfdSSVDVH-------DVIrHTETENI 106
Cdd:cd02032    8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTL---TGFLIPTVIDVL--QSVDFHyeevwpeDVI-FTGYGGV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490212002 107 DIIPANIDLSAA---------EVQLVTEVGreqilagvlrkVRDEYDVIIVD 149
Cdd:cd02032   82 DCVEAGGPPAGTgcggyvvgeTVKLLKELN-----------AFDEYDVILFD 122
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 26-63 9.84e-05

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: 42.49  E-value: 9.84e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFD 63
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
chlL CHL00072
photochlorophyllide reductase subunit L
 34-72 1.39e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.42  E-value: 1.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGL 72
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTL 46
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 34-71 2.60e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 42.00  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 490212002   34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPqgAATVG 71
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDP--ASNVG 46
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
36-154 3.14e-04

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 42.06  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  36 GVGKTTSSINIAGALSQYGRRVLIVDFD-PQGAATVGLGI-NANALdntvyTALFDSSVDVHDVIRHTETENIDIIP-AN 112
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDmRKGYTHELLGTnNVNGL-----SDILIGQGDITTAAKPTSIANFDLIPrGQ 611

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490212002 113 IDLSAAEVqLVTEvgreqILAGVLRKVRDEYDVIIVDCQPSL 154
Cdd:PRK11519 612 VPPNPSEL-LMSE-----RFAELVNWASKNYDLVLIDTPPIL 647
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 26-64 5.05e-04

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: 40.76  E-value: 5.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 490212002  26 RIIAMCNqKGGVGKTTSSINIAGALSQYGRRVLIVDFDP 64
Cdd:cd02034    1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADP 38
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 26-171 5.53e-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: 40.22  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490212002  26 RIIAMCNQKGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGLGINANAL-DNTVYTALFDS---SVDVHDVIRHT 101
Cdd:cd17869    4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRYLmSDHLYTLKSRKanlADKLESCVKQH 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490212002 102 EtENIDIIPanidlSAAEVQLVTEVGREQI--LAGVLRKVrDEYDVIIVDCQPSLGLLTVNALTAADGVIIP 171
Cdd:cd17869   84 E-SGVYYFS-----PFKSALDILEIKKDDIlhMITKLVEA-HAYDYIIMDLSFEFSSTVCKLLQASHNNVVI 148
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 34-93 2.91e-03

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


Pssm-ID: 349771  Cd Length: 155  Bit Score: 37.32  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490212002  34 KGGVGKTTSSINIAGALSQYGRRVLIVDFDPQGAATVGL-GINANALD----NTVYTALFDSSVD 93
Cdd:cd05386    9 KGGVGKSVIASLLAQYLIDKGQPVSCIDTDPVNKTFAGYkALNVQRINiidnDEIIQSKFDQLVE 73
 
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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