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Database: UniProt
Entry: A0A0L0G7G7_9EUKA
LinkDB: A0A0L0G7G7_9EUKA
Original site: A0A0L0G7G7_9EUKA 
ID   A0A0L0G7G7_9EUKA        Unreviewed;       538 AA.
AC   A0A0L0G7G7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN   ORFNames=SARC_02803 {ECO:0000313|EMBL:KNC84982.1};
OS   Sphaeroforma arctica JP610.
OC   Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX   NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC84982.1, ECO:0000313|Proteomes:UP000054560};
RN   [1] {ECO:0000313|EMBL:KNC84982.1, ECO:0000313|Proteomes:UP000054560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP610 {ECO:0000313|EMBL:KNC84982.1,
RC   ECO:0000313|Proteomes:UP000054560};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA   King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Sphaeroforma arctica JP610.";
RL   Submitted (FEB-2011) 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; KQ241727; KNC84982.1; -; Genomic_DNA.
DR   RefSeq; XP_014158884.1; XM_014303409.1.
DR   AlphaFoldDB; A0A0L0G7G7; -.
DR   STRING; 667725.A0A0L0G7G7; -.
DR   EnsemblProtists; KNC84982; KNC84982; SARC_02803.
DR   GeneID; 25903307; -.
DR   eggNOG; KOG0822; Eukaryota.
DR   OrthoDB; 5489665at2759; -.
DR   Proteomes; UP000054560; 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; 2.
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; 3.
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:UP000054560};
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          112..224
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          241..400
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          399..536
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        375
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        384
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         264
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         273..274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         359..360
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            267
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   538 AA;  61506 MW;  C6C1C9530BF6BB40 CRC64;
     MVKQASLGRI IQDDEDDNKV FSTFRRQEGL NFIVCPLTNE KWRKDVTTCI GEKREPPVLD
     RDHVRVIDVQ NNHHTVGMVS PFLALHSKSQ FVRESFQHVF NAAPTDTPID DDIEDFEAAE
     RPWRMWNQFR SLCDHSNKLN VCLELTEDLP CTGDALDRWM GEPVKAVALD TKLFMTDKEG
     NPVLSKAHEN VLRRFISFDA QILLTGQVQH SDGVEPYVHY LQMLNERTRT SPDFAEYEVW
     GNGYEDYLQA PLQPLMNNLE SGVYAVFEQD PVKYREYQEA VFRALCDRVP AEKKDEVTTV
     IMVVGAGRGP LVRMCLKASE RANRKVKMYA VEKNPNAIIT LQGWKADTWG DKVTLHAGDM
     RDFKPNEKCD ILVSELLGSF GDNELSPECL DGAQRYLKDD MPYVVLMHNH TRIAPSLPLF
     TFDHPNTAEA IDNRRYGSLT FSAEGDHQMH GIGGYFETTL YKDVTLSINP QTHSPGMFSW
     FPIYFPLPKP IDVRAGDSIT MHFWRCVDAK KVWYEWCVSS PSCTPIQNVA ARTYHIGL
//
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