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Database: UniProt
Entry: A0A1Q8CSI9_9PSEU
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ID   A0A1Q8CSI9_9PSEU        Unreviewed;       971 AA.
AC   A0A1Q8CSI9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=BU204_11825 {ECO:0000313|EMBL:OLF17303.1};
OS   Actinophytocola xanthii.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF17303.1, ECO:0000313|Proteomes:UP000185596};
RN   [1] {ECO:0000313|EMBL:OLF17303.1, ECO:0000313|Proteomes:UP000185596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-183 {ECO:0000313|EMBL:OLF17303.1,
RC   ECO:0000313|Proteomes:UP000185596};
RA   Wang W., Yuan L.;
RT   "The draft genome sequence of Actinophytocola sp. 11-183.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
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:OLF17303.1}.
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DR   EMBL; MSIE01000018; OLF17303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8CSI9; -.
DR   STRING; 1912961.BU204_11825; -.
DR   Proteomes; UP000185596; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185596};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..137
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          149..475
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          634..661
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   971 AA;  108223 MW;  07C723FF66E2521D CRC64;
     MQVDSLQYVT NDGFSRTLTA RLFDAFWAAG ISNPVETVEQ ISHLLYLREL DRLQEHWDQR
     VAPSEMPEGG SIFAQGDQHL RWSHFLRLTP QRMYTSMADE VFPWLRSHTI AGVVYSQHVK
     DARFTIPTPG LLAKTVSLLE ESFSAGDAAD LYEHLLAKAL TAGAMGQFLT PRHLAALMVA
     MAEPGPDDEV CDPTCGMGGL LSAAAQFVDR SDPNTSQRSA LEVSSRLHGF DFDRTMLRLS
     SMRLMLQGRE GADLRHRDNL VNRPGGDDER YSVVLADPPF GGNIDYKAVA PELLELVQTR
     NSDLLHLAAI LRLLKRGGRA AVIVPAGLLF GTSAAHVELR RMLVDEHGLE AVVKLPNGAF
     KPYSGVSGAI LFFIKDAGQA DSVWFYELKA DGWSLANRRA PLLAENKLGL SRDSTLDAGD
     HARNNLPDLL RRWRLRHSNE RGRARTDQSF CVIRAEIAAE NYNLTLEHFR QTHELRQVAQ
     EGIRLGDFAE TFSGAVRSSD LDKEPNSTDT DERRRVLTPT LLTSTLPDVA ELPVRADARD
     PRHRLRQGDI VGRDLAGARH WTPIPSQYDG VQPGQGLIII RIIQEVLPLE YLIAYLSSPL
     AEQQFPKYGT IPRIKAREMA DIWIPKCDGD PSEIRASLAR LEEGEREAAH IQDELRRART
     RIFESGSGSA RRIRLDDAAA ISSLTAQNLR RHNDPYMLFQ ESYPYAVARA VRKFRHSLSL
     AEKHEAAIQC TEALILSLGI MALAVAADRG RQDLPPIVQW SQSVEQGGVS LGHWLAVVKA
     VAEDARQHGE PAVGLVEATA RKKGGTGLIA DLEQLVKLRN KIRHGAGPRT RAELEKSLGR
     VETPMLSSLS GCAFLARTRW VHTERLQWLP TSGRFRVSGL ALMGDHPDFE MFTFDTSRPL
     ANDHLYLITQ HDMPLPLSPF CLLSDCPTCL APELYYPDRM TRSTALLKSL DRGHELESEF
     VFTTLQEWGR S
//
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