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Conserved domains on  [gi|1490718103|gb|RLC90869|]
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ParA family protein [Chloroflexi bacterium]

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 ...
 2-253 8.29e-116

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: 332.59  E-value: 8.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELR---LKRALAPLaDDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPVMIPRSVRLSEAPSYGEPGIFYAPRSQG 240
Cdd:COG1192   158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKG 237

                         250
                  ....*....|...
gi 1490718103 241 ALAYRTLTWELLR 253
Cdd:COG1192   238 AKAYRALAEELLE 250
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-253 8.29e-116

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: 332.59  E-value: 8.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELR---LKRALAPLaDDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPVMIPRSVRLSEAPSYGEPGIFYAPRSQG 240
Cdd:COG1192   158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKG 237

                         250
                  ....*....|...
gi 1490718103 241 ALAYRTLTWELLR 253
Cdd:COG1192   238 AKAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-180 3.20e-73

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: 221.69  E-value: 3.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENI---LKEALEPVkDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGL 157

                         170       180
                  ....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLAL 180
Cdd:pfam13614 158 SQLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-203 2.99e-46

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: 151.15  E-value: 2.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLglnprslsvsiydvllgaqpaaeiiratrwagl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 ellpgvpalagatvelntaldpheralclrqalenvtdYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGLTQ 162
Cdd:cd02042    48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1490718103 163 LMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQ 203
Cdd:cd02042    90 LLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-224 3.16e-27

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 108.61  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSlSVSIYDVLLGA-------QPAAEIIR 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPET-DVGANETLYAAiryddtrRPLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  76 ATRWAGLELLPGvpalagaTVELNTALDPHERALCLR------------QALENVTD-YDYVLIDSPPSLGTLTVNALCA 142
Cdd:PRK13869  201 PTYFDGLHLVPG-------NLELMEFEHTTPKALSDKgtrdglfftrvaQAFDEVADdYDVVVIDCPPQLGFLTLSGLCA 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 143 AEGVIVPVQCEYLALEGLTQLMntitLIQRRM---------NLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPV 213
Cdd:PRK13869  274 ATSMVITVHPQMLDIASMSQFL----LMTRDLlgvvkeaggNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTN 349

                         250
                  ....*....|.
gi 1490718103 214 MIPRSVRLSEA 224
Cdd:PRK13869  350 PMVKSAAVSDA 360
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-150 4.92e-27

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: 107.76  E-value: 4.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRsLSVSIYDVLLGA-------QPAAEIIRA 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPE-FDVGENETLYGAirydderRPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  77 TRWAGLELLPGVPALAGATVELNTAL---DPHERALCLR--QALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPV 150
Cdd:TIGR03453 185 TYFPGLDLVPGNLELMEFEHETPRALsrgQGGDTIFFARvgEALAEVeDDYDVVVIDCPPQLGFLTLSALCAATGVLITV 264
ParA_partition NF041546
ParA family partition ATPase;
4-228 5.12e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 98.39  E-value: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNattslglnprslsvsiydvllgaqpaaeiirATRWAGL- 82
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGS-------------------------------ALDWAAAr 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 --ELLPGVPALAGATvelntaldpheralcLRQALENVT-DYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEG 159
Cdd:NF041546   50 edERPFPVVGLARPT---------------LHRELPSLArDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWA 114

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 160 LTQLMNtitLIQRRMNLHLALR-GLVMTMYDRRTTLSRQVAAEVqRHFSSQVFPVMIPRSVRLSEAPSYG 228
Cdd:NF041546  115 SADTVD---LIKEAREYTPGLKaAFVLNRAIARTALGREVAEAL-AEYGLPVLKTRIGQRVAFAESAAEG 180
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-232 1.41e-22

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 94.05  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANQKGGVGKTTTVVNLAASMAD-WGFRVLVVDIDPQSNATTSLG--LNPRSLSVSIYDVLLGAQPAAEIIRAT 77
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSvFNKKVLVIDTDLQGNATQFLSktFNVPNFPQSFMKCVEDGDLEKGIVHLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  78 RwaGLELLPGvpalAGATVELNTALDP-----HERALCLRQALENVTD-YDYVLIDSPPSLGTLTVNALCAAEGVIVPVQ 151
Cdd:NF041283   81 P--NLDLIAG----DYDTRELGDFLADkfkseYDRTFYLKKLLDKIKDdYDFIFIDVPPSTDIKVDNAMVAADYVIVIQE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 152 CEYLALEGLTQLMNTI--TLIQRRMN-LHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQ-VFPVMIPRSVRLSeapSY 227
Cdd:NF041283  155 TQQFAFEGSKKLILTYlqTLVDDFGDeINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDnVFNNIIKNHARLE---WY 231


                  ....*
gi 1490718103 228 GEPGI 232
Cdd:NF041283  232 GEQGI 236
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 5-58 1.44e-03

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


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490718103   5 YAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNAT----TSLGLNPRSLSV 58
Cdd:NF041417  335 YLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgTEVGHEPTKVGV 392
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-253 8.29e-116

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: 332.59  E-value: 8.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAG 81
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGRELR---LKRALAPLaDDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPVMIPRSVRLSEAPSYGEPGIFYAPRSQG 240
Cdd:COG1192   158 AQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKG 237

                         250
                  ....*....|...
gi 1490718103 241 ALAYRTLTWELLR 253
Cdd:COG1192   238 AKAYRALAEELLE 250
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-180 3.20e-73

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: 221.69  E-value: 3.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAG 81
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENI---LKEALEPVkDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGL 157

                         170       180
                  ....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLAL 180
Cdd:pfam13614 158 SQLLNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 6-230 2.37e-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: 162.52  E-value: 2.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   6 AFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGL--NPRSLSVSIYDVLLGAQPAAEIIRATR--WAG 81
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLegDIAPALQALAEGLKGRVNLDPILLKEKsdEGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  82 LELLPGVPALAGATVELnTALDPHERalcLRQALENVTD-YDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGL 160
Cdd:pfam01656  82 LDLIPGNIDLEKFEKEL-LGPRKEER---LREALEALKEdYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490718103 161 TQLMNTI-TLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPVmIPRSVRLSEAPSYGEP 230
Cdd:pfam01656 158 KRLGGVIaALVGGYALLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGV-IPRDEAVAEAPARGLP 227
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-203 2.99e-46

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: 151.15  E-value: 2.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLglnprslsvsiydvllgaqpaaeiiratrwagl 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 ellpgvpalagatvelntaldpheralclrqalenvtdYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEGLTQ 162
Cdd:cd02042    48 --------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAK 89

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1490718103 163 LMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAEVQ 203
Cdd:cd02042    90 LLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-224 3.16e-27

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 108.61  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSlSVSIYDVLLGA-------QPAAEIIR 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPET-DVGANETLYAAiryddtrRPLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  76 ATRWAGLELLPGvpalagaTVELNTALDPHERALCLR------------QALENVTD-YDYVLIDSPPSLGTLTVNALCA 142
Cdd:PRK13869  201 PTYFDGLHLVPG-------NLELMEFEHTTPKALSDKgtrdglfftrvaQAFDEVADdYDVVVIDCPPQLGFLTLSGLCA 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 143 AEGVIVPVQCEYLALEGLTQLMntitLIQRRM---------NLHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQVFPV 213
Cdd:PRK13869  274 ATSMVITVHPQMLDIASMSQFL----LMTRDLlgvvkeaggNLQYDFIRYLLTRYEPQDAPQTKVAALLRNMFEDHVLTN 349

                         250
                  ....*....|.
gi 1490718103 214 MIPRSVRLSEA 224
Cdd:PRK13869  350 PMVKSAAVSDA 360
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-150 4.92e-27

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: 107.76  E-value: 4.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRsLSVSIYDVLLGA-------QPAAEIIRA 76
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPE-FDVGENETLYGAirydderRPISEIIRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  77 TRWAGLELLPGVPALAGATVELNTAL---DPHERALCLR--QALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPV 150
Cdd:TIGR03453 185 TYFPGLDLVPGNLELMEFEHETPRALsrgQGGDTIFFARvgEALAEVeDDYDVVVIDCPPQLGFLTLSALCAATGVLITV 264
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-258 1.02e-26

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: 103.82  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  18 TTVVNLAASMADWGFRVLVVDIDPQS-NATTSLGLNPRslsVSIYDVLLGAQPAAEIIRATRwAGLELLPGVPALAGAtv 96
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLaNLDVLLGLEPK---ATLADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAEL-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  97 elnTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEylaLEGLTQLMNTITLIQRRMN 175
Cdd:COG0455    75 ---AELDPEER---LIRVLEELeRFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPE---PTSITDAYALLKLLRRRLG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 176 LHLAlrGLVMTMYDRRT---TLSRQVAAEVQRHFSSQV-FPVMIPRSVRLSEAPSYGEPGIFYAPRSQGALAYRTLTWEL 251
Cdd:COG0455   146 VRRA--GVVVNRVRSEAearDVFERLEQVAERFLGVRLrVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARL 223


                  ....*..
gi 1490718103 252 LRGDGHE 258
Cdd:COG0455   224 AGWPVPE 230
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-251 1.30e-25

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: 100.74  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID-PQSNATTSLGLNPRSLsVSIYDVLLG-AQPAAEIIRATRWA 80
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIV-YTLVDVLEGeCRLEQALIKDKRWE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  81 GLELLPgvpalAGATVElNTALDPheralclrQALENVTD-----YDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEyl 155
Cdd:cd02036    80 NLYLLP-----ASQTRD-KDALTP--------EKLEELVKelkdsFDFILIDSPAGIESGFINAIAPADEAIIVTNPE-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 156 aLEGLTQLMNTITLIQRR--MNLHLALRGLVMTMYDRRTTLSRQvaaEVQRHFSSQVFPVmIPRSVRLSEAPSYGEPGIF 233
Cdd:cd02036   144 -ISSVRDADRVIGLLESKgiVNIGLIVNRYRPEMVKSGDMLSVE---DIQEILGIPLLGV-IPEDPEVIVATNRGEPLVL 218

                         250
                  ....*....|....*...
gi 1490718103 234 YAPRSQGALAYRTLTWEL 251
Cdd:cd02036   219 YKPNSLAAKAFENIARRL 236
ParA_partition NF041546
ParA family partition ATPase;
4-228 5.12e-25

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 98.39  E-value: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNattslglnprslsvsiydvllgaqpaaeiirATRWAGL- 82
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGS-------------------------------ALDWAAAr 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 --ELLPGVPALAGATvelntaldpheralcLRQALENVT-DYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALEG 159
Cdd:NF041546   50 edERPFPVVGLARPT---------------LHRELPSLArDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWA 114

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 160 LTQLMNtitLIQRRMNLHLALR-GLVMTMYDRRTTLSRQVAAEVqRHFSSQVFPVMIPRSVRLSEAPSYG 228
Cdd:NF041546  115 SADTVD---LIKEAREYTPGLKaAFVLNRAIARTALGREVAEAL-AEYGLPVLKTRIGQRVAFAESAAEG 180
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-251 9.69e-24

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: 96.34  E-value: 9.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDpQSNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRwAGL 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD-ITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGP-FGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 ELLPgvpalAGATVELNTALDPhERalcLRQALENVT-DYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEylaLEGLT 161
Cdd:TIGR01969  79 KVIP-----AGVSLEGLRKADP-DK---LEDVLKEIIdDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE---ISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 162 QLMNTITLIQRrmnLHLALRGLVMTMYDR-RTTLSRQvaaEVQRHFSSQVFpVMIPRSVRLSEAPSYGEPGIFYAPRSQG 240
Cdd:TIGR01969 147 DALKTKIVAEK---LGTAILGVVLNRVTRdKTELGRE---EIETILEVPVL-GVVPEDPEVRRAAAFGEPVVIYNPNSPA 219

                         250
                  ....*....|.
gi 1490718103 241 ALAYRTLTWEL 251
Cdd:TIGR01969 220 AQAFMELAAEL 230
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 4-153 4.21e-23

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 96.97  E-value: 4.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVD-IDPQSNATTSLGLNPrSLSVSIYDVLL-----GAQPAAEIIRAT 77
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVP-DLHIHAEDTLLpfylgEKDDATYAIKPT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  78 RWAGLELLPGVPALAGATVELNTALD----PHERALCLRQALENVT-DYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQC 152
Cdd:PRK13705  187 CWPGLDIIPSCLALHRIETELMGKFDegklPTDPHLMLRLAIETVAhDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 266


                  .
gi 1490718103 153 E 153
Cdd:PRK13705  267 E 267
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-232 1.41e-22

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 94.05  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANQKGGVGKTTTVVNLAASMAD-WGFRVLVVDIDPQSNATTSLG--LNPRSLSVSIYDVLLGAQPAAEIIRAT 77
Cdd:NF041283    1 MGYVIVLANQKGGVGKTTDTVMEAVVASSvFNKKVLVIDTDLQGNATQFLSktFNVPNFPQSFMKCVEDGDLEKGIVHLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  78 RwaGLELLPGvpalAGATVELNTALDP-----HERALCLRQALENVTD-YDYVLIDSPPSLGTLTVNALCAAEGVIVPVQ 151
Cdd:NF041283   81 P--NLDLIAG----DYDTRELGDFLADkfkseYDRTFYLKKLLDKIKDdYDFIFIDVPPSTDIKVDNAMVAADYVIVIQE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 152 CEYLALEGLTQLMNTI--TLIQRRMN-LHLALRGLVMTMYDRRTTLSRQVAAEVQRHFSSQ-VFPVMIPRSVRLSeapSY 227
Cdd:NF041283  155 TQQFAFEGSKKLILTYlqTLVDDFGDeINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDnVFNNIIKNHARLE---WY 231


                  ....*
gi 1490718103 228 GEPGI 232
Cdd:NF041283  232 GEQGI 236
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 4-153 1.37e-21

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 92.77  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVD-IDPQSNATTSLGLNPrSLSVSIYDVLL----GAQPAAEI-IRAT 77
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVP-DLHIHADDTLLpfylGERDNAEYaIKPT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  78 RWAGLELLPGVPALAGATVELNTALD----PHERALCLRQALENVTD-YDYVLIDSPPSLGTLTVNALCAAEGVIVPVQC 152
Cdd:PHA02519  187 CWPGLDIIPSCLALHRIETDLMQYHDagklPHPPHLMLRAAIESVWDnYDIIVIDSAPNLGTGTINVVCAADVIVVATPA 266


                  .
gi 1490718103 153 E 153
Cdd:PHA02519  267 E 267
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 11-191 1.01e-20

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: 89.09  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDP-QSNATTSLGLNPRslsVSIYDVLLGAQPAAEIIRATRWAGLELLPgvp 89
Cdd:COG0489   101 KGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGLENR---PGLSDVLAGEASLEDVIQPTEVEGLDVLP--- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  90 alAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPslGTLTVNALCAAE---GVIVPVQCEYLALEGLTQLMN 165
Cdd:COG0489   175 --AGPLPPNPSELLASKR---LKQLLEELrGRYDYVIIDTPP--GLGVADATLLASlvdGVLLVVRPGKTALDDVRKALE 247

                         170       180
                  ....*....|....*....|....*.
gi 1490718103 166 TItliqRRMNLHLAlrGLVMTMYDRR 191
Cdd:COG0489   248 ML----EKAGVPVL--GVVLNMVCPK 267
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-148 2.13e-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: 76.07  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID-PQSNATTSLGLNPRslsVSIYDVLLGAQPAAEIIRATRwAG 81
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPK---KTLGDVLKGRVSLEDIIVEGP-EG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490718103  82 LELLPGvpalaGATVELNTALDPHERALCLRQALENVTDYDYVLIDSPPSLGTLTVNALCAAEGVIV 148
Cdd:cd02038    77 LDIIPG-----GSGMEELANLDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADEVIV 138
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 11-259 1.20e-15

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: 74.30  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDID-PQSNATTSLGLNPRSLSVSIyDVLLG-AQPAAEIIRATRWAGLELLPgv 88
Cdd:TIGR01968  10 KGGVGKTTTTANLGTALARLGKKVVLIDADiGLRNLDLLLGLENRIVYTLV-DVVEGeCRLQQALIKDKRLKNLYLLP-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  89 palaGATVELNTALDPHERALCLRQALEnvtDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLALE------GL-- 160
Cdd:TIGR01968  87 ----ASQTRDKDAVTPEQMKKLVNELKE---EFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRdadrviGLle 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 161 TQLMNTITLIQRRMNLHLALRGLVMTMYDRRTTLSRQVAAevqrhfssqvfpvMIPRSVRLSEAPSYGEPgIFYAPRSQG 240
Cdd:TIGR01968 160 AKGIEKIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIG-------------VIPEDEAIIVSTNKGEP-VVLNDKSRA 225

                         250
                  ....*....|....*....
gi 1490718103 241 ALAYRTLTWELLrgdGHEV 259
Cdd:TIGR01968 226 GKAFENIARRIL---GEEV 241
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 11-249 4.82e-15

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: 72.38  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLsvsiyDVLLGAQPAAEIIRATRW---AGLELLP- 86
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVR-----DGWARALLNGADWAAAAYrspDGVLFLPy 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  87 GVPALAGAtvELNTALDPHERALCLRQ---ALEnvtdyDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEylalegltql 163
Cdd:TIGR03371  85 GDLSADER--EAYQAHDAGWLARLLQQldlAAR-----DWVLIDLPRGPSPITRQALAAADLVLVVVNAD---------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 164 MNTITLIQRRMNLHLALRG------LVMTMYDRRTTLSRQVAAEVQRHFSSQVFPVMIPRSVRLSEAPSYGEPGIFYAPR 237
Cdd:TIGR03371 148 AACYATLHQLALALFAGSGprdgprFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVLNYAPH 227

                         250
                  ....*....|...
gi 1490718103 238 SQGALAYRTL-TW 249
Cdd:TIGR03371 228 SQAAHDIRTLaGW 240
minD CHL00175
septum-site determining protein; Validated
 1-157 3.56e-14

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 70.57  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID-PQSNATTSLGLNPRSLSVSIyDVLLG-AQPAAEIIRATR 78
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRVLYTAM-DVLEGeCRLDQALIRDKR 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490718103  79 WAGLELLPgvpaLAGATVELNTAldpHERALCLRQALENVtDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEYLAL 157
Cdd:CHL00175   93 WKNLSLLA----ISKNRQRYNVT---RKNMNMLVDSLKNR-GYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAI 163
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-252 3.59e-14

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: 71.30  E-value: 3.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMAD-WGFRVLVVDIDPQS-NATTSLGLNPRSlsvSIYDVL--LGAQPAAEIIRA-- 76
Cdd:COG4963   103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFgDVALYLDLEPRR---GLADALrnPDRLDETLLDRAlt 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  77 TRWAGLELLPGVPALAGAtvelnTALDPHE-RALC--LRQAlenvtdYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCE 153
Cdd:COG4963   180 RHSSGLSVLAAPADLERA-----EEVSPEAvERLLdlLRRH------FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 154 YLALEGLTQLMNTItliqRRMNLHLALRGLVMTMYDRRTTLSrqvAAEVQRHFSSQVFpVMIPRSVR-LSEAPSYGEPGI 232
Cdd:COG4963   249 LPSLRNAKRLLDLL----RELGLPDDKVRLVLNRVPKRGEIS---AKDIEEALGLPVA-AVLPNDPKaVAEAANQGRPLA 320

                         250       260
                  ....*....|....*....|
gi 1490718103 233 FYAPRSQGALAYRTLTWELL 252
Cdd:COG4963   321 EVAPKSPLAKAIRKLAARLT 340
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 13-148 5.53e-13

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: 65.67  E-value: 5.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  13 GVGKTTTVVNLAASMADWGFRVLVVDIDP-QSNATTSLGL-NPRSLSvsiyDVLLGAQPAAEIIRATRWAGLELLPgvpa 90
Cdd:cd05387    30 GEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLpNEPGLS----EVLSGQASLEDVIQSTNIPNLDVLP---- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  91 lAGATVELNTALDPHERalcLRQALENV-TDYDYVLIDSPPSLGTLTVNALCA-AEGVIV 148
Cdd:cd05387   102 -AGTVPPNPSELLSSPR---FAELLEELkEQYDYVIIDTPPVLAVADALILAPlVDGVLL 157
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-249 6.21e-13

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: 66.53  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMA-DWGFRVLVVDID-PQSNATTSLGLNPRslsvsiYDVllgaqpaAEIIRATRWA 80
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDlPFGDLGLYLNLRPD------YDL-------ADVIQNLDRL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  81 GLELL--------PGVPALAG-ATVELNTALDPhERALCLRQALENvtDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQ 151
Cdd:cd03111    68 DRTLLdsavtrhsSGLSLLPApQELEDLEALGA-EQVDKLLQVLRA--FYDHIIVDLGHFLDEVTLAVLEAADEILLVTQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 152 ceyLALEGLTQLMNTITLIQRRMNLHLALRgLVMTMYDRRTTLSRQVAAEVqrhFSSQVFPVMIPRSVRLSEAPSYGEPG 231
Cdd:cd03111   145 ---QDLPSLRNARRLLDSLRELEGSSDRLR-LVLNRYDKKSEISPKDIEEA---LGLEVFATLPNDYKAVSESANTGRPL 217

                         250
                  ....*....|....*...
gi 1490718103 232 IFYAPRSQGALAYRTLTW 249
Cdd:cd03111   218 VEVAPRSALVRALQDLAA 235
PHA02518 PHA02518
ParA-like protein; Provisional
 3-151 2.61e-12

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 64.49  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTslglnprslsvsiydvllgaqpAAEiiraTRWAGL 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTD----------------------WAE----AREEGE 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490718103  83 ELLPgVPALAGAtvelntaldpheralCLRQALENVTDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQ 151
Cdd:PHA02518   55 PLIP-VVRMGKS---------------IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQ 107
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-148 3.27e-12

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 64.69  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDpqsnattsLGLnpRSLsvsiyDVLLG-------------- 66
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD--------IGL--RNL-----DLVMGlenrivydlvdvie 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  67 --AQPAAEIIRATRWAGLELLPgvpalAGATVElNTALDPHE-RALC--LRQalenvtDYDYVLIDSPPSLGTLTVNALC 141
Cdd:COG2894    66 geCRLKQALIKDKRFENLYLLP-----ASQTRD-KDALTPEQmKKLVeeLKE------EFDYILIDSPAGIEQGFKNAIA 133


                  ....*..
gi 1490718103 142 AAEGVIV 148
Cdd:COG2894   134 GADEAIV 140
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
3-247 1.74e-10

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 59.76  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANqKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNaTTSLGLNPRsLSVSIYDVLLGAQPAAEI--------- 73
Cdd:pfam00142   1 RQIAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD-STRLLLGGK-LQPTVLDTAREKGYVEDVevedvvykg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  74 ---IRATRWAGLEllPGVpALAGATVelNTALDPHERalclrqaLENVTDYDYVLIDsppSLGTLTVNALCA------AE 144
Cdd:pfam00142  78 yggVKCVESGGPE--PGV-GCAGRGV--ITAINLLEE-------LGAYDDLDFVLYD---VLGDVVCGGFAMpiregkAQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 145 GVIVPVQCEYLALEGLTQLMNTitlIQRRMNLH-LALRGLVMTmyDRRTTLSRQVAAEVQRHFSSQVFPVmIPRSVRLSE 223
Cdd:pfam00142 143 EIYIVTSNEMMALYAANNIAKG---IQKYAKSGgVRLGGIICN--SRKVDDERELIDAFAEELGTQVLHF-VPRDNIVRK 216

                         250       260
                  ....*....|....*....|....
gi 1490718103 224 APSYGEPGIFYAPRSQGALAYRTL 247
Cdd:pfam00142 217 AELRKQTVIEYAPDSEQAQEYREL 240
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-142 5.97e-10

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: 57.45  E-value: 5.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQsNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAGL 82
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMR-NSVMSGTFKSQNKITGLTNFLSGTTDLSDAICDTNIENL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  83 ELLPgvpalAGATVELNTALDPHERALCLRQALENVtdYDYVLIDSPPsLGTLTVNALCA 142
Cdd:TIGR01007  97 DVIT-----AGPVPPNPTELLQSSNFKTLIETLRKR--FDYIIIDTPP-IGTVTDAAIIA 148
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-148 4.32e-09

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 55.20  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID---PqsNATTSLGLNPRSLSVSiydvllgaqpaaeiirATRW 79
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADiygP--SIPRLLGVEGKPLHQS----------------EEGI 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  80 aglellpgVPALAG--ATVELNTALDPHERAL--------CLRQALENVT--DYDYVLIDSPPSLG--TLTV-NALCAAE 144
Cdd:cd02037    63 --------VPVEVGgiKVMSIGFLLPEDDAVIwrgpmksgAIKQFLKDVDwgELDYLIIDLPPGTGdeHLSLvQLIPIDG 134


                  ....
gi 1490718103 145 GVIV 148
Cdd:cd02037   135 AVVV 138
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-247 6.99e-09

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 55.16  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLN--PRSLSV---------SIYDVLLGAQPAAEIIRAtrw 79
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEkiPTVLDVlrekgidnlGLEDIIYEGFNGIYCVES--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  80 AGLEllPGVpALAGATVElnTALDPHERAlclrQALENVtDYDYVLIDsppSLGTLTVNALCA------AEGVIVPVQCE 153
Cdd:PRK13230   86 GGPE--PGY-GCAGRGVI--TAIDLLKKL----GVFEEL-GPDVVIYD---ILGDVVCGGFAMplqkglADDVYIVTTCD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 154 YLALEGLTQLMNTITLIQRRMNlhLALRGLVmtmYDRRTTLSR-QVAAEVQRHFSSQVFPvMIPRSVRLSEAPSYGEPGI 232
Cdd:PRK13230  153 PMAIYAANNICKGIKRFAKRGK--SALGGII---YNGRSVIDApDIVEEFAKKIGTNVIG-KIPMSNIITEAEIYGKTVI 226

                         250
                  ....*....|....*
gi 1490718103 233 FYAPRSQGALAYRTL 247
Cdd:PRK13230  227 EYAPDSEISNIFREL 241
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 1.04e-08

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: 1.04e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID 40
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-148 1.39e-08

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 54.00  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID------PqsnatTSLGLNPRSL----------------SVS 59
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADiygpsiP-----RMLGLEGERPeqsdggiipveahgikVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  60 IyDVLLGAQPAAEIiratrWAGlellpgvPALAGAtvelntaldpheralcLRQALENV--TDYDYVLIDSPPslGT--- 134
Cdd:pfam10609  78 I-GFLLPDEDDAVI-----WRG-------PMKSGA----------------IKQFLTDVdwGELDYLIIDLPP--GTgde 126

                         170
                  ....*....|....*.
gi 1490718103 135 -LTV-NALCAAEGVIV 148
Cdd:pfam10609 127 qLTLaQLLPLTGAVIV 142
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-128 1.66e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 54.02  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLN-PRSLSVSIYDVLlgaqpaAEIIRATrwaglellpgvP 89
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEvEADLIKPLGEMR------ELIKERT-----------G 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490718103  90 ALAGATVELNTALDP-HERAL----------------------C-----LRQALENVTD--YDYVLIDS 128
Cdd:COG3640    71 APGGGMFKLNPKVDDiPEEYLvegdgvdllvmgtieeggsgcyCpenalLRALLNHLVLgnYEYVVVDM 139
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-135 6.57e-08

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 52.51  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANqKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSnattSLGlnprslsvsiyDVL---LGAQP-------- 69
Cdd:COG0003     2 MTRIIFFTG-KGGVGKTTVAAATALALAERGKRTLLVSTDPAH----SLG-----------DVLgteLGNEPtevavpnl 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  70 -AAEI--IRATR--WAGL-----ELLP--GVPALAGA---TVELnTALDpheralCLRQALENvTDYDYVLIDSPPSLGT 134
Cdd:COG0003    66 yALEIdpEAELEeyWERVraplrGLLPsaGVDELAESlpgTEEL-AALD------ELLELLEE-GEYDVIVVDTAPTGHT 137


                  .
gi 1490718103 135 L 135
Cdd:COG0003   138 L 138
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 2-205 9.54e-08

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: 52.80  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTS-LGLNPRSlsvSIYDVLLGAQPAAEIIRATRWA 80
Cdd:TIGR01005 553 NNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQmFGKAPKP---GLLDLLAGEASIEAGIHRDQRP 629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  81 GLELLPgvpalAGAtvelnTALDPHERA-LCLRQALENVTD-----YDYVLIDSPPSLGTLTVNALCA-AEGVIVPVQCE 153
Cdd:TIGR01005 630 GLAFIA-----AGG-----ASHFPHNPNeLLANPAMAELIDnarnaFDLVLVDLAALAAVADAAAFAAlADGILFVTEFE 699

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490718103 154 YLALEGLTQLMNTITLIQRRMnLHLALRGLVMTMYDRRTTLSRqvaAEVQRH 205
Cdd:TIGR01005 700 RSPLGEIRDLIHQEPHANSDV-LGVIFNALDMNELGKYGDFDG---AEKYRH 747
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 11-247 1.53e-07

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: 50.84  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPqSNAttsLGLNprsLSVSIYDVLLGAQPAAEIiRATRWAGLELLPG--- 87
Cdd:pfam06564  10 RGGVGTTSILAALAWALQRLGERVLLIDLSP-DNL---LRLH---FNVPFEHRQGWARAELDG-ADWRDAALEYTPGldl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  88 VP--ALAGATVELNTALDPHERALCLRQAlENVTDYDYVLIDSPPSLGTLTVNALCAAEGVIVPVQCEylalegltqlMN 165
Cdd:pfam06564  82 LPfgRLSVEEQENLQQLQPDPGAWCRRLQ-QLKGRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPD----------AN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 166 TITLIQRRMNLHLALrgLVMTMYDRRTTLSRQVAaEVQRHFSSQVFPVMIPRSVRLSEAPSYGEPGIFYAPRSQGALAYR 245
Cdd:pfam06564 151 CHVLLHQQPLPDADH--LLINDFRPASQLQQDLL-QLWRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRPDSLAAEEVL 227


                  ..
gi 1490718103 246 TL 247
Cdd:pfam06564 228 TL 229
PRK10818 PRK10818
septum site-determining protein MinD;
1-252 7.16e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 49.17  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   1 MTRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID-PQSNATTSLGLNPRslsvSIYDVLLGAQPAAE----IIR 75
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERR----VVYDFVNVIQGDATlnqaLIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  76 ATRWAGLELLPgvpalagatvelntALDPHERALCLRQALENVTD------YDYVLIDSPPSLGTLTVNALCAAEGVIVP 149
Cdd:PRK10818   77 DKRTENLYILP--------------ASQTRDKDALTREGVAKVLDdlkamdFEFIVCDSPAGIETGALMALYFADEAIIT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 150 VQCEYLALEGLTQLMNTITLIQRRmnlhlALRG-------LVMTMYD-----RRTTLSRQVAAEVQRhfssqvFPVM--I 215
Cdd:PRK10818  143 TNPEVSSVRDSDRILGILASKSRR-----AENGeepikehLLLTRYNpgrvsRGDMLSMEDVLEILR------IKLVgvI 211

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1490718103 216 PRSVRLSEAPSYGEPGIFYAPRSQGAlAYRTLTWELL 252
Cdd:PRK10818  212 PEDQSVLRASNQGEPVILDIEADAGK-AYADTVDRLL 247
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 11-135 1.31e-06

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: 48.50  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTS----LGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAGLELLP 86
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSfnqkFGHEPTKVKENLSAMEIDPNMELEEYWQEVQKYMNALL 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490718103  87 GVPALAGATVELNTALDPHERALCLRQALENVT--DYDYVLIDSPPSLGTL 135
Cdd:pfam02374  89 GLRMLEGILAEELASLPGIDEAASFDEFKKYMDegEYDVVVFDTAPTGHTL 139
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-135 1.47e-06

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


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 48.27  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGlnpRSLS----VSIYDVL----LGAQPAAEIIRATRWAGL 82
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFG---QKLGgetpVKGAPNLwameIDPEEALEEYWEEVKELL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490718103  83 ELLPGVPALAGATVELNTALdP--HERA--LCLRQALENvTDYDYVLIDSPPSLGTL 135
Cdd:cd02035    85 AQYLRLPGLDEVYAEELLSL-PgmDEAAafDELREYVES-GEYDVIVFDTAPTGHTL 139
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-150 2.07e-06

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: 47.83  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   3 RIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQsNATTSLGLNPRSLSVsiydvllgaqpaaeiiratRWAGL 82
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENRSATA-------------------DRTGL 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490718103  83 ElLPGVPALAGATVELNTALDPhERALCLRqaLENVTD-----YDYVLIDSPPSLGTLTVNALCAAEGVIVPV 150
Cdd:pfam09140  61 S-LPTPEHLNLPDNDVAEVPDG-ENIDDAR--LEEAFAdlearCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 11-51 2.62e-06

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: 47.31  E-value: 2.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGL 51
Cdd:cd02034     8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGV 48
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 5-44 3.94e-06

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: 47.78  E-value: 3.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1490718103   5 YAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSN 44
Cdd:TIGR04291   5 YLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 11-268 8.03e-06

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 46.20  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSL--GLNPRSLSVSIYDVLLGAQPAAEIIRATRWAGLELL--- 85
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLtgGKVPPTIDEMLTEDGTAEELRREDLLFSGFNGVDCVeag 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  86 ---PGVpALAGATVelNTALDpheralCLRQALENVTDYDYVLIDsppSLGTLTVNALCA------AEGVIVPVQCEYLA 156
Cdd:cd02117    88 gpePGV-GCGGRGI--GTMLE------LLEEHGLLDDDYDVVIFD---VLGDVVCGGFAAplrrgfAQKVVIVVSEELMS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103 157 LEGltqlMNTIT-LIQRRMNLHLALRGLVMtmydrrtTLSRQVAAEVQRHFSSQV-FPVM--IPRSVRLSEAPSYGEPGI 232
Cdd:cd02117   156 LYA----ANNIVkAVENYSKNGVRLAGLVA-------NLRDPAGTEEIQAFAAAVgTKILavIPRDPAVRRAELARVTVF 224

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1490718103 233 FYAPRSQGALAYRTLTWELLRGDGHEVDWSPPAVAE 268
Cdd:cd02117   225 EHDPVSPAASEFARLAAKIADAVPPVPGPRPLSDRE 260
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-46 2.52e-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: 44.43  E-value: 2.52e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNAT 46
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADST 43
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
13-132 3.44e-05

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 44.76  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  13 GVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSL-GLNP-RSLSvsiyDVLLGAQPAAEIIRATRWAGLELLPgvpa 90
Cdd:PRK11519  537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELlGTNNvNGLS----DILIGQGDITTAAKPTSIANFDLIP---- 608

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490718103  91 lAGATVELNTALDPHERalcLRQALENVTD-YDYVLIDSPPSL 132
Cdd:PRK11519  609 -RGQVPPNPSELLMSER---FAELVNWASKnYDLVLIDTPPIL 647
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 11-64 3.61e-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: 44.21  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLglnPRSLSVSIYDVL 64
Cdd:cd02032     8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTL---TGFLIPTVIDVL 58
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 11-49 9.87e-05

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 42.90  E-value: 9.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNaTTSL 49
Cdd:cd02033    39 KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSD-TTSL 76
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 11-49 1.21e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.64  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSL 49
Cdd:PRK13185   10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTL 48
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 11-49 2.25e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 41.71  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1490718103  11 KGGVGKTTTVVNLAASMADwGFRVLVVDIDPQSNATTSL 49
Cdd:PRK13231   10 KGGIGKSTTVSNMAAAYSN-DHRVLVIGCDPKADTTRTL 47
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-150 2.82e-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: 40.99  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103   2 TRIYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNAttslglnprslsvsiyDVLLGAQPAA---EIIRA-- 76
Cdd:cd17869     3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQST----------------DVFFGASGRYlmsDHLYTlk 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490718103  77 TRWAGLELL---------PGVPALAGATVELNTALDPHERALCLRQALENVTDYDYVLIDSPPSLGTLTVNALCAAEGVI 147
Cdd:cd17869    67 SRKANLADKlescvkqheSGVYYFSPFKSALDILEIKKDDILHMITKLVEAHAYDYIIMDLSFEFSSTVCKLLQASHNNV 146


                  ...
gi 1490718103 148 VPV 150
Cdd:cd17869   147 VIA 149
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-62 3.08e-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: 3.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSLGLNPRSLSVSIYD 62
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRID 380
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-40 3.47e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 41.57  E-value: 3.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1490718103   4 IYAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDID 40
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 5-58 1.44e-03

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


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490718103   5 YAFANQKGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNAT----TSLGLNPRSLSV 58
Cdd:NF041417  335 YLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgTEVGHEPTKVGV 392
chlL CHL00072
photochlorophyllide reductase subunit L
 11-49 3.17e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.18  E-value: 3.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1490718103  11 KGGVGKTTTVVNLAASMADWGFRVLVVDIDPQSNATTSL 49
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTL 46
nifH PRK13233
nitrogenase iron protein;
1-46 3.30e-03

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 38.26  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1490718103   1 MTRIYAFANqKGGVGKTTTVVNLAASMADW-GFRVLVVDIDPQSNAT 46
Cdd:PRK13233    1 MTRKIAIYG-KGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPKADST 46
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 13-83 3.54e-03

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 37.74  E-value: 3.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490718103  13 GVGKTTTVVNLAASMADWGFRVLVVDIDPQ-SNATTSLGLNPRSLSVSIYDVLLGAQPAAEIIRATRWAGLE 83
Cdd:cd03115    10 GSGKTTTLAKLARYYQEKGKKVLLIAADTFrAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKLE 81
 
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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