ID A0A084QE13_STAC4 Unreviewed; 541 AA.
AC A0A084QE13;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Vacuolar aminopeptidase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=S40285_01669 {ECO:0000313|EMBL:KFA62198.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA62198.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA62198.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA62198.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL660812; KFA62198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QE13; -.
DR STRING; 1283841.A0A084QE13; -.
DR HOGENOM; CLU_019532_3_0_1; -.
DR InParanoid; A0A084QE13; -.
DR OMA; LLDTHYY; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000028524; 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:UP000028524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 57901 MW; D5A0A7E05886E064 CRC64;
MTRILSPQAY DNASPAMPCP EPTPHGSGSL PPTSALADLA SVFSSSDATP GLRFDGALRA
EIEKLYSSYS DPLSRTVDGK PETFTKPFLD FLTENPTVFH AVQYFKDKLN AKGFKELPAR
SSWVGSIKPG GKYWVSRNGS SIIAFTVGKA YKPGDGVGMI GGHIDALSAK VKPISTKPSR
AGYVQLGVAP YAGGLNATWW DRDLSIGGRV IVRDADTGKT SSRLVKLDWP IAKIPTLAPH
FGQGMMGQNN PETQAVPIIG LESSSNDAEA ETLGPAGSFV NTQPPKLVKL IAKELGISSY
SSIINWELQL YDTQPAQTLG LDKEFITAGR IDDKLCSWPA LIALLSASDN DDEGYIKLVA
LFDDEEIGSL LRQGAKSNFL PQVIERTVEA LNPDKFGPGV LGQTYARSFL VSADVTHAGN
PNFLGTYLEG HIPKLNVGIT VCEDSNGHMT TDGVSTSILR RVAELSGSTL QTFQIRNDTR
SGGTIGPSLS SMMGIRAADA GMAQLSMHSI RATTGALDPG LGVQFFKAFL NNWEKVDGEW
E
//
