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
//