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Database: UniProt
Entry: D7G6X2_ECTSI
LinkDB: D7G6X2_ECTSI
Original site: D7G6X2_ECTSI 
ID   D7G6X2_ECTSI            Unreviewed;       738 AA.
AC   D7G6X2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Methyltransferase {ECO:0000313|EMBL:CBJ25665.1};
GN   ORFNames=Esi_0008_0070 {ECO:0000313|EMBL:CBJ25665.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ25665.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ25665.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
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DR   EMBL; FN649035; CBJ25665.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7G6X2; -.
DR   STRING; 2880.D7G6X2; -.
DR   EnsemblProtists; CBJ25665; CBJ25665; Esi_0008_0070.
DR   eggNOG; KOG4626; Eukaryota.
DR   InParanoid; D7G6X2; -.
DR   OrthoDB; 91541at2759; -.
DR   Proteomes; UP000002630; Chromosome LG02.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44523; TETRATRICOPEPTIDE REPEAT PROTEIN 13; 1.
DR   PANTHER; PTHR44523:SF1; TETRATRICOPEPTIDE REPEAT PROTEIN 13; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:CBJ25665.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:CBJ25665.1}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..738
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003096215"
FT   REPEAT          292..325
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          326..359
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          435..468
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          562..655
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
FT   REGION          34..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  80169 MW;  9D0196CACEC908B3 CRC64;
     MRCCSLAGVD VALLLLAGAA RSGEAFLFSG LRVPSTPRRQ HDPSPSSNTQ QQHAASGGRL
     LPTTSRPPST ASTLRATPAD DATGQQILEY PGMTDDQEGG APEGRQEGAA QPPPIPKDTT
     RRAVALDGTA LAFRPPTTQD FHKLGMGDWV AQKGLAVALV ALGATEQAAG EPVIGAPLAG
     AVVEAMGGGS SVATQVCLLR HRREDGVAEA VEHALLDETI NRFLNDGARI SQLRVEIDDS
     PQSVDYYSRH GFIRSVEAAS EGRVLLAGDR VAALGAIQAS LTGGDDQGTV GAVVMNLMAR
     LLHDAGNLQG AVDAYLKALE LDPTRSEVFR GLGGAYQSQG QHQMAFASYQ QAINLAPWDL
     LAYLKLGMLY EDLAVGKYEE AGDHAIRCFQ YYLQHSGSED TDVLTRLGNL QVMRLDPGSA
     VETYRRALAV DKSLSNVWFN LANAYLKLGE EEEAATCLKE KLRLDPDPNA GVSARYLLAS
     LEADPGRLTE SDQLAYAREL FDYYAPKYDD HMRKKLLYTG PRLLRKNMKE VYNATFQSFP
     DEIQSAHNGD VLSYLNGSLD ILDLGCGTGL IGSWFKDYAR KLVGVDISPT MLDMATKKGC
     YHELRRGDVR AYLAASEEQQ FDLVVAAETL QYLGPLETVV ADASKVLKPG GYFSFTVDRR
     RTNEGEEQEG RDEQGHDEDD PEEGYSLKTD GTYAYSRGYL ERLARLGGYE IVVLKRHSTM
     VQRGEAAPGY MGVFRKPE
//
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