ID A0A117MHK5_9EURY Unreviewed; 344 AA.
AC A0A117MHK5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Type II methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.113 {ECO:0000256|RuleBase:RU362026};
DE AltName: Full=N-4 cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU362026};
GN ORFNames=XE11_0602 {ECO:0000313|EMBL:KUL04531.1};
OS Methanomicrobiales archaeon 53_19.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=1641394 {ECO:0000313|EMBL:KUL04531.1, ECO:0000313|Proteomes:UP000054757};
RN [1] {ECO:0000313|Proteomes:UP000054757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893,
CC ECO:0000256|RuleBase:RU362026};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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:KUL04531.1}.
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DR EMBL; LGHF01000005; KUL04531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117MHK5; -.
DR PATRIC; fig|1641394.3.peg.1448; -.
DR Proteomes; UP000054757; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU362026};
KW Restriction system {ECO:0000256|RuleBase:RU362026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU362026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 93..323
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 344 AA; 39150 MW; 2E6229451EE4C48F CRC64;
MISHAAQSGA PEHNLPEKTL YANQSNMDRQ LESFIHPEIA AVAGEMGQRA IPFIAKDPIL
MKEIEALSAS IPTAHRFINT DCRNLGYIPD ESVHLVVTSP PYWILKTYPE KESQLGQIGD
YDTFLEELDR VWQHIHRILV PGGRLVIVVG DVCLPRRNTG RHSVIPLHAS IQEHCRLIGF
DNLAPIIWYK IANASFESQS AGSFLGKPYE PNAIVKNDIE YILFQRKPGG YRKTTRPARL
LSIISEENQK IWFRQIWDLK GASTRNHPAP YPLELAERLI RMFSFVGDTI LDPFGGTGTT
TLAAARWGRN SISIEIEEDY HSMQIERFNQ KYQQPYRRAG WKCS
//
