ID A0A1V4MDQ5_9FIRM Unreviewed; 523 AA.
AC A0A1V4MDQ5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN ORFNames=AVO34_06860 {ECO:0000313|EMBL:OPL12651.1};
OS Firmicutes bacterium ML8_F2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1775675 {ECO:0000313|EMBL:OPL12651.1, ECO:0000313|Proteomes:UP000189969};
RN [1] {ECO:0000313|EMBL:OPL12651.1, ECO:0000313|Proteomes:UP000189969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML8_F2 {ECO:0000313|EMBL:OPL12651.1};
RA Hamilton T.L., Pearson A., Macalady J.;
RT "Carbon and sulfur cycling below the chemocline in a meromictic lake.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
CC -!- SIMILARITY: Belongs to the ParB family.
CC {ECO:0000256|ARBA:ARBA00006295}.
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:OPL12651.1}.
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DR EMBL; LQBG01000051; OPL12651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4MDQ5; -.
DR Proteomes; UP000189969; 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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2830; -; 1.
DR Gene3D; 3.90.1530.30; -; 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; IPR004437; ParB/RepB/Spo0J.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00180; parB_part; 1.
DR PANTHER; PTHR33375; CHROMOSOME-PARTITIONING PROTEIN PARB-RELATED; 1.
DR PANTHER; PTHR33375:SF1; CHROMOSOME-PARTITIONING PROTEIN PARB-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF02195; ParBc; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; ParB/Sulfiredoxin; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..98
FT /note="ParB/Sulfiredoxin"
FT /evidence="ECO:0000259|SMART:SM00470"
FT COILED 232..263
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 523 AA; 61295 MW; 876D2BC36801FA27 CRC64;
MITTELQSAE HKIINIKEIV PGYNPRSSLD IDEDFIKSIK SLGILEPLLV RPKEGKYEII
AGHRRLKAAE SVGITEIPAL VRDLDDEQAE HIAYIDNKER KDYTPIDEAC HFAYMKEKHG
WSLRDMEKAG YGDHTIIRHK IGLLTLPERV AELLARANSL TERHCRHIVQ LCDREKLTKI
FAENRDNFIV PENWESEEEQ EYWRWRLNQE IKYRQDYQIK LAEQTVQNEW TAKSLEIRVR
ELKEELDERM KKIKEEIEEG KKLNLIMDGI YFKSSADMKE LQENSVGVVI TSPPYLANKE
YEEEEVKNHE NPIEWYKDLL HKSFKECYRA LMPGSYVCLN INDIPNINTV LEKDAPSEMQ
PIAEIVHPIM KEIGFRLKDI ITWKKDDPWR NNPHVKYEEQ EGCYRILPSR EYVFLYQKPG
TRKITPSQRI DSSIAKEEWA EWASGLWNIP SVRKNDDHPA KYPDELVRRL VKMYSFKGDI
VLDPFLGSGT TVKVARELDR KGVGYEINEK YKPAIHAVLS SEE
//