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Database: UniProt
Entry: A0A0K0Y489_9RHOB
LinkDB: A0A0K0Y489_9RHOB
Original site: A0A0K0Y489_9RHOB 
ID   A0A0K0Y489_9RHOB        Unreviewed;      1040 AA.
AC   A0A0K0Y489;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=OSB_12430 {ECO:0000313|EMBL:AKS45798.1}, SAMN05444287_0897
GN   {ECO:0000313|EMBL:SIO00773.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS45798.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS45798.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS45798.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
RN   [2] {ECO:0000313|EMBL:SIO00773.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO00773.1};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000184809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; CP012160; AKS45798.1; -; Genomic_DNA.
DR   EMBL; FSRP01000001; SIO00773.1; -; Genomic_DNA.
DR   RefSeq; WP_049834153.1; NZ_FSRP01000001.1.
DR   AlphaFoldDB; A0A0K0Y489; -.
DR   REBASE; 116706; OteSB1ORF12430P.
DR   KEGG; otm:OSB_12430; -.
DR   PATRIC; fig|1458307.3.peg.1257; -.
DR   OrthoDB; 9803459at2; -.
DR   Proteomes; UP000067444; Chromosome.
DR   Proteomes; UP000184809; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF18135; Type_ISP_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AKS45798.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067444};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          284..388
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          446..537
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          661..1008
FT                   /note="Type ISP restriction-modification enzyme LLaBIII C-
FT                   terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF18135"
SQ   SEQUENCE   1040 AA;  119188 MW;  05DD0F39C9EECB56 CRC64;
     MSQRLINSYL ADIDKIRMVS GSLTEGVISE AFKDLLKAWA KSDGLTFINQ YPMQSSLKKP
     IRPDGAILHD VRVPLGYWEA KDTDDDLDAE IKAKLLTGYP QDNIIFEDSR VAVLWQDRNE
     ITRCDMTDTA GLEQLLNLFF GYQRPEIAQF RLAVEQFKAD LPAVLTALRE KIDEAYKINV
     TFKTAAKKFL AHACETINPT LGRDDVREML IQHILTEEIF ARVFDEADFH RDNNVAKLLY
     ELEGAFFTGA VKKSTLKALQ PYYTAINANA AQITSHTEKQ TFLKVIYENF YKVYNPDAAD
     RLGVVYTPNE IVKFMIEGAD WLTDKHFGKR LIDEGVEILD PATGTGTYIC ELIEYFRGQP
     DKLRHKYTEE LHANEVAILP YYVANLNIEA TYQAVSGQYA EYPNLCFVDT LDNIGGLGIK
     SGHQFDMFAS VSDENVARVK RQNKRKISVV IGNPPYNANQ QNENDNNKNR TYPHIDDLIK
     RSFVKLSTAQ KTKVYDMYAR FFRWASDRLH DDGVIAFVTN RSFIDSRTFD GFRRYVAQEF
     DEIYLVDLGG DVRANPKLSG TKNNVFGIQT GVAISFFVRR QLGKKKKRDC KIHYVRRPEL
     ETSDDKLSWL SAVKASDAKY EVVTPDEKGN WINQTENNWD DLLPVADKKT KAAKVASQEK
     AIFKLFSLGV ATNRDDWVYD FSENDLAAKA KHLVGIYEQD RKRLKTLKSP KEIADALDYS
     IKWTRSVKKD LLGRKKHRFN KSSIITANYR PYVKKAMYRD TAFNEMSNLT RTIFGMGQHL
     NSSITFMGDS SGKPFLSLAI NQVPDLNFVS PASGGSQTLA RYRYNLEGGR IDNITDWAFN
     KFTAHYGKKA KITKDDIFAY VYAVLHDPVY RETYAINLKR EFPRIPFYPD FPQWRDWGQT
     LLDLHIGYEK VKPYKLKRSD EEDVKAVKAG LAPKVSLKAD KDAGTITLDS ETTLSGIPPE
     CWDYKLGNRS GLEWILDQYK EKTPRDPTIR EKFNTYRFAD YKEQVVDLLK RVTRVSVETM
     EVVEKMKAVK RSSNEDSKDD
//
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