ID A0A162NB42_PHYB8 Unreviewed; 383 AA.
AC A0A162NB42;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Secreted aspartyl protease {ECO:0000313|EMBL:OAD67514.1};
GN ORFNames=PHYBLDRAFT_24046 {ECO:0000313|EMBL:OAD67514.1};
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:OAD67514.1, 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; KV440999; OAD67514.1; -; Genomic_DNA.
DR RefSeq; XP_018285554.1; XM_018439828.1.
DR AlphaFoldDB; A0A162NB42; -.
DR STRING; 763407.A0A162NB42; -.
DR GeneID; 29000734; -.
DR VEuPathDB; FungiDB:PHYBL_24046; -.
DR InParanoid; A0A162NB42; -.
DR OrthoDB; 1379710at2759; -.
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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:OAD67514.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..383
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007837650"
FT DOMAIN 77..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 383 AA; 41294 MW; 7E2B8D0FD4AFEB60 CRC64;
MKFFVGISAI SILALSTIDA SLVPDILGIA PKFLSITANP SFQANAANAL SRAKQKFSGS
SKSTSVTVVD YKNDVEYFGT IQVGTPPQDV IIDFDTGSSD LWFASTLCLL CDTHKNKFNA
FLSTSYKPSL KTWSISYGDG SFAGGNVGYD TVSVNGISVK EQAIQLAKFE SPSFKDSPVD
GILGLGFRSL SSAFGSNTVM DNMIEQHLIE KPIFSVYLGK SGEDPAGEFM FGDYNPDHIG
GRLTTVPVDS IDGLWKITVD EASVGFKTVD KFDAIIDTGT TLLVFTKDVA EQIAQFYDAT
EVGDGTYLID CDTSKFDPLV FTINGADFEI PPSELVFENK LVSCVASFTH GDSDFAILGD
VFLKSNYVIF NAEVPHVQIA PSR
//