ID G0W518_NAUDC Unreviewed; 962 AA.
AC G0W518;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN Name=NDAI0A07520 {ECO:0000313|EMBL:CCD22906.1};
GN OrderedLocusNames=NDAI_0A07520 {ECO:0000313|EMBL:CCD22906.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22906.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22906.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000256|ARBA:ARBA00003273}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|ARBA:ARBA00010918, ECO:0000256|RuleBase:RU361240}.
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DR EMBL; HE580267; CCD22906.1; -; Genomic_DNA.
DR RefSeq; XP_003668149.1; XM_003668101.1.
DR AlphaFoldDB; G0W518; -.
DR STRING; 1071378.G0W518; -.
DR MEROPS; M28.A05; -.
DR GeneID; 11493761; -.
DR KEGG; ndi:NDAI_0A07520; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; TPWPVTI; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000000689; Chromosome 1.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF56; VACUOLAR MEMBRANE PROTEASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 139..326
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 556..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 109667 MW; 9C27614F3FC998F0 CRC64;
MQSSHNSMPT LKSIFRFRKT NVSFLFQITI CGIFLLYVYD QTRYKYTLPS QSEKVHQRLL
QTAWSDLQNI TLKPHPYTSR DNDRVHDYIL ERAMKITQKI EYANISDDYE TQTDTFFRQP
DVFNLSSTRT RVIYFQSSNI IVKLEGKDKA LPGLLLSSHF DSVPTSTGAT DDGKGIASLL
ALLEYFCQKQ PERTLIFNFN NNEEFGLLGA SVFFEHPWSK LVHYFLNLEG TGVGGKAVLF
RTSDVSTAQM YKEAVLKQPF GNSVYQQGFY NRYIHSETDY KVYEENGLRG WDIAFYKPRA
LYHTVNDSIS YTSREALWHM LHTSLQLSNY VAFNNEDPHA YTPAIYFDIV GYNFFVINSK
SLFALNCILL VAAPVIILVL QLLRSRKNSS TNRVSLLLAV RLPFSLAITC IILKITESAL
FQINPFISSR NHLSPLITFG AEFLFINYLL LTLFETLSPS SDFKRIALGE ILSILWVLLL
SLTYRMHKNE YRDTGIYPFT ILYVCILMGI LFDYFAKSLK QTPKVFFSRE VDGVSGSSNQ
ELHDGELEAA GAYTSDVERA SPTNSDNSSP HTANQTIPAF EPDERAPLLE TNAHYPVKEV
NTIPKKPTNY SWALQFLLTV PIGIFIMFNS FDLILDALNQ TSQESLKSTS DVLNISLLGG
ILVVLPVIPF VYKFNVVTAI ALFLTFSIGA IQIFFSSPFT IEAPLKVRFS QDLKWSNGAI
ESVVHISGRQ GFLEPLIHDL PSVKREYLAV DCEDKYDGNE VCSYSGELPN PIDTYNSNFT
IDKLFSIDVL KNDRNSKYKS PYEPINAEVL INVVENRACT ILFTNPLEDK SSPVKQIQIF
ADENNNTDVT DDKIIRWRDG IDELQLHKLD FEKKFYHIGI QWYPKILNDN ESNSDSPADI
DDNALNLRVI CYWGEYDSES IVNGKHKKKI PAYDELLTYA PLNYSISNLN KGLITMERSI
EL
//
