ID F1D295_9CAUD Unreviewed; 278 AA.
AC F1D295;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 28-JUN-2023, entry version 31.
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=TUST1-191_00965 {ECO:0000313|EMBL:ADX88239.1};
OS Vibrio phage ICP1_2006_D.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=979532 {ECO:0000313|EMBL:ADX88239.1, ECO:0000313|Proteomes:UP000007655};
RN [1] {ECO:0000313|EMBL:ADX88239.1, ECO:0000313|Proteomes:UP000007655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21304168;
RA Seed K.D., Bodi K.L., Kropinski A.M., Ackermann H.W., Calderwood S.B.,
RA Qadri F., Camilli A.;
RT "Evidence of a dominant lineage of Vibrio cholerae-specific lytic
RT bacteriophages shed by cholera patients over a 10-year period in Dhaka,
RT Bangladesh.";
RL MBio 2:E00334-E00310(2011).
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}.
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DR EMBL; HQ641348; ADX88239.1; -; Genomic_DNA.
DR REBASE; 36041; M.Vph6DORF965P.
DR Proteomes; UP000007655; Genome.
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 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:ADX88239.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 278 AA; 32540 MW; FBF941B869219230 CRC64;
MTIRSSIYLQ GSKFKLYPQI KPYLQDGKRK VLVDLFGGSG TMTLNCVKDD MFEKYIYNDK
SSWLYDMQSY LKDYDNVVET LTRINEEYPK TREGYLMLRE DYNLRPSMAR LYILMCRSFS
NQVRFNPTSG FDMPYGDRKP FFPERIRKHQ QLLKDVELYN HDFGDMVEIL LEGGDLSGTT
VYIDPPYQFT TATYNENGGW TQNDNTSLLE YLLELRSKGA LVVMSNVFEN RGCIHQELID
FCEQHKDKFD AHQMNISYNN SSFRKGSGVT REVLIVSK
//
