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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//