ID A0A0M8P5U8_9EURO Unreviewed; 574 AA.
AC A0A0M8P5U8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g7229 {ECO:0000313|EMBL:KOS41904.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS41904.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS41904.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS41904.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS41904.1}.
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DR EMBL; LHQQ01000119; KOS41904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8P5U8; -.
DR STRING; 229535.A0A0M8P5U8; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000037696; 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:UP000037696};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 574 AA; 62904 MW; F0455BAE9B270EAC CRC64;
MYYVHERDNK DFQGIQSLLS TDITMMSDPP RRDSAFSPHE SFSPTLSLPY THTIQPSIYN
MTRKYNTTQG LDLPWASQMS AQLPSAFMPV PAAQPVRAQA PIANEAIRPE DYSKPYCEFM
TSNPTIFHAV KSFSKQLEEH GYKQLSERAV WTSELKRGGK FYITRNDSSL IAFNIGSKYE
SGNGMAIVAG HVDALTAKLK PVSKLPNKAG FQQLGVAPYA GGLGTTWWDR DLGIGGRVLV
RDPETGKVET KLVKLDWPIA RIPTLAPHFG TPANGPFNQE TEMVPVVGVD NSDLFGNAKT
ESSDIKFGTF TSTQPEKLVK IISKEIGVTD YSTIVNWELE LFDTQPAQLG GLEKDMIFAG
RIDDKLCCYA AQEALIASSD STSPGTVKVV GMFDDEEIGS LLRQGARSNF MSSVMERIAE
AFAKDNYGPN LLSQTVANSF LVSSDVIHAV NPNFLNVYLE NHAPRLNVGV AVSTDSNGHM
TTDSVSEGVL RRVAERCGST LQVFQIRNDS RSGGTIGPMT SAQIGMRAID CGIPQLSMHS
IRATTGSLDP GLGVKLFKGF FDHYEEVDKE FADF
//