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Database: UniProt
Entry: A0A162ZK79_PHYB8
LinkDB: A0A162ZK79_PHYB8
Original site: A0A162ZK79_PHYB8 
ID   A0A162ZK79_PHYB8        Unreviewed;       405 AA.
AC   A0A162ZK79;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Secreted aspartyl protease {ECO:0000313|EMBL:OAD67371.1};
GN   ORFNames=PHYBLDRAFT_63629 {ECO:0000313|EMBL:OAD67371.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD67371.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KV441024; OAD67371.1; -; Genomic_DNA.
DR   RefSeq; XP_018285411.1; XM_018441150.1.
DR   AlphaFoldDB; A0A162ZK79; -.
DR   STRING; 763407.A0A162ZK79; -.
DR   GeneID; 29002056; -.
DR   VEuPathDB; FungiDB:PHYBL_63629; -.
DR   InParanoid; A0A162ZK79; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000077315; 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:SF51; NAPSIN-A; 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:OAD67371.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007841278"
FT   DOMAIN          45..402
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   405 AA;  44752 MW;  FE3F16970B241AA9 CRC64;
     MVNIHVFCSL FVAATLATTV ATKLLSVPFL AVDRKNSGVT IWGRQRMGNT IGSFLENVDL
     AYLIDVSFGS STTWVPTKGC GRYCGYPSHT LNISDSSTFR PSQLVFNIRY GDGFSNGYYA
     KDTMSLNGVS IPNVHFGVSD FNDGELTMDG ADGIMGIGKR QKYPVLLYMF WKLVYSINNS
     PFTGPDNLTV YNNPYGVIVP TVVTTMHRQK IIDKSIFSIY FHPVDHQDQE IDRINGEITF
     GGVDMKRVDG NITYMPLTTN TDFQDYWAAN IDSISINGKN VSIDDGLSGL LDTGSTLVLL
     PEPVITGIFS IVRGTRRDYS GQYLVPCTSS DLPSVTLTMG GTDFTLEPKD YVITSGILEN
     GSNFCYTYFQ EAPPFVGAIL GYGFLQQFVS VYDNEYKRLG LVKRS
//
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