ID K9UZ34_9CYAN Unreviewed; 280 AA.
AC K9UZ34;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Tocopherol O-methyltransferase {ECO:0000313|EMBL:AFZ01103.1};
DE EC=2.1.1.95 {ECO:0000313|EMBL:AFZ01103.1};
GN ORFNames=Cal6303_2077 {ECO:0000313|EMBL:AFZ01103.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ01103.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ01103.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ01103.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. gTMT family. {ECO:0000256|PROSITE-ProRule:PRU00914}.
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DR EMBL; CP003610; AFZ01103.1; -; Genomic_DNA.
DR RefSeq; WP_015197749.1; NC_019751.1.
DR AlphaFoldDB; K9UZ34; -.
DR STRING; 1170562.Cal6303_2077; -.
DR KEGG; calt:Cal6303_2077; -.
DR PATRIC; fig|1170562.3.peg.2263; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_039068_0_1_3; -.
DR OrthoDB; 9769602at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0050342; F:tocopherol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025774; MTs_g-TMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44068:SF11; GERANYL DIPHOSPHATE 2-C-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR44068; ZGC:194242; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51581; SAM_GTMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:AFZ01103.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00914};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:AFZ01103.1}.
FT DOMAIN 67..165
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REGION 66..75
FT /note="SAM motif I"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 129..137
FT /note="SAM motif II"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 156..165
FT /note="SAM motif III"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
SQ SEQUENCE 280 AA; 31535 MW; 5A4DBB6E7DEEAF81 CRC64;
MSATLYRDIQ QFYDASSKLW EDIWGEHMHH GYYGVDGKTK KERRQAQIDL IEELLKWSQV
DTATNILDVG CGIGGSTLYL ANKYQANATG ITLSPVQADR AKERARGLGL GERVNFQVAN
ALEMPFADNS FDLVWSLESG EHMPDKVKFL QECHRVLKPG GKLIMVTWCH RPTDNSPLTA
EEQKQLQEIY RVYCLPYVIS LPEYQAIASQ LPLYNLRTDD WSQAVAPFWN VVIDSAITPQ
AIWGLLCSGW TTIQGALSLG LMQRGYETGL IRFGLVCGNK
//
