ID   ANM9_XENLA              Reviewed;         827 AA.
AC   A0JMU5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Protein arginine N-methyltransferase 9;
DE   AltName: Full=Protein arginine N-methyltransferase 10;
DE            EC=2.1.1.320 {ECO:0000250|UniProtKB:Q6P2P2};
GN   Name=prmt9; Synonyms=prmt10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC       formation of omega-N monomethylarginine (MMA) and symmetrical
CC       dimethylarginine (sDMA). {ECO:0000250|UniProtKB:Q6P2P2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC         Evidence={ECO:0000250|UniProtKB:Q6P2P2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P2P2}.
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; BC126010; AAI26011.1; -; mRNA.
DR   RefSeq; NP_001090430.1; NM_001096961.1.
DR   RefSeq; XP_018106530.1; XM_018251041.1.
DR   AlphaFoldDB; A0JMU5; -.
DR   SMR; A0JMU5; -.
DR   DNASU; 779342; -.
DR   GeneID; 779342; -.
DR   KEGG; xla:779342; -.
DR   CTD; 779342; -.
DR   Xenbase; XB-GENE-5998467; prmt9.L.
DR   OMA; QTCILES; -.
DR   OrthoDB; 519653at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 779342; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; ISS:UniProtKB.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11006; PTHR11006; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51678; SAM_MT_PRMT; 2.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; TPR repeat; Transferase.
FT   CHAIN           1..827
FT                   /note="Protein arginine N-methyltransferase 9"
FT                   /id="PRO_0000325931"
FT   REPEAT          54..87
FT                   /note="TPR 1"
FT   REPEAT          88..121
FT                   /note="TPR 2"
FT   DOMAIN          124..453
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          511..827
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   827 AA;  92178 MW;  46520E200D993B42 CRC64;
     MAGQAASKRR LISRSLQSAD ICLQHQDYGT AYAHLLLVLT LAPEQKEALK EMFQYSLFKW
     AEELYALNRS QDLFNCYEQA LELFPIDDVI CNSMGEHLFR LGFRDEAAGY FYKALKLNPS
     SAEAKENFYR VANWLIERWH FIMLNDTKRN LMYRAAIQNA IQNGCKTVLD IGTGTGILSM
     FAKKAGAPFV YACELSKTMY ELACEIVTAN QMDGHIKLLH MKSHDIQIPE HIPERVSLVV
     TETVDAGLFG EGIVETLIHA WKNLLLQPKP KDGRVEAYGK VIPSSAVIYG MAVECPEIRR
     HYSVGVTEVA GIKLGDAVKF CSPIHSSHGP DDVTEPYTTE KMSRVPGGYK ALSQPFQVMT
     VDFNSLQALE YIASGKSNRI SVPVYQQGQF DCFITWFALQ LDNEHSLSTE PSEETCWEQA
     VFPVQKLPDE GCLVNTGDTI VVDVSCPDCY LRLDLSTIVL SESSCDQTEN MVMGNETDIC
     DALANLHTTT NKGNMQELCI LEPGEIALLN NAVYHESFMA AISKVIGSLE LKESCSVVRN
     SQEQDVNFAQ PVSEDRLHVL DVSEGFSILP LIAAKLGKVK AFSSVEKEQH RVALEKLSVI
     NDLNNNESLE FCLSQLETDD GAAQKPKSDK MWSIIILDVI ETCGLIRQDL LEKAAIARCL
     LEPGGKIFPH AVVMQGMLIE SKTLLHEGSV QGNEPTLGFL IAPFINRFKV PAHVFLNLST
     VPCIPLSEQF ELLRLDLMNP CSNNQSSSVM RIKVNICRSG QVTAVTFWYH IHIDEAISLD
     TSSEASHWKQ AAYVLETPTC VLEGEELLLE VQFQNSSMSM KLTRPLQ