ID   A0A093ZJV6_9PEZI        Unreviewed;       581 AA.
AC   A0A093ZJV6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=V492_00754 {ECO:0000313|EMBL:KFY17344.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY17344.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY17344.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY17344.1,
RC   ECO:0000313|Proteomes:UP000029299};
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   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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:KFY17344.1}.
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DR   EMBL; JPJU01000134; KFY17344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ZJV6; -.
DR   STRING; 1420902.A0A093ZJV6; -.
DR   HOGENOM; CLU_024336_0_0_1; -.
DR   Proteomes; UP000029299; 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; cd03876; M28_SGAP_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000029299};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           20..581
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005107331"
FT   DOMAIN          145..225
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          251..465
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          21..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  60597 MW;  22A8CB2D896022E4 CRC64;
     MKVSLSLAVL FAALNTVSAA PPNGGGHGNG NGNGNGNGHG HGKGPMVNSK ALRGLIKEKA
     LLEKAQTLQD FSELSGTPIT RVIGSPGHNA TVNWYYDTIK KLDDYYSVYI QSFPVVTAEG
     NLTVNGAVIE SATMSFTGAG HPIEDLVPVA NVACEAADFP AEVSGKVALL SRGTCTFGAK
     ALLAKAAGAV GVVVYNNEDG VVQGTLGEEG DYPPTIGISK AQGEEFLAAI KAGTAQKAEI
     IIEQKTVTTY NVIAETLAGD HDNVIHLGGH SDSVAAGPGI NDNGSGGIGI LEVALHLTKF
     KINNAVRFSW WAAEEEGLLG ALAYVKAQPQ SELDKIRIYL NFDMIASPNY VYAIYDGDGS
     TFNVTGPAGS AQAEHLFIDY FRDIEKVDSV PSDFDGRSDY GPFLDAGIAC GGLFTGAEGL
     KTAEEAIMFG GEAKVAYDIN YHAAGDTVAN CNGTAFLVNT RAIAHSVAVL AKSTAVLDEP
     LFDSTGVVPF QVFFSTASTR HPATLALEIP PKKVAGGCGT KAFIFHHQPV QNISDSPSAT
     IDVAVTRTTI TTDGTANRLE IDARATTTAL CTIRVATHNS V
//