ID A0A2T5MAB7_9EURO Unreviewed; 849 AA.
AC A0A2T5MAB7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=P175DRAFT_0514165 {ECO:0000313|EMBL:PTU25445.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU25445.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU25445.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU25445.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(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:PTU25445.1}.
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DR EMBL; MSFN02000001; PTU25445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5MAB7; -.
DR VEuPathDB; FungiDB:P175DRAFT_0514165; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000244073; 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; 1.
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 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 35..361
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 370..586
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 589..837
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 798..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 556
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 565
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 396
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 405..406
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 467
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 494..495
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 399
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 849 AA; 93252 MW; 64B36375A0FF896D CRC64;
MDSEGAAPSF CIGQHESKRA LPITSQAVQL AHESNYDMLT TPITTSHFHS RVLGLLSSHF
SNIQAVSRDV SGTLATTENT RALTIPQLSP SDTHLTPNDA MSQLVGVTSS WIDLCSPDPL
IADISRQVLM LEVAYAAFCG IGYLLIPGPK LHHKDLHSEG LAYYARAVQD AINLGPYIQF
HIWLGMVDNP DLEVDEMGDL APLAREEFLG RGDRQSLQVD LFGTWDAWDL IRRTCRYHSR
LFVALVFPKQ LPPMSVQSRW HSEPVHLLTI DSSSFIKNQK GYPVLSKGHQ ALIAKFMRLR
TVPWILLCDV GPIPGIEAEG NLANPTNLPS SEYPSLAQVA GSNKKQHDPT PHLSYMRNLQ
QRQPPRTAIE RFGVGYQDYL QAPLQPLTVN LESITYEVFE KDPIKYEWYE KAIAKALSDW
SEQKKPTSNP DGRVVVAVVG AGRGPLVTRA LKASADAGVE IDLWVVEKNP NAFVLLQRHN
ENLWGGKCTL VHSDMRSWKG PRLSGKSASS SAPVGQSLGI ENQLLYPSDS IQQTDPVTTA
YMPEPIYTKI DIVVSELLGS FGDNELSPEC LDGINHLLNP VHGISIPASY TAHLTPISAP
KLHADIANQT VSNPAAPETP YVVMLHAIDF LSTTNSNTYA NNARSSISTL PTDNSTPLVQ
TAWAFAHPNG NIPPPSPSTS TISNGHNVRR TRLTFPIQNR GVCHGLAGYF ETVLYRDVEL
STNPVTMESK SANMISWFPI YFPLKTPLNV PDNGEIVVTM YRQTDDRKVW YEWMVEVLAV
EGNAGETPEP ERIAPMMSGA GAIPPGADSA KNQDHHATGS SRLGSGSRIR RVRVGMSDLH
SSIKDGCLM
//
