NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1190332511|ref|NP_001338324|]
View 

dystrobrevin beta isoform 29 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-237 6.99e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511  95 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 160
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 161 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 233
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 1190332511 234 MPVR 237
Cdd:COG4942   257 WPVS 260
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-237 6.99e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511  95 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 160
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 161 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 233
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 1190332511 234 MPVR 237
Cdd:COG4942   257 WPVS 260
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 135-205 7.62e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.90  E-value: 7.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190332511 135 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 205
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-216 4.85e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511   91 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 170
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1190332511  171 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 216
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 103-197 2.39e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 103 YAARLAAEAGNVTRppTDLSFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPTLLAELRLL 180
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 1190332511 181 RQRKDELEQRMSALQES 197
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 173-211 8.47e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 35.93  E-value: 8.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1190332511 173 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 211
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-237 6.99e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511  95 EEHRLIARYAARLAAEAGNVTRPPTDLSFNFD--------------ANKQQRQLIAELENKNREILQEIQRLRLEHEQAS 160
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 161 QPTPEKAQQNPTLLAE-------LRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKAQATGSPHTSPTHGGGRpMP 233
Cdd:COG4942   178 ALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK-LP 256


                  ....
gi 1190332511 234 MPVR 237
Cdd:COG4942   257 WPVS 260
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-216 5.78e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 129 KQQRQLIAELENKNREILQEIQRLRLEHEQA-SQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 207
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                  ....*....
gi 1190332511 208 LMKLLKAQA 216
Cdd:COG4717   232 LENELEAAA 240
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 135-205 7.62e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.90  E-value: 7.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190332511 135 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 205
Cdd:PRK05431   30 LLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAELEELLLRI 103
PRK12704 PRK12704
phosphodiesterase; Provisional
 126-213 4.44e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 126 DANKQQRQLI----AELENKNREIL----QEIQRLRLEHEQasqptpEKAQQNPTLLAELRLLRQRKDELEQRMSALQES 197
Cdd:PRK12704   35 EAEEEAKRILeeakKEAEAIKKEALleakEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90
                  ....*....|....*.
gi 1190332511 198 RRELMVQLEELMKLLK 213
Cdd:PRK12704  109 EEELEKKEKELEQKQQ 124
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-216 4.85e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511   91 SRLDEEHRliaRYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQN 170
Cdd:TIGR02169  801 SKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1190332511  171 PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEEL---MKLLKAQA 216
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkrLSELKAKL 926
PRK12704 PRK12704
phosphodiesterase; Provisional
 125-216 7.21e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 125 FDANKQQRQLIAELENKNREILQEIQ----RLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRE 200
Cdd:PRK12704   60 LEAKEEIHKLRNEFEKELRERRNELQklekRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139

                          90
                  ....*....|....*.
gi 1190332511 201 LMVQLEELMKLLKAQA 216
Cdd:PRK12704  140 QLQELERISGLTAEEA 155
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 128-199 2.15e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 38.45  E-value: 2.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190332511 128 NKQQRQLIAELENKNREILQEIQRLRLEHE---QASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRR 199
Cdd:TIGR04211  89 LAELRQENQELKQQLSTLEAELEELQKELErikQISANAIELDEENRELREELAELKQENEALEAENERLQENEQ 163
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 103-197 2.39e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 103 YAARLAAEAGNVTRppTDLSFNFDANKQQRQLIAELENKNREILQEIQRL--RLEHEQASQPTPEKAQQNPTLLAELRLL 180
Cdd:pfam03961 131 KAKELGSPAGTKTE--IEVGVDFPELKEKLEELEKELEELEEELEKLKKRlkKLPKKARGQLPPEKREQLEKLLETKNKL 208

                          90
                  ....*....|....*..
gi 1190332511 181 RQRKDELEQRMSALQES 197
Cdd:pfam03961 209 SEELEELEEELKELKEE 225
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 131-215 3.01e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 131 QRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMK 210
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                  ....*
gi 1190332511 211 LLKAQ 215
Cdd:COG4942    98 ELEAQ 102
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
135-215 3.75e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 135 IAELENKNREILQEIQRLRLE----HEQASQPTPEKAQQN---PTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 207
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNaqvKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89


                  ....*...
gi 1190332511 208 LMKLLKAQ 215
Cdd:COG1340    90 LREELDEL 97
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 128-213 4.09e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 128 NKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEE 207
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486


                  ....*.
gi 1190332511 208 LMKLLK 213
Cdd:TIGR04523 487 KQKELK 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
124-210 7.14e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 124 NFDANKQQRQLIAELENKNREILQEIQRL-RLEHEQAsqptpEKAQQNPTLLAELRLLRQRKD--ELEQRMSALQESRRE 200
Cdd:COG4717    69 NLKELKELEEELKEAEEKEEEYAELQEELeELEEELE-----ELEAELEELREELEKLEKLLQllPLYQELEALEAELAE 143

                          90
                  ....*....|
gi 1190332511 201 LMVQLEELMK 210
Cdd:COG4717   144 LPERLEELEE 153
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 135-209 8.15e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 35.64  E-value: 8.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190332511 135 IAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPtllaELRLLRQRKDELEQRMSALQESRRELMVQLEELM 209
Cdd:pfam02403  31 LLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE----DADALIAEVKELKDELKALEAELKELEAELDKLL 101
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 173-211 8.47e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 35.93  E-value: 8.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1190332511 173 LLAELRLLRQRKDELEQRMSALQESRRELMV---QLEELMKL 211
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKL 46
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 126-215 8.95e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.44  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190332511 126 DANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQL 205
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90
                  ....*....|
gi 1190332511 206 EELMKLLKAQ 215
Cdd:COG4942   100 EAQKEELAEL 109
 
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