ID G0WE28_NAUDC Unreviewed; 590 AA.
AC G0WE28;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 2.
DT 03-MAY-2023, entry version 64.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=NDAI0G02620 {ECO:0000313|EMBL:CCD26039.2};
GN OrderedLocusNames=NDAI_0G02620 {ECO:0000313|EMBL:CCD26039.2};
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:CCD26039.2, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26039.2, 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; HE580273; CCD26039.2; -; Genomic_DNA.
DR RefSeq; XP_003671282.2; XM_003671234.2.
DR AlphaFoldDB; G0WE28; -.
DR STRING; 1071378.G0WE28; -.
DR MEROPS; A01.030; -.
DR GeneID; 11497435; -.
DR KEGG; ndi:NDAI_0G02620; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; IWGYDDV; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..590
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003411266"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..421
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 476..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 590 AA; 62404 MW; AAACC7BB6A6C2767 CRC64;
MTSRIISHIL LSLPYFISQA SASSKDNTSP PKYLALNFEK RYGDSFLNSS SSNGPSAQLI
KRDDGYEQVT LTNQQSFYSV EVEMGTPSQK LTVLLDTGSS DFWVTSSDNP YCGTTSTEGS
LYGGETQDTI DCSTYGTFDS SKSSTFQSND TDFLISYGDG SFAEGTWGTD VIKLDDSLSL
NDVSVAVASS TNSSMGVLGI GLRPLETTYS STKSVNEKTS YMYDNFPISL KKSGLIESTA
YSLYLNDPSS KSGNILFGGV DHSKYTGQLY TVPMLSSTTS YKTPVEFDVT LNGIGIIDSS
GNKKTLTATQ FYGLLDSGTT FSYLPSALVA MIGEELGASY DSNIGYYTID CSAEDSDDTK
IVFDMGGFHI NTTLSDFVIQ ISTSTCILSI VPQDGKVVLG DSFLNNAYIV YDLDNYEIAM
AQAAWDSTRE ANIDVISTTI PSAIRAPGYS STWSTSRSIS SGGDIFTTTE VTLSTSATSS
PESSASSVTS ASTLSSDSSA ASSYSRSTST LRSSSRSSSF VSSNNRATAS TSSSIRSSSS
SSSSSSSSSS SSSSSTGITS STNRTNSGIQ LAISPLLLAA VSMLSIFLFV
//