ID A0A0L9UH67_PHAAN Unreviewed; 643 AA.
AC A0A0L9UH67;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=HKW66_Vig0099290 {ECO:0000313|EMBL:KAG2400217.1},
GN LR48_Vigan04g211000 {ECO:0000313|EMBL:KOM41912.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM41912.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM41912.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM41912.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2400217.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2400217.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR EMBL; JABFOF010000004; KAG2400217.1; -; Genomic_DNA.
DR EMBL; CM003374; KOM41912.1; -; Genomic_DNA.
DR RefSeq; XP_017419811.1; XM_017564322.1.
DR AlphaFoldDB; A0A0L9UH67; -.
DR STRING; 3914.A0A0L9UH67; -.
DR EnsemblPlants; KOM41912; KOM41912; LR48_Vigan04g211000.
DR GeneID; 108329933; -.
DR Gramene; KOM41912; KOM41912; LR48_Vigan04g211000.
DR KEGG; var:108329933; -.
DR OMA; WEFSHPI; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000053144; Chromosome 4.
DR Proteomes; UP000743370; 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:UP000053144};
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 39..297
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 303..472
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 475..641
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 443
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 452
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 331
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 340..341
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 427..428
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 334
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 643 AA; 71969 MW; 6094DB21698A8500 CRC64;
MPLGERSGDK SESRYCGVET DFNDDMPHVL HFNLYSGSFD FVVAPLMDPS YRPSLMQKDV
LGSGVLPFAG SDLVLSPSQW SSHVVGKISS WIDLDSEDET LRIDSETTLK QEVAWASHLS
LQACLLPAPK GTSCANYARC VNQILQGANN IQLWLRIPLV KPDVDSMDEK SVTLDDSWES
WNSFRLLCEH HSQLSVALDI LSTLPSTNSL GRWFGEPVRA AILNTDCFLT NSHGCPCLSK
RHQRLISGFF NHSIQIIISG NSVHPKASMD ANETSDINSQ RHPLRPYLDY VGYLYQRMDP
LPEQERFELG YRDFLQSPLQ PLMDNLEAQT YETFEKDAVK YVQYQRAVSK ALLDRVPDEE
ASAKIIVLMV VGAGRGPLVR ASLQAAEETG RRLKVYAVEK NPNAVVTLHA LVKLEGWEDI
VTIVSSDMRH WNATEKADIL VSELLGSFGD NELSPECLDG AQRFLKQDGI SIPSSYTSFL
QPVTASKLYN DVKAHKDLVH FETAYVVKLH NVARLSPSQP VFTFTHPKRS ENESNQRYKK
LSFEIPSDTG SAMIHGFAGY FDATLYKDVH LGIEPSTATP NMFSWFSIFF PLRAPICVGP
GSTLEVHFWR CCGSTKVWYE WGVTSPSSSP IHNSNGRSYW VGL
//
