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Database: UniProt
Entry: S7QFD7_GLOTA
LinkDB: S7QFD7_GLOTA
Original site: S7QFD7_GLOTA 
ID   S7QFD7_GLOTA            Unreviewed;       475 AA.
AC   S7QFD7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=GLOTRDRAFT_136898 {ECO:0000313|EMBL:EPQ58122.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ58122.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ58122.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ58122.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; KB469298; EPQ58122.1; -; Genomic_DNA.
DR   RefSeq; XP_007863390.1; XM_007865199.1.
DR   AlphaFoldDB; S7QFD7; -.
DR   GeneID; 19303653; -.
DR   KEGG; gtr:GLOTRDRAFT_136898; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025286_0_0_1; -.
DR   OMA; AGEEQGM; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000030669; 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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF59; PEPTIDASE_M28 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           25..475
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005146597"
FT   DOMAIN          262..446
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   475 AA;  50831 MW;  EC4E6691AD4BC4A7 CRC64;
     MVANAGLGLA TLLITAFDPS LLSGQPCLSQ SYYGSFSGRS IFRPDPSCLE LVTDSLPSGT
     IVPASKDMAQ LVWIEEQAID DSLKSPSGGF DLQLEELLTK ISTLGTAYSA YDFAGEREQV
     LGPPITHYDV MYRSGPSALL SLPADAAKVI DTIIPPFWKS TLLLKEPITY VPVPSDAVQR
     VRALLDSVKF DPTVAAIVSN ISVPQMKNDI RFLTGEDGKS GIISRHSFSS GVRTAAAWLS
     DRFEDTGATC ELRPFLAGFA PNVVCRYPST VNTTATVLLS AHYDSRGSFG STRAPGGDDD
     GSGTVALLAI ARTIARKGIT FRSNVELVAF SGEEQGLLGS KAYAREMREA GTNLTLMVQA
     DMLAYHAPGE PAQLGLPDLI GTPEVSQLVA NLSAIYSPEL QVGLTPACCS DHQSFHEQGF
     PSTQVFERAG PIIDPMYHNS GDLSEREGYD FEQLKSIAKV QFATLLTAAG FDLPE
//
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