ID F0XHH5_GROCL Unreviewed; 928 AA.
AC F0XHH5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=CMQ_2943 {ECO:0000313|EMBL:EFX03014.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX03014.1, 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 S9C family.
CC {ECO:0000256|ARBA:ARBA00010040}.
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DR EMBL; GL629769; EFX03014.1; -; Genomic_DNA.
DR RefSeq; XP_014172496.1; XM_014317021.1.
DR AlphaFoldDB; F0XHH5; -.
DR STRING; 655863.F0XHH5; -.
DR GeneID; 25975988; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR InParanoid; F0XHH5; -.
DR OrthoDB; 5471261at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR015418; Eaf6.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF09340; NuA4; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 729..896
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 104..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..48
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 104..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 100660 MW; B662D3BA8621638A CRC64;
MADKPHNTTG VVADVPGLPY YEKSRQHLKE LLQRRRQLER QLHTREESIL QKETDYLDNT
PSGNIIAGFD NYTKGTTGTA AARRKTGITE SNRVFSRSSI SYNTAAGNSG SSSSHPPTPL
QTSFKDGGIS SGPGSGQATP TSASAAKAPH GIKKKKGLTA TAAAAADDSE TDTPMVLKAT
KFTPEVLLSA PRRSAGAPNS TGKKVLYTVS TYSFREHRKA SQIRVLDVKS GESTVLYEDP
AYTEPVWIGS DEFLFLKAGD KGTTHLLLGD ASRPGSPPTG IRTFDGGLSN LKVLPLSDGA
IAIALTGLSD KTGLLFNPDS DAEKGKPTHT TARVYSKLFV RHWDAYVTEN RQTVWYGRLE
RTGENSAKTS GRYSLVSNGQ ANGLTNALAG TKLQSPVPPF GGSSDFALGP HGIAFVSRDP
AYNEAIYTVS NLYFIPIKTY AEPKPLAPPY AVKTGALAGY SAGPVFSPSG NSLVFSRMRS
HQYESDKPRL LLVPEIEKLG ADIIGKSDEF EFYETEDGVG AWDARPDAVA WSADGAELFV
TAEHHGRNAL YRLPSDPRHT TSFGAPQLLV GGHEVFEDEK IDASHDDSGS GVTGDESVGF
RRLGGHGSVS DVRLLASGID GDTRLFLSLN SLVDNSFFCI LDPEPTAVST SKFPRTILQA
VSSQSRHGSA FGLSPKQVGE IWYKGAGNYQ VQALVVRPSD FGAEKNKNRK WPLALLIHGG
PQGAWNNSWS TRWNPAVFAE QGYVVVAPNP TGSTGYGMAL QDGIRNQWGG LPYKDIVRAV
DYVEAVFPYV DISRAVALGA SYGGYMMNWI QGQPLGRRFK ALVNHDGVFS TLNQYSSEEL
FFPLHDFGGS LWDNRAGYER WDPAKFTDNW ATPTLWVLKP ENSLVWHKEV LTWINKYVGV
GDEFEKKANA ANLVGNMANL DLPQVERE
//
