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Conserved domains on  [gi|1178468750|ref|WP_082991085|]
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MULTISPECIES: ComEA family DNA-binding protein [Dermabacter]

Protein Classification

ComEA family DNA-binding protein( domain architecture ID 11446237)

ComEA family DNA-binding protein contains a helix-hairpin-helix (HhH) motif, similar to Bacillus subtilis ComE operon protein 1, an integral membrane protein required for both DNA binding and transport

Gene Ontology:  GO:0003677
PubMed:  10908318|8692686
SCOP:  4001398

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
comE super family cl42947
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 149-280 3.07e-31

comEA protein; This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation. [Cellular processes, DNA transformation]


The actual alignment was detected with superfamily member TIGR01259:

Pssm-ID: 213597 [Multi-domain]  Cd Length: 120  Bit Score: 112.69  E-value: 3.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 149 SRVGEALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEdipaglpAPSPQQGatpgdsTGENPSDHGLLNINTATES 228
Cdd:TIGR01259   2 LRVWDAIEKAGGFTEQADGLSVNLAGKLMDEMFVYVPMKGE-------EAVSQQG------TQSSAGKLAAVNINAASLE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 229 ELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERITV 280
Cdd:TIGR01259  69 ELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
58-208 1.19e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750  58 AGALALGGAHMATSMTPREDTVAVNEEAPPGPPHSTSSPRDFASAAPTASSPPAIVGGAAQPVASPEAPHTILVHVVGAV 137
Cdd:PRK12323  412 AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178468750 138 KD---PRVVELPADSRVGE--ALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEDIPAGLPAPSPQQGATPGD 208
Cdd:PRK12323  492 ADddpPPWEELPPEFASPApaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
 
Name Accession Description Interval E-value
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 149-280 3.07e-31

comEA protein; This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation. [Cellular processes, DNA transformation]


Pssm-ID: 213597 [Multi-domain]  Cd Length: 120  Bit Score: 112.69  E-value: 3.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 149 SRVGEALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEdipaglpAPSPQQGatpgdsTGENPSDHGLLNINTATES 228
Cdd:TIGR01259   2 LRVWDAIEKAGGFTEQADGLSVNLAGKLMDEMFVYVPMKGE-------EAVSQQG------TQSSAGKLAAVNINAASLE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 229 ELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERITV 280
Cdd:TIGR01259  69 ELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 210-279 5.46e-30

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 107.64  E-value: 5.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 210 TGENPSDHGLLNINTATESELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERIT 279
Cdd:COG1555     3 ASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYLT 72
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 220-278 1.50e-24

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 93.32  E-value: 1.50e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178468750 220 LNINTATESELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERI 278
Cdd:pfam12836   4 VDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
PRK13766 PRK13766
Hef nuclease; Provisional
 230-279 8.44e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 8.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 230 LEELPGVGPAIASRIVEHRTTNGA-FT-SIEQLQDVKGIGPAIFEKLRERIT 279
Cdd:PRK13766  717 VESLPDVGPVLARNLLEHFGSVEAvMTaSEEELMEVEGIGEKTAKRIREVVT 768
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 225-276 6.23e-04

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 40.64  E-value: 6.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 225 ATESELEELPGVGPAIASRIVEHRTT----------NGAFTSIEQLQDVKGIGPAIFEKLRE 276
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILETgklrkleelrEDVPPGLLLLLRVPGVGPKTARKLYE 103
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
58-208 1.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750  58 AGALALGGAHMATSMTPREDTVAVNEEAPPGPPHSTSSPRDFASAAPTASSPPAIVGGAAQPVASPEAPHTILVHVVGAV 137
Cdd:PRK12323  412 AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178468750 138 KD---PRVVELPADSRVGE--ALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEDIPAGLPAPSPQQGATPGD 208
Cdd:PRK12323  492 ADddpPPWEELPPEFASPApaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
 
Name Accession Description Interval E-value
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 149-280 3.07e-31

comEA protein; This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation. [Cellular processes, DNA transformation]


Pssm-ID: 213597 [Multi-domain]  Cd Length: 120  Bit Score: 112.69  E-value: 3.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 149 SRVGEALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEdipaglpAPSPQQGatpgdsTGENPSDHGLLNINTATES 228
Cdd:TIGR01259   2 LRVWDAIEKAGGFTEQADGLSVNLAGKLMDEMFVYVPMKGE-------EAVSQQG------TQSSAGKLAAVNINAASLE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 229 ELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERITV 280
Cdd:TIGR01259  69 ELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 210-279 5.46e-30

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 107.64  E-value: 5.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 210 TGENPSDHGLLNINTATESELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERIT 279
Cdd:COG1555     3 ASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYLT 72
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 220-278 1.50e-24

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 93.32  E-value: 1.50e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178468750 220 LNINTATESELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERI 278
Cdd:pfam12836   4 VDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 219-280 4.37e-13

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 63.03  E-value: 4.37e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178468750 219 LLNINTATESELE-ELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFEKLRERITV 280
Cdd:TIGR00426   7 RVNINTATAEELQrAMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVEKNLAVITL 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
221-272 5.49e-11

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 62.74  E-value: 5.49e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 221 NINTATESELEELPGVGPAIASRIVEHRTTNGAFTSIEQLQDVKGIGPAIFE 272
Cdd:COG2183   488 DLNTASAPLLSYVSGLNPTLAKNIVAYRDENGAFKSRKELLKVPRLGPKAFE 539
SLBB pfam10531
SLBB domain;
131-182 9.53e-10

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 53.44  E-value: 9.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 131 VHVVGAVKDPRVVELPADSRVGEALEAAGGATDEADLsRLNLARVVSDGEQV 182
Cdd:pfam10531   2 VTVTGEVKRPGNYEVPIGTTLSDLIELAGGFTDDADL-DINLRRLKRPGGPM 52
Wza COG1596
Periplasmic protein Wza involved in polysaccharide export, contains SLBB domain of the ...
 125-188 6.53e-06

Periplasmic protein Wza involved in polysaccharide export, contains SLBB domain of the beta-grasp fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441204 [Multi-domain]  Cd Length: 182  Bit Score: 45.66  E-value: 6.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750 125 APHTILVHVVGAVKDPRVVELPADSRVGEALEAAGGATDEADLSRLNLAR------------------------VVSDGE 180
Cdd:COG1596    91 EYRSRRVYVLGEVNRPGRYPLSSGLTLLDAIALAGGLTERADLRNVQLIRggkevvytvdlydlllggdpsqniRLQPGD 170


                  ....*...
gi 1178468750 181 QVFVPRQG 188
Cdd:COG1596   171 VIFVPEAG 178
PRK13766 PRK13766
Hef nuclease; Provisional
 230-279 8.44e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 8.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 230 LEELPGVGPAIASRIVEHRTTNGA-FT-SIEQLQDVKGIGPAIFEKLRERIT 279
Cdd:PRK13766  717 VESLPDVGPVLARNLLEHFGSVEAvMTaSEEELMEVEGIGEKTAKRIREVVT 768
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 219-247 8.47e-05

Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 425789 [Multi-domain]  Cd Length: 30  Bit Score: 38.94  E-value: 8.47e-05
                          10        20
                  ....*....|....*....|....*....
gi 1178468750 219 LLNINTATESELEELPGVGPAIASRIVEH 247
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILSY 30
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
230-276 1.41e-04

ERCC4-type crossover junction endonuclease [Replication, recombination and repair];


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 42.09  E-value: 1.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1178468750 230 LEELPGVGPAIASRIVEH-RTTNGAFT-SIEQLQDVKGIGPAIFEKLRE 276
Cdd:COG1948   157 VESLPGIGPKLARRLLEHfGSVEAVFNaSEEELMKVEGIGEKTAERIRE 205
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
225-274 3.22e-04

DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 41.72  E-value: 3.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178468750 225 ATESELEELPGVGPAIASRIVEHRTTnGAFTSIEQLQ-----------DVKGIGP----AIFEKL 274
Cdd:COG1796    48 VAEGDLTEIPGIGKAIAAKIEELLET-GRLEELEELReevppgllellRIPGLGPkkvkKLYEEL 111
HHH_5 pfam14520
Helix-hairpin-helix domain;
229-278 5.22e-04

Helix-hairpin-helix domain;


Pssm-ID: 434010 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 5.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178468750 229 ELEELPGVGPAIASRIVEHrttnGAFT-------SIEQLQDVKGIGPAIFEKLRERI 278
Cdd:pfam14520   3 ELLSISGIGPKTALALLSA----GIGTvedlaeaDVDELAEIPGIGEKTAQRIILEL 55
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 225-276 6.23e-04

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 40.64  E-value: 6.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178468750 225 ATESELEELPGVGPAIASRIVEHRTT----------NGAFTSIEQLQDVKGIGPAIFEKLRE 276
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILETgklrkleelrEDVPPGLLLLLRVPGVGPKTARKLYE 103
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
58-208 1.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178468750  58 AGALALGGAHMATSMTPREDTVAVNEEAPPGPPHSTSSPRDFASAAPTASSPPAIVGGAAQPVASPEAPHTILVHVVGAV 137
Cdd:PRK12323  412 AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178468750 138 KD---PRVVELPADSRVGE--ALEAAGGATDEADLSRLNLARVVSDGEQVFVPRQGEDIPAGLPAPSPQQGATPGD 208
Cdd:PRK12323  492 ADddpPPWEELPPEFASPApaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
polC PRK00448
DNA polymerase III PolC; Validated
 233-276 3.41e-03

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 39.05  E-value: 3.41e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1178468750  233 LPGVGPAIASRIVEHRTtNGAFTSIEQLQDVKGIGPAIFEKLRE 276
Cdd:PRK00448  1378 LPGLGENVAKSIVEARE-EGEFLSKEDLRKRTKVSKTLIEKLDE 1420
uvrC PRK00558
excinuclease ABC subunit UvrC;
224-276 7.37e-03

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 37.79  E-value: 7.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178468750 224 TATESELEELPGVGPAIASRIVEHrttngaFTSI--------EQLQDVKGIGPAIFEKLRE 276
Cdd:PRK00558  539 ARLTSALDDIPGIGPKRRKALLKH------FGSLkaikeasvEELAKVPGISKKLAEAIYE 593
 
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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