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Database: UniProt
Entry: A0A2P5I0G4_9PEZI
LinkDB: A0A2P5I0G4_9PEZI
Original site: A0A2P5I0G4_9PEZI 
ID   A0A2P5I0G4_9PEZI        Unreviewed;       363 AA.
AC   A0A2P5I0G4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=FAM86A protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DHEL01_v205607 {ECO:0000313|EMBL:POS76005.1};
OS   Diaporthe helianthi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=158607 {ECO:0000313|EMBL:POS76005.1, ECO:0000313|Proteomes:UP000094444};
RN   [1] {ECO:0000313|EMBL:POS76005.1, ECO:0000313|Proteomes:UP000094444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7/96 {ECO:0000313|EMBL:POS76005.1,
RC   ECO:0000313|Proteomes:UP000094444};
RA   Baroncelli R.;
RT   "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EEF2KMT family. {ECO:0000256|ARBA:ARBA00005511}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POS76005.1}.
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DR   EMBL; MAVT02000418; POS76005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5I0G4; -.
DR   STRING; 158607.A0A2P5I0G4; -.
DR   InParanoid; A0A2P5I0G4; -.
DR   OrthoDB; 53021at2759; -.
DR   Proteomes; UP000094444; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF164; PROTEIN-LYSINE N-METHYLTRANSFERASE EEF2KMT; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094444};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   363 AA;  40129 MW;  D4019E163427F1B7 CRC64;
     MAESHSSSLN PPSELSSTAI IDRFCCQYLQ LEAHLDYPDG QLLKTPEVQD EIYERMFAGR
     STSSKSARFQ LRVLKELVKR IQDSIGENET DDFEVSDKLM DRLGELMFEP LMAEAVEAQR
     RCLVTYRISM VQPPENIDIL ENRSLLAAGG TTGLRTWEAA LHLGQYLSIN GHLVAGKRVL
     ELGAGTGYLS ILCAKLGAAH VTSSDGSEEV VEKLADSFIL NGLQWDHSVS SSARLRPKLL
     KWGHALVGTE EPGWNGGHKV DLVIGADVTY DQKVIPFLVS TLSELVDLGP DTEILISATQ
     RNADTLTVFR DSCAKACLQV KELAFSVKDQ QDILERHGRP EVALTPFYST HMPIRIFQIT
     GSK
//
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