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Conserved domains on  [gi|491147476|ref|WP_005005874|]
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MULTISPECIES: ParA family protein [Acinetobacter]

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 ...
 16-274 3.77e-61

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: 193.92  E-value: 3.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  16 FKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISnvPDIDDIDGTLKDIFENYKTINihDVIQgpdKTNFENV 95
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLE--DAIV---PTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  96 SLIPCAKNIRDVEINIqRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEY-SIQGLEDI 174
Cdd:COG1192   82 DLIPANIDLAGAEIEL-VSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYlSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 175 LNSMDDL-ETSNPDLKILSPVLNFYNKRNTVDLTLAEDIRNEYAQPKLQEKlvnkelicIPHATVFSQASYVKCSVFDLD 253
Cdd:COG1192  161 LETIEEVrEDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTV--------IPRSVALAEAPSAGKPVFEYD 232

                        250       260
                 ....*....|....*....|.
gi 491147476 254 agKETPAKQAINQLVDLMVSE 274
Cdd:COG1192  233 --PKSKGAKAYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 16-274 3.77e-61

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: 193.92  E-value: 3.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  16 FKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISnvPDIDDIDGTLKDIFENYKTINihDVIQgpdKTNFENV 95
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLE--DAIV---PTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  96 SLIPCAKNIRDVEINIqRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEY-SIQGLEDI 174
Cdd:COG1192   82 DLIPANIDLAGAEIEL-VSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYlSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 175 LNSMDDL-ETSNPDLKILSPVLNFYNKRNTVDLTLAEDIRNEYAQPKLQEKlvnkelicIPHATVFSQASYVKCSVFDLD 253
Cdd:COG1192  161 LETIEEVrEDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTV--------IPRSVALAEAPSAGKPVFEYD 232

                        250       260
                 ....*....|....*....|.
gi 491147476 254 agKETPAKQAINQLVDLMVSE 274
Cdd:COG1192  233 --PKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 14-190 3.14e-40

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: 137.72  E-value: 3.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATkhISNVPDIDDIDGTLKDIFenYKTINIHDVIQgpdKTNFE 93
Cdd:pfam13614   7 ANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT--SGLGIDKNNVEKTIYELL--IGECNIEEAII---KTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   94 NVSLIPCAKNIRDVEINIQrSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGE-YSIQGLE 172
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELI-GIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEyYALEGLS 158

                         170
                  ....*....|....*....
gi 491147476  173 DILNSMDDL-ETSNPDLKI 190
Cdd:pfam13614 159 QLLNTIKLVkKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 14-213 1.04e-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: 98.38  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHIsnvpdiddidgtlkdifenyktinihdviqgpdktnfe 93
Cdd:cd02042    6 ANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  94 nvslipcaknirdveiniqrsspvpneiirsvlrkikgdFDFILLDCPPRMETLTFNALLASNSLLIPLQGE-YSIQGLE 172
Cdd:cd02042   48 ---------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSpFDLDGLA 88

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491147476 173 DILNSMDDL-ETSNPDLKILSPVLNFYNKRNTVDLTLAEDIR 213
Cdd:cd02042   89 KLLDTLEELkKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 14-161 1.05e-18

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: 84.64  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDID-DIDGTLkdifenYKTI-------NIHDVIQ 85
Cdd:TIGR03453 110 TNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDvGENETL------YGAIrydderrPISEIIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   86 gpdKTNFENVSLIPCAKNIRDVE-------INIQRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSL 158
Cdd:TIGR03453 184 ---KTYFPGLDLVPGNLELMEFEhetpralSRGQGGDTIFFARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGV 260


                  ...
gi 491147476  159 LIP 161
Cdd:TIGR03453 261 LIT 263
ParA_partition NF041546
ParA family partition ATPase;
17-269 1.57e-18

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 81.44  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQrnatkhisnvpdiddidGTLKDIFEnyktinihdviQGPDKTNFENVS 96
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQ-----------------GSALDWAA-----------AREDERPFPVVG 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  97 LipcaknirdveiniqrsspvPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQ-GEYSIQGLEDIL 175
Cdd:NF041546  60 L--------------------ARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQpSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 176 NSMDDLETSNPDLKILSpVLNfynkR---NTVdltLAEDIR---NEYAQPKLQEKlvnkelicIPHATVFSQASYVKCSV 249
Cdd:NF041546 120 DLIKEAREYTPGLKAAF-VLN----RaiaRTA---LGREVAealAEYGLPVLKTR--------IGQRVAFAESAAEGLTV 183

                        250       260
                 ....*....|....*....|
gi 491147476 250 FDLDAGKetPAKQAINQLVD 269
Cdd:NF041546 184 FEAEPDG--KAAREIRALAK 201
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 15-160 4.81e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 65.47  E-value: 4.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  15 HFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDID-DIDGTL-KDIFENYKTINIHDVIQgpdKTNF 92
Cdd:PRK13869 128 NFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDvGANETLyAAIRYDDTRRPLRDVIR---PTYF 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491147476  93 ENVSLIPcaKNIRDVEINIQRSSPVPNEIIRSVL---------RKIKGDFDFILLDCPPRMETLTFNALLASNSLLI 160
Cdd:PRK13869 205 DGLHLVP--GNLELMEFEHTTPKALSDKGTRDGLfftrvaqafDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 16-274 3.77e-61

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: 193.92  E-value: 3.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  16 FKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISnvPDIDDIDGTLKDIFENYKTINihDVIQgpdKTNFENV 95
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLLDDAPLE--DAIV---PTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  96 SLIPCAKNIRDVEINIqRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEY-SIQGLEDI 174
Cdd:COG1192   82 DLIPANIDLAGAEIEL-VSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYlSLEGLAQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 175 LNSMDDL-ETSNPDLKILSPVLNFYNKRNTVDLTLAEDIRNEYAQPKLQEKlvnkelicIPHATVFSQASYVKCSVFDLD 253
Cdd:COG1192  161 LETIEEVrEDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTV--------IPRSVALAEAPSAGKPVFEYD 232

                        250       260
                 ....*....|....*....|.
gi 491147476 254 agKETPAKQAINQLVDLMVSE 274
Cdd:COG1192  233 --PKSKGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 14-190 3.14e-40

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: 137.72  E-value: 3.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATkhISNVPDIDDIDGTLKDIFenYKTINIHDVIQgpdKTNFE 93
Cdd:pfam13614   7 ANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAT--SGLGIDKNNVEKTIYELL--IGECNIEEAII---KTVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   94 NVSLIPCAKNIRDVEINIQrSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGE-YSIQGLE 172
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELI-GIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEyYALEGLS 158

                         170
                  ....*....|....*....
gi 491147476  173 DILNSMDDL-ETSNPDLKI 190
Cdd:pfam13614 159 QLLNTIKLVkKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 16-215 4.99e-36

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: 128.23  E-value: 4.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   16 FKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDIDDIDGTLKDIFENYKtiNIHDVIQGPdKTNFENV 95
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRV--NLDPILLKE-KSDEGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   96 SLIPCakNIRDVEINIQRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGE-YSIQGLEDI 174
Cdd:pfam01656  83 DLIPG--NIDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEvILVEDAKRL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 491147476  175 LNSMDDLETSNPD--LKILSPVLNFYNKRNTVDLtLAEDIRNE 215
Cdd:pfam01656 161 GGVIAALVGGYALlgLKIIGVVLNKVDGDNHGKL-LKEALEEL 202
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 14-213 1.04e-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: 98.38  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHIsnvpdiddidgtlkdifenyktinihdviqgpdktnfe 93
Cdd:cd02042    6 ANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL-------------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  94 nvslipcaknirdveiniqrsspvpneiirsvlrkikgdFDFILLDCPPRMETLTFNALLASNSLLIPLQGE-YSIQGLE 172
Cdd:cd02042   48 ---------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSpFDLDGLA 88

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491147476 173 DILNSMDDL-ETSNPDLKILSPVLNFYNKRNTVDLTLAEDIR 213
Cdd:cd02042   89 KLLDTLEELkKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 14-161 1.05e-18

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: 84.64  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDID-DIDGTLkdifenYKTI-------NIHDVIQ 85
Cdd:TIGR03453 110 TNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYQPEFDvGENETL------YGAIrydderrPISEIIR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   86 gpdKTNFENVSLIPCAKNIRDVE-------INIQRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSL 158
Cdd:TIGR03453 184 ---KTYFPGLDLVPGNLELMEFEhetpralSRGQGGDTIFFARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALCAATGV 260


                  ...
gi 491147476  159 LIP 161
Cdd:TIGR03453 261 LIT 263
ParA_partition NF041546
ParA family partition ATPase;
17-269 1.57e-18

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 81.44  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQrnatkhisnvpdiddidGTLKDIFEnyktinihdviQGPDKTNFENVS 96
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQ-----------------GSALDWAA-----------AREDERPFPVVG 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  97 LipcaknirdveiniqrsspvPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQ-GEYSIQGLEDIL 175
Cdd:NF041546  60 L--------------------ARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQpSPYDLWASADTV 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 176 NSMDDLETSNPDLKILSpVLNfynkR---NTVdltLAEDIR---NEYAQPKLQEKlvnkelicIPHATVFSQASYVKCSV 249
Cdd:NF041546 120 DLIKEAREYTPGLKAAF-VLN----RaiaRTA---LGREVAealAEYGLPVLKTR--------IGQRVAFAESAAEGLTV 183

                        250       260
                 ....*....|....*....|
gi 491147476 250 FDLDAGKetPAKQAINQLVD 269
Cdd:NF041546 184 FEAEPDG--KAAREIRALAK 201
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 17-160 1.26e-16

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: 76.86  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLD-SQRNatkhisnvpdIDDIDGtlkdiFENYKTINIHDVIQG--------- 86
Cdd:cd02036    9 KGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRN----------LDLILG-----LENRIVYTLVDVLEGecrleqali 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491147476  87 PDKtNFENVSLIPCAKNIRDVEINIqrsspvpnEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLI 160
Cdd:cd02036   74 KDK-RWENLYLLPASQTRDKDALTP--------EKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAII 138
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 17-203 3.25e-15

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: 73.23  E-value: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSqrnATKHISNVPDIDDIDGTLKDIFENykTINIHDVI-QGPdktnfENV 95
Cdd:TIGR01969   9 KGGTGKTTITANLGVALAKLGKKVLALDADI---TMANLELILGMEDKPVTLHDVLAG--EADIKDAIyEGP-----FGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   96 SLIPCAKNIRdveiNIQRSSPvpnEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEysIQGLEDIL 175
Cdd:TIGR01969  79 KVIPAGVSLE----GLRKADP---DKLEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPE--ISSITDAL 149

                         170       180
                  ....*....|....*....|....*...
gi 491147476  176 NSMDDLETSnpDLKILSPVLNFYNKRNT 203
Cdd:TIGR01969 150 KTKIVAEKL--GTAILGVVLNRVTRDKT 175
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 17-274 3.28e-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: 71.68  E-value: 3.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKL-GYTVLVIDLDSQR---------NATKHISN-VPDIDDIDGTLkdiFENYktinihdVIQ 85
Cdd:COG4963  111 KGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFgdvalyldlEPRRGLADaLRNPDRLDETL---LDRA-------LTR 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  86 GPDktnfeNVSLIPCAKNIrdveiniQRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGe 165
Cdd:COG4963  181 HSS-----GLSVLAAPADL-------ERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP- 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 166 ySIQGLEDILNSMDDLETSNPDLKILSPVLNFYNKRNTVDltlAEDIrneyaqpklqEKLVNKELI-CIPH-ATVFSQAs 243
Cdd:COG4963  248 -DLPSLRNAKRLLDLLRELGLPDDKVRLVLNRVPKRGEIS---AKDI----------EEALGLPVAaVLPNdPKAVAEA- 312

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491147476 244 yvkcsvfdLDAGK-------ETPAKQAINQLVDLMVSE 274
Cdd:COG4963  313 --------ANQGRplaevapKSPLAKAIRKLAARLTGR 342
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 24-190 2.08e-13

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: 67.99  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  24 TSTVNCAAKLGKLGYTVLVIDLDSQRnatkhisnvPDIDDIDG-----TLKDIFENYKTINihDVI-QGPDktnfeNVSL 97
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGL---------ANLDVLLGlepkaTLADVLAGEADLE--DAIvQGPG-----GLDV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  98 IPCAKNIRDveinIQRSSPvpNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEysIQGLEDILNS 177
Cdd:COG0455   65 LPGGSGPAE----LAELDP--EERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPE--PTSITDAYAL 136

                        170
                 ....*....|...
gi 491147476 178 MDDLETSNPDLKI 190
Cdd:COG0455  137 LKLLRRRLGVRRA 149
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 17-141 2.23e-13

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 68.16  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLD-SQRNatkhisnvpdIDDIDGtlkdiFENYKTINIHDVIQG--------- 86
Cdd:COG2894   11 KGGVGKTTTTANLGTALALLGKKVVLIDADiGLRN----------LDLVMG-----LENRIVYDLVDVIEGecrlkqali 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491147476  87 PDKtNFENVSLIPcAKNIRDVEIniqrsspVPNEIIRSVLRKIKGDFDFILLDCP 141
Cdd:COG2894   76 KDK-RFENLYLLP-ASQTRDKDA-------LTPEQMKKLVEELKEEFDYILIDSP 121
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 17-142 1.17e-12

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 66.36  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDsQRNATKH----ISNVPdiddidgTLKDIFENykTINIHDVIQgpdKTNF 92
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDAD-LRGPSLHrmlgLENRP-------GLSDVLAG--EASLEDVIQ---PTEV 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491147476  93 ENVSLIPCAKNIRDveiniqRSSPVPNEIIRSVLRKIKGDFDFILLDCPP 142
Cdd:COG0489  168 EGLDVLPAGPLPPN------PSELLASKRLKQLLEELRGRYDYVIIDTPP 211
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 15-160 4.81e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 65.47  E-value: 4.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  15 HFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDID-DIDGTL-KDIFENYKTINIHDVIQgpdKTNF 92
Cdd:PRK13869 128 NFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPETDvGANETLyAAIRYDDTRRPLRDVIR---PTYF 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491147476  93 ENVSLIPcaKNIRDVEINIQRSSPVPNEIIRSVL---------RKIKGDFDFILLDCPPRMETLTFNALLASNSLLI 160
Cdd:PRK13869 205 DGLHLVP--GNLELMEFEHTTPKALSDKGTRDGLfftrvaqafDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
PHA02518 PHA02518
ParA-like protein; Provisional
 17-269 1.72e-11

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 62.17  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATkhisnvpdiddidgtlkdifenyktinihDVIQgpdkTNFENVS 96
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-----------------------------DWAE----AREEGEP 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  97 LIPCaknirdVEINIQRSSPVPneiirsvlrKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQ-GEYSIQGLEDIL 175
Cdd:PHA02518  56 LIPV------VRMGKSIRADLP---------KVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQpSPFDIWAAPDLV 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 176 NSMDDLETSNPDLkilsPVLNFYNKRNTVDLTLAEDIRN---EYAQPKLQEKLVNKeliciphaTVFSQASYVKCSVFDL 252
Cdd:PHA02518 121 ELIKARQEVTDGL----PKFAFIISRAIKNTQLYREARKalaGYGLPILRNGTTQR--------VAYADAAEAGGSVLEL 188

                        250
                 ....*....|....*..
gi 491147476 253 DagKETPAKQAINQLVD 269
Cdd:PHA02518 189 P--EDDKAAEEIIQLVK 203
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 17-160 2.96e-11

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: 61.82  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQrnatkhISNVpdiDDIDG-----TLKDIFEnyKTINIHDVI-QGPdkt 90
Cdd:cd02038    9 KGGVGKTNVSANLALALSKLGKRVLLLDADLG------LANL---DILLGlapkkTLGDVLK--GRVSLEDIIvEGP--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491147476  91 nfENVSLIPCAKNIRDveinIQRSSPVPNEIIRSVLRKIKGDFDFILLDCPPRM--ETLTFnaLLASNSLLI 160
Cdd:cd02038   75 --EGLDIIPGGSGMEE----LANLDPEQKAKLIEELSSLESNYDYLLIDTGAGIsrNVLDF--LLAADEVIV 138
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 17-160 3.71e-11

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: 61.97  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLD-SQRNatkhisnvpdIDDIDGtlkdiFENYKTINIHDVIQG--------- 86
Cdd:TIGR01968  10 KGGVGKTTTTANLGTALARLGKKVVLIDADiGLRN----------LDLLLG-----LENRIVYTLVDVVEGecrlqqali 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491147476   87 PDKtNFENVSLIPCAKNiRDVEIniqrsspVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLI 160
Cdd:TIGR01968  75 KDK-RLKNLYLLPASQT-RDKDA-------VTPEQMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIV 139
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 17-242 2.35e-10

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 60.38  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVID-LDSQRNATKHISNVPDID-DIDGTLKDIFENYKTinihDVIQGPDKTNFEN 94
Cdd:PRK13705 115 KGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHiHAEDTLLPFYLGEKD----DATYAIKPTCWPG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  95 VSLIPCAKNIRDVEINI-----QRSSPV-PNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGEY-- 166
Cdd:PRK13705 191 LDIIPSCLALHRIETELmgkfdEGKLPTdPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELfd 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 167 ---SIQ---GLEDILNSMdDLETSNPDLKILspVLNFYNKRNTVDLTLAEDIRNEYAQPKLQEKLVNKELIC---IPHAT 237
Cdd:PRK13705 271 ytsALQffdMLRDLLKNV-DLKGFEPDVRIL--LTKYSNSNGSQSPWMEEQIRDAWGSMVLKNVVRETDEVGkgqIRMRT 347


                 ....*
gi 491147476 238 VFSQA 242
Cdd:PRK13705 348 VFEQA 352
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 17-244 5.44e-10

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 59.25  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVID-LDSQRNATKHISNVPDID-DIDGTLKDIFENYKTinihDVIQGPDKTNFEN 94
Cdd:PHA02519 115 KGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVPDLHiHADDTLLPFYLGERD----NAEYAIKPTCWPG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  95 VSLIPCAKNIRDVEINI-----QRSSPV-PNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQGE--- 165
Cdd:PHA02519 191 LDIIPSCLALHRIETDLmqyhdAGKLPHpPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAElfd 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476 166 YS-----IQGLEDILNSMdDLETSNPDLKILspVLNFYNKRNTVDLTLAEDIRNEYAQPKLQEKL-VNKEL--ICIPHAT 237
Cdd:PHA02519 271 YVsvlqfFTMLLDLLATV-DLGGFEPVVRLL--LTKYSLTVGNQSRWMEEQIRNTWGSMVLRQVVrVTDEVgkGQIKMRT 347


                 ....*..
gi 491147476 238 VFSQASY 244
Cdd:PHA02519 348 VFEQAAN 354
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 19-196 3.96e-09

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 54.88  E-value: 3.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  19 GVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISNVPDIDDIDGTLKDifenykTINIHDVIQgpdKTNFENVSLI 98
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVLSG------QASLEDVIQ---STNIPNLDVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  99 PCAKnirdveiniqrSSPVPNEIIRS-----VLRKIKGDFDFILLDCPPrMETLTFNALLASN---SLLIPLQGEYSiqg 170
Cdd:cd05387  101 PAGT-----------VPPNPSELLSSprfaeLLEELKEQYDYVIIDTPP-VLAVADALILAPLvdgVLLVVRAGKTR--- 165

                        170       180
                 ....*....|....*....|....*.
gi 491147476 171 LEDILNSMDDLETSNPdlKILSPVLN 196
Cdd:cd05387  166 RREVKEALERLEQAGA--KVLGVVLN 189
minD CHL00175
septum-site determining protein; Validated
 2-160 9.50e-09

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 55.16  E-value: 9.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   2 EKNSGKTYICTSIHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLD-SQRNatkhisnvpdIDDIDGtlkdiFENYKTINI 80
Cdd:CHL00175   9 EKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRN----------LDLLLG-----LENRVLYTA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  81 HDVIQGP---------DKtNFENVSLIPCAKNirdveiniQRSSPVPNEIIRSVLRKIK-GDFDFILLDCPPRMETLTFN 150
Cdd:CHL00175  74 MDVLEGEcrldqalirDK-RWKNLSLLAISKN--------RQRYNVTRKNMNMLVDSLKnRGYDYILIDCPAGIDVGFIN 144

                        170
                 ....*....|
gi 491147476 151 ALLASNSLLI 160
Cdd:CHL00175 145 AIAPAQEAIV 154
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 17-212 1.83e-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: 53.82  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKL-GYTVLVIDLD----------SQRNATKHISNVPDIDDIDGTLKDIFenyktinihdVIQ 85
Cdd:cd03111    9 KGGVGASTLAVNLAQELAQRaKDKVLLIDLDlpfgdlglylNLRPDYDLADVIQNLDRLDRTLLDSA----------VTR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  86 GPDktnfeNVSLIPCAKNIRDVEiniqrssPVPNEIIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPLQge 165
Cdd:cd03111   79 HSS-----GLSLLPAPQELEDLE-------ALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQ-- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491147476 166 YSIQGLEDILNSMDDLETSNPDLKILSPVLNFYNKRNTVDLTLAEDI 212
Cdd:cd03111  145 QDLPSLRNARRLLDSLRELEGSSDRLRLVLNRYDKKSEISPKDIEEA 191
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 10-196 2.18e-07

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 50.13  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   10 ICTSIHFKG-------------GVGKTTSTVNCAAKLGKLGYTVLVIDLDSqRNATKHIsnVPDIDDIDGTLKDIFENYK 76
Cdd:TIGR01007   6 IRTNIQFSGaeikvllitsvkpGEGKSTTSANIAIAFAQAGYKTLLIDGDM-RNSVMSG--TFKSQNKITGLTNFLSGTT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   77 TINihDVIQGpdkTNFENVSLIPCAKnirdveiniqrSSPVPNEIIRS-----VLRKIKGDFDFILLDCPPrMETLTFNA 151
Cdd:TIGR01007  83 DLS--DAICD---TNIENLDVITAGP-----------VPPNPTELLQSsnfktLIETLRKRFDYIIIDTPP-IGTVTDAA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491147476  152 LLAS---NSLLIPLQGEYSiqgLEDILNSMDDLETSNPdlKILSPVLN 196
Cdd:TIGR01007 146 IIARacdASILVTDAGKIK---KREVKKAKEQLEQAGS--NFLGVVLN 188
PRK10818 PRK10818
septum site-determining protein MinD;
17-167 1.31e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 48.40  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLD-SQRNatkhisnvpdIDDIDGTLKDIFenYKTINihdVIQGPDKTN---- 91
Cdd:PRK10818  11 KGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRN----------LDLIMGCERRVV--YDFVN---VIQGDATLNqali 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  92 ----FENVSLIPcAKNIRDVEiniqrssPVPNEIIRSVLRKIKG-DFDFILLDCPPRMETLTFNALLASNSLLIPLQGEY 166
Cdd:PRK10818  76 kdkrTENLYILP-ASQTRDKD-------ALTREGVAKVLDDLKAmDFEFIVCDSPAGIETGALMALYFADEAIITTNPEV 147


                 .
gi 491147476 167 S 167
Cdd:PRK10818 148 S 148
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 17-46 3.48e-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: 3.48e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLD 46
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 17-147 4.09e-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: 46.73  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDsqrnATKHISNVPDIDDIDGTLKDIFENYKTINIhDVIQGPDKtNFENVS 96
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTD----PAHSLSDAFGQKLGGETPVKGAPNLWAMEI-DPEEALEE-YWEEVK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491147476  97 --LIPCAKNIRDVEINIQRSSPVP--------NEIIRSVLRkikGDFDFILLDCPPRMETL 147
Cdd:cd02035   82 elLAQYLRLPGLDEVYAEELLSLPgmdeaaafDELREYVES---GEYDVIVFDTAPTGHTL 139
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 17-142 6.18e-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: 45.96  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSqrnatkHISNVPDIDDIDGTlkdifenyktiNIHDVIQG--PDKTNfeN 94
Cdd:cd02037    9 KGGVGKSTVAVNLALALAKKGYKVGLLDADI------YGPSIPRLLGVEGK-----------PLHQSEEGivPVEVG--G 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491147476  95 VSLIPCAKNIRDVEINIQRsSPVPNEIIRSVLRKIK-GDFDFILLDCPP 142
Cdd:cd02037   70 IKVMSIGFLLPEDDAVIWR-GPMKSGAIKQFLKDVDwGELDYLIIDLPP 117
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 7-46 1.17e-05

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: 43.57  E-value: 1.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 491147476   7 KTYICTSihFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLD 46
Cdd:cd01983    1 RVIAVTG--GKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 17-162 1.19e-05

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: 45.52  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDS-QRNATKHISNvpdiddidgtlKDIFENYKTINihdvIQGPDktnFENV 95
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFEN-----------RSATADRTGLS----LPTPE---HLNL 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491147476   96 SLIPCAKNIRDVEINIQRsspvpneiIRSVLRKIKGDFDFILLDCPPRMETLTFNALLASNSLLIPL 162
Cdd:pfam09140  71 PDNDVAEVPDGENIDDAR--------LEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 17-149 4.05e-04

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 41.18  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNatkhISNVPDIdDIDGTLKDIFENYKTINIH---DVIQGPDKTnFE 93
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHS----LSDSFNQ-KFGHEPTKVKENLSAMEIDpnmELEEYWQEV-QK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491147476   94 NVSLIPCAKNIRDVEINIQRSSPVPNEIIrSVLRKIK----GDFDFILLDCPPRMETLTF 149
Cdd:pfam02374  83 YMNALLGLRMLEGILAEELASLPGIDEAA-SFDEFKKymdeGEYDVVVFDTAPTGHTLRL 141
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 13-84 5.28e-04

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 40.74  E-value: 5.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491147476  13 SIHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHISN--VPDIDDidgTLKDIFENYKTINIHDVI 84
Cdd:cd02032    4 AVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGflIPTVID---VLQSVDFHYEEVWPEDVI 74
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-50 7.28e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 40.15  E-value: 7.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRN 50
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN 41
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 17-76 1.26e-03

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: 40.07  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSqrnaTKHISNVPD-------IDDIDGtlKDIFENYK 76
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP----AAHLSVTLTgslnnlqVSRIDP--KQETERYR 389
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 17-66 1.60e-03

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: 39.25  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491147476   17 KGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQrNATKHISNVPdIDDIDG 66
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDPQ-NLLRLHFGMD-WSVRDG 57
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 17-78 1.66e-03

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: 39.03  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491147476  17 KGGVGKTTSTVNCAAKLGKLGYTVLVI--D--LDSQRN--ATKHISNVPDI---DDIDGTLKDI-FENYKTI 78
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVLHVgcDpkADSTRLllGGKAIPTVLDTlreKGEVEELEDViKEGFNGI 79
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 14-64 3.79e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.21  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491147476  14 IHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATKHIS--NVPDIDDI 64
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVgeKIPTVLDV 58
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
13-84 4.07e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 37.81  E-value: 4.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491147476   13 SIHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNATK---HISNVPDIDDIdGTLKDIFENYKtinIHDVI 84
Cdd:pfam00142   4 AIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRlllGGKLQPTVLDT-AREKGYVEDVE---VEDVV 74
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 13-52 4.63e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 37.63  E-value: 4.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 491147476  13 SIHFKGGVGKTTSTVNCAAKLGKLGYTVLVIDLDSQRNAT 52
Cdd:PRK13185   6 AVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDST 45
 
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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