ID   A0A166UZS4_9PEZI        Unreviewed;       980 AA.
AC   A0A166UZS4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=CT0861_13137 {ECO:0000313|EMBL:KZL74003.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL74003.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL74003.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL74003.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-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 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:KZL74003.1}.
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DR   EMBL; LFIV01000037; KZL74003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166UZS4; -.
DR   STRING; 708197.A0A166UZS4; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000076552; 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   CDD; cd04816; PA_SaNapH_like; 1.
DR   CDD; cd02130; PA_ScAPY_like; 1.
DR   Gene3D; 3.50.30.30; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
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; 2.
DR   Pfam; PF04389; Peptidase_M28; 2.
DR   SUPFAM; SSF52025; PA domain; 2.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
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:UP000076552};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           17..980
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5007749005"
FT   DOMAIN          120..203
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          230..445
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          613..705
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          733..923
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   980 AA;  104531 MW;  32D2DA0DEA631FEA CRC64;
     MRTAALTLAL PALASAVKCK PYVESEKLQE LITIEDLLAG SQKLQDIADA HEGNRAFGGG
     GHNATVDWLV EELEKLDYFD VYKQPFTESF AGSKATLTVA GAAIEARPLT YTPGGDVTGA
     PLVSVANLGC EAGDFSADVS GAVALVSRGT CNFAVKATLA KSAGAVAAII YNNDVGPLAG
     TLGEASDAYA PVVGITREEG LALVASINAG EDVAVDLDVI SIIEDRVNYN VIAETRGGDH
     DNVLMIGGHS DSVFAGPGIN DDGSGTVGVL VVAKALSQFT TKNAVRLGFW GAEEYGKLGS
     YFYVKQLNSS EEEVSKIRAY LNFDMIASPN PKLAIYDGDG SAFNFSGPAG SDVIEKDFEE
     FFEANGRGHV PTEFNGRSDY AAFIENGIPS GGLFTGAEGL KTEAEAALFG GEVGVAYDVN
     YHLIGDDITN LDNDAYLINA KAIAHSVALY STSWETIPPV SLAKRRWAAD TAQHLKRAAE
     LTGHSHDGPC GGDLRHPRRG SVRAAILRDR PSHGRQGRGR HQDHRRNLWN LNKIARDNGG
     NRAFGLPGYK ASSDYILERV QGRFHKQLDT KLQYFNHTFS QTRDLKVTGP DGEDVYVVSL
     QYNHPTALPG GNTAPLIDTP VDDVRGSGCF ADQWEGIDAT GKLPLVKRGV CAIADKLKLA
     KAAGAVGVIL YNQTPGRNIG SATLSAENLG LLVPVGLIPL EDATAWRERL AAGETLEVNL
     LVDAVWDERE TWNIISETKE GDPNNVIVLG AHLDSVQAGP GVNDDGSGTS ALLEIAGSFK
     KYSGFKNKVR FIWWGAEESG LIGSLYYTAQ LSAAEADAIR FYWNYDMIGS INPVYNVYLG
     DNEGDKFGAQ PIHDYIAAQG KPAAFGGFGS SSDYVGFLQL GIPSSGIFTG AGAPTDPCYH
     LACDTLDNIN WDAITINTKA AARVAADFAN ELPAGLPRRA STTPARRSRD AIRREFQKWA
     LASEQAEHAK SCSHGEHNIY
//