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Conserved domains on  [gi|149935804|gb|ABR42501|]
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chromosome-partitioning ATPase [Parabacteroides distasonis ATCC 8503]

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

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 ...
 4-252 1.52e-111

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: 321.04  E-value: 1.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFS-AELPQTIYGAMKGEYDLP---IYEHKDG 79
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDpDDLDPTLYDLLLDDAPLEdaiVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  80 LRVVPSCLDLSAVETELINEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 160 MQVVHKVQQRLNSDLSIAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAED 239
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|...
gi 149935804 240 YEKVCNELLTEIK 252
Cdd:COG1192  241 YRALAEELLERLE 253
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 4-252 1.52e-111

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: 321.04  E-value: 1.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFS-AELPQTIYGAMKGEYDLP---IYEHKDG 79
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDpDDLDPTLYDLLLDDAPLEdaiVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  80 LRVVPSCLDLSAVETELINEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 160 MQVVHKVQQRLNSDLSIAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAED 239
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|...
gi 149935804 240 YEKVCNELLTEIK 252
Cdd:COG1192  241 YRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 4-176 2.53e-66

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: 203.58  E-value: 2.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSA-ELPQTIYGAMKGEYDLP---IYEHKDG 79
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKnNVEKTIYELLIGECNIEeaiIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   80 LRVVPSCLDLSAVETELINEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 149935804  160 MQVVHKVQQRLNSDLSI 176
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-199 1.55e-49

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: 158.86  E-value: 1.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLgfsaelpqtiygamkgeydlpiyehkdglrvvp 84
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  85 scldlsavetelineagrelilahlikgqkekFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVH 164
Cdd:cd02042   48 --------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLE 95

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 149935804 165 KVQQRLNSDLSIAGVLITQYDGRKNLNKSVSELVQ 199
Cdd:cd02042   96 ELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-185 2.16e-35

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: 129.71  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    3 KAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSAELP----QTIYGAMKgeYD---LPIYE 75
Cdd:TIGR03453 103 HLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDvgenETLYGAIR--YDderRPISE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   76 -----HKDGLRVVPSCLDLSAVETE----LINEAGRELI----LAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRL 142
Cdd:TIGR03453 181 iirktYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGV 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149935804  143 IIPVQ---------AQFLAMrgMAKLMQVVHKVQQRLNSDLsiAGVLITQYD 185
Cdd:TIGR03453 261 LITVHpqmldvmsmSQFLLM--TGDLLGVVREAGGNLSYDF--MRYLVTRYE 308
ParA_partition NF041546
ParA family partition ATPase;
6-246 7.43e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 110.72  E-value: 7.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTEslgfsaelpqtiYGAMKgeydlpiyEHKDGLRVVps 85
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALD------------WAAAR--------EDERPFPVV-- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  86 clDLSAVEtelineagreliLAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVHK 165
Cdd:NF041546  59 --GLARPT------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKE 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 166 VqQRLNSDLSiAGVLITQYDGRKNLNKSVSELVQEtFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAEDYEKVCN 245
Cdd:NF041546 125 A-REYTPGLK-AAFVLNRAIARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAK 201


                 .
gi 149935804 246 E 246
Cdd:NF041546 202 E 202
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-247 1.09e-28

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 112.08  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSAELP----QTIYGAMKgeYD---LPIYE-- 75
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDvganETLYAAIR--YDdtrRPLRDvi 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  76 ---HKDGLRVVPSCLDLSAVE----TELINEAGRELI----LAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLII 144
Cdd:PRK13869 200 rptYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 145 PVQAQFLAMRGMAK-------LMQVVHKVQQRLNSDLsiAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITL 217
Cdd:PRK13869 280 TVHPQMLDIASMSQfllmtrdLLGVVKEAGGNLQYDF--IRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAV 357

                        250       260       270
                 ....*....|....*....|....*....|
gi 149935804 218 AEAPTQGQDIFHYAPKSAGAEDYEKVCNEL 247
Cdd:PRK13869 358 SDAGLTKQTLYEIGRENLTRSTYDRAMESL 387
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 4-252 1.52e-111

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: 321.04  E-value: 1.52e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFS-AELPQTIYGAMKGEYDLP---IYEHKDG 79
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDpDDLDPTLYDLLLDDAPLEdaiVPTEIPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  80 LRVVPSCLDLSAVETELINEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:COG1192   81 LDLIPANIDLAGAEIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 160 MQVVHKVQQRLNSDLSIAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAED 239
Cdd:COG1192  161 LETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKA 240

                        250
                 ....*....|...
gi 149935804 240 YEKVCNELLTEIK 252
Cdd:COG1192  241 YRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 4-176 2.53e-66

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: 203.58  E-value: 2.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSA-ELPQTIYGAMKGEYDLP---IYEHKDG 79
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKnNVEKTIYELLIGECNIEeaiIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   80 LRVVPSCLDLSAVETELINEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 149935804  160 MQVVHKVQQRLNSDLSI 176
Cdd:pfam13614 161 LNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 7-227 8.21e-53

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: 170.60  E-value: 8.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    7 ISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLG---FSAELPQTIYGAMKGEYDLP--IYEHK---D 78
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGlegDIAPALQALAEGLKGRVNLDpiLLKEKsdeG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   79 GLRVVPSCLDLSAVETELINEAGRELILAHLiKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAK 158
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERLREAL-EALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  159 LMQVVHKVQQRLNS-DLSIAGVLITQYDGRkNLNKSVSELVQETFQGKVFSTHIRNAITLAEAPTQGQDI 227
Cdd:pfam01656 160 LGGVIAALVGGYALlGLKIIGVVLNKVDGD-NHGKLLKEALEELLRGLPVLGVIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-199 1.55e-49

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: 158.86  E-value: 1.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLgfsaelpqtiygamkgeydlpiyehkdglrvvp 84
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  85 scldlsavetelineagrelilahlikgqkekFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVH 164
Cdd:cd02042   48 --------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLE 95

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 149935804 165 KVQQRLNSDLSIAGVLITQYDGRKNLNKSVSELVQ 199
Cdd:cd02042   96 ELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-185 2.16e-35

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: 129.71  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    3 KAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSAELP----QTIYGAMKgeYD---LPIYE 75
Cdd:TIGR03453 103 HLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDvgenETLYGAIR--YDderRPISE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   76 -----HKDGLRVVPSCLDLSAVETE----LINEAGRELI----LAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRL 142
Cdd:TIGR03453 181 iirktYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIffarVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGV 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149935804  143 IIPVQ---------AQFLAMrgMAKLMQVVHKVQQRLNSDLsiAGVLITQYD 185
Cdd:TIGR03453 261 LITVHpqmldvmsmSQFLLM--TGDLLGVVREAGGNLSYDF--MRYLVTRYE 308
ParA_partition NF041546
ParA family partition ATPase;
6-246 7.43e-30

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 110.72  E-value: 7.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTEslgfsaelpqtiYGAMKgeydlpiyEHKDGLRVVps 85
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALD------------WAAAR--------EDERPFPVV-- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  86 clDLSAVEtelineagreliLAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVHK 165
Cdd:NF041546  59 --GLARPT------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKE 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 166 VqQRLNSDLSiAGVLITQYDGRKNLNKSVSELVQEtFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAEDYEKVCN 245
Cdd:NF041546 125 A-REYTPGLK-AAFVLNRAIARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDGKAAREIRALAK 201


                 .
gi 149935804 246 E 246
Cdd:NF041546 202 E 202
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 5-247 1.09e-28

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 112.08  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSAELP----QTIYGAMKgeYD---LPIYE-- 75
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDvganETLYAAIR--YDdtrRPLRDvi 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  76 ---HKDGLRVVPSCLDLSAVE----TELINEAGRELI----LAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLII 144
Cdd:PRK13869 200 rptYFDGLHLVPGNLELMEFEhttpKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 145 PVQAQFLAMRGMAK-------LMQVVHKVQQRLNSDLsiAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITL 217
Cdd:PRK13869 280 TVHPQMLDIASMSQfllmtrdLLGVVKEAGGNLQYDF--IRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAV 357

                        250       260       270
                 ....*....|....*....|....*....|
gi 149935804 218 AEAPTQGQDIFHYAPKSAGAEDYEKVCNEL 247
Cdd:PRK13869 358 SDAGLTKQTLYEIGRENLTRSTYDRAMESL 387
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 5-247 2.52e-28

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: 107.89  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSaELPQTIYGAMKGEYDL--PIYEHKDGLR 81
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGME-DKPVTLHDVLAGEADIkdAIYEGPFGVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   82 VVPSCLDLsavetELINEAGRELiLAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQ 161
Cdd:TIGR01969  80 VIPAGVSL-----EGLRKADPDK-LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKTKI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  162 VVHKVqqrlnsDLSIAGVLITQYdGRKNLNKSVSElVQETFQGKVFST-----HIRnaitlaEAPTQGQDIFHYAPKSAG 236
Cdd:TIGR01969 154 VAEKL------GTAILGVVLNRV-TRDKTELGREE-IETILEVPVLGVvpedpEVR------RAAAFGEPVVIYNPNSPA 219

                         250
                  ....*....|.
gi 149935804  237 AEDYEKVCNEL 247
Cdd:TIGR01969 220 AQAFMELAAEL 230
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 20-248 3.33e-27

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: 104.59  E-value: 3.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  20 TTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAElpQTIYGAMKGEYDLP--IYEHKDGLRVVPSCLDLSAVEtel 96
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADlGLANLDVLLGLEPK--ATLADVLAGEADLEdaIVQGPGGLDVLPGGSGPAELA--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  97 inEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVHKVQqrlnsDLSI 176
Cdd:COG0455   76 --ELDPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRL-----GVRR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149935804 177 AGVLITQYDGRK---NLNKSVSELVQETFQGKV-FSTHIRNAITLAEAPTQGQDIFHYAPKSAGAEDYEKVCNELL 248
Cdd:COG0455  149 AGVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLA 224
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 5-247 2.16e-26

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: 102.67  E-value: 2.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAELPQTIYGAMKGEYDL--PIYEHK--DG 79
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIVYTLVDVLEGECRLeqALIKDKrwEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  80 LRVVPSCLDLSAveteliNEAGRElILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKL 159
Cdd:cd02036   81 LYLLPASQTRDK------DALTPE-KLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 160 MQVVHKvqqrlnSDLSIAGVLITQYDG---RKNLNKSVSElVQETFQGKV-----FSTHIRnaitlaEAPTQGQDIFHYA 231
Cdd:cd02036  154 IGLLES------KGIVNIGLIVNRYRPemvKSGDMLSVED-IQEILGIPLlgvipEDPEVI------VATNRGEPLVLYK 220

                        250
                 ....*....|....*.
gi 149935804 232 PKSAGAEDYEKVCNEL 247
Cdd:cd02036  221 PNSLAAKAFENIARRL 236
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 4-249 1.42e-22

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: 92.79  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFSAELPQTIYGAM-KGEYDLPI-YEHKDGLR 81
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALlNGADWAAAaYRSPDGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   82 VVP-SCLDLSAVETELINEAGreLILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLM 160
Cdd:TIGR03371  81 FLPyGDLSADEREAYQAHDAG--WLARLLQQLDLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  161 QVVHKVQQRLNSdlsiAGVLITQYDGRKNLNKSVSELVQETFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAEDY 240
Cdd:TIGR03371 159 LALFAGSGPRDG----PRFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQAAHDI 234


                  ....*....
gi 149935804  241 EKVCNELLT 249
Cdd:TIGR03371 235 RTLAGWLLS 243
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-248 2.59e-22

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: 94.03  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   2 SKAKVISVLNHKGGVGKTTTTINLGGAL-RQKGYKVLLIDLDGQANlTESLGFSAELPQTIYGAMKGEYDLP-------I 73
Cdd:COG4963  100 RRGRVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFG-DVALYLDLEPRRGLADALRNPDRLDetlldraL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  74 YEHKDGLRVVPSCLDLsaVETELINEAGRELILAHLikgqKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAM 153
Cdd:COG4963  179 TRHSSGLSVLAAPADL--ERAEEVSPEAVERLLDLL----RRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 154 RGMAKLMQVVHkvqqRLNSDLSIAGVLITQYDGRKNLnkSVSElVQETFQGKVFSThIRN-AITLAEAPTQGQDIFHYAP 232
Cdd:COG4963  253 RNAKRLLDLLR----ELGLPDDKVRLVLNRVPKRGEI--SAKD-IEEALGLPVAAV-LPNdPKAVAEAANQGRPLAEVAP 324

                        250
                 ....*....|....*.
gi 149935804 233 KSAGAEDYEKVCNELL 248
Cdd:COG4963  325 KSPLAKAIRKLAARLT 340
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 5-144 8.41e-21

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: 87.62  E-value: 8.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAelPQTIYGAMKGEYDLP--IYEHKDGLR 81
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAP--KKTLGDVLKGRVSLEdiIVEGPEGLD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149935804  82 VVPScldlSAVETELIN-EAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLII 144
Cdd:cd02038   79 IIPG----GSGMEELANlDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 6-251 9.31e-19

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 84.26  E-value: 9.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLID-LDGQANLTESLGFSAEL----PQTIYGAMKGEYDLPIYEHK--- 77
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLhihaEDTLLPFYLGEKDDATYAIKptc 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  78 -DGLRVVPSCLDLSAVETELIN--EAGRELILAHL-----IKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQA- 148
Cdd:PRK13705 188 wPGLDIIPSCLALHRIETELMGkfDEGKLPTDPHLmlrlaIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAe 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 149 --------QFLAMrgMAKLMQVVHkvqqrLNSDLSIAGVLITQYdgrKNLNKSVSELVQETFQGKVFSTHIRNAITLAEA 220
Cdd:PRK13705 268 lfdytsalQFFDM--LRDLLKNVD-----LKGFEPDVRILLTKY---SNSNGSQSPWMEEQIRDAWGSMVLKNVVRETDE 337

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 149935804 221 PTQGQ----DIFHYAP---KSAGA-----EDYEKVCNELLTEI 251
Cdd:PRK13705 338 VGKGQirmrTVFEQAIdqrSSTGAwrnalSIWEPVCNEIFDRL 380
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 5-243 2.89e-18

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: 80.78  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQK-GYKVLLIDLDGQANlTESLGFSAELPQTIYGAMKG-------EYDLPIYEH 76
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFG-DLGLYLNLRPDYDLADVIQNldrldrtLLDSAVTRH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  77 KDGLRVVPScldlsAVETELINEAGRELILA--HLIKGQkekFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMR 154
Cdd:cd03111   80 SSGLSLLPA-----PQELEDLEALGAEQVDKllQVLRAF---YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 155 GMAKLMQVVHkvQQRLNSD-LSIagvLITQYDgrKNLNKSVSELVqETFQGKVFSThIRNA-ITLAEAPTQGQDIFHYAP 232
Cdd:cd03111  152 NARRLLDSLR--ELEGSSDrLRL---VLNRYD--KKSEISPKDIE-EALGLEVFAT-LPNDyKAVSESANTGRPLVEVAP 222

                        250
                 ....*....|.
gi 149935804 233 KSAGAEDYEKV 243
Cdd:cd03111  223 RSALVRALQDL 233
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 4-154 8.40e-18

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: 80.07  E-value: 8.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAELPQTIYGAMKGEYDLPIYEHKDglRV 82
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKD--KR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149935804   83 VPSCLDLSAVETELINEAGRELILAhLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMR 154
Cdd:TIGR01968  79 LKNLYLLPASQTRDKDAVTPEQMKK-LVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVR 149
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 6-251 1.01e-16

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 78.51  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLID-LDGQANLTESLGFSAEL----PQTIYGAMKGEYDLPIYEHK--- 77
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLhihaDDTLLPFYLGERDNAEYAIKptc 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  78 -DGLRVVPSCLDLSAVETELI--NEAGR-----ELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQA- 148
Cdd:PHA02519 188 wPGLDIIPSCLALHRIETDLMqyHDAGKlphppHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAe 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 149 --------QFLAMrgMAKLMQVVHkvqqrLNSDLSIAGVLITQYdgrKNLNKSVSELVQETFQGKVFSTHIRNAITLAEA 220
Cdd:PHA02519 268 lfdyvsvlQFFTM--LLDLLATVD-----LGGFEPVVRLLLTKY---SLTVGNQSRWMEEQIRNTWGSMVLRQVVRVTDE 337

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 149935804 221 PTQGQ----DIFHYAPKSA--------GAEDYEKVCNELLTEI 251
Cdd:PHA02519 338 VGKGQikmrTVFEQAANQRstlnawrnAVAIWEPVCAEIFNDL 380
PHA02518 PHA02518
ParA-like protein; Provisional
 5-248 1.28e-16

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 76.04  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQanlteslGFSAELPQTiygAMKGEYDLPIYEHKDGLRvvp 84
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQ-------GSSTDWAEA---REEGEPLIPVVRMGKSIR--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  85 scldlsavetelineagrelilAHLIKgQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAKLMQVVH 164
Cdd:PHA02518  68 ----------------------ADLPK-VASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIK 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 165 KVQQrLNSDLSIAGVLITQYDGRKNLNKSVSELVQEtFQGKVFSTHIRNAITLAEAPTQGQDIFHYAPKSAGAEDYEKVC 244
Cdd:PHA02518 125 ARQE-VTDGLPKFAFIISRAIKNTQLYREARKALAG-YGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAEEIIQLV 202


                 ....
gi 149935804 245 NELL 248
Cdd:PHA02518 203 KELF 206
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 4-144 1.42e-14

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 70.86  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAELPQTIYGAMKGEYDLP--IYEHK--D 78
Cdd:COG2894    2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADiGLRNLDLVMGLENRIVYDLVDVIEGECRLKqaLIKDKrfE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149935804  79 GLRVVPscldlsAVET---ELINEAGRELILAHLikgqKEKFDYILIDCPPSLSLLTLNALTASDRLII 144
Cdd:COG2894   82 NLYLLP------ASQTrdkDALTPEQMKKLVEEL----KEEFDYILIDSPAGIEQGFKNAIAGADEAIV 140
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 13-188 3.36e-14

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: 70.60  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDG-QANLTESLGFSAELPQTIYGAMKGEYDLPIYE-HKDGLRVVPSCLdLS 90
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLEDVIQPtEVEGLDVLPAGP-LP 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  91 AVETELINEAGRELILAHLikgqKEKFDYILIDCPPSLSLLTLNALTA-SDRLIIPVQAQFLAMRGMAKLMQVVHKVQQR 169
Cdd:COG0489  180 PNPSELLASKRLKQLLEEL----RGRYDYVIIDTPPGLGVADATLLASlVDGVLLVVRPGKTALDDVRKALEMLEKAGVP 255

                        170
                 ....*....|....*....
gi 149935804 170 lnsdlsIAGVLITQYDGRK 188
Cdd:COG0489  256 ------VLGVVLNMVCPKG 268
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 6-151 1.18e-13

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: 68.63  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDG-QANLTESLGFSAELpqtiygAMKGEYDLPIyehkdglrvvP 84
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSAT------ADRTGLSLPT----------P 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149935804   85 SCLDLSAVETELI--NEAGRELILAHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFL 151
Cdd:pfam09140  66 EHLNLPDNDVAEVpdGENIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFV 134
minD CHL00175
septum-site determining protein; Validated
 4-154 2.30e-13

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 67.87  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAELPQTIYGAMKGEYDLPIYEHKDglRV 82
Cdd:CHL00175  15 SRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRD--KR 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149935804  83 VPSCLDLSAVETELINEAGRELIlAHLIKGQKEK-FDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMR 154
Cdd:CHL00175  93 WKNLSLLAISKNRQRYNVTRKNM-NMLVDSLKNRgYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIR 164
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 2-183 7.35e-11

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: 59.51  E-value: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   2 SKAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDG-QANLTESLGFSAElpQTIYGAMKGEYDLPiyehkDGL 80
Cdd:cd05387   17 AGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNE--PGLSEVLSGQASLE-----DVI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  81 RVVPScLDLSAVETELINEAGRELI----LAHLIKGQKEKFDYILIDCPPSLSLLTLNAL-TASDRLIIPVQAqflamrG 155
Cdd:cd05387   90 QSTNI-PNLDVLPAGTVPPNPSELLssprFAELLEELKEQYDYVIIDTPPVLAVADALILaPLVDGVLLVVRA------G 162

                        170       180
                 ....*....|....*....|....*...
gi 149935804 156 MAKLMQVVHKVQQRLNSDLSIAGVLITQ 183
Cdd:cd05387  163 KTRRREVKEALERLEQAGAKVLGVVLNK 190
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 5-239 3.63e-10

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 58.16  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDgQANLtesLGFSAELP-QTIYGAMKGEYDL-----PIYEHKD 78
Cdd:pfam06564   2 KILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLS-PDNL---LRLHFNVPfEHRQGWARAELDGadwrdAALEYTP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   79 GLRVVPSClDLSAVETELIneagrELILAHL------IKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQfla 152
Cdd:pfam06564  78 GLDLLPFG-RLSVEEQENL-----QQLQPDPgawcrrLQQLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  153 mrgmAKLMQVVHkvQQRLNSDlsiAGVLITQYDGRKNLNKSVSELVQETfQGKVFSTHIRNAITLAEAPTQGQDIFHYAP 232
Cdd:pfam06564 149 ----ANCHVLLH--QQPLPDA---DHLLINDFRPASQLQQDLLQLWRQS-QRRLLPLVIHRDEALAEALAAKQPLGEYRP 218


                  ....*..
gi 149935804  233 KSAGAED 239
Cdd:pfam06564 219 DSLAAEE 225
PRK10818 PRK10818
septum site-determining protein MinD;
4-250 4.85e-10

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 58.41  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   4 AKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGFSAELPQTIYGAMKGEYDLPIYEHKD---- 78
Cdd:PRK10818   2 ARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDkrte 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  79 GLRVVPSCldlSAVETELINEAGRELILAHLikgQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVQAQFLAMRGMAK 158
Cdd:PRK10818  82 NLYILPAS---QTRDKDALTREGVAKVLDDL---KAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804 159 LMQVVHKVQQRL-NSDLSIA-GVLITQYD-GRKNLNKSVS-ELVQETFQGKVFSThIRNAITLAEAPTQGQDIFHYAPKS 234
Cdd:PRK10818 156 ILGILASKSRRAeNGEEPIKeHLLLTRYNpGRVSRGDMLSmEDVLEILRIKLVGV-IPEDQSVLRASNQGEPVILDIEAD 234

                        250
                 ....*....|....*.
gi 149935804 235 AGaEDYEKVCNELLTE 250
Cdd:PRK10818 235 AG-KAYADTVDRLLGE 249
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 5-42 4.10e-09

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: 55.54  E-value: 4.10e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149935804    5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 5-42 9.42e-09

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: 52.05  E-value: 9.42e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 13-68 1.04e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 54.40  E-value: 1.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFS--AELPQTIyGAMKGE 68
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEveADLIKPL-GEMREL 64
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-126 1.13e-08

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: 53.59  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    1 MSKAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLDGQaNLTESLGFSAelPQTIYGA---MKGEYDLP--IYE 75
Cdd:TIGR01007  14 GAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSVMSGTFKS--QNKITGLtnfLSGTTDLSdaICD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 149935804   76 HK-DGLRVVPSClDLSAVETELINEAGreliLAHLIKGQKEKFDYILIDCPP 126
Cdd:TIGR01007  91 TNiENLDVITAG-PVPPNPTELLQSSN----FKTLIETLRKRFDYIIIDTPP 137
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 5-42 1.22e-08

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: 53.66  E-value: 1.22e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 149935804   5 KVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 13-133 8.92e-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: 51.35  E-value: 8.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLG--FSAELPQTIYG---AMkgEYDlPIYE--------HKDG 79
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGqkLGGETPVKGAPnlwAM--EID-PEEAleeyweevKELL 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149935804  80 LRVVPSCLDLSAVETELINEAGRELILA-----HLIkgQKEKFDYILIDCPP---SLSLLTL 133
Cdd:cd02035   85 AQYLRLPGLDEVYAEELLSLPGMDEAAAfdelrEYV--ESGEYDVIVFDTAPtghTLRLLSL 144
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
13-163 2.19e-07

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 50.59  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLG--FSAElPQTI-----YGAM---KGEYDLPIYEHKDGLR- 81
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGteLGNE-PTEVavpnlYALEidpEAELEEYWERVRAPLRg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  82 VVPScLDLSAVETEL--INE-AGRELILAHLikgQKEKFDYILIDCPPSLSllTLNALTASDRLIIPVQAQFLAMRGMAK 158
Cdd:COG0003   90 LLPS-AGVDELAESLpgTEElAALDELLELL---EEGEYDVIVVDTAPTGH--TLRLLSLPELLGWWLDRLLKLRRKASG 163


                 ....*
gi 149935804 159 LMQVV 163
Cdd:COG0003  164 LGRPL 168
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 13-68 7.43e-07

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: 48.85  E-value: 7.43e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLGFsaELPQTIYGAMKGE 68
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGV--EVEKLPLIKTIGD 61
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 2-185 4.09e-06

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 47.41  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804    2 SKAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLTESLGfsaELPQT-IYGAMKGEYDLPIYEHKDg 79
Cdd:TIGR01005 551 AENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFG---KAPKPgLLDLLAGEASIEAGIHRD- 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   80 lrVVPSCLDLSAVETELINEAGRELIL----AHLIKGQKEKFDYILIDCPPSLSLLTLNALTASDRLIIPVqAQFlaMRG 155
Cdd:TIGR01005 627 --QRPGLAFIAAGGASHFPHNPNELLAnpamAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGILFV-TEF--ERS 701

                         170       180       190
                  ....*....|....*....|....*....|
gi 149935804  156 MAKLMQVVHKVQQRLNSDlsIAGVLITQYD 185
Cdd:TIGR01005 702 PLGEIRDLIHQEPHANSD--VLGVIFNALD 729
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 4-42 3.36e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.18  E-value: 3.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 149935804   4 AKVISVLNhKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:PRK13185   2 ALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCD 39
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
6-42 3.66e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 44.26  E-value: 3.66e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 149935804   6 VISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 13-52 9.36e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 42.84  E-value: 9.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLG 52
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 3-146 1.42e-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: 41.76  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804   3 KAKVISVLNHKGGVGKTTTTINLGGALRQKGYKVLLIDLD------------GQANLTESLGFSAELPQTIygAMKGEyd 70
Cdd:cd17869    2 ATSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMErlqstdvffgasGRYLMSDHLYTLKSRKANL--ADKLE-- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149935804  71 LPIYEHKDGLRVVP---SCLDLSAVETELINEAGRELILAHLikgqkekFDYILIDCPPSLSLLTLNALTASDRLIIPV 146
Cdd:cd17869   78 SCVKQHESGVYYFSpfkSALDILEIKKDDILHMITKLVEAHA-------YDYIIMDLSFEFSSTVCKLLQASHNNVVIA 149
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 13-39 1.99e-04

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 41.73  E-value: 1.99e-04
                         10        20
                 ....*....|....*....|....*..
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLI 39
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHV 34
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 15-56 2.70e-04

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 40.39  E-value: 2.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 149935804  15 GVGKTTTTINLGGALRQKGYKVLLidLDGQA---NLTESLGFSAE 56
Cdd:PRK00889  14 GAGKTTIARALAEKLREAGYPVEV--LDGDAvrtNLSKGLGFSKE 56
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 5-42 2.92e-04

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: 41.13  E-value: 2.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 149935804   5 KVISVLNhKGGVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCD 37
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 13-52 3.11e-04

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: 41.18  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 149935804   13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESLG 52
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFN 48
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 13-51 4.51e-04

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 40.43  E-value: 4.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESL 51
Cdd:cd02117    8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 7-70 9.97e-04

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 39.29  E-value: 9.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149935804   7 ISVLNHKGGVGKTTTTINLGGALrqkgYKVLLIDLDGQA-NLTESLGFSAELPQTIYGAMKGEYD 70
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDApNLHLLLGPEPEEEEDFVGGKKAFID 62
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
13-51 1.08e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 39.35  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 149935804   13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESL 51
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLL 46
chlL CHL00072
photochlorophyllide reductase subunit L
 13-53 2.08e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.56  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 149935804  13 KGGVGKTTTTINLGGALRQKGYKVLLIDLDGQANLTESL-GF 53
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLtGF 49
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 15-183 4.68e-03

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 36.95  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  15 GVGKTTTTINLG-GALRQKGyKVLLIDldgqanlTESlGFSAE-LPQTIYGAMKGEYDLpiyehkdglrvvPSCLDLSAV 92
Cdd:cd01393   11 GSGKTQLALQLAaNALLLGG-GVVWID-------TEG-AFPPSrLVQILEASPSSELEL------------AEALSRLLY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149935804  93 ETELINEAGRELILAHLIKgqkekfdyilIDCPPSLSLLTLNALTA-----SDRLIIPVQAQFLAMRGMAKLMQVVhkvq 167
Cdd:cd01393   70 FRPPDTLAHLLALDSLPES----------LFPPPNTSLVVVDSVSAlfrkaFPRGGDGDSSSSLRARLLSQLARAL---- 135

                        170
                 ....*....|....*.
gi 149935804 168 QRLNSDLSIAGVLITQ 183
Cdd:cd01393  136 QKLAAQFNLAVVVTNQ 151
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
15-36 5.10e-03

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 37.80  E-value: 5.10e-03
                         10        20
                 ....*....|....*....|..
gi 149935804  15 GVGKTTTTINLGGALRQKGYKV 36
Cdd:PRK01077  14 GSGKTTVTLGLMRALRRRGLRV 35
lpxK PRK00652
tetraacyldisaccharide 4'-kinase; Reviewed
 1-36 5.63e-03

tetraacyldisaccharide 4'-kinase; Reviewed


Pssm-ID: 234808  Cd Length: 325  Bit Score: 37.50  E-value: 5.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 149935804   1 MSKAKVISVLN-HKGGVGKTTTTINLGGALRQKGYKV 36
Cdd:PRK00652  46 RAPVPVIVVGNiTVGGTGKTPVVIALAEQLQARGLKP 82
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 15-48 8.02e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 36.46  E-value: 8.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 149935804   15 GVGKTTTTINLGGALRQKGYKVLLIDLD-GQANLT 48
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDvGQSEIG 38
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 15-42 9.63e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 35.98  E-value: 9.63e-03
                          10        20
                  ....*....|....*....|....*...
gi 149935804   15 GVGKTTTTINLGGALRQKGYKVLLIDLD 42
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
 
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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