HPM1_SCHPO
ID HPM1_SCHPO Reviewed; 339 AA.
AC Q9UTQ8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Histidine protein methyltransferase 1;
DE EC=2.1.1.85 {ECO:0000250|UniProtKB:P40481};
DE AltName: Full=Methyltransferase-like protein 18 homolog C1071.05;
GN ORFNames=SPAC1071.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Protein-histidine N-methyltransferase that mediates
CC methylation of target protein on His residues.
CC {ECO:0000250|UniProtKB:P40481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC Evidence={ECO:0000250|UniProtKB:P40481};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB59881.1; -; Genomic_DNA.
DR PIR; T37487; T37487.
DR RefSeq; NP_594355.1; NM_001019776.2.
DR AlphaFoldDB; Q9UTQ8; -.
DR BioGRID; 279391; 8.
DR STRING; 4896.SPAC1071.05.1; -.
DR iPTMnet; Q9UTQ8; -.
DR MaxQB; Q9UTQ8; -.
DR PaxDb; Q9UTQ8; -.
DR PRIDE; Q9UTQ8; -.
DR EnsemblFungi; SPAC1071.05.1; SPAC1071.05.1:pep; SPAC1071.05.
DR GeneID; 2542951; -.
DR KEGG; spo:SPAC1071.05; -.
DR PomBase; SPAC1071.05; -.
DR VEuPathDB; FungiDB:SPAC1071.05; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_038704_1_1_1; -.
DR InParanoid; Q9UTQ8; -.
DR OMA; WRTFLPL; -.
DR PhylomeDB; Q9UTQ8; -.
DR PRO; PR:Q9UTQ8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0042038; P:peptidyl-histidine methylation, to form tele-methylhistidine; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..339
FT /note="Histidine protein methyltransferase 1"
FT /id="PRO_0000339342"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 339 AA; 38247 MW; ABB17A062E1BA312 CRC64;
MQANGFSFGF YDEPNNLNGQ DVGADSLPSV AIESDSLGHM LKYIPEKLSY ARVSGLGHTF
VQRELWDVKM QLMEQDDSIE SDDKLKVLDG CNDLVPNVYE GGYKTWECSL DLANEIKKID
VVKNNLTTVL ELGCGSAIPI LSCFQEFYKH RIPCTLVFQD FNVDVLRYVT LPNLLLNWYF
CTQEHDSSEK HGTIDVSPSL LQEFSDDLAR TNIYCEFLCG CWSEEMQLLI QRTYGDHYFS
LVLASETIYS LPSLENFLYM LLKNTKNLAL VAGKDLYFGV GGSILEFNSR LQKLVDDPNS
LKAIKTSTQN VGRSIVYWEK EFPPSNIDSS PQSPLPGSL
