ID G0RTT5_HYPJQ Unreviewed; 537 AA.
AC G0RTT5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR45489.1};
GN ORFNames=TRIREDRAFT_111121 {ECO:0000313|EMBL:EGR45489.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR45489.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR45489.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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DR EMBL; GL985079; EGR45489.1; -; Genomic_DNA.
DR RefSeq; XP_006968676.1; XM_006968614.1.
DR AlphaFoldDB; G0RTT5; -.
DR EnsemblFungi; EGR45489; EGR45489; TRIREDRAFT_111121.
DR GeneID; 18482268; -.
DR KEGG; tre:TRIREDRAFT_111121; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_111121; -.
DR eggNOG; ENOG502RP86; Eukaryota.
DR HOGENOM; CLU_499655_0_0_1; -.
DR OrthoDB; 2421643at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.2080; -; 3.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR037221; H-type_lectin_dom_sf.
DR InterPro; IPR019019; H-type_lectin_domain.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR46938; DISCOIDIN-1 SUBUNIT A-RELATED-RELATED; 1.
DR PANTHER; PTHR46938:SF2; DISCOIDIN-2; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF09458; H_lectin; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF141086; Agglutinin HPA-like; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT DOMAIN 51..200
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 537 AA; 61219 MW; 9460C94B6C2BE3CC CRC64;
MPAETKMDDF VMASCWPMPS TDLSDLPPSN LTKNEGDAED DSAVTSLAVS KEWFWPVGAW
LHVRFMNKEP NPRYEKMVKD AAKIWEKYAN IHFVFDNAEN AEIRILFDSK LKGGQSFIGR
HRRDETPKEE STMVLGLTLD DGLFRRTALH ELGHALGCIH EHSSPAAEIE WNKEEVIKWY
ATQKLSASWV ENNIFKHYQK SPSIQTSTFD NRSIMIYRIC PGWAQNVPYI DWPNELSDRD
KMLIQRIYRS NKRTTEFGIF DTQEKGGKKK PQLHHVKSVP LQNPDDKALD ITLGLTKFDL
ECNDGIQDVQ LKAYADAIET TSFNLNLSSV ESGRLYAAAA ISLASEQHNS SIQTGCYTTS
REDTQDGVEY VTPIKFKDAF NTVPEVVVWL KGFHFKSGEC FNLHATADNI TSTGFKLHVE
TWDNAALESA EVSWIAYEKD PPGIRSGKIE FHNFKERDAD ANPHHIKEKY RAKQIQLDEW
RPQSVYAAVS KFEFEKGHNP RLEITTTLGR SSFEVEAVTW EDSRCQAVEV SYLAVCI
//
