ID   M9RMU9_9RHOB            Unreviewed;       314 AA.
AC   M9RMU9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Homocysteine S-methyltransferase-like protein {ECO:0000313|EMBL:AGI73482.1};
GN   ORFNames=OA238_c35130 {ECO:0000313|EMBL:AGI73482.1};
OS   Octadecabacter arcticus 238.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI73482.1, ECO:0000313|Proteomes:UP000004688};
RN   [1] {ECO:0000313|EMBL:AGI73482.1, ECO:0000313|Proteomes:UP000004688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=238 {ECO:0000313|EMBL:AGI73482.1,
RC   ECO:0000313|Proteomes:UP000004688};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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DR   EMBL; CP003742; AGI73482.1; -; Genomic_DNA.
DR   RefSeq; WP_015496487.1; NC_020908.1.
DR   AlphaFoldDB; M9RMU9; -.
DR   STRING; 391616.OA238_c35130; -.
DR   KEGG; oar:OA238_c35130; -.
DR   eggNOG; COG2040; Bacteria.
DR   HOGENOM; CLU_062282_0_0_5; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000004688; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   PANTHER; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000004688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          4..310
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   314 AA;  34005 MW;  DD527602135F942F CRC64;
     MSQPTPLLPH QTNVIFLTDG GTETWLMYKR GFELPKFSAF HLLNDKRAAR ALREYYTAFA
     NVAVKLGTPF IFDSLTYRAS RDWGALLGYS TAGLAEMNHK CFELYRECAT AAGLPPENTV
     ISGCIGPKGD AYQTHQDLTS QSAELYHSEQ IGTFKEAGAD IVTALTLNTT DEAIGIARAA
     AKVGLPSVIA FTIEKDRKLR SGESLKQAIE TVDAATANAP AYYMINCSHP VDFGPALAVE
     TWAKRIRGLR ANASSLDHGT LCQLGHLEEG DPDELASQYV DLRAAHPNMN VFGGCCGTDY
     VHVEKTGRAL LAAA
//