ID D4ARW8_ARTBC Unreviewed; 512 AA.
AC D4ARW8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARB_06983 {ECO:0000313|EMBL:EFE34032.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE34032.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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, ECO:0000256|RuleBase:RU004386}.
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:EFE34032.1}.
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DR EMBL; ABSU01000007; EFE34032.1; -; Genomic_DNA.
DR RefSeq; XP_003014421.1; XM_003014375.1.
DR AlphaFoldDB; D4ARW8; -.
DR STRING; 663331.D4ARW8; -.
DR GeneID; 9520473; -.
DR KEGG; abe:ARB_06983; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_3_0_1; -.
DR OMA; LLDTHYY; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000008866; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 512 AA; 56000 MW; C274124677CF48FC CRC64;
MTKKVPSIAS FGSSSEYLSQ SQASLQYRPR ALDESIHHEH TEFNPGAYTR PFCEFMTKNP
TIFHAVNAFA EKLEAKGYIK LTEREPWCLA RGKKYYVTRN DSAIISFAIG KHYTPGNGMA
IVGGHVDALC TKLKPLPTVP NKAGYVQLGV APYAGAMNST WWDRDLGIGG RVLVRDPKTN
KVERRLVKLD WPIARIPTLA PHFGSAAVGP FNKETQMTPI IGVDNSDLFK GPELSTKDSY
GGDLGTDNFT STQPKGLVNA IAKQLDVDHS TIVNWELELF DIQPAQVGGL NKDLIFAGRI
DDKLCCYSAH EAVLASPDHM SSGIIKMVGM FDDEEIGSLL RGGANSNFMS SVMERITQSL
CRESYGPNIL SQTVANSFFV SSDVTHAVNP NFLNAYLENH SPRLNYGVAV STDPNGHMTT
EGVSTALFQR LAVKGGCKLQ VFQIRNDSRS GGTIGPMTSA RIGMRAIDVG IPQLSMHSIR
ATTGSLDPGL GVQMFKAFFD HFEEVDKEFA DF
//