ID G3ATC3_SPAPN Unreviewed; 495 AA.
AC G3ATC3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=SPAPADRAFT_62787 {ECO:0000313|EMBL:EGW30886.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW30886.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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}.
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DR EMBL; GL996504; EGW30886.1; -; Genomic_DNA.
DR RefSeq; XP_007376919.1; XM_007376857.1.
DR AlphaFoldDB; G3ATC3; -.
DR STRING; 619300.G3ATC3; -.
DR GeneID; 18874465; -.
DR KEGG; spaa:SPAPADRAFT_62787; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; G3ATC3; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000000709; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 495 AA; 55208 MW; B6E5C3FC24B9FE84 CRC64;
MSTKDLTRAL KYAQEFVDFV NASPTPYHAV NTVKSHLAAA GFVELHERSN WFAQSNPVSR
GGKYYVTRNG SSLIAFTVGG KFQNGDGIAI VGAHTDSPCL RIKPISNKTS EGFIQVGVEQ
YGGLIAHSWF DRDLSIAGRV YVNEDGKYVP KLVKVDKPLL RIPTLAIHLD REVNTKFEFN
KETKLVPIAG QLALDKNEQE KEEKKKTCAD DPELQMTPEQ FESVQNVISR HNESLINLIA
SELNVIPSQI EDFELVLYDH QKSVIGGLND EFIFSPRLDN LVSCFTSTRG LIESSTELEQ
QNGIQLISLF DHEEIGSRSA QGADSTFLPD IINRLTKFDF NNGKHGQVDY FHETMAKSFL
LSSDMAHGVH PNYGDKYEGQ NRPQLNLGPV IKINANQRYA TNSPGIVLLK KVADRVQVPL
QLFVVRNDSP CGSTIGPILS AKLGIRTLDL GNPQLSMHSI RETGGTFDIV KLTDLFKSFF
VNYHELEEKI LCDHL
//