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Database: UniProt
Entry: A0A423VDB9_9PEZI
LinkDB: A0A423VDB9_9PEZI
Original site: A0A423VDB9_9PEZI 
ID   A0A423VDB9_9PEZI        Unreviewed;       361 AA.
AC   A0A423VDB9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=FAM86 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VMCG_10157 {ECO:0000313|EMBL:ROV88981.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV88981.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROV88981.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROV88981.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) 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:ROV88981.1}.
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DR   EMBL; LKEA01000074; ROV88981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423VDB9; -.
DR   STRING; 356882.A0A423VDB9; -.
DR   Proteomes; UP000283895; 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:UP000283895};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   361 AA;  39815 MW;  95E3F71F03C9C620 CRC64;
     MTGSEEGLSR LDRAAIDRFC YQYLQLETHL DYPDGQLLKR AGVQDEIFDR IFSGQSHSAK
     QPRLQLRALK ELVARIQASI SDDEADDYEV SDKLMDHLGE LMFHPLMPVA DEAQQKCIVT
     YHMSLLQSPV DIDILENRAL ISAAGTTGLR TWEAALHLGQ FLCVNGPLVA GKRVLELGAG
     TGYLSVLCAK CLGAAHVTAS DGAEEVVDNL ADNFTLNGLD WDFSGSRKAR LSPKLLKWGH
     ALVGTEEPEW MGGQKIDLII GADVIYDQRT IPSLVSTLNE LLELHPGAEV IIAATQRAIE
     TLSAFQDACA RSSLRVDELK FPAQEQQNVL EDRGQPHGPL TPFYPSHTPI RILHISARTR
     K
//
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