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Conserved domains on  [gi|489823262|ref|WP_003727049|]
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methylated-DNA--[protein]-cysteine S-methyltransferase [Listeria monocytogenes]

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, ...
 8-159 8.34e-67

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


:

Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 200.48  E-value: 8.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   8 SPVGDLFITIDEKWIRNISYDEPKNWELLEGT----IIEKELFQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQAL 83
Cdd:COG0350    9 TPLGPLLIAATDRGLCALSFGDDREEALLARFpaalREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPFQRRVWEAL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489823262  84 SEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGaDVDKKQYLLALEKGLSLS 159
Cdd:COG0350   89 RKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAG-GLERKRALLELEGALAAA 163
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 8-159 8.34e-67

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 200.48  E-value: 8.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   8 SPVGDLFITIDEKWIRNISYDEPKNWELLEGT----IIEKELFQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQAL 83
Cdd:COG0350    9 TPLGPLLIAATDRGLCALSFGDDREEALLARFpaalREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPFQRRVWEAL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489823262  84 SEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGaDVDKKQYLLALEKGLSLS 159
Cdd:COG0350   89 RKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAG-GLERKRALLELEGALAAA 163
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 8-154 6.95e-55

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 169.85  E-value: 6.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   8 SPVGDLFITIDEKWIRNISYDEPKNweLLEGTIIEKELFQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQALSEIP 87
Cdd:PRK00901   9 TPIGKIGIAENGTAITHLCFGEDKI--PKDVTILETDLLKEANKQLEEYFEGKRKKFDLPLAPQGTEFQKKVWKALQEIP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489823262  88 YGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLALEK 154
Cdd:PRK00901  87 YGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGG-LDIKEKLLKLEK 152
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 74-154 1.16e-43

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: 139.03  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   74 DFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLALE 153
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGG-LERKRALLELE 79


                  .
gi 489823262  154 K 154
Cdd:pfam01035  80 G 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 75-154 4.31e-40

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: 129.91  E-value: 4.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  75 FQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGaDVDKKQYLLALEK 154
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRG-GLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 73-153 2.42e-39

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: 127.82  E-value: 2.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   73 TDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLAL 152
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGG-LERKEFLLEH 79


                  .
gi 489823262  153 E 153
Cdd:TIGR00589  80 E 80
 
Name Accession Description Interval E-value
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
 8-159 8.34e-67

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


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 200.48  E-value: 8.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   8 SPVGDLFITIDEKWIRNISYDEPKNWELLEGT----IIEKELFQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQAL 83
Cdd:COG0350    9 TPLGPLLIAATDRGLCALSFGDDREEALLARFpaalREDPPLLAEAARQLDAYFAGERKDFDLPLDLRGTPFQRRVWEAL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489823262  84 SEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGaDVDKKQYLLALEKGLSLS 159
Cdd:COG0350   89 RKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAG-GLERKRALLELEGALAAA 163
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
 8-154 6.95e-55

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 169.85  E-value: 6.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   8 SPVGDLFITIDEKWIRNISYDEPKNweLLEGTIIEKELFQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQALSEIP 87
Cdd:PRK00901   9 TPIGKIGIAENGTAITHLCFGEDKI--PKDVTILETDLLKEANKQLEEYFEGKRKKFDLPLAPQGTEFQKKVWKALQEIP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489823262  88 YGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLALEK 154
Cdd:PRK00901  87 YGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGG-LDIKEKLLKLEK 152
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
 74-154 1.16e-43

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: 139.03  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   74 DFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLALE 153
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGG-LERKRALLELE 79


                  .
gi 489823262  154 K 154
Cdd:pfam01035  80 G 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
 75-154 4.31e-40

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: 129.91  E-value: 4.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  75 FQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGaDVDKKQYLLALEK 154
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRG-GLERKRELLELEG 79
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
 73-153 2.42e-39

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: 127.82  E-value: 2.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   73 TDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYLLAL 152
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGG-LERKEFLLEH 79


                  .
gi 489823262  153 E 153
Cdd:TIGR00589  80 E 80
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
1-158 1.13e-30

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


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 108.80  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262   1 MLKQQKTSPVGDLFITIDEKW-IRNISYDEPKN-WELLEGTIIEKELFQ--------ALTIQLDDYFEGKREHFD-LPVL 69
Cdd:PRK10286   4 LLEEKIATPLGPLWVICDEQFrLRAVEWEEYSErMVQLLDIHYRKEGYErisatnpgGLSDKLRDYFAGNLSIIDtLPTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  70 LKGTDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGAdVDKKQYL 149
Cdd:PRK10286  84 TGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGG-VQRKEWL 162


                 ....*....
gi 489823262 150 LALEKGLSL 158
Cdd:PRK10286 163 LRHEGYLLL 171
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
46-153 2.74e-26

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 101.41  E-value: 2.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  46 FQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPC 125
Cdd:PRK15435 242 FQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPC 321

                         90       100
                 ....*....|....*....|....*...
gi 489823262 126 HRCVKSNGELGGYNGAdVDKKQYLLALE 153
Cdd:PRK15435 322 HRVVRGDGALSGYRWG-VSRKAQLLRRE 348
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 46-158 3.50e-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: 101.28  E-value: 3.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  46 FQALTIQLDDYFEGKREHFDLPVLLKGTDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPC 125
Cdd:COG2169  243 FEQLVAEVVGFVEGPLLGLDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPC 322

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489823262 126 HRCVKSNGELGGYnGADVDKKQYLLALEKGLSL 158
Cdd:COG2169  323 HRVVRADGALSGY-RWGVERKRALLEREAAAAA 354
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
 73-153 5.33e-18

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


Pssm-ID: 442910  Cd Length: 104  Bit Score: 74.07  E-value: 5.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  73 TDFQQKVWQALSEIPYGVVVSYKDIAISAGSPKAVQAVGQANRANPIPIIIPCHRCVKSNGELGGYNGADVDKKQYLLAL 152
Cdd:COG3695    4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLSPGHAGGAEEQRELLEA 83


                 .
gi 489823262 153 E 153
Cdd:COG3695   84 E 84
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
 73-153 1.26e-09

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 53.97  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  73 TDFQQKVWQALSE-IPYGVVVSYKDIAISAG-SPKAVqavGQANRANPIPIIIPCHRCVKSNGElgGYNGADVDKKQYLL 150
Cdd:PRK03887  91 TPFERKVYEWLTKnVKRGEVITYGELAKALNtSPRAV---GGAMKRNPYPIIVPCHRVVGRKNP--GLYTPKPEYKKFLL 165


                 ...
gi 489823262 151 ALE 153
Cdd:PRK03887 166 EVE 168
GT29_ST6GALNAC2 cd23972
alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2; ST6GalNAc family members are ...
 48-152 9.59e-05

alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2; ST6GalNAc family members are alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferases that catalyze an alpha-2,6-linkage between sialic acid and the N-acetylgalactosamine residues of glycochains through an 2,6-linkage, by transfering sialic acid from CMP-Sia. ST6GalNAc2 utilize mainly GalNAc-,Galbeta1,3GalNAc-, and Sia2,3Galbeta1,3GalNAc on O-glycans of glycoproteins as acceptors. The ST6GalNac family belongs to glycosyltransferase family 29 (GT29).


Pssm-ID: 467700  Cd Length: 308  Bit Score: 41.35  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489823262  48 ALTIQLDDYFEGKREhFDLPVLLKGTDFQQKVWQALSE--IPYGvvvsYKDIAISAGSPKAVQAVGQANRANPIPIIIP- 124
Cdd:cd23972    6 HLRIQRDPHFRGLFN-FDIPVLLWGQHFTPALWDRLSQrkVPYG----WKGLSHQVVASTLSLLNDSANAKLFFPRDTPg 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489823262 125 -CHRC-VKSNGEL--GGYNGADVDKKQYLLAL 152
Cdd:cd23972   81 kCIRCaVVGNGGIlnGSRQGRAIDAHDYVFRL 112
 
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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