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Database: UniProt
Entry: F0XCL9_GROCL
LinkDB: F0XCL9_GROCL
Original site: F0XCL9_GROCL 
ID   F0XCL9_GROCL            Unreviewed;       524 AA.
AC   F0XCL9;
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=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=CMQ_402 {ECO:0000313|EMBL:EFX03474.1};
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:EFX03474.1, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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DR   EMBL; GL629765; EFX03474.1; -; Genomic_DNA.
DR   RefSeq; XP_014172956.1; XM_014317481.1.
DR   AlphaFoldDB; F0XCL9; -.
DR   STRING; 655863.F0XCL9; -.
DR   MEROPS; M28.001; -.
DR   GeneID; 25977185; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_024336_0_1_1; -.
DR   InParanoid; F0XCL9; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03876; M28_SGAP_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:EFX03474.1}; Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           19..524
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005128767"
FT   DOMAIN          163..247
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          275..484
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   524 AA;  54897 MW;  DAD2B9A748F73B45 CRC64;
     MKGPLATALL LGSATALGFP SFENQQQPLA TTGDADLQVD DVEYKSKPLV DSASLQKTIN
     ADRLLGHAKA LFGIAQAGIP DYGHPTRVIG SAGHTGTLDY IYSIVSSLGG GKGGEGGYYR
     VWNQTFPAVT GKVYEARLVL NDSVPASAQA MSLTPPTHDN KPVFGALVLA TGTGCEASDY
     PAAVTGAITL VRRGDCPFGQ KSELAGAAGA VAVVVYNSED GPLSGTLGTP TATQVATFGL
     SGADAAPLVA ALKKGSSLDS IAYMDSVVST IHTTNILAQT VEGDPDNCVM LGGHSDSVPE
     GPGINDDGSG TLSLLEIATQ LTHYRVNNCV RFAWWAAEEE GLLGSDYYAA TLPPAENLKV
     RLFMDYDMLG SPNFAYQVYD ALDSENPAGS QALRDLYIDW YTAQGLNYSL IPFDGRSDYD
     GFIRAGIPAG GIATGAEGIK TKDEAALFGG TAGDWYDPCY HQLCDDVANV NLTAWELNTK
     LVAHSVATYA ISFDGFPKRT LDSVAAASST YGRGHKYHGG KLIM
//
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