NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1586112922|gb|QBJ57366|]
View 

ParA family protein (plasmid) [Lactiplantibacillus plantarum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-251 5.36e-45

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: 151.55  E-value: 5.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKD--HGTLANIFTKDSEKVEIIEL--HKN 76
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdlDPTLYDLLLDDAPLEDAIVPteIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  77 LSIIPASMNLDMVNNDLQTRANKELlmymWFSDNYDKLK-KFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFIS 155
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGREL----RLKRALAPLAdDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 156 KSNLELRMEQLKqEVINvesrksfitAELKFIG---NRIKHNTKSSHEFVEQMKK---DPRTIALIPEREVFNKTTLNHE 229
Cdd:COG1192   157 LAQLLETIEEVR-EDLN---------PKLEILGillTMVDPRTRLSREVLEELREefgDKVLDTVIPRSVALAEAPSAGK 226

                         250       260
                  ....*....|....*....|....*.
gi 1586112922 230 PLINMEKGKSSTPK----AREFFEKI 251
Cdd:COG1192   227 PVFEYDPKSKGAKAyralAEELLERL 252
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-251 5.36e-45

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: 151.55  E-value: 5.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKD--HGTLANIFTKDSEKVEIIEL--HKN 76
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdlDPTLYDLLLDDAPLEDAIVPteIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  77 LSIIPASMNLDMVNNDLQTRANKELlmymWFSDNYDKLK-KFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFIS 155
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGREL----RLKRALAPLAdDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 156 KSNLELRMEQLKqEVINvesrksfitAELKFIG---NRIKHNTKSSHEFVEQMKK---DPRTIALIPEREVFNKTTLNHE 229
Cdd:COG1192   157 LAQLLETIEEVR-EDLN---------PKLEILGillTMVDPRTRLSREVLEELREefgDKVLDTVIPRSVALAEAPSAGK 226

                         250       260
                  ....*....|....*....|....*.
gi 1586112922 230 PLINMEKGKSSTPK----AREFFEKI 251
Cdd:COG1192   227 PVFEYDPKSKGAKAyralAEELLERL 252
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-206 3.15e-31

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: 112.25  E-value: 3.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTqtydiykdhgtlaniftkdsekveiielhknlsiip 81
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  82 asmnldmvnndlqtrankellmyMWFsdnydklkkFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFISKSNLEL 161
Cdd:cd02042    45 -----------------------SWL---------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1586112922 162 RMEQLKQEVINVesrksfiTAELKFIGNRIKHNTKSSHEFVEQMK 206
Cdd:cd02042    93 TLEELKKQLNPP-------LLILGILLTRVDPRTKLAREVLEELK 130
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-152 1.07e-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: 109.98  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHG--TLANIFTKDSEKVEII--ELHKN 76
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVekTIYELLIGECNIEEAIikTVIEN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112922  77 LSIIPASMNLDMVNNDLQTRANKELLmymwFSDNYDKLKK-FDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYG 152
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENI----LKEALEPVKDnYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153
ParA_partition NF041546
ParA family partition ATPase;
3-151 5.18e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 60.26  E-value: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   3 IITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLANIfTKDSEkveiiELHKnlsiipa 82
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVV-GLARP-----TLHR------- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112922  83 smNLDMVNNDlqtrankellmymwfsdnydklkkFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEY 151
Cdd:NF041546   68 --ELPSLARD------------------------YDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPY 110
PHA02518 PHA02518
ParA-like protein; Provisional
 2-200 2.66e-10

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 58.71  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTqtydiykDHGTLANiftKDSEKVEIIELHKNLSiip 81
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-------DWAEARE---EGEPLIPVVRMGKSIR--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  82 asmnldmvnNDLQTRAnkellmymwfsdnydklKKFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFISKSNLeL 161
Cdd:PHA02518   68 ---------ADLPKVA-----------------SGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDL-V 120

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1586112922 162 RMEQLKQEVINVESRKSFITAelkfignRIKHNTKSSHE 200
Cdd:PHA02518  121 ELIKARQEVTDGLPKFAFIIS-------RAIKNTQLYRE 152
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-249 2.53e-07

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: 50.50  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-HQCSLTQTYDIYKDHGTLANIFTKDSEKVEIIELHKN-LSI 79
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFgVKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  80 IPASMNLDMVNndlqtRANKELLmymwfSDNYDKLKK-FDYVLIDTHPDFSTITQNMIVISD---LVFSPiepsEYGFIS 155
Cdd:TIGR01969  81 IPAGVSLEGLR-----KADPDKL-----EDVLKEIIDdTDFLLIDAPAGLERDAVTALAAADellLVVNP----EISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 156 KSnlelrmeqLKqeVINVESRKSfiTAELKFIGNRI-KHNTKSSHEFVEQMKKDPrTIALIPEREVFNKTTLNHEPLINM 234
Cdd:TIGR01969 147 DA--------LK--TKIVAEKLG--TAILGVVLNRVtRDKTELGREEIETILEVP-VLGVVPEDPEVRRAAAFGEPVVIY 213

                         250
                  ....*....|....*
gi 1586112922 235 EKgksSTPKAREFFE 249
Cdd:TIGR01969 214 NP---NSPAAQAFME 225
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 2-131 1.67e-03

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


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.48  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLAnifTKDSEKVEIIEL-------- 73
Cdd:NF041417   13 EFVFFSG-KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTS---IDDVENLSAIEIdpdaaaee 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586112922  74 HKNLSIIPASMNLD-----MVNNDLQTRANKELLMYMWFSDNYDKlKKFDYVLIDTHPDFSTI 131
Cdd:NF041417   89 YRQRTIEPMRQLLDdeqlkTVEEQLDSPCIEEIAAFDKFVEFMDE-PEYDVVVFDTAPTGHTI 150
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-251 5.36e-45

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: 151.55  E-value: 5.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKD--HGTLANIFTKDSEKVEIIEL--HKN 76
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDdlDPTLYDLLLDDAPLEDAIVPteIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  77 LSIIPASMNLDMVNNDLQTRANKELlmymWFSDNYDKLK-KFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFIS 155
Cdd:COG1192    81 LDLIPANIDLAGAEIELVSRPGREL----RLKRALAPLAdDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 156 KSNLELRMEQLKqEVINvesrksfitAELKFIG---NRIKHNTKSSHEFVEQMKK---DPRTIALIPEREVFNKTTLNHE 229
Cdd:COG1192   157 LAQLLETIEEVR-EDLN---------PKLEILGillTMVDPRTRLSREVLEELREefgDKVLDTVIPRSVALAEAPSAGK 226

                         250       260
                  ....*....|....*....|....*.
gi 1586112922 230 PLINMEKGKSSTPK----AREFFEKI 251
Cdd:COG1192   227 PVFEYDPKSKGAKAyralAEELLERL 252
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 2-206 3.15e-31

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: 112.25  E-value: 3.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTqtydiykdhgtlaniftkdsekveiielhknlsiip 81
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  82 asmnldmvnndlqtrankellmyMWFsdnydklkkFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFISKSNLEL 161
Cdd:cd02042    45 -----------------------SWL---------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLD 92

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1586112922 162 RMEQLKQEVINVesrksfiTAELKFIGNRIKHNTKSSHEFVEQMK 206
Cdd:cd02042    93 TLEELKKQLNPP-------LLILGILLTRVDPRTKLAREVLEELK 130
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-152 1.07e-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: 109.98  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHG--TLANIFTKDSEKVEII--ELHKN 76
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVekTIYELLIGECNIEEAIikTVIEN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112922  77 LSIIPASMNLDMVNNDLQTRANKELLmymwFSDNYDKLKK-FDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYG 152
Cdd:pfam13614  81 LDLIPSNIDLAGAEIELIGIENRENI----LKEALEPVKDnYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-231 2.04e-24

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: 97.42  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   4 ITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTY----DIYKDHGTLANIFTK----DSEKVEIIELHK 75
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEglegDIAPALQALAEGLKGrvnlDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  76 NLSIIPASMNLDMVNNDLQTRANKELLmymwfSDNYDKLKK-FDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFI 154
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERL-----REALEALKEdYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 155 SksnlelrMEQLKQEVINVesRKSFITAELKFIG---NRIK--HNTKSSHEFVEQMKKDPRTIALIPEREVFNKTTLNHE 229
Cdd:pfam01656 156 D-------AKRLGGVIAAL--VGGYALLGLKIIGvvlNKVDgdNHGKLLKEALEELLRGLPVLGVIPRDEAVAEAPARGL 226


                  ..
gi 1586112922 230 PL 231
Cdd:pfam01656 227 PV 228
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-126 1.56e-11

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: 62.90  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   3 IITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-HQCSLTQTYDIYKDHGtLANIFTKDSEKVEIIE--LHKNLSI 79
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlRGPSLHRMLGLENRPG-LSDVLAGEASLEDVIQptEVEGLDV 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1586112922  80 IPASMnldMVNND---LQTRANKELLmymwfsdnyDKLK-KFDYVLIDTHP 126
Cdd:COG0489   173 LPAGP---LPPNPselLASKRLKQLL---------EELRgRYDYVIIDTPP 211
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-188 3.54e-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: 61.43  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD------HQC-SLTQTYdiykdhgTLANIFTKDSEKVEII-EL 73
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanlDILlGLAPKK-------TLGDVLKGRVSLEDIIvEG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  74 HKNLSIIPASMNL-DMVNNDLQTRANkellmymwFSDNYDKL-KKFDYVLIDTHPDFSTITQNMIVISD---LVFSPiEP 148
Cdd:cd02038    74 PEGLDIIPGGSGMeELANLDPEQKAK--------LIEELSSLeSNYDYLLIDTGAGISRNVLDFLLAADeviVVTTP-EP 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1586112922 149 SE----YGFISKSNLELRMEQLKQEVINVESRKS--------------FITAELKFIG 188
Cdd:cd02038   145 TSitdaYALIKVLSRRGGKKNFRLIVNMARSPKEgratferlkkvakrFLDINLDFVG 202
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-251 4.39e-11

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: 61.06  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-------------------------HQCSLTQTydIYKDHGT 56
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiglrnldlilglenrivytlvdvleGECRLEQA--LIKDKRW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  57 laniftkdsekveiielhKNLSIIPASMNLDmvNNDLQTRANKELLmymwfsdnyDKLK-KFDYVLIDTHPDFSTITQNM 135
Cdd:cd02036    79 ------------------ENLYLLPASQTRD--KDALTPEKLEELV---------KELKdSFDFILIDSPAGIESGFINA 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 136 IVISD---LVFSPiEPSEygfISKSNlelrmeqlkqEVINVESRKSfiTAELKFIGNRIK-HNTKS----SHEFVEQMKK 207
Cdd:cd02036   130 IAPADeaiIVTNP-EISS---VRDAD----------RVIGLLESKG--IVNIGLIVNRYRpEMVKSgdmlSVEDIQEILG 193

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1586112922 208 DPrTIALIPEREVFNKTTLNHEPLInMEKGKSSTPKArefFEKI 251
Cdd:cd02036   194 IP-LLGVIPEDPEVIVATNRGEPLV-LYKPNSLAAKA---FENI 232
ParA_partition NF041546
ParA family partition ATPase;
3-151 5.18e-11

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 60.26  E-value: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   3 IITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLANIfTKDSEkveiiELHKnlsiipa 82
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVV-GLARP-----TLHR------- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112922  83 smNLDMVNNDlqtrankellmymwfsdnydklkkFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEY 151
Cdd:NF041546   68 --ELPSLARD------------------------YDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPY 110
PHA02518 PHA02518
ParA-like protein; Provisional
 2-200 2.66e-10

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 58.71  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTqtydiykDHGTLANiftKDSEKVEIIELHKNLSiip 81
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSST-------DWAEARE---EGEPLIPVVRMGKSIR--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  82 asmnldmvnNDLQTRAnkellmymwfsdnydklKKFDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSEYGFISKSNLeL 161
Cdd:PHA02518   68 ---------ADLPKVA-----------------SGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDL-V 120

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1586112922 162 RMEQLKQEVINVESRKSFITAelkfignRIKHNTKSSHE 200
Cdd:PHA02518  121 ELIKARQEVTDGLPKFAFIIS-------RAIKNTQLYRE 152
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 1-131 6.41e-09

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: 55.43  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTlanifTKDSEKVEIIELHKNLSI- 79
Cdd:pfam02374   1 MRWIFFGG-KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEP-----TKVKENLSAMEIDPNMELe 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112922  80 ---------IPASMNLDMVNNDLQTRAN-----KELLMYMWFSDNYDKLkKFDYVLIDTHPDFSTI 131
Cdd:pfam02374  75 eywqevqkyMNALLGLRMLEGILAEELAslpgiDEAASFDEFKKYMDEG-EYDVVVFDTAPTGHTL 139
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-126 2.73e-08

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: 52.57  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-HQCSLTQTYDIYKDHGtLANIFTKDSEKVEIIELH--KNL 77
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADlRRPSLHRLLGLPNEPG-LSEVLSGQASLEDVIQSTniPNL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1586112922  78 SIIPASMNLDMVNNDLQTRANKELLmymwfsdnyDKLK-KFDYVLIDTHP 126
Cdd:cd05387    98 DVLPAGTVPPNPSELLSSPRFAELL---------EELKeQYDYVIIDTPP 138
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-123 9.79e-08

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 51.60  E-value: 9.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-------------------------HQCSLTQTydIYKDhgt 56
Cdd:COG2894     3 KVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADiglrnldlvmglenrivydlvdvieGECRLKQA--LIKD--- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112922  57 laniftKDSEkveiielhkNLSIIPASmnldmvnndlQTRaNKE---------LLmymwfsdnyDKLKK-FDYVLID 123
Cdd:COG2894    78 ------KRFE---------NLYLLPAS----------QTR-DKDaltpeqmkkLV---------EELKEeFDYILID 119
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 1-166 1.36e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 51.98  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKD-----HGTLANIFTKDSEKVEIIELHK 75
Cdd:PRK13869  121 LQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPEtdvgaNETLYAAIRYDDTRRPLRDVIR 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  76 -----NLSIIPASMNL----DMVNNDLQTRANKELLMYMWFSDNYDKL-KKFDYVLIDTHPDFSTITQNMIVISDLVFSP 145
Cdd:PRK13869  201 ptyfdGLHLVPGNLELmefeHTTPKALSDKGTRDGLFFTRVAQAFDEVaDDYDVVVIDCPPQLGFLTLSGLCAATSMVIT 280

                         170       180
                  ....*....|....*....|.
gi 1586112922 146 IEPSEYGFISKSNLELRMEQL 166
Cdd:PRK13869  281 VHPQMLDIASMSQFLLMTRDL 301
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-249 2.53e-07

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: 50.50  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-HQCSLTQTYDIYKDHGTLANIFTKDSEKVEIIELHKN-LSI 79
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFgVKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  80 IPASMNLDMVNndlqtRANKELLmymwfSDNYDKLKK-FDYVLIDTHPDFSTITQNMIVISD---LVFSPiepsEYGFIS 155
Cdd:TIGR01969  81 IPAGVSLEGLR-----KADPDKL-----EDVLKEIIDdTDFLLIDAPAGLERDAVTALAAADellLVVNP----EISSIT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 156 KSnlelrmeqLKqeVINVESRKSfiTAELKFIGNRI-KHNTKSSHEFVEQMKKDPrTIALIPEREVFNKTTLNHEPLINM 234
Cdd:TIGR01969 147 DA--------LK--TKIVAEKLG--TAILGVVLNRVtRDKTELGREEIETILEVP-VLGVVPEDPEVRRAAAFGEPVVIY 213

                         250
                  ....*....|....*
gi 1586112922 235 EKgksSTPKAREFFE 249
Cdd:TIGR01969 214 NP---NSPAAQAFME 225
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 3-155 5.10e-07

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 50.01  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   3 IITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLID-SDHQ--CSLTQTY----DIYKDHGTLANIFTKDSEKVEIIE--L 73
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQgtASMYHGYvpdlHIHADDTLLPFYLGERDNAEYAIKptC 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  74 HKNLSIIPASMNLDMVNNDLQTRANKELLMY------------MWfsDNYdklkkfDYVLIDTHPDFSTITQNMIVISDL 141
Cdd:PHA02519  188 WPGLDIIPSCLALHRIETDLMQYHDAGKLPHpphlmlraaiesVW--DNY------DIIVIDSAPNLGTGTINVVCAADV 259

                         170
                  ....*....|....
gi 1586112922 142 VFSPIEPSEYGFIS 155
Cdd:PHA02519  260 IVVATPAELFDYVS 273
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-123 6.85e-07

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: 49.26  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD------------HQCSLTQTYDIYKDHGTLANIFTKDSEkve 69
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglrnldlllglENRIVYTLVDVVEGECRLQQALIKDKR--- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1586112922  70 iielHKNLSIIPASMNLDmvNNDLQTRANKELLMymwfsdnyDKLKKFDYVLID 123
Cdd:TIGR01968  79 ----LKNLYLLPASQTRD--KDAVTPEQMKKLVN--------ELKEEFDYVIID 118
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
1-145 7.38e-07

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 48.69  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQtydiYKDHGTLANIFTKDSEkveiielhknlsiI 80
Cdd:PRK13849    1 MKLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTR----WKENALRSNTWDPACE-------------V 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112922  81 PASMNLDMvnndlqtrankellmymwFSDNYD--KLKKFDYVLIDTHPDFSTITQNMIVISDLVFSP 145
Cdd:PRK13849   64 YAADELPL------------------LEAAYEdaELQGFDYALADTHGGSSELNNTIIASSNLLLIP 112
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-183 8.81e-07

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: 49.34  E-value: 8.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLS-SKGYNVLLIDSDHQ-CSLTQTYDIYKDHG---TLANIFTKDSEKVE--IIELH 74
Cdd:COG4963   103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQfGDVALYLDLEPRRGladALRNPDRLDETLLDraLTRHS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  75 KNLSIIPASMNLDMVnNDLQTRANKELLmymwfsdnyDKLKK-FDYVLIDTHPDFSTITQNMIVISDLVFSPIEPSeygF 153
Cdd:COG4963   183 SGLSVLAAPADLERA-EEVSPEAVERLL---------DLLRRhFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD---L 249

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1586112922 154 ISKSNLELRMEQLKQE---------VINVESRKSFITAE 183
Cdd:COG4963   250 PSLRNAKRLLDLLRELglpddkvrlVLNRVPKRGEISAK 288
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 1-126 1.42e-06

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: 48.82  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDI-----YKDHGTLANIFTKDSEKVEIIEL-H 74
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqpefdVGENETLYGAIRYDDERRPISEIiR 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586112922  75 K----NLSIIPASMNLDMVNND----LQTRANKELLMYMWFSDNYDKLKK-FDYVLIDTHP 126
Cdd:TIGR03453 184 KtyfpGLDLVPGNLELMEFEHEtpraLSRGQGGDTIFFARVGEALAEVEDdYDVVVIDCPP 244
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-39 2.53e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.47  E-value: 2.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1586112922   1 MKIitfsAI--KGGVGKTTLTFNYSEWLSSKGYNVLLIDSD 39
Cdd:COG3640     1 MKI----AVagKGGVGKTTLSALLARYLAEKGKPVLAVDAD 37
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-39 2.92e-06

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 2.92e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD 39
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 1-145 3.26e-06

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 46.79  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQtydiYKDHGTLANIFTKDSEKVEIIELhknlsii 80
Cdd:pfam07015   1 MQLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTK----WRENALRKGTWDPACEIFNADEL------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112922  81 PAsmnldmvnndlqtrankellmymwFSDNYD--KLKKFDYVLIDTHPDFSTITQNMIVISDLVFSP 145
Cdd:pfam07015  70 PL------------------------LEQAYEhaEGSGFDYALADTHGGSSELNNTIIASSDLLLIP 112
minD CHL00175
septum-site determining protein; Validated
 2-123 4.42e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 46.69  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD------------HQCSLTQTYDIYKDHGTLANIFTKDSEKve 69
Cdd:CHL00175   16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiglrnldlllglENRVLYTAMDVLEGECRLDQALIRDKRW-- 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112922  70 iielhKNLSIIPASMNLDMVNndlQTRANKELLMymwfsdnyDKLKK--FDYVLID 123
Cdd:CHL00175   94 -----KNLSLLAISKNRQRYN---VTRKNMNMLV--------DSLKNrgYDYILID 133
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 1-168 7.60e-06

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: 45.51  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSlTQTYdIYKDHGT---LANIFTKDSEKVEIIELHK-- 75
Cdd:TIGR01007  17 IKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNS-VMSG-TFKSQNKitgLTNFLSGTTDLSDAICDTNie 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  76 NLSIIPASmnldmvnndlQTRAN-KELLMYMWFSDNYDKLKK-FDYVLIDTHPdFSTITQNMIvISDLVFSPIEPSEYGF 153
Cdd:TIGR01007  95 NLDVITAG----------PVPPNpTELLQSSNFKTLIETLRKrFDYIIIDTPP-IGTVTDAAI-IARACDASILVTDAGK 162

                         170
                  ....*....|....*
gi 1586112922 154 ISKSNLELRMEQLKQ 168
Cdd:TIGR01007 163 IKKREVKKAKEQLEQ 177
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-126 7.83e-06

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 46.62  E-value: 7.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  10 KGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLANIftkdSEKVEiIELHKN--LSIIPASMN-- 85
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRI----DPKQE-TERYRQevLATKGKELDed 403

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1586112922  86 -LDMVNNDLQTRANKELLMYMWFSDNYDKLKKfDYVLIDTHP 126
Cdd:TIGR04291 404 gKAYLEEDLRSPCTEEIAVFQAFSRIIREAGD-RFVVMDTAP 444
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-251 1.48e-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: 44.99  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   1 MKIitfsAI--KGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLA--------NIFTKDSEKVEI 70
Cdd:cd02034     1 MKI----AVagKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIktigdireRTGAKKGEPPEG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  71 IELHKNLSIIPASMNLDMVNNDLQT-------------RAN---KELLMYMwfsdnydKLKKFDYVLIDTHPDFSTITQN 134
Cdd:cd02034    77 MSLNPYVDDIIKEIIVEPDGIDLLVmgrpegggsgcycPVNallRELLRHL-------ALKNYEYVVIDMEAGIEHLSRG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922 135 MIVISDLVFSPIEPSEYGFISKsnleLRMEQLKQEV-INvesrksfitaELKFIGNRIKHntKSSHEFVEQMKKDPRTIA 213
Cdd:cd02034   150 TIRAVDLLIIVIEPSKRSIQTA----KRIKELAEELgIK----------KIYLIVNKVRN--EEEQELIEELLIKLKLIG 213

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1586112922 214 LIPEREVFNKTTLNHEPLINmekgksSTPKAREFFEKI 251
Cdd:cd02034   214 VIPYDEEIMEADLKGKPLFD------LDSAAVKAIEKI 245
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-127 2.14e-05

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: 44.42  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLI--DSDHqcsltqtydiykdhgTLANIFTKDSEKVEIIELHKNLSI 79
Cdd:cd02035     1 RIIFFGG-KGGVGKTTIAAATAVRLAEQGKRVLLVstDPAH---------------SLSDAFGQKLGGETPVKGAPNLWA 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112922  80 ipasMNLD----------MVNNDLQTRANK------------------ELLMYMWFSDnYDKLKKFDYVLIDTHPD 127
Cdd:cd02035    65 ----MEIDpeealeeyweEVKELLAQYLRLpgldevyaeellslpgmdEAAAFDELRE-YVESGEYDVIVFDTAPT 135
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-39 2.34e-05

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 44.03  E-value: 2.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1586112922   2 KIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD 39
Cdd:cd02037     2 IIAVLSG-KGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-41 4.52e-05

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: 43.49  E-value: 4.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1586112922   1 MKIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQ 41
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 17-143 8.94e-05

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: 42.57  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  17 TLTFNYSEWLSSKGYNVLLIDSD-------HQCSLTQTYDIY---KDHGTLANIftkdsekveIIELHKNLSIIPASMNL 86
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADlglanldVLLGLEPKATLAdvlAGEADLEDA---------IVQGPGGLDVLPGGSGP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112922  87 -DMVNNDLQTRANKELlmymwfsdnyDKLKK-FDYVLIDTHPDFSTITQNMIVISDLVF 143
Cdd:COG0455    72 aELAELDPEERLIRVL----------EELERfYDVVLVDTGAGISDSVLLFLAAADEVV 120
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-143 1.61e-04

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: 41.88  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSK-GYNVLLIDSDHQ-------CSLTQTYDIYKDHGTLANIftkDSEKVEIIEL 73
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPfgdlglyLNLRPDYDLADVIQNLDRL---DRTLLDSAVT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586112922  74 H--KNLSIIPASMNLDMVNNdLQTRANKELLMYMWFSdnydklkkFDYVLIDTHPDFSTITQNMIVISDLVF 143
Cdd:cd03111    78 RhsSGLSLLPAPQELEDLEA-LGAEQVDKLLQVLRAF--------YDHIIVDLGHFLDEVTLAVLEAADEIL 140
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 10-39 3.29e-04

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: 40.90  E-value: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1586112922  10 KGGVGKTTLTFNYSEWLSSKGYNVLLIDSD 39
Cdd:pfam10609  12 KGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 2-176 3.32e-04

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


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 41.63  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD-HQCSLTQTYDIYKDHGTLANIFTKDS-EKVEIIELHKNLSI 79
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAPKPGLLDLLAGEASiEAGIHRDQRPGLAF 633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922  80 IPASmnldmvNNDLQTRANKELLMYMWFSDNYDKLK-KFDYVLIDTHPDFSTI-TQNMIVISDLVFSPIEpseygfISKS 157
Cdd:TIGR01005 634 IAAG------GASHFPHNPNELLANPAMAELIDNARnAFDLVLVDLAALAAVAdAAAFAALADGILFVTE------FERS 701

                         170       180
                  ....*....|....*....|
gi 1586112922 158 NLELRMEQLKQE-VINVESR 176
Cdd:TIGR01005 702 PLGEIRDLIHQEpHANSDVL 721
PRK10818 PRK10818
septum site-determining protein MinD;
2-124 4.26e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 40.69  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAIKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD---------HQCSLTQTYD---IYKDHGTLANIFTKDSEKve 69
Cdd:PRK10818    3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiglrnldliMGCERRVVYDfvnVIQGDATLNQALIKDKRT-- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1586112922  70 iielhKNLSIIPASMNLDmvnNDLQTRANKELLMymwfsDNYDKLkKFDYVLIDT 124
Cdd:PRK10818   81 -----ENLYILPASQTRD---KDALTREGVAKVL-----DDLKAM-DFEFIVCDS 121
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-50 1.19e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 39.42  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1586112922   1 MKIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLIDSD--HqcSLTQTYDI 50
Cdd:COG0003     3 TRIIFFTG-KGGVGKTTVAAATALALAERGKRTLLVSTDpaH--SLGDVLGT 51
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 2-131 1.67e-03

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


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.48  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112922   2 KIITFSAiKGGVGKTTLTFNYSEWLSSKGYNVLLIDSDHQCSLTQTYDIYKDHGTLAnifTKDSEKVEIIEL-------- 73
Cdd:NF041417   13 EFVFFSG-KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTS---IDDVENLSAIEIdpdaaaee 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586112922  74 HKNLSIIPASMNLD-----MVNNDLQTRANKELLMYMWFSDNYDKlKKFDYVLIDTHPDFSTI 131
Cdd:NF041417   89 YRQRTIEPMRQLLDdeqlkTVEEQLDSPCIEEIAAFDKFVEFMDE-PEYDVVVFDTAPTGHTI 150
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH