ID C7GVK8_YEAS2 Unreviewed; 514 AA.
AC C7GVK8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 22-FEB-2023, entry version 48.
DE SubName: Full=Lap4p {ECO:0000313|EMBL:EEU05166.1};
GN Name=LAP4 {ECO:0000313|EMBL:EEU05166.1};
GN ORFNames=C1Q_04507 {ECO:0000313|EMBL:EEU05166.1};
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU05166.1, ECO:0000313|Proteomes:UP000008073};
RN [1] {ECO:0000313|EMBL:EEU05166.1, ECO:0000313|Proteomes:UP000008073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU05166.1,
RC ECO:0000313|Proteomes:UP000008073};
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.,
RA Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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:EEU05166.1}.
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DR EMBL; ACFL01000357; EEU05166.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GVK8; -.
DR MEROPS; M18.001; -.
DR Proteomes; UP000008073; 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; cd05639; M18; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 514 AA; 57068 MW; B6C1CD5CE930D35F CRC64;
MEEQREILEQ LKKTLQMLTV EPSKNNQIAN EEKEKKENEN SWCILEHNYE DIAQEFIDFI
YKNPTTYHVV SFFAELLDKH NFKYLSEKSN WQDSIGEDGG KFYTIRNGTN LSAFILGKNW
RAEKGVGVIG SHVDALTVKL KPVSFKDTAE GYGRIAVAPY GGTLNELWLD RDLGIGGRLL
YKKKGTNEIK SALVDSTPLP VCRIPSLAPH FGKPAEGPFD KEDQTIPVIG FPSPDEEGNE
PPTDDEKKSP LFGKHCIHLL RYVAKLAGVE VSELIQMDLD LFDVQKGTIG GIGKHFLFAP
RLDDRLCSFA AMIALICYAK DVDTEESELF STVTLYDNEE IGSLTRQGAK GGLLESVVER
SSSAFTKKAV DLHTVWANSI ILSADVNHLY NPNFPEVYLK NHFPVPNVGI TLSLDPNGHM
ATDVVGTALV EELARRNGDK VQYFQIKNNS RSGGTIGPSL ASQTGARTID LGIAQLSMHS
IRAATGSKDV GLGVKFFNGF FKHWRSVYDE FGEL
//
