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Conserved domains on  [gi|493290677|ref|WP_006248379|]
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methylated-DNA--[protein]-cysteine S-methyltransferase [Mannheimia haemolytica]

Protein Classification

methylated-DNA--[protein]-cysteine S-methyltransferase( domain architecture ID 11417447)

methylated-DNA--[protein]-cysteine S-methyltransferase is involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA; it repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme

CATH:  3.30.160.70|1.10.10.10
EC:  2.1.1.63
Gene Ontology:  GO:0003908|GO:0003677|GO:0046872|GO:0006281|GO:0032259
PubMed:  17500045|17485252
SCOP:  4000565|4000678

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 5-165 2.84e-74

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 220.13  E-value: 2.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   5 IYYDYYPSPIGQLLLLATEEGLIYIELGQEQQTTSLDNFLSAQAASGQILEifcKTKEILDRYFAGEPLDFqqlDF-LAP 83
Cdd:COG0350    2 IRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA---EAARQLDAYFAGERKDF---DLpLDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  84 QGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQ 163
Cdd:COG0350   76 RGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ..
gi 493290677 164 LE 165
Cdd:COG0350  156 LE 157
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 5-165 2.84e-74

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 220.13  E-value: 2.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   5 IYYDYYPSPIGQLLLLATEEGLIYIELGQEQQTTSLDNFLSAQAASGQILEifcKTKEILDRYFAGEPLDFqqlDF-LAP 83
Cdd:COG0350    2 IRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA---EAARQLDAYFAGERKDF---DLpLDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  84 QGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQ 163
Cdd:COG0350   76 RGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ..
gi 493290677 164 LE 165
Cdd:COG0350  156 LE 157
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 87-165 6.35e-48

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 150.59  E-value: 6.35e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493290677   87 PFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 6-165 9.82e-48

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 152.90  E-value: 9.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   6 YYDYYPSPIGQLLLLATEEGLIYIELGQEQQttsldnflsAQAASGQILEIFCKTKEILDRYFAGEPLDFqqlDF-LAPQ 84
Cdd:PRK00901   3 NIYFYETPIGKIGIAENGTAITHLCFGEDKI---------PKDVTILETDLLKEANKQLEEYFEGKRKKF---DLpLAPQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  85 GTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQL 164
Cdd:PRK00901  71 GTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKL 150


                 .
gi 493290677 165 E 165
Cdd:PRK00901 151 E 151
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 86-165 1.28e-45

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 144.76  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   86 TPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 88-165 1.07e-42

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 137.23  E-value: 1.07e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290677  88 FQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 5-165 2.84e-74

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 220.13  E-value: 2.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   5 IYYDYYPSPIGQLLLLATEEGLIYIELGQEQQTTSLDNFLSAQAASGQILEifcKTKEILDRYFAGEPLDFqqlDF-LAP 83
Cdd:COG0350    2 IRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLARFPAALREDPPLLA---EAARQLDAYFAGERKDF---DLpLDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  84 QGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQ 163
Cdd:COG0350   76 RGTPFQRRVWEALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ..
gi 493290677 164 LE 165
Cdd:COG0350  156 LE 157
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 87-165 6.35e-48

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 150.59  E-value: 6.35e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493290677   87 PFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELE 79
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 6-165 9.82e-48

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 152.90  E-value: 9.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   6 YYDYYPSPIGQLLLLATEEGLIYIELGQEQQttsldnflsAQAASGQILEIFCKTKEILDRYFAGEPLDFqqlDF-LAPQ 84
Cdd:PRK00901   3 NIYFYETPIGKIGIAENGTAITHLCFGEDKI---------PKDVTILETDLLKEANKQLEEYFEGKRKKF---DLpLAPQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  85 GTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQL 164
Cdd:PRK00901  71 GTEFQKKVWKALQEIPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKL 150


                 .
gi 493290677 165 E 165
Cdd:PRK00901 151 E 151
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 86-165 1.28e-45

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 144.76  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   86 TPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 88-165 1.07e-42

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 137.23  E-value: 1.07e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290677  88 FQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELE 78
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
64-165 2.10e-36

methylated-DNA--[protein]-cysteine S-methyltransferase;


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 124.60  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  64 LDRYFAGeplDFQQLDFL--APQGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRV 141
Cdd:PRK10286  66 LRDYFAG---NLSIIDTLptATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRV 142

                         90       100
                 ....*....|....*....|....
gi 493290677 142 LGKNQALTGFGGGLPNKRFLLQLE 165
Cdd:PRK10286 143 IGRNGTMTGYAGGVQRKEWLLRHE 166
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 4-165 4.84e-26

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 102.05  E-value: 4.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677   4 QIYYDYYPSPIGQLLLLATEEGLIYIELGQEQQTTS---LDNFLSAQAASGQilEIFCKTKEILDRYFAGEPLDFQQLdf 80
Cdd:COG2169  189 AIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLrdlQDRFPAAELIGGD--AAFEQLVAEVVGFVEGPLLGLDLP-- 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  81 LAPQGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGFGGGLPNKRF 160
Cdd:COG2169  265 LDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRA 344


                 ....*
gi 493290677 161 LLQLE 165
Cdd:COG2169  345 LLERE 349
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
72-165 3.65e-24

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 96.79  E-value: 3.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  72 PLDFQqldflapqGTPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALTGF 151
Cdd:PRK15435 263 PLDIR--------GTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGALSGY 334

                         90
                 ....*....|....
gi 493290677 152 GGGLPNKRFLLQLE 165
Cdd:PRK15435 335 RWGVSRKAQLLRRE 348
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 86-174 1.94e-20

Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like DNA-binding domain [Transcription];


Pssm-ID: 442910  Cd Length: 104  Bit Score: 81.38  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  86 TPFQQSVWKILREIPYGQTTTYGEIATQLGKPSAMRAVGGAVGRNPISILVPCHRVLGKNQALT-GFGGGLPNKRFLLQL 164
Cdd:COG3695    4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQRELLEA 83

                         90
                 ....*....|
gi 493290677 165 EDITYKDKGI 174
Cdd:COG3695   84 EGVPVVDDGR 93
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 34-165 6.75e-16

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 71.30  E-value: 6.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290677  34 EQQTTSLDNFLSAQAASGQILEIFCKTKEILDRYFAGEPLDFQQLDFLAPQG-TPFQQSVWKIL-REIPYGQTTTYGEIA 111
Cdd:PRK03887  38 RERISNLAEFLKKRGVKVSLKERPSDYPELVFKVLIGKISNEEGLEELSFEGlTPFERKVYEWLtKNVKRGEVITYGELA 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493290677 112 TQLGkpSAMRAVGGAVGRNPISILVPCHRVLGKNQaLTGFGGGLPNKRFLLQLE 165
Cdd:PRK03887 118 KALN--TSPRAVGGAMKRNPYPIIVPCHRVVGRKN-PGLYTPKPEYKKFLLEVE 168
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 5-75 2.30e-04

6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the N-terminal ribonuclease-like domain associated with 6-O-methylguanine DNA methyltransferase activity. The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase (also known as O-6-methylguanine-DNA-alkyltransferase)


Pssm-ID: 397139 [Multi-domain]  Cd Length: 77  Bit Score: 38.11  E-value: 2.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290677    5 IYYDYYPSPIGQLLLLATEEGLIYIELGQEQqtTSLDNFLSAQAASGQILEIFCKTKEILDRYFAGE-------PLDF 75
Cdd:pfam02870   2 LYYTLIDSPLGRLLLAGDERGLTAIDFLDKD--YALRKELPKVLPQPELLPALALLVQALEEYFAGElkpeftlPLDQ 77
 
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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