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Database: UniProt
Entry: R0FA85_9BRAS
LinkDB: R0FA85_9BRAS
Original site: R0FA85_9BRAS 
ID   R0FA85_9BRAS            Unreviewed;       642 AA.
AC   R0FA85;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN   ORFNames=CARUB_v10007189mg {ECO:0000313|EMBL:EOA18616.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA18616.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR   EMBL; KB870811; EOA18616.1; -; Genomic_DNA.
DR   RefSeq; XP_006285718.1; XM_006285656.1.
DR   AlphaFoldDB; R0FA85; -.
DR   STRING; 81985.R0FA85; -.
DR   GeneID; 17878662; -.
DR   KEGG; crb:17878662; -.
DR   eggNOG; KOG0822; Eukaryota.
DR   OrthoDB; 5489665at2759; -.
DR   Proteomes; UP000029121; 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:UP000029121};
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..296
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          303..471
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          474..640
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        442
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        451
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         339..340
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         426..427
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            333
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   642 AA;  71916 MW;  CB79FBA51DFDD2E3 CRC64;
     MPLGERAGWE RSESRYCGVE TDFSNDVTHL LNFNISTGGF DYVLAPLMNP SYRPSLVEGN
     GVDTQVLPVS GSDLVLSPSQ WSSHVVGKIS SWIDLDSEDE VLRMDSETTL KQEIAWATHL
     SLQACLLPTP KGKSCANYAR CVNQILQGLT TLQLWLRVPL VKSDGDSMDD TSEGRNDSWE
     LWNSFRLLCE HDSKLSVALD VLNTLPSETS LGRWMGESVR AAIVSTDSFL TNARGYPCLS
     KRHQKLIAGF FDHAAQVVIS GKPVHNLQKS HDSNTEGTEK HPLRTYLDYV AYLFQKMESL
     PEQERIELGY RDFLQAPLQP LMDNLEAQTY ETFERDSVKY IQYQRAVEKA LVDRVPDEKA
     SELTTVLMVV GAGRGPLVRA SLQAAEETGR KLKVYAVEKN PNAVVTLHSL VKMEGWEDIV
     TIISCDMRFW NAPEQADILV SELLGSFGDN ELSPECLDGA QRFLKPDGIS IPSSYTSFIQ
     PVTASKLYND VKAHKDLAHF ETAYVVKLHS VAKLAPSQSV FTFTHPNFST KANNQRYKKL
     QFNLPSNAGS ALVHGFAGYF DSVLYKDVHL GIEPTTATPN MFSWFPIFFP LRKPVEVHPD
     TPLEVHFWRC CGSSKVWYEW SVSSPTPSPM HNTNGRSYWV GL
//
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