GenomeNet

Database: UniProt
Entry: Q4WIX2_ASPFU
LinkDB: Q4WIX2_ASPFU
Original site: Q4WIX2_ASPFU 
ID   Q4WIX2_ASPFU            Unreviewed;       273 AA.
AC   Q4WIX2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Acetylornithine deacetylase (ArgE), putative {ECO:0000313|EMBL:EAL87133.1};
DE            EC=3.5.1.16 {ECO:0000313|EMBL:EAL87133.1};
GN   ORFNames=AFUA_2G00350 {ECO:0000313|EMBL:EAL87133.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL87133.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL87133.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL87133.1}.
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; AAHF01000008; EAL87133.1; -; Genomic_DNA.
DR   RefSeq; XP_749171.1; XM_744078.1.
DR   AlphaFoldDB; Q4WIX2; -.
DR   STRING; 330879.Q4WIX2; -.
DR   EnsemblFungi; EAL87133; EAL87133; AFUA_2G00350.
DR   GeneID; 3507236; -.
DR   KEGG; afm:AFUA_2G00350; -.
DR   VEuPathDB; FungiDB:Afu2g00350; -.
DR   HOGENOM; CLU_021802_2_0_1; -.
DR   InParanoid; Q4WIX2; -.
DR   OMA; CTITVEY; -.
DR   OrthoDB; 5487978at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000313|EMBL:EAL87133.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          66..172
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   273 AA;  28877 MW;  401E12DC022B02CA CRC64;
     MKGGLAAALA ALAAIKASGR TLRGDVIVAA VSDEEDASQG TRDIIAAGWR ADAAVVPEPT
     MGAIAIAHKG FVWVEVDILG VAAHGSDSQA GVDAILQAGW FLQSLEQYQK RLPIDDTLGQ
     ATLHCGLIKG GQEPSSYPQR CTITIEFRTI PAQSNESILE DVNALLSGIA KEKPRFRYAP
     PRLTISRPTQ KLSADHPLVQ TAVACATEVL VDGPGVISVP FWCDAALLSE AGVPAIVYGP
     SGAGLHSKEE WVEVDSLQEM SRVFEKLIQE LCA
//
DBGET integrated database retrieval system