ID   G2XHN2_VERDV            Unreviewed;       499 AA.
AC   G2XHN2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=VDAG_09786 {ECO:0000313|EMBL:EGY19326.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY19326.1};
RN   [1] {ECO:0000313|EMBL:EGY19326.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY19326.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
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, ECO:0000256|RuleBase:RU004386}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS572721; EGY19326.1; -; Genomic_DNA.
DR   RefSeq; XP_009652940.1; XM_009654645.1.
DR   AlphaFoldDB; G2XHN2; -.
DR   STRING; 498257.G2XHN2; -.
DR   EnsemblFungi; EGY19326; EGY19326; VDAG_09786.
DR   GeneID; 20711249; -.
DR   KEGG; vda:VDAG_09786; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   InParanoid; G2XHN2; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
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:SF3; ASPARTYL AMINOPEPTIDASE; 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:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   499 AA;  54444 MW;  C44C305C15A543F6 CRC64;
     MAPDKTALDF IDFVNASPTP YHACANAAAR LEKAGFSKIK ERDSWASTLR PGGKYYLTRN
     GSSIVAFAIG KKWRPGNPVG MIGAHTDSPC LRIKPVSKKG NNGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKDSTGTF TQKLIKVDKP LLRIPTLAIH LDRSSSFDPN KEVELFPIAG
     LASAELNKSA SETQVEGNEE TEEDFKPLRD LTERHHPHII DVIASHAEVD VSNVVDFELV
     LYDTQPACLG GLNDEFVFSP RLDNLGMTYC SIMGLITSLR DSAALDEDHT IRLVTCFDHE
     EIGSTSAQGA NSNLLPAILR RLSVLPAGRS DTASDASYDS VNDALPHLEE SIQSTAYEQT
     LSRSFLVSAD MAHSVHPNYA GKYEASHQPA MNGGTVIKIN ANQRYATNSP GIVLLQESAR
     HAGVPLQLFV VRNDSPCGST IGPMLSAKLG VRTLDLGNPQ LSMHSIRETG GSKDVEFAVR
     LFESFYERYG ELEEKILVD
//