ID F0XNX0_GROCL Unreviewed; 592 AA.
AC F0XNX0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EFX00447.1};
GN ORFNames=CMQ_7449 {ECO:0000313|EMBL:EFX00447.1};
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:EFX00447.1, 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 M18 family.
CC {ECO:0000256|ARBA:ARBA00008290}.
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DR EMBL; GL629801; EFX00447.1; -; Genomic_DNA.
DR RefSeq; XP_014169929.1; XM_014314454.1.
DR AlphaFoldDB; F0XNX0; -.
DR STRING; 655863.F0XNX0; -.
DR GeneID; 25980994; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_3_0_1; -.
DR InParanoid; F0XNX0; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF4; VACUOLAR AMINOPEPTIDASE 1; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EFX00447.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 63593 MW; E327CC74CC1A567C CRC64;
MAKITSTKLP IHYGLPPSKQ ANEPPQARST ASSGISCHDE VASEQGSDAS QPSQALRSIE
SQCFAITDMS QRPAAKNTIC ADCAYRMSLD EVKQCRVFFG GEKAVMDSQE CVICSWKTGN
PAAFTWPYLN FMTENPTIFH AVDYFKQILR VAGFEELTAR EDWSARLRPG GKYYVTRNGS
TLAAFTIGGA YRPGNGVAIV AGHIDALTAK LKPVSNKPDR AGYVQLGVAP YAGALNETWW
DRDLGIGGRV VVRDPETGWT TTRLVKLDWP IAKIPTLAPH FGVSMTGQGN KETQLVPVIG
LDSGSKTGSM AEQARTVEPA LGPAGSFIAS QPPKLVKLIA AELGVKSYAS IVNWELELFD
TQPATVFGLD KEMISAGRID DKICSWAALV ALLRARDNDS SGVVRLVALF DDEEIGSLLR
QGAKSNFLPL TVERIVEALS PPIVGSFGPG VIGRTYASSF LISSDVTHAI HPNFVANYLD
DHAPKLNVGV AITHDSNGHM TTDSVSTAQL QRVAELSGST LQRFMIRNDS RSGGTIGPSL
SSAMGVKSAD AGIPQLSMHS IRASTGALDP GLGVRFFQGF LENWETVDAE WQ
//