ID I3C8H9_9FLAO Unreviewed; 461 AA.
AC I3C8H9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=JoomaDRAFT_2965 {ECO:0000313|EMBL:EIJ39922.1};
OS Galbibacter orientalis DSM 19592.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ39922.1, ECO:0000313|Proteomes:UP000004690};
RN [1] {ECO:0000313|EMBL:EIJ39922.1, ECO:0000313|Proteomes:UP000004690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ39922.1,
RC ECO:0000313|Proteomes:UP000004690};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL Submitted (FEB-2012) 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; JH651379; EIJ39922.1; -; Genomic_DNA.
DR RefSeq; WP_008613791.1; NZ_JH651379.1.
DR AlphaFoldDB; I3C8H9; -.
DR STRING; 926559.JoomaDRAFT_2965; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_006958_0_2_10; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000004690; 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; 3.40.50.150; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004690};
KW 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 78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 461 AA; 53354 MW; 6E0D3AA0B300C892 CRC64;
MTKKKLKFID LFAGLGGFHK ALHELGHECV FASELDPTLR NVYQANWGIE AQGDIKRIVE
KEIESIPPHD ILCAGFPCQP FSKAGKQLGR DDDRGTLFDE IAKILAFRKP KFFILENVPF
IKQHDNEETW NYMHNELSNL GYEVDHQVYS PQDFGVPQHR KRIFIVGSLI GLDHFSFDEI
DEQKTSLIDI HQFIEEKPKL FKELPKTNQE CLKLWQTFID QIPKETKLPG FPIWGMEFGA
TYPYDSTPPS KMPKYELANY KGNFGKQLTL EMTKKEQLQN LPSYARVTRK FPDWKQRYIK
QSRDFYEDNK KHINGVVAEI AKYPSQSWQK LEWNVGDGER KLDNYILQFR ASGIRVKKVD
FFPSLVCTNT QIPIIGWQKR YITREEGLKL QSLDGISLPQ NDNAAFKALG NAVNSKIVKL
IAEKLIQEQP KIVELNGAKK VINGTSICSY ETNEIKYERI K
//
