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Database: UniProt
Entry: V5GUV5_KALBG
LinkDB: V5GUV5_KALBG
Original site: V5GUV5_KALBG 
ID   V5GUV5_KALBG            Unreviewed;       398 AA.
AC   V5GUV5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Aspartyl protease {ECO:0000313|EMBL:EST09697.1};
GN   ORFNames=PSEUBRA_SCAF1g00135 {ECO:0000313|EMBL:EST09697.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09697.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KI545851; EST09697.1; -; Genomic_DNA.
DR   RefSeq; XP_016294686.1; XM_016435697.1.
DR   AlphaFoldDB; V5GUV5; -.
DR   STRING; 1365824.V5GUV5; -.
DR   GeneID; 27418326; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_1_4_1; -.
DR   OMA; SINQDFW; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
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   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EST09697.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..398
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004737539"
FT   DOMAIN          108..395
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          132..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   398 AA;  42104 MW;  0748B0B86909C765 CRC64;
     MQLKLSFVAG LIAASALATA APLEQQERGI NIDISKRAKL TVDGSSQIDW NKVDAHMASL
     RTKYAKSFAN YEKNTGKVHS LKRDLPEHLT KRATGSVALT DQEGGELWTG TMAYGTPSQS
     FPIDFDTGSS DTLVNPGAYT PSQSSTSKTN GDQFSTSYGD GTTASGTIYT DTVHIGGLNA
     ANTAIGVSNQ QFIDSSEGSQ GISGMAFPQL AAFGSNYLPY FYSLKQAGVV SSGKFQFDLR
     TSGSSLYLGG TNSAKYSSTP VYVGIDSNQG FWQVPATVNT QSIDSIVDTG TTIIVAPTSQ
     AKTLFKQLNL PTFTQDGSLY AYFNCNSPPK VTFKYGSYSK TLSAATTSFG TTNSGQCVLS
     VAGSDLGLNA WVTGDSFLQN VVAIFDTDNN RVGFANKA
//
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