ID A0A0F4ZJU6_9PEZI Unreviewed; 614 AA.
AC A0A0F4ZJU6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Vacuolar aminopeptidase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TD95_000651 {ECO:0000313|EMBL:KKA30490.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30490.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA30490.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30490.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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}.
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:KKA30490.1}.
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DR EMBL; LAEV01000372; KKA30490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZJU6; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000033483; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 614 AA; 65534 MW; 88DD1CF85188C26F CRC64;
MVANNPYADG ANSLNYENDM ARLTIQAVQQ QQQQQLLRSQ WLQRQASSQA LRSASASFAP
SVPVSFATPP STFAAPAAAA AMRAPMPPQM TPTKRAFVLG DMARNNVHNN TICHVCAAEL
SSEEHGRVVP MMDGEECVLC KIKAGAPEAY TKPFCDFLTE NPTIFHAVDY FKAKLGEAGY
TELPMRDNWQ SKVSPGGKYW TTRNGSALIA FTVGPAYVPG NGVAMIAGHI DALTAKLKPV
SGKPNRAGYI ELGVAPYAGA LNATWWDRDL SIGGRVVVRD AATGKTGTRL VKLGWPIAKV
PTLAPHFGVG MMGTNNAETQ AVPIIGLDTP AERDIPTVAP LGGVGSFASK QPPKLVKLIA
KELGISDYSL IVNWELELFD SQPAQTGGMD HEFIFGGRID DKLCSWAAFQ GLLAAEQKHD
DSYIKLVALF DDEEIGSLLR QGAKGNFLPL VVERAVEALT ASDNSGAVYG PGLVGQTYAR
SFLVSADVTH AVNPNFMGNY LDEHMARLNV GVAICADSNG HMTTDAVSTS VLTRVGELAG
CTTQTFMIRN DSRSGGTVGP TLSSMMGVKA ADAGLPQLSM HSIRATTGAL DPGLGVKFFK
GFLDTWEQID GEWH
//
