(data stored in ACNUC9543 zone)

SWISSPROT: Q4N9L4_THEPA

ID   Q4N9L4_THEPA            Unreviewed;       702 AA.
AC   Q4N9L4;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN   OrderedLocusNames=TP01_0100 {ECO:0000313|EMBL:EAN33344.1};
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN33344.1, ECO:0000313|Proteomes:UP000001949};
RN   [1] {ECO:0000313|EMBL:EAN33344.1, ECO:0000313|Proteomes:UP000001949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga {ECO:0000313|EMBL:EAN33344.1,
RC   ECO:0000313|Proteomes:UP000001949};
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M.,
RA   Hall N., Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M.,
RA   Sato S., Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J.,
RA   Jiang L., Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D.,
RA   Crabtree J., Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C.,
RA   Suh B., Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M.,
RA   Allen J., Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R.,
RA   Fitzhugh H.A., Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAN33344.1}.
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DR   EMBL; AAGK01000001; EAN33344.1; -; Genomic_DNA.
DR   RefSeq; XP_765627.1; XM_760534.1.
DR   STRING; 5875.XP_765627.1; -.
DR   EnsemblProtists; EAN33344; EAN33344; TP01_0100.
DR   GeneID; 3503195; -.
DR   KEGG; tpv:TP01_0100; -.
DR   EuPathDB; PiroplasmaDB:TP01_0100; -.
DR   eggNOG; KOG0822; Eukaryota.
DR   eggNOG; ENOG410XNZM; LUCA.
DR   HOGENOM; HOG000135868; -.
DR   InParanoid; Q4N9L4; -.
DR   KO; K02516; -.
DR   OMA; NMDQIYV; -.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
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.
DR   PANTHER; PTHR10738; PTHR10738; 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; SSF53335; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4N9L4.
DR   SWISS-2DPAGE; Q4N9L4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001949};
KW   Kinase {ECO:0000313|EMBL:EAN33344.1};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR015894, ECO:0000256|PROSITE-
KW   ProRule:PRU01015, ECO:0000256|SAAS:SAAS00496483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR015894,
KW   ECO:0000256|PIRSR:PIRSR015894-2, ECO:0000256|PROSITE-ProRule:PRU01015,
KW   ECO:0000256|SAAS:SAAS00419651};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015894, ECO:0000256|PROSITE-
KW   ProRule:PRU01015, ECO:0000256|SAAS:SAAS00419659}.
FT   DOMAIN       40    329       PRMT5_TIM. {ECO:0000259|Pfam:PF17285}.
FT   DOMAIN      337    514       PRMT5. {ECO:0000259|Pfam:PF05185}.
FT   DOMAIN      531    699       PRMT5_C. {ECO:0000259|Pfam:PF17286}.
FT   REGION      373    374       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR015894-2}.
FT   REGION      467    468       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR015894-2}.
FT   ACT_SITE    493    493       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR015894-1}.
FT   ACT_SITE    502    502       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR015894-1}.
FT   BINDING     364    364       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR015894-2}.
FT   SITE        367    367       Critical for specifying symmetric
FT                                addition of methyl groups.
FT                                {ECO:0000256|PIRSR:PIRSR015894-3}.
SQ   SEQUENCE   702 AA;  80506 MW;  CA4347A5C8DF631B CRC64;
     MPKIESSGAL RNPLLFGWKI DDPNNDNLLG CVKLIESLGI SFLVLDLNTL SAKLGSNGAF
     QHLNHVDNSE FCHSEEFKLL IGFSPLGKSD LALPNELWSQ RIVSFIQTSD FKVLKTQIEW
     SCYVSSRFIM IDLESVLSNS PIDMVNSVPG KTSNSPNHSN LESDSYELMD KLVLFCQILS
     SYLTQPNLPT VCISLDCCKD SLNTWNMIYE LCGYSDKVKV CLKLQPVETD IEMWLSEPVK
     CVVLSEDTFL SNKRVMLNKS VSNQLSVLMK NNVKIVLDSN LNYNSLISND CFIQNNNDSG
     NFVEEVVMRD FESEIDVKDV LKAVKRCYSR IGPLTINELY GRGYEDLLQV PLQPLRDNLD
     SSTYNEFEKC SFKYNCYDQA ISSFITTKHG ELNQPNNLNS NINYSVYVLG AGRGPLVEVV
     MDVFRRNHIP TSDFVVYALD KNPYTMLTLD HKAQSNRWAN VRLICKDMRE LNKSMFQSNG
     NSGSKPVHLV VSELLGPFGD NELAPECLHG FERSFNLLFN NRVRLEFIPS SYTSYVMPLH
     CPQIWAKIKS FGNTKNFHMP YTVYLKAYYN VGTMHMDCFK FEHPDTQPPK REQIRDLERY
     KVMKFIARSD CYVHGFGAYF KCTLFDKVEI SILPRDSENV KSWFPMFFPI EIPFPVKKSQ
     VITLHIWRKV NDLKVWYEWA FTTPYTTAIH NVNGHSYSIS KC
//

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