ID H5SPY5_9ZZZZ Unreviewed; 435 AA.
AC H5SPY5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN ORFNames=HGMM_F55D02C21 {ECO:0000313|EMBL:BAL58221.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:BAL58221.1};
RN [1] {ECO:0000313|EMBL:BAL58221.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL58221.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR EMBL; AP011797; BAL58221.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SPY5; -.
DR REBASE; 416958; M.UprJFFORF21P.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF00565; SNase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:BAL58221.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..254
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT DOMAIN 356..427
FT /note="TNase-like"
FT /evidence="ECO:0000259|Pfam:PF00565"
SQ SEQUENCE 435 AA; 50981 MW; 93E01FE4BEE86CB3 CRC64;
MKTTHKIIIG DSRWMREVPD ESVHLVITSP PYWQLKGYGN SRQIGFNDTY EEYINNLNLV
WKECHRVLHK GCRLCINIGD QFARSVYYGR YKVIPIRTEI IKFCETIGFD YMGAIIWQKV
TTCHTTGGAT VMGSYPYPRN GILKLDYEFI LIFKKYGNPP KVSKEIKERS KLSDEEWNKY
FTGQWNFPGE KQDEHLAMFP EELPRRLIKM FSFVGETVLD PFLGSGTTTL AARNLGRNSI
GYEINEDFLP IIKEKVGLNE GTIFQDAVFE IIRQEELQID FEEEIKKLPY IFKDPVKFDR
KVDPKKLRFG SKIDKSPSER EEYYKVKEIL SPEILMLHNG LKVRLLGIKK KPGKEEQAIQ
FLKDKLKGQR VFMRFDNLKY DGEGNLLCYL YLWNKTFVNA HLIKNGLVDV DNSFDYRYKG
KFLNLQNQLI KEGYP
//
