ID G0WGR7_NAUDC Unreviewed; 652 AA.
AC G0WGR7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=NDAI0J01030 {ECO:0000313|EMBL:CCD26995.1};
GN OrderedLocusNames=NDAI_0J01030 {ECO:0000313|EMBL:CCD26995.1};
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:CCD26995.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26995.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; HE580276; CCD26995.1; -; Genomic_DNA.
DR RefSeq; XP_003672238.1; XM_003672190.1.
DR AlphaFoldDB; G0WGR7; -.
DR STRING; 1071378.G0WGR7; -.
DR MEROPS; A01.031; -.
DR GeneID; 11494175; -.
DR KEGG; ndi:NDAI_0J01030; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; IWGYDDV; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000000689; Chromosome 10.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..652
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003411246"
FT DOMAIN 106..533
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 428
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 463..497
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 652 AA; 69692 MW; 00C9E0F0CB5AA467 CRC64;
MKIPSILRDT ILTTTSSLLL LSTIKNVIAT TSIPSQQEQN KKQGEASENQ PAPTLKYVKL
PFEKYTGDSF ESATRNNKPL NQLLKRDNED GAGYEDVKIT NQQSFYSVEL AIGTPPQHVT
VLVDTGSADL WVTGSMNPFC QSSLNSRNVV IKRDDDDDDD DDDDDTQQAA GMFTEILVTN
LSDLGNLSDL LGSFTIISTG IPGGIIPTGV TTATTTGGGG GAGGAGGLPT ATNDIPRSER
TLDCQEYGTF NSSRSSTFKN NYTSFSISYG DSTFASGTWA QDVLNLSDLN VTGLSFAVAN
MTNSTVGVLG IGLPALESTY SGASGATQRQ MYQYMNFPMV LKQSGAIHTT TYSLFLDDLD
ESHGSVLFGA IDHSKYTGQL YTVPMINIMR NSGYSNPIQF DVTLFGIGLQ NGERNLTLTT
TKLAALLDSG TTISYFPTSV VELVARQINA QYSARLGFYT VPCRSVSSNT NLVFDFGGFH
ISGPLQDFLI QTSQQTCILA MAPQESQHVI LGDIFLTHAY VVYDLDNYVI ALAQADTSTS
NQSSSSDIEL ITNSTIPRAI RAPLYSETWT ANRPVQSGGN IFAGNGTVIY NQGSGSMTTL
SGTAGAQQFT SSSTGSASSG TRRENEANAK VAKSYVGSTF ALLVTIFMVS LV
//
