ID A0A1V6TM92_9EURO Unreviewed; 859 AA.
AC A0A1V6TM92;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=PENSTE_c004G09891 {ECO:0000313|EMBL:OQE27286.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE27286.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE27286.1}.
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DR EMBL; MLKD01000004; OQE27286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TM92; -.
DR STRING; 303698.A0A1V6TM92; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000191285; 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:UP000191285};
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 38..365
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 374..596
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 599..811
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 575
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 400
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 409..410
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 471
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 498..499
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 403
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 859 AA; 94915 MW; EBFB7286E019409B CRC64;
MDNYASDDPG PSFLVGHHES NRAVPVDADM IFKVHEANYD MLTVPITTPH FHSRVLGLLS
SYLSKLQSPT YDSIGTMGTS QNTRPLVVPA LSKLDTHLTP NEATSQIVGV ISSWIDLCSP
DPLIADLSRQ VLLLEVAYAA FCGIGYLLIP SPKLHHGGLH SEGVVYYARA IQDALSLGPY
IQFHIWLRMT DNPELEVDTM GDLAPLAREE YLQPDEGLSP KLDLFGTWDA WDLIRKTCRY
HTRLLVALSM PKQLPPLTVQ SRWHSEPVHL LTLDSSCFLK NQKGYPVLSK AHQALIAKMM
RLRTVPWILL CDVGPIPGIE DIEDADGNKS PLSGSEYPSL SQVAGSTKKH FDPTPHLSYI
RNLQQRQPPR TPIERFGVGY QDYLQAPLQP LTVNLESITY EVFEKDPIKY EWYERAITKA
LKDWSEQKKP TSHPDGKVVV AVVGAGRGPL VTRALKASEE AGVEIDMWAV EKNQNAFVLL
QRHNETTWGG KVTLVQSDMR SWKGPRVRGQ AGGTDNQDHI GESLGIEDNL LYTPKKGEND
PGPASDFSGQ KTTSLSYSHV DIVISELLGS FADNELSPEC LDGINHLINP VHGISIPASY
SAHFTPVSAP KLHSDVMNQT VSNPAAPETP YVVMLHAIDF LSSQETPINS DAGSQNTANR
SSGSAAPINA TEFQTPFVQT AWSFSHPNPN IPDQPSSGST IPNSHNVRQT RLSFPAQNRG
ACHGLAGYFE TVLYGDVELS TNPVTMEEKS ASMISWFPIY FPLKTPLNVP DNGEIVVTMY
RQTDDRKVWY EWMVEVFALE RRSVSVNKRA TPVMSGAQSI SNSAESLKIK ENDLGRAGYR
RVRVGISDLH SSIKDGCLM
//
