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Conserved domains on  [gi|446378138|ref|WP_000455993|]
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MULTISPECIES: methylated-DNA--[protein]-cysteine S-methyltransferase [Staphylococcus]

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, ...
 1-163 6.10e-65

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 196.25  E-value: 6.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENQQGDSTRE-----ENTSLAIFREATQWLDAYFKGDNPEITIPLKPTGSHF 75
Cdd:COG0350    1 TIRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLArfpaaLREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  76 QQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLE 155
Cdd:COG0350   81 QRRVWEALRKIPYGETVTYGELARAIGR----PK-AARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ....*...
gi 446378138 156 LENIDMSK 163
Cdd:COG0350  156 LEGALAAA 163
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 1-163 6.10e-65

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 196.25  E-value: 6.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENQQGDSTRE-----ENTSLAIFREATQWLDAYFKGDNPEITIPLKPTGSHF 75
Cdd:COG0350    1 TIRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLArfpaaLREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  76 QQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLE 155
Cdd:COG0350   81 QRRVWEALRKIPYGETVTYGELARAIGR----PK-AARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ....*...
gi 446378138 156 LENIDMSK 163
Cdd:COG0350  156 LEGALAAA 163
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 1-157 6.87e-45

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 145.19  E-value: 6.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENqqgDSTRE----ENTSLaiFREATQWLDAYFKGDNPEITIPLKPTGSHFQ 76
Cdd:PRK00901   1 MNNIYFYETPIGKIGIAENGTAITHLCFGE---DKIPKdvtiLETDL--LKEANKQLEEYFEGKRKKFDLPLAPQGTEFQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  77 QCVWNELRQVPYGTLTTYGAIAKKVGkllnKPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLEL 156
Cdd:PRK00901  76 KKVWKALQEIPYGETRSYKEIAVNIG----NPK-ACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKL 150


                 .
gi 446378138 157 E 157
Cdd:PRK00901 151 E 151
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 75-159 2.19e-41

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: 133.64  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   75 FQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkpKMSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGR-----PKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALL 76


                  ....*
gi 446378138  155 ELENI 159
Cdd:pfam01035  77 ELEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 75-158 1.28e-35

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: 119.12  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  75 FQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGT----PK-AARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELL 75


                 ....
gi 446378138 155 ELEN 158
Cdd:cd06445   76 ELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 75-157 1.17e-34

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: 116.64  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   75 FQQCVWNELRQVPYGTLTTYGAIAKkvgkLLNKPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAK----AIGNPK-AARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLL 77


                  ...
gi 446378138  155 ELE 157
Cdd:TIGR00589  78 EHE 80
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 1-163 6.10e-65

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 196.25  E-value: 6.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENQQGDSTRE-----ENTSLAIFREATQWLDAYFKGDNPEITIPLKPTGSHF 75
Cdd:COG0350    1 TIRYAIFDTPLGPLLIAATDRGLCALSFGDDREEALLArfpaaLREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  76 QQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLE 155
Cdd:COG0350   81 QRRVWEALRKIPYGETVTYGELARAIGR----PK-AARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLE 155


                 ....*...
gi 446378138 156 LENIDMSK 163
Cdd:COG0350  156 LEGALAAA 163
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 1-157 6.87e-45

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 145.19  E-value: 6.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENqqgDSTRE----ENTSLaiFREATQWLDAYFKGDNPEITIPLKPTGSHFQ 76
Cdd:PRK00901   1 MNNIYFYETPIGKIGIAENGTAITHLCFGE---DKIPKdvtiLETDL--LKEANKQLEEYFEGKRKKFDLPLAPQGTEFQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  77 QCVWNELRQVPYGTLTTYGAIAKKVGkllnKPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLEL 156
Cdd:PRK00901  76 KKVWKALQEIPYGETRSYKEIAVNIG----NPK-ACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKL 150


                 .
gi 446378138 157 E 157
Cdd:PRK00901 151 E 151
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 75-159 2.19e-41

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: 133.64  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   75 FQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkpKMSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:pfam01035   2 FQRRVWEALRQIPYGKTTTYGEIAKLLGR-----PKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALL 76


                  ....*
gi 446378138  155 ELENI 159
Cdd:pfam01035  77 ELEGV 81
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 75-158 1.28e-35

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: 119.12  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  75 FQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGT----PK-AARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELL 75


                 ....
gi 446378138 155 ELEN 158
Cdd:cd06445   76 ELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 75-157 1.17e-34

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: 116.64  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138   75 FQQCVWNELRQVPYGTLTTYGAIAKkvgkLLNKPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLL 154
Cdd:TIGR00589   3 FQQKVWKALRTIPYGETKSYGQLAK----AIGNPK-AARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLL 77


                  ...
gi 446378138  155 ELE 157
Cdd:TIGR00589  78 EHE 80
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
53-157 2.19e-26

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 98.40  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  53 LDAYFKGDNPEI-TIPLKPTGSHFQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkpKMSAQAVGGAVGSNPLSIIVPCH 131
Cdd:PRK10286  66 LRDYFAGNLSIIdTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGR-----PGAARAVGAANGSNPISIVVPCH 140

                         90       100
                 ....*....|....*....|....*.
gi 446378138 132 RVVGKTGSLTGFGGTINNKIKLLELE 157
Cdd:PRK10286 141 RVIGRNGTMTGYAGGVQRKEWLLRHE 166
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
47-157 8.30e-21

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 87.16  E-value: 8.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  47 REATQWLDAYfkgdNPEITIPLKPTGSHFQQCVWNELRQVPYGTLTTYGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSI 126
Cdd:PRK15435 247 REVIASLNQR----DTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGK----PK-AVRAVASACAANKLAI 317

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446378138 127 IVPCHRVVGKTGSLTGFGGTINNKIKLLELE 157
Cdd:PRK15435 318 VIPCHRVVRGDGALSGYRWGVSRKAQLLRRE 348
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 14-157 2.44e-16

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: 75.09  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  14 LELVSDGGSLTAVLFENQQGDSTREENTSLAIFREATQWLDAYFKGDNPEITIPLKPTGSHFQQCVWNELRQVPYGTLTT 93
Cdd:COG2169  211 VCAILLGDDPEALLRDLQDRFPAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETAS 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446378138  94 YGAIAKKVGKllnkPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLTGFGGTINNKIKLLELE 157
Cdd:COG2169  291 YAEIAARIGA----PK-AVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLERE 349
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 75-159 9.90e-16

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 68.67  E-value: 9.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378138  75 FQQCVWNELRQVPYGTLTTYGAIAkkvgKLLNKPKmSAQAVGGAVGSNPLSIIVPCHRVVGKTGSLT-GFGGTINNKIKL 153
Cdd:COG3695    6 FYERVYEVVAQIPPGRVATYGDIA----ALAGLPR-GARQVGRALRALPEGSDLPWHRVVNADGRLSpGHAGGAEEQREL 80


                 ....*.
gi 446378138 154 LELENI 159
Cdd:COG3695   81 LEAEGV 86
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 84-138 1.93e-10

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 56.67  E-value: 1.93e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446378138  84 RQVPYGTLTTYGAIAKKVgkllnkpKMSAQAVGGAVGSNPLSIIVPCHRVVGKTG 138
Cdd:PRK03887 103 KNVKRGEVITYGELAKAL-------NTSPRAVGGAMKRNPYPIIVPCHRVVGRKN 150
Methyltransf_1N pfam02870
6-O-methylguanine DNA methyltransferase, ribonuclease-like domain; This entry represents the ...
 1-70 5.64e-08

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: 47.74  E-value: 5.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446378138    1 MEYKSYYDSPVGRLELVSDGGSLTAVLFENQQgDSTREE-------NTSLAIFREATQWLDAYFKGDN-PEITIPLKP 70
Cdd:pfam02870   1 ALYYTLIDSPLGRLLLAGDERGLTAIDFLDKD-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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