ID A0A074ZDU2_AURSE Unreviewed; 758 AA.
AC A0A074ZDU2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=AUEXF2481DRAFT_106667 {ECO:0000313|EMBL:KEQ96841.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ96841.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ96841.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ96841.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL584755; KEQ96841.1; -; Genomic_DNA.
DR RefSeq; XP_013345563.1; XM_013490109.1.
DR AlphaFoldDB; A0A074ZDU2; -.
DR STRING; 1043005.A0A074ZDU2; -.
DR GeneID; 25361820; -.
DR HOGENOM; CLU_010247_2_1_1; -.
DR InParanoid; A0A074ZDU2; -.
DR OMA; WEFSHPI; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000030641; 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 Reference proteome {ECO:0000313|Proteomes:UP000030641};
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 42..358
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 368..539
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 542..755
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 309..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 509
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 518
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 393
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 402..403
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 458
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 487..488
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 396
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 758 AA; 84670 MW; 2DA109E0C9E88430 CRC64;
METLPGVTPQ EQQNTYFYIG QHETKRTVPV TTELGNQAQD AGYDMMTRPI TSPGFQAKVL
ALVDAYFEAV SASANADAIP YPLVAPLTPE DTNLVPDEYI STMICCTSTW IDLASPDPVI
AHVSRQVFNH EVAYAAFCGV NNIMIQGPDL EASSVISQYA RAIWNSLEAG PYINLQILLP
MQPAESKTAE DGLSLAGRAR DSFKTIKSMS TDALWSWDTW ELIRSTCKYH PRLTVALEVP
QKLPSSEIQS RWFSEPLRTL MLPESTFARN AKGFPVLNKP VQALLTRYMR LKTVPWIILS
DVGPIPGQNH PGMPVNLPDR SASPDLPTPA QSKRKQQTQT QKPKDLTPHL SYIRHLQRTQ
PPRPIIDRFA AGYQDFLQSP LQPLTDNLES ITYEVFEKDP IKYEWYERAV AAALKDLHKK
LQRPIVVAVV GAGRGPLVTR CLKASASTGI PVKQWAVEKN PNAYVLLQRR NATDPLWNKR
VTVVKTDMRA WKGPVIDSSP AKVDILVSEL LGSFADNELS PECLDGVQHV LHPEHGVSVP
ASYTAHFTPI AHPKIYADLL SRTDDQKWEL PYVTMLHQYD DLCIDPKTLQ PDIQTAWEFT
HPLPEAIIAQ SNLRRGGSVQ AGGGGMVGGD GWNEHNARFC RLRFTASSRG VCHGLGGYFE
TVLYSPENGS KKIELSINPN TMEDKSKDMI SWFPIFFPLK TPLYIPTASE IEVSMWRQTD
DRKVWYEWQI EVFASLGGSR QRIAASDLHS SIKNGCLM
//
