ID W1QH16_OGAPD Unreviewed; 413 AA.
AC W1QH16;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Vacuolar aspartic protease {ECO:0000313|EMBL:ESW99655.1};
DE EC=3.4.23.- {ECO:0000313|EMBL:ESW99655.1};
GN ORFNames=HPODL_03532 {ECO:0000313|EMBL:ESW99655.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW99655.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW99655.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:ESW99655.1}.
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; AEOI02000007; ESW99655.1; -; Genomic_DNA.
DR RefSeq; XP_013935327.1; XM_014079852.1.
DR AlphaFoldDB; W1QH16; -.
DR SMR; W1QH16; -.
DR STRING; 871575.W1QH16; -.
DR MEROPS; A01.018; -.
DR GeneID; 25772970; -.
DR KEGG; opa:HPODL_03532; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000008673; Chromosome IV.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 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; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ESW99655.1};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ESW99655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..413
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004808325"
FT DOMAIN 99..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 130..135
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 336..369
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 413 AA; 44878 MW; 6069C4BC93E55AF5 CRC64;
MKLSFPTLYS LALVLGLVSL ADAKVHKAPI KKAPAQATYQ DVTVGDYVES LKQKYVTTYN
KFIAAQQNDQ QIISIGKRSD ESASSGHNTP LTNYLNAQYF TEIQLGTPGQ SFKVILDTGS
SNLWVPSSDC TSLACYLHTK YDHDESSTYQ KNGSSFAIQY GSGSLEGYVS QDTLTIGDLV
IPKQDFAEAT SEPGLAFAFG KFDGILGLAY DTISVNRIVP PIYNAINLGL LDTPQFGFYL
GDTSKSEQDG GEATFGGYDV SKYTGDITWL PVRRKAYWEV KFSGIALGDE YAPLENTGAA
IDTGTSLIAL PSQLAEILNS QIGAEKSWSG QYQIDCDKRD SLPDLTFNFD GYNFTISPYD
YTLEVSGSCI SAFTPMDLPA PIGPMAIIGD AFLRRYYSVY DLGRDAVGLA KAV
//
