ID   ANM1_CHLRE              Reviewed;         345 AA.
AC   A8IEF3; Q84X73;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01015};
GN   Name=PRMT1; ORFNames=CHLREDRAFT_205758 {ECO:0000312|EMBL:EDP05986.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12836870; DOI=10.1111/j.1550-7408.2003.tb00109.x;
RA   Li J.B., Lin S., Jia H., Wu H., Roe B.A., Kulp D., Stormo G.D.,
RA   Dutcher S.K.;
RT   "Analysis of Chlamydomonas reinhardtii genome structure using large-scale
RT   sequencing of regions on linkage groups I and III.";
RL   J. Eukaryot. Microbiol. 50:145-155(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503, and cw92;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=24152136; DOI=10.1021/bi4011623;
RA   Werner-Peterson R., Sloboda R.D.;
RT   "Methylation of structural components of the axoneme occurs during
RT   flagellar disassembly.";
RL   Biochemistry 52:8501-8509(2013).
CC   -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC       asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC       present in target proteins. Mediates asymmetric dimethylation of
CC       components of the axoneme during flagellum resorption, such as
CC       CCDC40/FAP172, CCDC65/FAP250, RSP1, RSP2, RPS5, RSP6, and tektin
CC       (PubMed:24152136). {ECO:0000305|PubMed:24152136}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24152136}. Cell
CC       projection, cilium, flagellum {ECO:0000269|PubMed:24152136}.
CC       Note=Localizes to the flagellum in a punctate pattern along the length
CC       of the axoneme. During resorption, localization is enhanced at the
CC       flagellar tip, the site of the disassembly of the flagellar axoneme.
CC       {ECO:0000269|PubMed:24152136}.
CC   -!- PTM: Phosphorylated during flagellum resorption.
CC       {ECO:0000269|PubMed:24152136}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR   EMBL; AY207498; AAO32621.1; -; Genomic_DNA.
DR   EMBL; DS496116; EDP05986.1; -; Genomic_DNA.
DR   RefSeq; XP_001703304.1; XM_001703252.1.
DR   AlphaFoldDB; A8IEF3; -.
DR   SMR; A8IEF3; -.
DR   STRING; 3055.EDP05986; -.
DR   PaxDb; A8IEF3; -.
DR   PRIDE; A8IEF3; -.
DR   EnsemblPlants; PNW85120; PNW85120; CHLRE_03g172550v5.
DR   GeneID; 5728909; -.
DR   Gramene; PNW85120; PNW85120; CHLRE_03g172550v5.
DR   KEGG; cre:CHLRE_03g172550v5; -.
DR   eggNOG; KOG1499; Eukaryota.
DR   HOGENOM; CLU_017375_1_2_1; -.
DR   InParanoid; A8IEF3; -.
DR   OrthoDB; 840669at2759; -.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Flagellum; Methyltransferase; Nucleus;
KW   Phosphoprotein; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..345
FT                   /note="Protein arginine N-methyltransferase 1"
FT                   /id="PRO_0000431955"
FT   DOMAIN          24..345
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         46
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   CONFLICT        120..122
FT                   /note="Missing (in Ref. 1; AAO32621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  38836 MW;  36E17566A4AD968E CRC64;
     MATAMDTGAG ASAPAVPQGD RTSADYYFDS YSHFGIHEEM LKDSVRTRTY MNAILNNAYL
     FKDKIVLDIG CGTGILSLFS AKAGAKHVYG IECSTIAEQA TQIVKDNKFD DRVTIIKGKV
     EEVTLPVDKV DIIISEWMGY FLFYESMLDT VIYARDKWLV PGGIIMPDKA TLSLCAIEDG
     EYKHDKIEFW DNVYGFNMSC IKQLAIAEPL VDIVEPDQIA STIQTVVSVD ISTMKKEDAT
     FTVPYELTMT RNDYVHALVG FFDVSFTRGH KPLSFTTSPR ARATHWKQTV FYLEDTLMAS
     KDETISGKLE CKPNAKNPRD LDISIAYEFE GERGQVKNTQ QYRMR