ID G3ARY6_SPAPN Unreviewed; 460 AA.
AC G3ARY6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 50.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SPAPADRAFT_51807 {ECO:0000313|EMBL:EGW31835.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31835.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; GL996503; EGW31835.1; -; Genomic_DNA.
DR RefSeq; XP_007376613.1; XM_007376551.1.
DR AlphaFoldDB; G3ARY6; -.
DR GeneID; 18871597; -.
DR KEGG; spaa:SPAPADRAFT_51807; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_034490_0_0_1; -.
DR InParanoid; G3ARY6; -.
DR OMA; SKSCLAH; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-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 Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..460
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003442331"
FT DOMAIN 78..418
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 460 AA; 50227 MW; E56B41987208DCE0 CRC64;
MRITCIVAVL VHFFLITHAL LPVKDFRVKG LANEIQGVKS RAVVNSWSEQ VLSYSPDVVF
TSLNNTQVLY TDDTNSIYYI YLILDDGHGY KQRFPLLLDT GSAVSWIYNQ SCTSNSCQNN
NVTKFNYNGN LKLGSTFSIT YTNDQVDGTY ISIAENNINM QLGRVTSDFK VQDFSLGLTS
DSPSIFNGFS VSGILGITTD SSDENIVSQM YDSGLINKKV FGLYLTNPGQ IYRGNVPAKE
LGGVVLFGQD VADNTKKFIG SNTVNYVDVV DNNNNYWLIN ISDTSVVSSQ GESSNVISDS
RLTIIDSGTT GIVFPFDDAV AIHKQLFGDT GYLNDQNGNF AFLCNYTNEN IVFNVGGTKL
SVSSSNFKGQ AYTDPSLFGY CASKIQGLNN YGHWVLGQAF LKSFYTVFDL DANQIGFGQA
SLQSFGIEFG NESSSSASSS VLSTTCVETS TKSVLTTITH
//