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YMX7_YEAST
ID   YMX7_YEAST              Reviewed;         284 AA.
AC   Q04299; D6VZR0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable ADP-ribose 1''-phosphate phosphatase YML087W;
DE            EC=3.1.3.84;
GN   OrderedLocusNames=YMR087W; ORFNames=YM9582.12;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP-RIBOSE AND
RP   XYLITOL, SUBUNIT, AND PROBABLE FUNCTION.
RX   PubMed=15722447; DOI=10.1110/ps.041132005;
RA   Kumaran D., Eswaramoorthy S., Studier F.W., Swaminathan S.;
RT   "Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase),
RT   a ubiquitous cellular processing enzyme.";
RL   Protein Sci. 14:719-726(2005).
CC   -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC       ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC       tRNA splicing. + phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC         phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15722447}.
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DR   EMBL; Z49259; CAA89234.1; -; Genomic_DNA.
DR   EMBL; AY558403; AAS56729.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09984.1; -; Genomic_DNA.
DR   PIR; S54463; S54463.
DR   RefSeq; NP_013805.1; NM_001182587.1.
DR   PDB; 1NJR; X-ray; 1.90 A; A=1-284.
DR   PDB; 1TXZ; X-ray; 2.05 A; A=1-284.
DR   PDB; 1TY8; X-ray; 2.10 A; A=1-284.
DR   PDBsum; 1NJR; -.
DR   PDBsum; 1TXZ; -.
DR   PDBsum; 1TY8; -.
DR   AlphaFoldDB; Q04299; -.
DR   SMR; Q04299; -.
DR   BioGRID; 35262; 39.
DR   DIP; DIP-1320N; -.
DR   IntAct; Q04299; 1.
DR   MINT; Q04299; -.
DR   STRING; 4932.YMR087W; -.
DR   MaxQB; Q04299; -.
DR   PaxDb; Q04299; -.
DR   PRIDE; Q04299; -.
DR   EnsemblFungi; YMR087W_mRNA; YMR087W; YMR087W.
DR   GeneID; 855112; -.
DR   KEGG; sce:YMR087W; -.
DR   SGD; S000004693; YMR087W.
DR   VEuPathDB; FungiDB:YMR087W; -.
DR   eggNOG; ENOG502QVAE; Eukaryota.
DR   HOGENOM; CLU_093588_0_0_1; -.
DR   OMA; RYIIHCP; -.
DR   BioCyc; YEAST:G3O-32787-MON; -.
DR   EvolutionaryTrace; Q04299; -.
DR   PRO; PR:Q04299; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04299; protein.
DR   GO; GO:0016791; F:phosphatase activity; ISS:SGD.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; TAS:SGD.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR028071; Macro-like_dom.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   Pfam; PF14519; Macro_2; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Hydrolase; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Probable ADP-ribose 1''-phosphate phosphatase
FT                   YML087W"
FT                   /id="PRO_0000203285"
FT   DOMAIN          34..230
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="substrate"
FT   BINDING         55
FT                   /ligand="substrate"
FT   BINDING         80
FT                   /ligand="substrate"
FT   BINDING         90
FT                   /ligand="substrate"
FT   BINDING         148
FT                   /ligand="substrate"
FT   BINDING         195
FT                   /ligand="substrate"
FT   DISULFID        128..136
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           26..35
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           54..62
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           89..97
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           100..109
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           125..129
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          140..145
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           167..179
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:1TXZ"
FT   HELIX           202..217
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           224..234
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           245..254
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           258..262
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:1NJR"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:1NJR"
SQ   SEQUENCE   284 AA;  32067 MW;  A8584DBB7B4B0A6B CRC64;
     MTGSLNRHSL LNGVKKMRII LCDTNEVVTN LWQESIPHAY IQNDKYLCIH HGHLQSLMDS
     MRKGDAIHHG HSYAIVSPGN SYGYLGGGFD KALYNYFGGK PFETWFRNQL GGRYHTVGSA
     TVVDLQRCLE EKTIECRDGI RYIIHVPTVV APSAPIFNPQ NPLKTGFEPV FNAMWNALMH
     SPKDIDGLII PGLCTGYAGV PPIISCKSMA FALRLYMAGD HISKELKNVL IMYYLQYPFE
     PFFPESCKIE CQKLGIDIEM LKSFNVEKDA IELLIPRRIL TLDL
 
 
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