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Database: UniProt
Entry: A0A409VMK5_PSICY
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Original site: A0A409VMK5_PSICY 
ID   A0A409VMK5_PSICY        Unreviewed;       778 AA.
AC   A0A409VMK5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN   ORFNames=CVT25_006024 {ECO:0000313|EMBL:PPQ67483.1};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ67483.1, ECO:0000313|Proteomes:UP000283269};
RN   [1] {ECO:0000313|EMBL:PPQ67483.1, ECO:0000313|Proteomes:UP000283269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2631 {ECO:0000313|EMBL:PPQ67483.1,
RC   ECO:0000313|Proteomes:UP000283269};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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:PPQ67483.1}.
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DR   EMBL; NHYD01003973; PPQ67483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409VMK5; -.
DR   STRING; 93625.A0A409VMK5; -.
DR   InParanoid; A0A409VMK5; -.
DR   OrthoDB; 5489665at2759; -.
DR   Proteomes; UP000283269; Unassembled WGS sequence.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR   InterPro; IPR035075; PRMT5.
DR   InterPro; IPR035248; PRMT5_C.
DR   InterPro; IPR035247; PRMT5_TIM.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10738; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR   PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR   Pfam; PF05185; PRMT5; 1.
DR   Pfam; PF17286; PRMT5_C; 1.
DR   Pfam; PF17285; PRMT5_TIM; 1.
DR   PIRSF; PIRSF015894; Skb1_MeTrfase; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR015894};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283269};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR015894};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015894}.
FT   DOMAIN          50..307
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          354..515
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          518..776
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        486
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        495
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         389..390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         443
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         470..471
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            383
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   778 AA;  86542 MW;  96E79B8D21D66B82 CRC64;
     MDYQESWDHC ATLSTSLTLS DISKACRGLS DFQGDETAVL KVIGDSKQKG YKRVCMPLTT
     EKWKERWSKM CLLPNESSDE DKESASKAAE AWRLNPAFQR DEVTITRLDE AEGIIVMVSE
     WLELDAADDW VRHDAEIALK QELAYASYLN IHTVILPSPR NRDHVASYAR IVNSCLTKFP
     YIYISIRLPI YNPSVFQPSS PSSPVLRPTS PPMHASLGSS SSIAPSLVIS ESEQLPASNS
     GVSLNATWEM WDLIRTMCDY NMKLTLTLDL SPALPTTLGV LSKWAAESVR HIFLPASTFI
     ANVKGYPHRP MIILAEVGEG RHTRGGENAY SQYVRHLEKT SPAVQAAKKA GTVENFAQGY
     QDYLQAPLQP LMDNLPSITY QTFEQDPIKY MQYEEAMFRA FLDHPVDEKL VVCVAGAGRG
     PLVARCFKAL ERSNREATVI AVEKNPNAFV TLQERQIKEW GNKVQLIFGD MRLIDVPEKA
     DILVSELLGS FGDNELSPEC LDGAMRFLKP TGISIPSSYT AHLAPLSSSK LYNEARSTKT
     EKGLETPYVV MFQAVNILSG TKASADGRCG PQVQECWEFE HPRRDAVLDS QGLPFTNSHN
     ARSAKLRFYI PHAGILHGLA GYFEAVLYGN IGISIHPHRK DQVSKDMLSW FPLFFPFREP
     LYLPSSSELQ VSIWRITNDR RVWYEWHAES FISVPNSAGT SEELLMGQPF SGSFSASSSS
     FSSMGAPSPL VDSKEPAFLD MTRMNTNYAG SGGVEYETVK IGHTSLHNAG GRSSWIGL
//
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