ID A0A167M5U3_PHYB8 Unreviewed; 387 AA.
AC A0A167M5U3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Secreted aspartyl protease {ECO:0000313|EMBL:OAD71889.1};
GN ORFNames=PHYBLDRAFT_75110 {ECO:0000313|EMBL:OAD71889.1};
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:OAD71889.1, 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; KV440984; OAD71889.1; -; Genomic_DNA.
DR RefSeq; XP_018289929.1; XM_018443047.1.
DR AlphaFoldDB; A0A167M5U3; -.
DR STRING; 763407.A0A167M5U3; -.
DR GeneID; 29003953; -.
DR VEuPathDB; FungiDB:PHYBL_75110; -.
DR InParanoid; A0A167M5U3; -.
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 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:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:OAD71889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..387
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007890165"
FT DOMAIN 79..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 315..348
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 387 AA; 42179 MW; 8C482FCD8E10D63B CRC64;
MKIISCVAAI CLALSVNAAP TNTTTELPSF SLHSNHEFKF NATRGVLSAR TKYSRFIEGS
TSFSVGKVPL TDYLYDIMYY GNVTVGTPPQ LMRLVFDTGS SDLWTVSTSC DSCGSKQNKF
DPTLSNTYKT TEKSWEISYG DGSTASGLLG YDTVRLGDLA IKEQGIELAE FESPSFMYKP
IDGLLGLGFS SLNTLKNIAT PVDNLISQKI ISKPIFSTYY GKEASGGGGE IIFGDYNPKH
IDGPLTTIPV NNTQGFWGVN VKNVKVGKTS VVTAPFDAII DTGTTLLLFT DEVAHSIAAA
YNAIDRRDGT FIIDCDTTNL KPLHLTLGKR QFTIPVESLI FYNEPERCTA GFGYGGLPFA
ILGDTFIKNH YIIFNQEIPN VKIARSK
//