ID A0A0D1WD98_9EURO Unreviewed; 511 AA.
AC A0A0D1WD98;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_02316 {ECO:0000313|EMBL:KIV86720.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV86720.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV86720.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV86720.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-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}.
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DR EMBL; KN846951; KIV86720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1WD98; -.
DR STRING; 1016849.A0A0D1WD98; -.
DR HOGENOM; CLU_019532_3_0_1; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000053599; 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:UP000053599};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55322 MW; E1829F4045776297 CRC64;
MVRKTSSGFF TSIHEDMPLH ISRGYDRKVL HSAYPSSSSS SPPSPQKEKR FSPEKYTQPY
LDFMTKNPTV FHAVDAFTKQ LEDAGYVHLS QRTSWTIKPG GKYYTTRNGS AFIAFAVGKD
YKAGNGVGIV AGHIDALTAK VKPVPTLPTK AGYVQLGVAP YAGGMNTTWW DRDLGIGGKV
LVKSSDGKIK EELVKLDWPI ARIPTLAPHF GAAANGPFNL ETNMVPIIGL DNSDLTGKAE
SSLNIPAGTF VATQPERLVK AIAGELGIED YTSIVNWELE LFDTQPAQLG GLDKEFIFAG
RIDDKLCCFA AIEALLASSD DASSGIVKMV GCFDDEEIGS YLRQGARSNF MSGAIERICE
NFSEHCGPNL VNQTLANSFL VSSDVIHAVN PNFLGAYLEN HYPRLNIGVT VSADPNGHMT
TTSVSTALLS RIAEKAGSTL QVFQIRNDSR SGGTIGPMTS SRLGCRAIDC GIPQLSMHSI
RATTGSLDPG LGVKLYKGFF DYYEEVDKEF Q
//
