YJH0_YEAST
ID YJH0_YEAST Reviewed; 888 AA.
AC P40361; D6VWB3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inactive deaminase YJL070C;
GN OrderedLocusNames=YJL070C; ORFNames=HRD888, J1095;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Sor F.J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-41, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-41, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-41; SER-178 AND
RP SER-180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- MISCELLANEOUS: Present with 1100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved His residues essential for binding the
CC catalytic zinc ion. Lacks the conserved residues important for
CC substrate binding and catalysis. Its enzyme activity is therefore
CC unsure. {ECO:0000305}.
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DR EMBL; X88851; CAA61309.1; -; Genomic_DNA.
DR EMBL; Z34288; CAA84052.1; -; Genomic_DNA.
DR EMBL; Z49345; CAA89362.1; -; Genomic_DNA.
DR EMBL; Z49344; CAA89361.1; -; Genomic_DNA.
DR EMBL; AY692645; AAT92664.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08729.1; -; Genomic_DNA.
DR PIR; S50801; S50801.
DR RefSeq; NP_012465.3; NM_001181503.3.
DR AlphaFoldDB; P40361; -.
DR SMR; P40361; -.
DR BioGRID; 33685; 152.
DR DIP; DIP-5674N; -.
DR IntAct; P40361; 3.
DR MINT; P40361; -.
DR STRING; 4932.YJL070C; -.
DR iPTMnet; P40361; -.
DR MaxQB; P40361; -.
DR PaxDb; P40361; -.
DR PRIDE; P40361; -.
DR EnsemblFungi; YJL070C_mRNA; YJL070C; YJL070C.
DR GeneID; 853375; -.
DR KEGG; sce:YJL070C; -.
DR SGD; S000003606; YJL070C.
DR VEuPathDB; FungiDB:YJL070C; -.
DR eggNOG; KOG1096; Eukaryota.
DR GeneTree; ENSGT00950000183011; -.
DR HOGENOM; CLU_003782_2_0_1; -.
DR InParanoid; P40361; -.
DR OMA; SYNIRWN; -.
DR BioCyc; YEAST:G3O-31529-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-74217; Purine salvage.
DR PRO; PR:P40361; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40361; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; IEA:UniProt.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF19326; AMP_deaminase; 2.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..888
FT /note="Inactive deaminase YJL070C"
FT /id="PRO_0000194416"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 888 AA; 104264 MW; DB31A8086224114D CRC64;
MQAVERRPSL LFDEYQNSVT KPNETKNKEA RVLSENDGDV SPSVLKQKEI SVDDMDMISL
PTEFDRQMVL GSPMFFDLED EENKIDPLPS VSHHYGNGES DSFVSSYTPS NLKTGEETKD
LFINPFELVS QMRKRYIAAS KQDGISNIKN DTEKWFLYPK PLPKFWRFED DKRFQDPSDS
DLNDDGDSTG TGAATPHRHG YYYPSYFTDH YYYYTKSGLK GKGNIKVPYT GEYFDLEDYK
KQYIYHLSNQ ENTQNPLSPY SSKEESLEEE FLTDVPTFQE FRDDFAYIIE LIQSHKFNEV
SRKRLSYLLD KFELFQYLNS KKEILANKNV PYRDFYNSRK VDRDLSLSGC ISQRQLSEYI
WEKINLEPER IVYQDPETSR KLSLRDIFQF GCSSNDQPIA IGLKLIDDEF LDWYRNIYLI
DYHLTPNKVA KLVGKEMRFY LLAKVFLEFD NFIEGEYLAE IFIKYVIHIL EKSKYQLAQV
SVNFQFYSSG EDWYKKFSQW LLRWKLVSYN IRWNIQIARI FPKLFKENVV SNFQEFLDLI
FNPLFTLEKE QLPIDSSVNT DIIGLQFFLS NVCSMDLVIK ESDEYYWKEF TDMNCKPKFW
TAQGDNPTVA HYMYYIYKSL AKVNFLRSQN LQNTITLRNY CSPLSSRTSQ FGVDLYFTDQ
VESLVCNLLL CNGGLLQVEP LWDTATMIQY LFYLFQIPIL AAPLSSVSLL NSQKSTFLKN
KNVLLEHDYL KDQETAKINP SRDITVGEQR SYETNPFMKM FKMGLKISLS SKSILYNSSY
TLEPLIEEYS VAASIYLLNP TDLCELSRTS VLSSGYEGWY KAHWIGVGVK KAPYFEENVG
GIDNWYDTAK DTSIKHNVPM IRRRYRKETL DQEWNFVRDH FGVINSIW
