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
//