ID A0A1G7VX89_9FLAO Unreviewed; 415 AA.
AC A0A1G7VX89;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN05421825_3744 {ECO:0000313|EMBL:SDG64343.1};
OS Epilithonimonas hungarica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=454006 {ECO:0000313|EMBL:SDG64343.1, ECO:0000313|Proteomes:UP000199203};
RN [1] {ECO:0000313|Proteomes:UP000199203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19684 {ECO:0000313|Proteomes:UP000199203};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000256|RuleBase:RU000417};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
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DR EMBL; FNBH01000006; SDG64343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7VX89; -.
DR STRING; 454006.SAMN05421825_3744; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000199203; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.120.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT ACT_SITE 87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 415 AA; 46959 MW; E5A568A482CC0156 CRC64;
MKKIKVIELF AGVGGFRIGL QNSNKASSKE NFEVVWSNQW EPSTKTQHAS LVYESRFGKK
GHSNQDISTV PSEEIPEHDM LVGGFPCQDY SVATTLKNSK GLQGKKGVLW WEIYRILESK
KDKPKFLFLE NVDRLLKSPT TQRGRDFAIM LKCLSDLGYA VEWRVVNAAD YGMPQKRRRT
FILGYLKDSA IYNSLIKTPE VDWLLDEGVF AKTFEVGQIS ELKTFDLDQS VEEISTSFNK
EKGDSPFQNS GMILNGKVTT VKTSPNYEGK RTLLKDILIP ADEVPQEYFI DESEIDKWNY
LKGAKKEVRQ SADGFSYNYG EGAMIFPDNL ESPSRTIITG EGGKSASRFK HVVRTNKGLR
RLTPIELERL NMFPDDHTLL EGVSDVKRAF FMGNALVVGV IEKIGEMLLK FNQKG
//
