GenomeNet

Database: UniProt
Entry: T2IT67_CROWT
LinkDB: T2IT67_CROWT
Original site: T2IT67_CROWT 
ID   T2IT67_CROWT            Unreviewed;       324 AA.
AC   T2IT67;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=CWATWH0005_641 {ECO:0000313|EMBL:CCQ55330.1};
OS   Crocosphaera watsonii WH 0005.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=423472 {ECO:0000313|EMBL:CCQ55330.1, ECO:0000313|Proteomes:UP000017981};
RN   [1] {ECO:0000313|EMBL:CCQ55330.1, ECO:0000313|Proteomes:UP000017981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ55330.1,
RC   ECO:0000313|Proteomes:UP000017981};
RA   Bench S.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCQ55330.1, ECO:0000313|Proteomes:UP000017981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ55330.1,
RC   ECO:0000313|Proteomes:UP000017981};
RA   Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT   "Whole genome comparison of six Crocosphaera watsonii strains with
RT   differing phenotypes.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCQ55330.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAQL01000361; CCQ55330.1; -; Genomic_DNA.
DR   RefSeq; WP_007304475.1; NZ_CAQL01000361.1.
DR   AlphaFoldDB; T2IT67; -.
DR   Proteomes; UP000017981; Unassembled WGS sequence.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CCQ55330.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCQ55330.1}.
FT   BINDING         33
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   324 AA;  38224 MW;  CD5DDE6643B8D8CD CRC64;
     MINQVKPQQI KQLSILEDDN YQDGLKPSPV LKWAGGKTQL LPEIKKQYPQ QLQQGKIKTY
     IEPFFGGGAV FFDIYHNFEI EQAYLFDKNI ELIILYKVIQ NDVNALIEEL SILESKYLTL
     DTENRKEFYY QLRDDYNTFD KQTDANNYRQ EWINRAAYTI FLNKTCFNGL YRVNSKGYFN
     VPMGRYKKPK ILNQDNLIAV HESFKIVEIQ HTDFAEVLNY ADESTFIYYD PPYRPISETS
     NFNSYSSLEF NDDEQKRLRD VFTKTSKQGA LQILSNSDPT NYIDDPFFDE LYQDFNISRI
     LASRMINSKG KKRGKIREIL VNNY
//
DBGET integrated database retrieval system