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Database: UniProt
Entry: D8LQH7_ECTSI
LinkDB: D8LQH7_ECTSI
Original site: D8LQH7_ECTSI 
ID   D8LQH7_ECTSI            Unreviewed;       739 AA.
AC   D8LQH7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-NOV-2023, entry version 57.
DE   SubName: Full=Arginine-N-methyltransferase {ECO:0000313|EMBL:CBN78741.1};
GN   Name=SKB1 {ECO:0000313|EMBL:CBN78741.1};
GN   ORFNames=Esi_0006_0115 {ECO:0000313|EMBL:CBN78741.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN78741.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBN78741.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
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DR   EMBL; FN648818; CBN78741.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8LQH7; -.
DR   STRING; 2880.D8LQH7; -.
DR   EnsemblProtists; CBN78741; CBN78741; Esi_0006_0115.
DR   eggNOG; KOG0822; Eukaryota.
DR   InParanoid; D8LQH7; -.
DR   OMA; WEFSHPI; -.
DR   OrthoDB; 5489665at2759; -.
DR   Proteomes; UP000002630; Chromosome LG04.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; 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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01015}.
FT   DOMAIN          31..299
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          307..473
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          476..617
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   REGION          160..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  82450 MW;  1A1A9BB0D366F47A CRC64;
     MAEKGKLIIG FETNCVPDLN ALLDDARKDH FDFVAIPLVH PRFKRDALGV SSRREDPLTR
     SDFLLDSRQW SSLIVGKISE WLDMDSPCEE SAWASELAFK QEMAWATHLA LAAVIAPAPK
     PGRCSNYARC INQVAQELTY LAVWLRIPLV HPESLDPELN GTKGSAINGK GGSGGEGEGG
     DVGKVSTGGG TGAVEDPWET WNAIRVMCEH KSCLSVVLEM TADLPAQSIL DRWVGEPVKA
     VIVSTKVFLT NKKGFPTLSR RHQDFATAMI KQKVQFVVKG RSHHASGYLP YLQYLEHLRT
     RLPAPKEHEN FEAPYLDYLQ APLQPLMDNL ESQTYEAFEK DPVKYKQYER AIVKALELEK
     KKEGIDTTVL MVVGAGRGPL VQAALNAGAT AGRPLKVYAV EKNANAVITL RNRAIMDKWT
     NVTIVAKDMR EFAPEEKADI LVSELLGSWG DNELSPECLD GAQRFLKDGG VSIPQEYTSY
     VAPMSSHKLW REVSNFEELK RLETAYVVKL HNFVQLAEEK ACFTFHHPSE EVGGEVHNKR
     HVEVDFDVEQ ASTLHGFAGF FDSRLFADIH ISIVPSTFSE GMFSWFPLYI PLRTPVVLKP
     GDKVSAHFWR CTSSNKVVVR VGPHLPRPLT NTQSQRSILL DRPLACGTRR TSRVRLASWC
     GCRQCQRYVA SELFRFCLKQ RCCDFLGSQA VSRRPCLGMR PAVLPPFCGE ALDGVCVCTT
     RHPHSIWGTN SSCCQVCRH
//
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