YFH6_YEAST
ID YFH6_YEAST Reviewed; 535 AA.
AC P43590; D6VTN6; Q66RB5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Uncharacterized peptidase YFR006W;
DE EC=3.4.-.-;
GN OrderedLocusNames=YFR006W;
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 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; D50617; BAA09245.1; -; Genomic_DNA.
DR EMBL; AY723803; AAU09720.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12446.1; -; Genomic_DNA.
DR PIR; S56261; S56261.
DR RefSeq; NP_116661.1; NM_001179971.1.
DR AlphaFoldDB; P43590; -.
DR SMR; P43590; -.
DR BioGRID; 31154; 110.
DR DIP; DIP-6829N; -.
DR IntAct; P43590; 1.
DR STRING; 4932.YFR006W; -.
DR MEROPS; M24.A09; -.
DR iPTMnet; P43590; -.
DR MaxQB; P43590; -.
DR PaxDb; P43590; -.
DR PRIDE; P43590; -.
DR EnsemblFungi; YFR006W_mRNA; YFR006W; YFR006W.
DR GeneID; 850556; -.
DR KEGG; sce:YFR006W; -.
DR SGD; S000001902; YFR006W.
DR VEuPathDB; FungiDB:YFR006W; -.
DR eggNOG; KOG2737; Eukaryota.
DR GeneTree; ENSGT00940000153657; -.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; P43590; -.
DR OMA; DQKFIYN; -.
DR BioCyc; YEAST:G3O-30459-MON; -.
DR PRO; PR:P43590; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43590; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Isopeptide bond; Manganese; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..535
FT /note="Uncharacterized peptidase YFR006W"
FT /id="PRO_0000185099"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 316
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 326
FT /note="S -> G (in Ref. 3; AAU09720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61754 MW; 4D251041CE9627FC CRC64;
MCLEPISLVV FGSLVFFFGL VKYFKRGERQ RTRGILQPEY KDKYYYSKEK GEEMGEVANV
NEIPVKIRNH KYPAKEHNLR VKDLLLNRNP KLSKISTAFF IAGEELEGNK YCDTNKDFRQ
NRYFYHLSGV DIPASAILFN CSTDKLTLFL PNIDEEDVIW SGMPLSLDEA MRVFDIDEAL
YISDLGKKFK ELQDFAIFTT DLDNVHDENI ARSLIPSDPN FFYAMDETRA IKDWYEIESI
RKACQISDKS HLAVMSALPI ELNELQIQAE FEYHATRQGG RSLGYDPICC SGPACGTLHY
VKNSEDIKGK HSILIDAGAE WRQYTSDITR CFPTSGKFTA EHREVYETVL DMQNQAMERI
KPGAKWDDLH ALTHKVLIKH FLSMGIFKKE FSEDEIFKRR ASCAFYPHGL GHMLGLDVHD
VGGNPNYDDP DPMFRYLRIR RPLKENMVIT NEPGCYFNQF LIKEFLEKHP ERLEVVDMSV
LKRYMYVGGV RIEDDILVTK DGYENLTGIT SDPDEIEKIV QKGLKKPRSG FHVIV
