ID L1JQV0_GUITC Unreviewed; 604 AA.
AC L1JQV0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=GUITHDRAFT_159368 {ECO:0000313|EMBL:EKX50575.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX50575.1};
RN [1] {ECO:0000313|EMBL:EKX50575.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX50575.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX50575}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (MAR-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR EMBL; JH992978; EKX50575.1; -; Genomic_DNA.
DR RefSeq; XP_005837555.1; XM_005837498.1.
DR AlphaFoldDB; L1JQV0; -.
DR STRING; 905079.L1JQV0; -.
DR PaxDb; 55529-EKX50575; -.
DR EnsemblProtists; EKX50575; EKX50575; GUITHDRAFT_159368.
DR GeneID; 17307079; -.
DR KEGG; gtt:GUITHDRAFT_159368; -.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_3_0_1; -.
DR OMA; WEFSHPI; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000011087; 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:UP000011087};
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 30..259
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 267..436
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 439..602
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 406
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 415
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 303..304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 390..391
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 297
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 604 AA; 68880 MW; 653902D2DB11DD44 CRC64;
MQELRVGRIF SCATNAQQCI DVVSRNEMYF AVLPLVHPRA RREFSGRTER SEPFTRSDLT
LPSNIWSSNV IGSLSPWLNF DSPCHKVRMD SEQALKQEMA WAHHISCPAV IAPPPGRSCN
NYARCLYSQI AASGGTSIYV HMPLTWKDDP DSDKDPWETW NSVRMLCEHH FCLFVALEVT
SDLPTDETLT QWLCEPVKLL ILPTSIFLTN TSGFPVLSKR HQNFLRSFFW YNVEVAVSGR
PRHEGGLLVY SQYLQHLFSS RTPLSDSERF EQPYWDFLQI PLQPLADNLE SQTYEVFEKD
PVKYVNYEQA VYLALIDLQA NFGFRQDPFI VMVVGAGRGP LVRASLRASE RANIAIFVYA
LDKNPNAVVT LRNMRVTENW ADRVEVVQSD MRDFSPPVKA DILVSELLGS FGDNELSPEC
LDGAQRFLRP DTGISIPVSY TSWIAPISSS KLHQEVKAYN DVKHFETTYV VKMHTHKVLS
DAQECWTFSH PNREVPIDNS RQSRHRFQVK RSSCLHGFAG YFDALLYADV HISIYPETFS
TGMFSWFPLF FPIRTPMFVG KGEEIELQLS RCVGDKKVWY EWAVVAPSVG PVNNVNGRSF
SIGL
//
