ID A0A0G0G7R1_9BACT Unreviewed; 523 AA.
AC A0A0G0G7R1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=UR91_C0038G0003 {ECO:0000313|EMBL:KKP87747.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWC2_35_8.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618752 {ECO:0000313|EMBL:KKP87747.1, ECO:0000313|Proteomes:UP000034798};
RN [1] {ECO:0000313|EMBL:KKP87747.1, ECO:0000313|Proteomes:UP000034798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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:KKP87747.1}.
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DR EMBL; LBQZ01000038; KKP87747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0G7R1; -.
DR PATRIC; fig|1618752.3.peg.536; -.
DR Proteomes; UP000034798; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR006200; LexA.
DR InterPro; IPR039418; LexA-like.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR006199; LexA_DNA-bd_dom.
DR InterPro; IPR006197; Peptidase_S24_LexA.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR NCBIfam; TIGR00498; lexA; 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 Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW SOS response {ECO:0000256|ARBA:ARBA00023236};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT DOMAIN 5..67
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 82..191
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 523 AA; 59990 MW; 2C79C797E3543661 CRC64;
MANTKPLRKK QKQVLDFVKD YISENGISPT IEEIRKKLKL RAVSTIHEHL NTLKTKGYLL
KDENSARSIM PNKEIKKIIE IPIIGRIAAG EPIDVIENYF GTVSIINNDF KNIKDYYALR
VMGNSMIDEG IFDGDTVIIK KQSVAENAII DDEQATLKKL YRENGKFRLQ PRNPNIKPLF
RTDVEIRGIV IQVISNINNK PEVRLEKKIK HRFKTIDLFA GIGGIRIGFE RAGFETVFAN
DFDQQCKTTY DLNFAKSKLI VEDIRKVGIN DLPKFDFLLG GFPCQAFSIA GYRQGFNDEK
GRGNLFFDIA RIIEARRPEG FLLENVKNLK SHDEGKTFKI IQETLENLGY HLNIKVLNSM
EYGNIPQNRE RVYIVGFKNK NYSDRFEFPN PIKLTVKITD LLETNVPEKY YYNGKPLFKK
LKDFVKEEGR VYQWRRKYVR ENKSGVCPTL TANMGTGGHN VPIIKDKKGI RKLTPRECAL
IQGFPIDYKI PILADSALYK QFGNSVSVPV IEAVGKQMMK AME
//
