ID A0A1B8GFH5_9PEZI Unreviewed; 389 AA.
AC A0A1B8GFH5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN Name=LAP1 {ECO:0000313|EMBL:OBT94577.1};
GN ORFNames=VE01_07913 {ECO:0000313|EMBL:OBT94577.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT94577.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT94577.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT94577.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000256|ARBA:ARBA00043962}.
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DR EMBL; KV460242; OBT94577.1; -; Genomic_DNA.
DR RefSeq; XP_018128310.1; XM_018277343.1.
DR AlphaFoldDB; A0A1B8GFH5; -.
DR STRING; 342668.A0A1B8GFH5; -.
DR GeneID; 28841299; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03879; M28_AAP; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OBT94577.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 19..389
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5008448120"
FT DOMAIN 172..379
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 389 AA; 42870 MW; 3EFDB08B48BE8FF4 CRC64;
MKLTTLSVLA LSASAINARF VEKHETDQVV LTSDSGEDAT KYLIELSPGE TRLVIEEDKW
DLKRQNINFM DITDTQSLGS YNIHTSKKRV FPAAPVHQTS LEPLLKTLSK SKMRAHLEKF
TSFYTRYYKS TYGAQSSAWL LETVTEMVGA AGADKHGAHV KHFPHSWGQN SVIATIPGQS
DKTVVIGAHQ DSINLFLPAF LPAPGADDDG SGTVTILEAL RVLLADESVV AGNATNTIEF
HWYSAEEGGL LGSQAIFSAY EKEGRDVRAM LQQDMTGYVQ KTLDAGEPES VGVITDFVDP
ALTEFIKTIV TEYCDIPYVE TKCGYACSDH ASASKAGYPS AFVIESDFKY SDDKIHTQDD
KIEYLSFDHM LQHARLTLGL VYELAFAEL
//
