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Database: UniProt
Entry: A0A094CAL1_9PEZI
LinkDB: A0A094CAL1_9PEZI
Original site: A0A094CAL1_9PEZI 
ID   A0A094CAL1_9PEZI        Unreviewed;       601 AA.
AC   A0A094CAL1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=V494_01460 {ECO:0000313|EMBL:KFY44490.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY44490.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY44490.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFY44490.1}.
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DR   EMBL; JPJW01000471; KFY44490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CAL1; -.
DR   STRING; 1420907.A0A094CAL1; -.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000029288; Unassembled WGS sequence.
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   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:UP000029288};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          384..591
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   601 AA;  65239 MW;  DBF9C97C1E5D70B6 CRC64;
     MAAASHETYK QGAPKRIGAI SQSVRPTLGG VLPTKLYLVV FPGLNCGVAP SIRSGDSGPA
     KSCSRGPLQA VTRHPRHRQV SVLRSKGEPR RRTAYGLASH SVNMPLNAPI ISRPSISQAP
     SSLGNSASDA GQEAGYHRMA VLHTVVQHSE LGPPTPMLPP PPTTHQSTCL EHSDISPYET
     APIVPDSSSP STSVAAILIV YPFTSNTPSL TIMKLTTLSV LALSASAINA RFVEKHETDQ
     VVLTSDSGED ATKYLIELSP GETRLVTEED KWDLKRQNIN FMDITETESL GSYNIHTSKK
     RVFPEAPVHQ STLEPLLKTL SKTNMRKHLE KFTSFYTRYY KSSYGAQSSA WLLDTVTEMV
     GAAGADKHGA HVKHFPHSWG QNSVIATIPG QSDKTVVIGA HQDSINLFLP AFLPAPGADD
     DGSGTVTILE ALRVLLTDEA VVNGNATNTI EFHWYSAEEG GLLGSQAIFS SYEKEGRDVR
     AMLQQDMTGY VQKTLDAGEP ESVGVITDFV DAALTEFIKT VVTEYCDIPY VETKCGYACS
     DHASASKAGY PSAFVIESDF KYSDDKIHTQ DDKIEYLSFD HMLQHARLTL GLVYELAFAE
     L
//
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