ID A0A255GYX1_9ACTN Unreviewed; 372 AA.
AC A0A255GYX1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=CGZ93_11700 {ECO:0000313|EMBL:OYO20875.1};
OS Enemella dayhoffiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO20875.1, ECO:0000313|Proteomes:UP000216311};
RN [1] {ECO:0000313|EMBL:OYO20875.1, ECO:0000313|Proteomes:UP000216311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130396 {ECO:0000313|EMBL:OYO20875.1,
RC ECO:0000313|Proteomes:UP000216311};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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:OYO20875.1}.
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DR EMBL; NMVQ01000023; OYO20875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255GYX1; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000216311; 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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF59; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT1-RELATED; 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:UP000216311};
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 REGION 131..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 372 AA; 40290 MW; 79FB2056FEC468CD CRC64;
MHDLDVSSEP RLRIGSLFSG YGGLDLAVEH VFNAKTVWFS ELNQPVARVF SHHWPDAPNL
GAITAIDWSH VEPVDILIGG FPCQDVSTVG KRAGLAPGTR SGLWAHMASA IDALQPEWVV
IENVRGLLSS PATRPAAEGD DHDRRNPRDA TPDGASLRGV EPDSWHLGDK AARPLRALGA
VLGDLADLRL DARWIGLPAS LVGAPHQRFR IFALARRTVP HPAGDGLIAR RGNARPSASE
TRDDRIVPPD HRLRTPRTGW LTEQESRVGN AVVPDRRTVQ RWGRYADTIA RWEHITGRAA
PAPARLNDAD GPRPAPAFVE WLMGLPTEWV TGADDLTQNQ QITALGNGVL PLQACAALSS
ILAQVDRIDG GP
//
