YFI6_YEAST
ID YFI6_YEAST Reviewed; 1233 AA.
AC P43597; D6VTP7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Uncharacterized protein YFR016C;
GN OrderedLocusNames=YFR016C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-861; SER-975 AND SER-1046,
RP AND 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-462; SER-523;
RP THR-861; SER-975; SER-1037 AND SER-1046, AND IDENTIFICATION BY MASS
RP 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 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D50617; BAA09255.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12457.1; -; Genomic_DNA.
DR PIR; S56271; S56271.
DR RefSeq; NP_116671.1; NM_001179981.1.
DR PDB; 6ABR; X-ray; 2.00 A; A/B=1110-1233.
DR PDB; 6ABS; X-ray; 2.20 A; A/B=1110-1233.
DR PDBsum; 6ABR; -.
DR PDBsum; 6ABS; -.
DR AlphaFoldDB; P43597; -.
DR SMR; P43597; -.
DR BioGRID; 31168; 48.
DR DIP; DIP-4195N; -.
DR IntAct; P43597; 12.
DR STRING; 4932.YFR016C; -.
DR iPTMnet; P43597; -.
DR MaxQB; P43597; -.
DR PaxDb; P43597; -.
DR PRIDE; P43597; -.
DR EnsemblFungi; YFR016C_mRNA; YFR016C; YFR016C.
DR GeneID; 850570; -.
DR KEGG; sce:YFR016C; -.
DR SGD; S000001912; YFR016C.
DR VEuPathDB; FungiDB:YFR016C; -.
DR eggNOG; KOG1181; Eukaryota.
DR HOGENOM; CLU_267481_0_0_1; -.
DR InParanoid; P43597; -.
DR OMA; KKPDEHE; -.
DR BioCyc; YEAST:G3O-30468-MON; -.
DR PRO; PR:P43597; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43597; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..1233
FT /note="Uncharacterized protein YFR016C"
FT /id="PRO_0000202686"
FT DOMAIN 1132..1233
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 1133..1139
FT /evidence="ECO:0007829|PDB:6ABS"
FT STRAND 1144..1148
FT /evidence="ECO:0007829|PDB:6ABR"
FT HELIX 1157..1170
FT /evidence="ECO:0007829|PDB:6ABR"
FT STRAND 1176..1179
FT /evidence="ECO:0007829|PDB:6ABR"
FT TURN 1180..1182
FT /evidence="ECO:0007829|PDB:6ABR"
FT HELIX 1184..1193
FT /evidence="ECO:0007829|PDB:6ABR"
FT STRAND 1201..1204
FT /evidence="ECO:0007829|PDB:6ABR"
FT TURN 1205..1207
FT /evidence="ECO:0007829|PDB:6ABR"
FT STRAND 1208..1212
FT /evidence="ECO:0007829|PDB:6ABR"
FT HELIX 1213..1219
FT /evidence="ECO:0007829|PDB:6ABR"
FT HELIX 1224..1228
FT /evidence="ECO:0007829|PDB:6ABR"
SQ SEQUENCE 1233 AA; 137698 MW; C8A7CD2C6F0892F6 CRC64;
MVESLTVENQ EHNVQPPSVT SAGDSYSTLA TDLPLPSTND IIESRDQLTE SDLDEAINAT
ENFAQELSSQ RKSSKLKGHK KKNQGQIKAN RDRDTIVKLS SSVGETEEAS TRDAISHDLE
RKDDVIEIAT DTINDATESP TQIPIDVNVV IKETSTNNVA EGTENVPPIK ESTGIEVGNS
PITRRKKNKK KKTTNRRGRN SSNPADTTDL SKQSTLDSIL VGIEEYLQED GSKNEDIKVN
IVQDEPVNVE KMDIRTRNES SDKTFDIDVP NKDNVDETSS KSENNINEEK AEHTLPREEN
EILNVNEGNA ASFKHQLEPH GLEAGDENGQ ASTKDVESES LTKNGFNFKE NESKHLKAGE
KQQTESDRDG ISPSVLAKNQ KETEIGKEDH VFEQKDKEDE KCRKELSVNH ENNMSHNFNA
AGSDSIIPPE TERETYDDET MGPTKRISDN EKNLQHGTND ISVEVEKEEE EEEEEEENST
FSKVKKENVT GEQEAVRNNE VSGTEEESTS KGEEIMGGDE KQSEAGEKSS IIEIEGSANS
AKISKDNLVL EDEAEAPTQE NKPTEVVGEI DIPDAPRDDV EIVEAVEKNI IPEDLEVAKE
DQEGEQVKLD EPVKAMKDDK IAMRGAESIS EDMKKKQEGT AELSNEKAKK EVDETARESA
EGVEVEKSKT PESPKVVKRC TSGRPEDLQI NERDPEVLKE DVRVPDEDVK PEIATTIENS
EEEDPKSQRV QISTEQAETT QKDMGDVGST TSFKEEEKPK RFEITQEGDK ITGKDTNHEH
GEATEAASEN SKASDVGTAE KYIEPSSESV KKDTEEDAEV ENSEKTEFIK VKAELENLDA
PKEAEVTAEL NKENEDVEVD TEEDAEVENS EKTEFIKVKA ELGNLDAPKE AEVTAELNKE
NEDVEVAATS KEDIETKCSE PAETPIEDGT CTEAEVSKKD AEAVTKEDEN MENSKIAEAL
KDVTGDQEID DINISDEFQR TVELPELEKQ DIKDNKGEDK ELEVEETEKE TSLPDLVVEE
NITEEKNEIK QEEEEVSQLD FNETESISKE APNNDENGFE DQSTRENPKK ASADDIFKDI
LDETNEFLEQ LKIVDDSELN ALLQSLDAKD STTQTTEQSK KNNDKPQDVI TTSEIRKLNE
KEPVYIYTSL AGGGFHMIPR TNRLSTILTA NRIPFTYRDL GTDDEARKVW KTFSKGRSLP
GVVRGHNDLI GNWEEIEEAN EDYKLRELIY DTI
