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Database: UniProt
Entry: J9VUL8_CRYNH
LinkDB: J9VUL8_CRYNH
Original site: J9VUL8_CRYNH 
ID   J9VUL8_CRYNH            Unreviewed;       752 AA.
AC   J9VUL8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:AFR97111.2};
GN   ORFNames=CNAG_04380 {ECO:0000313|EMBL:AFR97111.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR97111.2, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR97111.2, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; CP003828; AFR97111.2; -; Genomic_DNA.
DR   RefSeq; XP_012051512.1; XM_012196122.1.
DR   AlphaFoldDB; J9VUL8; -.
DR   GeneID; 23887815; -.
DR   KEGG; cng:CNAG_04380; -.
DR   VEuPathDB; FungiDB:CNAG_04380; -.
DR   OrthoDB; 1696312at2759; -.
DR   Proteomes; UP000010091; Chromosome 9.
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:SF89; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 2.
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..752
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003828886"
FT   DOMAIN          119..608
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          26..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  78111 MW;  041BC1BB276B966B CRC64;
     MVNAHILTVL SILPLSLATL PEPDPHNGLS LEPAPAARQV TDTSVRPVKH DRGHGKQPIR
     KASARKRSAK RTPTAAATPF VGVGGIELDL VERENTNRGM VKRWDNGTLL PLGTSQNTFV
     VPVSIGSPPT TYPLQLDLAS SDILLASTLC GSHCPTSLGT TTNPYYDVSK PSAGFESINS
     NQTVWNTSYA DGTVASGFLA REIITLGQSV VQGQVFGMIN ATNLTLSSQK SSGILGLGFP
     RLSTLAHVLF EEQHEQASTI ASTSSSSSSV NGTTSTSVST LSNATGIMSA STASASGPTY
     LPTLLENLVR TPHLPYPVFA LALSAPIKSS SSSSSSSAAA SASSRYKPSI GSLTLGGLSS
     YYVDDTAGSG RTVGDIEWHD VVPFGQPVSA ANGTATTEEQ AVTTSASGGT LSASSTSENS
     TEEEAVSASS TFNNTARKRS DESQLDAFPS TVSELSQEEY LYWALDLQNV TVNGTDVGIN
     SSYASIGLGS VALLDAGFNG IAGPQQDVVN LFRLITDARK VSEGQWAVPC NTRMTLGFSF
     GGKYIQLQPS DWIYAGIAQS TMCLAWPIAQ PATGDGIDWQ LGTPFLKNVY TIFSYGINGK
     QAPLVGFLPL ESTTVANNST GDNTAADRNS PTPTSIAALS LTTTLRTALP NAVLPDPTFP
     TPTYAYSATP SLLQPGAPQY LGLANGSAYE VMDVPVISVD KSAVSSIAIG NNGGGSNVSD
     GPSSAAPRRM NTESVAGMGM MVIGMMVGVV MV
//
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