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Database: UniProt
Entry: A0A099NZ29_PICKU
LinkDB: A0A099NZ29_PICKU
Original site: A0A099NZ29_PICKU 
ID   A0A099NZ29_PICKU        Unreviewed;       578 AA.
AC   A0A099NZ29;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=JL09_g3650 {ECO:0000313|EMBL:KGK37177.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK37177.1, ECO:0000313|Proteomes:UP000029867};
RN   [1] {ECO:0000313|Proteomes:UP000029867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX   PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL   Microb. Cell Fact. 13:121-121(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGK37177.1}.
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DR   EMBL; JQFK01000042; KGK37177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099NZ29; -.
DR   VEuPathDB; FungiDB:C5L36_0E02560; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_420369_0_0_1; -.
DR   Proteomes; UP000029867; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965:SF12; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..578
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001959358"
FT   DOMAIN          72..505
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   578 AA;  64956 MW;  94A50B7CD5813023 CRC64;
     MVLHKLITIV LYLLIVKASY LSLPISKKSY STEEGIISKQ RPHRLIKNRK AVLKRNVSGE
     LETTIRFDQT FVEVHLRIGS NRDPVTLLLD TASSDLVVNS SDNEFCISDG PDPESSFDTS
     VNSLAFYKRE EAVSCPIPNS RTKIRKKSTT TVSENFKYKT ESVIDQHLMQ HSSNIAVSSA
     PPYPKIKNYS STPDSSFIQN HANYLMETTN CPHFGMYNPY NSTSFYNLTT PLDIQYLDGS
     AYSGFYGTDD VYFADTKISE VQFGLNVETD KEWGTLGIGF GSNENTAQDG LKEYDNFPKK
     LKREAIIKKQ VFSIYAPYNS APQSLIFGGY DRNGYIQESG LTLVPIIDYS PRDKKGSGPF
     YLSITINSIS FSYGNLKQKE EVAKGNAVTI LDTGSTSSIF PDYIIAQLVI KYSFQWSSQL
     NCYVIQEKEI PKDDFYVTFD FQNALIKVPL IDFTYPVIDG DTLSPTGMRS LQVTSSDSDL
     LVLGDDILQN VFFIVDMEDL NIALGQINPD KTSENIVVVR DKIVDAIKSN EWDNVWGYNG
     CRKLELINIS GSRTPEEYHS DKNISLYFPG LTGNGFSW
//
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