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Conserved domains on  [gi|446090001|ref|WP_000167856|]
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ParA family protein [Escherichia coli]

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 ...
 2-248 5.21e-38

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: 136.14  E-value: 5.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIACigdeefseLLEPSDDfpfGKTVKAFalpYIQQ 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL--------GLDPDDL---DPTLYDL---LLDD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  82 NTIGEVYttepkTKTDAGVLHIVPGDFWLNTFSDILnvgtdviSGAGLYRFILPDLITKKASEkndviYDYVLIDLPPSF 161
Cdd:COG1192   67 APLEDAI-----VPTEIPGLDLIPANIDLAGAEIEL-------VSRPGRELRLKRALAPLADD-----YDYILIDCPPSL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001 162 NTLVRSSLYCSDYFLVPCTPDLFSsycvgLIGemLPSFIRDWEQGKERYlsgNPRDNIIsqkgmpkfgGWIFNGFDTRK- 240
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLS-----LEG--LAQLLETIEEVREDL---NPKLEIL---------GILLTMVDPRTr 190


                 ....*....
gi 446090001 241 -QNDVKQEV 248
Cdd:COG1192  191 lSREVLEEL 199
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-248 5.21e-38

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: 136.14  E-value: 5.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIACigdeefseLLEPSDDfpfGKTVKAFalpYIQQ 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL--------GLDPDDL---DPTLYDL---LLDD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  82 NTIGEVYttepkTKTDAGVLHIVPGDFWLNTFSDILnvgtdviSGAGLYRFILPDLITKKASEkndviYDYVLIDLPPSF 161
Cdd:COG1192   67 APLEDAI-----VPTEIPGLDLIPANIDLAGAEIEL-------VSRPGRELRLKRALAPLADD-----YDYILIDCPPSL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001 162 NTLVRSSLYCSDYFLVPCTPDLFSsycvgLIGemLPSFIRDWEQGKERYlsgNPRDNIIsqkgmpkfgGWIFNGFDTRK- 240
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLS-----LEG--LAQLLETIEEVREDL---NPKLEIL---------GILLTMVDPRTr 190


                 ....*....
gi 446090001 241 -QNDVKQEV 248
Cdd:COG1192  191 lSREVLEEL 199
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-185 1.06e-29

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: 111.91  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIAC-----IGDEEFSELLepsddfpfgktvkafal 76
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgidknNVEKTIYELL----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   77 pyIQQNTIGEVYttepkTKTDAGVLHIVPgdfwlntfSDILNVGTDV-ISGAGLYRFILPDLITKKaseKNDviYDYVLI 155
Cdd:pfam13614  64 --IGECNIEEAI-----IKTVIENLDLIP--------SNIDLAGAEIeLIGIENRENILKEALEPV---KDN--YDYIII 123

                         170       180       190
                  ....*....|....*....|....*....|
gi 446090001  156 DLPPSFNTLVRSSLYCSDYFLVPCTPDLFS 185
Cdd:pfam13614 124 DCPPSLGLLTINALTASDSVLIPVQCEYYA 153
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-210 6.73e-25

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: 97.61  E-value: 6.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiacigdeefsellepsddfpfgktvkafalpyiqqn 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  83 tigevyttepktktdagvlhivpgdFWLntfsdilnvgtdvisgaglyrfilpdlitkkasekndviYDYVLIDLPPSFN 162
Cdd:cd02042   45 -------------------------SWL---------------------------------------YDYILIDTPPSLG 60

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446090001 163 TLVRSSLYCSDYFLVPCTPDLFSSYCVGLIGEMLPSFIRDWEQGKERY 210
Cdd:cd02042   61 LLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLIL 108
ParA_partition NF041546
ParA family partition ATPase;
4-186 2.93e-17

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 79.13  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   4 TISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiacigdeEFSELLEPSDDFPFgktvkafalpyiqqnt 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------DWAAAREDERPFPV---------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  84 igevyttepktktdagvlhivpgdfwlntfsdilnVGtdvISGAGLYRFIlpdlitKKASEKndviYDYVLIDLPPSFNT 163
Cdd:NF041546  58 -----------------------------------VG---LARPTLHREL------PSLARD----YDFVVIDGPPRAED 89

                        170       180
                 ....*....|....*....|....*.
gi 446090001 164 LVRSSLYCSDYFLVPCTP---DLFSS 186
Cdd:NF041546  90 LARSAIKAADLVLIPVQPspyDLWAS 115
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-211 2.07e-10

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: 60.44  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIacigdeefsellepsddfpfgktvkAFALPYIQQN 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRL-------------------------HFGMDWSVRD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   83 TIGEVYTTepktktdagvlhivpGDFWLNTFSDILNvGTDVI-----SGAGLYRFILPD------LITKKASEKNDViyd 151
Cdd:TIGR03371  57 GWARALLN---------------GADWAAAAYRSPD-GVLFLpygdlSADEREAYQAHDagwlarLLQQLDLAARDW--- 117

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  152 yVLIDLPPSFNTLVRSSLYCSDYFLVPCTPDlfSSYCVGLIGEMLPSFIRDWEQGKERYL 211
Cdd:TIGR03371 118 -VLIDLPRGPSPITRQALAAADLVLVVVNAD--AACYATLHQLALALFAGSGPRDGPRFL 174
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-184 7.30e-10

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 59.69  E-value: 7.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiACIGdeefselLEPSDDFPFGKTVKAfALPY-IQQ 81
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS-ALLG-------VLPETDVGANETLYA-AIRYdDTR 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  82 NTIGEVYTTepkTKTDAgvLHIVPGDFWLNTFSDIL-NVGTDVISGAGLYrfilpdlITKKASEKNDVI--YDYVLIDLP 158
Cdd:PRK13869 193 RPLRDVIRP---TYFDG--LHLVPGNLELMEFEHTTpKALSDKGTRDGLF-------FTRVAQAFDEVAddYDVVVIDCP 260

                        170       180
                 ....*....|....*....|....*.
gi 446090001 159 PSFNTLVRSSLYCSDYFLVPCTPDLF 184
Cdd:PRK13869 261 PQLGFLTLSGLCAATSMVITVHPQML 286
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-177 5.24e-09

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 56.69  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   1 MTKTISIFNNKGGVGKTTIIWNLAVSLADK-GKSVLLIDFDPQCNLSiacigdeefsellepsddFPFGKTvkaFALPYI 79
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNAT------------------QFLSKT---FNVPNF 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  80 QQNTIG--EVYTTEPKTKTDAGVLHIVPGDFWLNTFSDILNvgtDVISGAGLYRFILPDLITKKaseKNDviYDYVLIDL 157
Cdd:NF041283  60 PQSFMKcvEDGDLEKGIVHLTPNLDLIAGDYDTRELGDFLA---DKFKSEYDRTFYLKKLLDKI---KDD--YDFIFIDV 131

                        170       180
                 ....*....|....*....|
gi 446090001 158 PPSFNTLVRSSLYCSDYFLV 177
Cdd:NF041283 132 PPSTDIKVDNAMVAADYVIV 151
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 8-46 7.66e-04

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: 41.40  E-value: 7.66e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446090001   8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLS 46
Cdd:NF041417  17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLS 55
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 8-45 9.40e-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: 37.94  E-value: 9.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446090001   8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNL 45
Cdd:NF041417 338 FTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHL 375
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-248 5.21e-38

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: 136.14  E-value: 5.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIACigdeefseLLEPSDDfpfGKTVKAFalpYIQQ 81
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL--------GLDPDDL---DPTLYDL---LLDD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  82 NTIGEVYttepkTKTDAGVLHIVPGDFWLNTFSDILnvgtdviSGAGLYRFILPDLITKKASEkndviYDYVLIDLPPSF 161
Cdd:COG1192   67 APLEDAI-----VPTEIPGLDLIPANIDLAGAEIEL-------VSRPGRELRLKRALAPLADD-----YDYILIDCPPSL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001 162 NTLVRSSLYCSDYFLVPCTPDLFSsycvgLIGemLPSFIRDWEQGKERYlsgNPRDNIIsqkgmpkfgGWIFNGFDTRK- 240
Cdd:COG1192  130 GLLTLNALAAADSVLIPVQPEYLS-----LEG--LAQLLETIEEVREDL---NPKLEIL---------GILLTMVDPRTr 190


                 ....*....
gi 446090001 241 -QNDVKQEV 248
Cdd:COG1192  191 lSREVLEEL 199
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-185 1.06e-29

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: 111.91  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIAC-----IGDEEFSELLepsddfpfgktvkafal 76
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLgidknNVEKTIYELL----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   77 pyIQQNTIGEVYttepkTKTDAGVLHIVPgdfwlntfSDILNVGTDV-ISGAGLYRFILPDLITKKaseKNDviYDYVLI 155
Cdd:pfam13614  64 --IGECNIEEAI-----IKTVIENLDLIP--------SNIDLAGAEIeLIGIENRENILKEALEPV---KDN--YDYIII 123

                         170       180       190
                  ....*....|....*....|....*....|
gi 446090001  156 DLPPSFNTLVRSSLYCSDYFLVPCTPDLFS 185
Cdd:pfam13614 124 DCPPSLGLLTINALTASDSVLIPVQCEYYA 153
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-210 6.73e-25

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: 97.61  E-value: 6.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiacigdeefsellepsddfpfgktvkafalpyiqqn 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  83 tigevyttepktktdagvlhivpgdFWLntfsdilnvgtdvisgaglyrfilpdlitkkasekndviYDYVLIDLPPSFN 162
Cdd:cd02042   45 -------------------------SWL---------------------------------------YDYILIDTPPSLG 60

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446090001 163 TLVRSSLYCSDYFLVPCTPDLFSSYCVGLIGEMLPSFIRDWEQGKERY 210
Cdd:cd02042   61 LLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLIL 108
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-185 7.07e-23

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: 95.11  E-value: 7.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    5 ISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiacigdeeFSELLEPSDDFPFgKTVKAFALPYIQQNTI 84
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNS--------SVEGLEGDIAPAL-QALAEGLKGRVNLDPI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   85 geVYttepKTKTDAGVLHIVPGDFWLNTFsDILNVGTDVisgaglyRFILPDLItkKASEKNdviYDYVLIDLPPSFNTL 164
Cdd:pfam01656  72 --LL----KEKSDEGGLDLIPGNIDLEKF-EKELLGPRK-------EERLREAL--EALKED---YDYVIIDGAPGLGEL 132

                         170       180
                  ....*....|....*....|.
gi 446090001  165 VRSSLYCSDYFLVPCTPDLFS 185
Cdd:pfam01656 133 LRNALIAADYVIIPLEPEVIL 153
ParA_partition NF041546
ParA family partition ATPase;
4-186 2.93e-17

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 79.13  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   4 TISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiacigdeEFSELLEPSDDFPFgktvkafalpyiqqnt 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSAL-------DWAAAREDERPFPV---------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  84 igevyttepktktdagvlhivpgdfwlntfsdilnVGtdvISGAGLYRFIlpdlitKKASEKndviYDYVLIDLPPSFNT 163
Cdd:NF041546  58 -----------------------------------VG---LARPTLHREL------PSLARD----YDFVVIDGPPRAED 89

                        170       180
                 ....*....|....*....|....*.
gi 446090001 164 LVRSSLYCSDYFLVPCTP---DLFSS 186
Cdd:NF041546  90 LARSAIKAADLVLIPVQPspyDLWAS 115
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-211 2.07e-10

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: 60.44  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIacigdeefsellepsddfpfgktvkAFALPYIQQN 82
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRL-------------------------HFGMDWSVRD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   83 TIGEVYTTepktktdagvlhivpGDFWLNTFSDILNvGTDVI-----SGAGLYRFILPD------LITKKASEKNDViyd 151
Cdd:TIGR03371  57 GWARALLN---------------GADWAAAAYRSPD-GVLFLpygdlSADEREAYQAHDagwlarLLQQLDLAARDW--- 117

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  152 yVLIDLPPSFNTLVRSSLYCSDYFLVPCTPDlfSSYCVGLIGEMLPSFIRDWEQGKERYL 211
Cdd:TIGR03371 118 -VLIDLPRGPSPITRQALAAADLVLVVVNAD--AACYATLHQLALALFAGSGPRDGPRFL 174
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-183 4.66e-10

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: 60.13  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLAD-KGKSVLLIDFDPQcnlsiacigdeeFSEL-----LEPSDDFpfgktvkAFAL 76
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQ------------FGDValyldLEPRRGL-------ADAL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  77 PyiQQNTIGEVYTTEPKTKTDAGvLHIVPGDfwlNTFSDILNVGTDVISgaglyrfilpDLITKKASEkndviYDYVLID 156
Cdd:COG4963  164 R--NPDRLDETLLDRALTRHSSG-LSVLAAP---ADLERAEEVSPEAVE----------RLLDLLRRH-----FDYVVVD 222

                        170       180
                 ....*....|....*....|....*..
gi 446090001 157 LPPSFNTLVRSSLYCSDYFLVPCTPDL 183
Cdd:COG4963  223 LPRGLNPWTLAALEAADEVVLVTEPDL 249
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 5-181 4.97e-10

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: 60.38  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    5 ISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiACIGdeefselLEPSDDFPFGKTVKAfALPYIQQN-T 83
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-ALFG-------YQPEFDVGENETLYG-AIRYDDERrP 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   84 IGEVYTtepKTKTDAgvLHIVPGDFWLNTFS-DILNVGTDVISGAGLYRFILPDLItkkASEKNDviYDYVLIDLPPSFN 162
Cdd:TIGR03453 178 ISEIIR---KTYFPG--LDLVPGNLELMEFEhETPRALSRGQGGDTIFFARVGEAL---AEVEDD--YDVVVIDCPPQLG 247

                         170
                  ....*....|....*....
gi 446090001  163 TLVRSSLYCSDYFLVPCTP 181
Cdd:TIGR03453 248 FLTLSALCAATGVLITVHP 266
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-40 6.73e-10

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 58.75  E-value: 6.73e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-40 7.12e-10

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 58.92  E-value: 7.12e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446090001   1 MTKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-184 7.30e-10

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 59.69  E-value: 7.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSiACIGdeefselLEPSDDFPFGKTVKAfALPY-IQQ 81
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS-ALLG-------VLPETDVGANETLYA-AIRYdDTR 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  82 NTIGEVYTTepkTKTDAgvLHIVPGDFWLNTFSDIL-NVGTDVISGAGLYrfilpdlITKKASEKNDVI--YDYVLIDLP 158
Cdd:PRK13869 193 RPLRDVIRP---TYFDG--LHLVPGNLELMEFEHTTpKALSDKGTRDGLF-------FTRVAQAFDEVAddYDVVVIDCP 260

                        170       180
                 ....*....|....*....|....*.
gi 446090001 159 PSFNTLVRSSLYCSDYFLVPCTPDLF 184
Cdd:PRK13869 261 PQLGFLTLSGLCAATSMVITVHPQML 286
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-182 1.13e-09

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: 57.96  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDpqcnlsiacIGdeeFSELlepsdDFPFGKTVKafalpyiqqN 82
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD---------LG---LANL-----DILLGLAPK---------K 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  83 TIGEVYTTEPKtktdagvlhivpgdfwlntFSDILNVGT---DVISGAGLYrfilPDLITKKASEKNDVI---------Y 150
Cdd:cd02038   55 TLGDVLKGRVS-------------------LEDIIVEGPeglDIIPGGSGM----EELANLDPEQKAKLIeelsslesnY 111

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446090001 151 DYVLIDLPP--SFNTLvrSSLYCSDYFLVPCTPD 182
Cdd:cd02038  112 DYLLIDTGAgiSRNVL--DFLLAADEVIVVTTPE 143
PHA02518 PHA02518
ParA-like protein; Provisional
 3-42 1.36e-09

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 57.55  E-value: 1.36e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQ 40
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 11-159 4.92e-09

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: 56.73  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFD---PQCNLSIACIGDEEFSELLepSDDFPFGKTVKafalpyiqqntigev 87
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENRPGLSDVL--AGEASLEDVIQ--------------- 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446090001  88 yttepktKTDAGVLHIVPGDFWLNTFSDILNvgtdviSGAglyrfiLPDLITKKASEkndviYDYVLIDLPP 159
Cdd:COG0489  164 -------PTEVEGLDVLPAGPLPPNPSELLA------SKR------LKQLLEELRGR-----YDYVIIDTPP 211
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
1-177 5.24e-09

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 56.69  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   1 MTKTISIFNNKGGVGKTTIIWNLAVSLADK-GKSVLLIDFDPQCNLSiacigdeefsellepsddFPFGKTvkaFALPYI 79
Cdd:NF041283   1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTDLQGNAT------------------QFLSKT---FNVPNF 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  80 QQNTIG--EVYTTEPKTKTDAGVLHIVPGDFWLNTFSDILNvgtDVISGAGLYRFILPDLITKKaseKNDviYDYVLIDL 157
Cdd:NF041283  60 PQSFMKcvEDGDLEKGIVHLTPNLDLIAGDYDTRELGDFLA---DKFKSEYDRTFYLKKLLDKI---KDD--YDFIFIDV 131

                        170       180
                 ....*....|....*....|
gi 446090001 158 PPSFNTLVRSSLYCSDYFLV 177
Cdd:NF041283 132 PPSTDIKVDNAMVAADYVIV 151
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-196 1.79e-08

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: 54.74  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001    3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDpqcnLSIACIgdeefsELLEPSDDFPfgktvkafalPYIQQN 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD----ITMANL------ELILGMEDKP----------VTLHDV 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   83 TIGEVYTTEPKTKTDAGVLhIVPGdfwlntfsdilNVGTDVISGAGLYRfiLPDLITKKASEkndviYDYVLIDLPPSFN 162
Cdd:TIGR01969  61 LAGEADIKDAIYEGPFGVK-VIPA-----------GVSLEGLRKADPDK--LEDVLKEIIDD-----TDFLLIDAPAGLE 121

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446090001  163 TLVRSSLYCSDYFLVPCTPDLFS---SYCVGLIGEML 196
Cdd:TIGR01969 122 RDAVTALAAADELLLVVNPEISSitdALKTKIVAEKL 158
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-183 3.40e-08

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 53.44  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKS-VLLIDFDPQ---CNLSIACIGDEEFSELLEPSDDfpfgktvkafalpy 78
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDkVLLIDLDLPfgdLGLYLNLRPDYDLADVIQNLDR-------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  79 iqqntIGEVYTTEPKTKTDAGvLHIVPGDfwlNTFSDILNVGTDVISgaglyrfilpDLITKKASEkndviYDYVLIDLP 158
Cdd:cd03111   67 -----LDRTLLDSAVTRHSSG-LSLLPAP---QELEDLEALGAEQVD----------KLLQVLRAF-----YDHIIVDLG 122

                        170       180
                 ....*....|....*....|....*
gi 446090001 159 PSFNTLVRSSLYCSDYFLVPCTPDL 183
Cdd:cd03111  123 HFLDEVTLAVLEAADEILLVTQQDL 147
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 8-45 6.25e-08

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: 54.32  E-value: 6.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446090001    8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNL 45
Cdd:TIGR04291   8 FTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNV 45
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 11-40 2.24e-07

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: 48.58  E-value: 2.24e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:cd01983    9 KGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 11-46 2.81e-07

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: 50.97  E-value: 2.81e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLS 46
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLS 43
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-45 3.21e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 50.94  E-value: 3.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNL 45
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL 42
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 8-46 4.39e-07

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 50.81  E-value: 4.39e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446090001    8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLS 46
Cdd:pfam02374   6 FGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLS 44
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-46 5.84e-07

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 50.59  E-value: 5.84e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446090001   1 MTKTIsIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLS 46
Cdd:COG0003    2 MTRII-FFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLG 46
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-40 1.36e-06

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: 48.87  E-value: 1.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446090001    3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 5-40 2.18e-06

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 47.88  E-value: 2.18e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446090001   5 ISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:cd02037    3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 13-40 3.60e-06

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: 46.79  E-value: 3.60e-06
                         10        20
                 ....*....|....*....|....*...
gi 446090001  13 GVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDAD 57
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-185 5.37e-06

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: 46.81  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  18 TIIWNLAVSLADKGKSVLLIDFDPQC-NLSIAcigdeefsellepsddfpFGKTVKAfalpyiqqnTIGEV--------- 87
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLaNLDVL------------------LGLEPKA---------TLADVlageadled 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  88 YTTEpktkTDAGvLHIVPGDfwlNTFSDILNvgtdvISGAGLYRFILPDLITKkasekndviYDYVLIDLPPSFNTLVRS 167
Cdd:COG0455   54 AIVQ----GPGG-LDVLPGG---SGPAELAE-----LDPEERLIRVLEELERF---------YDVVLVDTGAGISDSVLL 111

                        170
                 ....*....|....*...
gi 446090001 168 SLYCSDYFLVPCTPDLFS 185
Cdd:COG0455  112 FLAAADEVVVVTTPEPTS 129
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 11-40 5.62e-06

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 47.06  E-value: 5.62e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 446090001   11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
minD CHL00175
septum-site determining protein; Validated
 1-40 1.02e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 46.69  E-value: 1.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446090001   1 MTKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-53 1.11e-05

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 47.00  E-value: 1.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446090001   11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIACIGDE 53
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSL 371
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 11-65 2.00e-05

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: 45.38  E-value: 2.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLSIACIGDEEFSELLEPSDDF 65
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGDI 62
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-42 2.19e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 45.34  E-value: 2.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446090001   1 MTKTISIFNnKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 3-68 4.15e-05

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: 44.66  E-value: 4.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446090001   3 KTISIFNnKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ------------CNLSIACIGDEEFSELLEPSDDFPFG 68
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKhdstllltggkvPPTIDEMLTEDGTAEELRREDLLFSG 77
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 3-42 4.78e-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: 4.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446090001   3 KTISIFNnKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
PRK10818 PRK10818
septum site-determining protein MinD;
1-40 6.93e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 43.77  E-value: 6.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446090001   1 MTKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 5-184 9.38e-05

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 43.14  E-value: 9.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   5 ISIFNNKGGVGKTTIIWNLAVSLADkgksVLLIDFD---PQCNLSIACIGDEE--FSELLEPSDD--------------- 64
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLLYN----VILVDCDvdaPNLHLLLGPEPEEEedFVGGKKAFIDqekcircgncervck 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  65 -------------FPF---GKTVKAFALPyiqQNTIGEVyttepktKTDAGVLHIVPGDFwLNTFSDILNVGTDViSGAg 128
Cdd:cd03110   78 fgaileffqklivDESlceGCGACVIICP---RGAIYLK-------DRDTGKIFISSSDG-GPLVHGRLNIGEEN-SGK- 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446090001 129 lyrfiLPDLITKKASEKNDViYDYVLIDLPPSFNTLVRSSLYCSDYFLVPCTPDLF 184
Cdd:cd03110  145 -----LVTELRKKALERSKE-CDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPS 194
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 8-42 1.35e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 43.22  E-value: 1.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446090001   8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPK 40
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-187 2.70e-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: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001   2 TKTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDpQCNLSIACIGdEEFSELlePSDDFPFGKTVKAFAL----P 77
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFG-ASGRYL--MSDHLYTLKSRKANLAdkleS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446090001  78 YIQQNTIGEVYTTEPKtktdagvlhiVPGdfwlntfsDILNVGTDVisgaglYRFILPDLITKKAsekndviYDYVLIDL 157
Cdd:cd17869   79 CVKQHESGVYYFSPFK----------SAL--------DILEIKKDD------ILHMITKLVEAHA-------YDYIIMDL 127

                        170       180       190
                 ....*....|....*....|....*....|
gi 446090001 158 PPSFNTLVRSSLYCSDYFLVPCTPDLFSSY 187
Cdd:cd17869  128 SFEFSSTVCKLLQASHNNVVIALQDANSSY 157
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 11-41 3.29e-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: 3.29e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDP 41
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-40 7.46e-04

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: 40.11  E-value: 7.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446090001    3 KTISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD 55
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 8-46 7.66e-04

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: 41.40  E-value: 7.66e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446090001   8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNLS 46
Cdd:NF041417  17 FSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLS 55
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-42 1.76e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 39.73  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446090001   11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPK 39
chlL CHL00072
photochlorophyllide reductase subunit L
 11-42 1.94e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 39.72  E-value: 1.94e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446090001  11 KGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:CHL00072   8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPK 39
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 2-42 2.48e-03

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: 39.43  E-value: 2.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446090001   2 TKTISIFNnKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQ 42
Cdd:cd02033   31 TQIIAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPK 70
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
5-40 3.31e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 38.87  E-value: 3.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446090001   5 ISIFNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFD 40
Cdd:PRK11670 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 8-45 9.40e-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: 37.94  E-value: 9.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446090001   8 FNNKGGVGKTTIIWNLAVSLADKGKSVLLIDFDPQCNL 45
Cdd:NF041417 338 FTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHL 375
 
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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