ID Q332I2_CBCP Unreviewed; 370 AA.
AC Q332I2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Putative DNA methylase {ECO:0000313|EMBL:BAE47742.1};
GN ORFNames=CST044 {ECO:0000313|EMBL:BAE47742.1};
OS Clostridium botulinum C phage (Clostridium botulinum C bacteriophage).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=12336 {ECO:0000313|EMBL:BAE47742.1, ECO:0000313|Proteomes:UP000001240};
OH NCBI_TaxID=36828; Clostridium botulinum C.
RN [1] {ECO:0000313|EMBL:BAE47742.1, ECO:0000313|Proteomes:UP000001240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16287978; DOI=10.1073/pnas.0505503102;
RA Sakaguchi Y., Hayashi T., Kurokawa K., Nakayama K., Oshima K., Fujinaga Y.,
RA Ohnishi M., Ohtsubo E., Hattori M., Oguma K.;
RT "The genome sequence of Clostridium botulinum type C neurotoxin-converting
RT phage and the molecular mechanisms of unstable lysogeny.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17472-17477(2005).
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; AP008983; BAE47742.1; -; Genomic_DNA.
DR RefSeq; YP_398474.1; NC_007581.1.
DR REBASE; 12844; M.CbocstORFAP.
DR GeneID; 3773117; -.
DR KEGG; vg:3773117; -.
DR OrthoDB; 8328at10239; -.
DR Proteomes; UP000001240; Genome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; 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:UP000001240};
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 73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 370 AA; 42528 MW; 9A1C8E286FA4FB0F CRC64;
MKFIDFFSGA GMFRKGMEDA GHECIGYVEI QKQARETYET NYDTTKEWTF HDVAQLKAED
IPNADIWCFG FPCKNMSTAN VTTRTGLKGE QSGLFLIMCD LLNKMKRKPQ ILFIENVQGF
STINGGSDFL EALVRLHKLG YDIKYEISSA MQYDVPQNRI RTYLICKLNN YIKINEGIEI
PNKKTIHINK LNIYDLYNYI SKENNKFKIK YGVNGEIRNG VCTVLKEKRE NDYNLTYLLK
DILEQEVEDK YYLTEEQLIK VKKMKGAKQK TLKDGRIWKE GAVPFPDSID KNARCITPSD
GSLNRSTHII FDGKGYRKLT IRERARLQGL PDDFTFPVSN SQASLQLGNG VVVKVIKEIA
NKEINLNISK
//
