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Database: UniProt
Entry: F1L720_ASCSU
LinkDB: F1L720_ASCSU
Original site: F1L720_ASCSU 
ID   F1L720_ASCSU            Unreviewed;       330 AA.
AC   F1L720;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=24-methylenesterol C-methyltransferase 3 {ECO:0000313|EMBL:ADY45924.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY45924.1};
RN   [1] {ECO:0000313|EMBL:ADY45924.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000256|ARBA:ARBA00038188,
CC       ECO:0000256|PROSITE-ProRule:PRU01022}.
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DR   EMBL; JI172772; ADY45924.1; -; mRNA.
DR   AlphaFoldDB; F1L720; -.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR030384; MeTrfase_SMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR44068:SF1; HYPOTHETICAL LOC100005854; 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; PS51685; SAM_MT_ERG6_SMT; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01022};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01022};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01022}.
FT   DOMAIN          48..330
FT                   /note="SAM-dependent methyltransferase Erg6/SMT-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51685"
SQ   SEQUENCE   330 AA;  37144 MW;  50EF2AC22BF2CF24 CRC64;
     MSINLTSNFF RLLLHFRRQD LVNFGDEHER LYAEAKRTSD HSAVTSHYYS VMSAVIDDYF
     NGSFHFVPPH HDRQTLEEAL VALHRNVAKC LKLEKGRKCV DIGCGIGTVM KDLASTEADL
     TGVTIAANEA FSGNAQFVEN GIKNCRIIEG DCHHMPFEES TFDAAYAIYA LKYFLDLSPV
     MNEISRVLKP GGLLLVYDLI KTRKYDPNSL EHRKIIEGIE YACGMPSLHT REEMIKAAAE
     CELHLIDAID LDARTGYPFH YCFSNSRFFM WLIRSSLVGH LISIAQAIGI LPKGFYQFNK
     VFLSGTVSKI TLAGKMGILS GSEILLFQKK
//
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