ID F0XR37_GROCL Unreviewed; 529 AA.
AC F0XR37;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:EFW99931.1};
GN ORFNames=CMQ_249 {ECO:0000313|EMBL:EFW99931.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW99931.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; GL629807; EFW99931.1; -; Genomic_DNA.
DR RefSeq; XP_014169346.1; XM_014313871.1.
DR AlphaFoldDB; F0XR37; -.
DR STRING; 655863.F0XR37; -.
DR MEROPS; A01.082; -.
DR GeneID; 25975484; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR InParanoid; F0XR37; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..529
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003264077"
FT DOMAIN 72..422
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 268..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 352..385
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 529 AA; 54506 MW; 549550FDB6BC619A CRC64;
MARLSSALVL LAAGVAAASP TKAVKVAPTT VSGTADMHDG CIHMQIVHST NTNYFGKRAV
ELALANRSDV AYYAKLSFGT PAQPQFVQLD TGSFELWLNP TCDGLSLSDA SFCEAVGNFN
TSNSSTITPL NETKVLQYGI GSANISYVRD SIGLPGTTSV LKQVQFGVAS STSDEFAGIL
GIGFGQGLTT NYANFVDELT DQNITQVRAF SLALGSKDEQ EGVVVFGGVD TSKFSGTLAR
VPIIPAAQSP DGVPRYWVNM SSVSLTAGKN TESTESTGSS KTTTKTATKT STSKATASTK
AVTSTYANSS MAVFLDSGST LTLLPAGLAD SIAADFGVVD GPSSSGFYYV DCSYASANGT
LNFAFPGVSI SVPFHELVRQ SGSQCMLGIQ ASSQFALLGD TFLRSAYVPV VIDQTDNDIW
MAQYTNCGST PAALATTQSL VALTGDCSPG ENIIVVTTTP SIPFFSPTTS SSATAITAVQ
TAKASASPSP STSSIKSAAA RTAPGILHSS AVLMLTSALL AVALVDQLL
//