ID G0RSR8_HYPJQ Unreviewed; 662 AA.
AC G0RSR8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR45726.1};
DE Flags: Fragment;
GN ORFNames=TRIREDRAFT_67761 {ECO:0000313|EMBL:EGR45726.1};
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:EGR45726.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR45726.1,
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).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; GL985077; EGR45726.1; -; Genomic_DNA.
DR RefSeq; XP_006968351.1; XM_006968289.1.
DR AlphaFoldDB; G0RSR8; -.
DR STRING; 431241.G0RSR8; -.
DR EnsemblFungi; EGR45726; EGR45726; TRIREDRAFT_67761.
DR GeneID; 18487633; -.
DR KEGG; tre:TRIREDRAFT_67761; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_67761; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_006072_1_1_1; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF397; CALPAIN CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 156..449
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 369
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 390
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT NON_TER 662
FT /evidence="ECO:0000313|EMBL:EGR45726.1"
SQ SEQUENCE 662 AA; 77140 MW; 00F6ADD217907418 CRC64;
MHGYSSSEES DDPRRPRSQP ASSGNNQDQK KKRKKRLPPQ QTINRLWKKF SSRKFHKAVS
VLPFDPVVAP RSGLDRPNEL LSESYERAAE ECRRKVQKIV QECKRVNMRY RDPGWDLDWD
LKYEKGNTLN YIGTEKFEIS KATLLGSKAV VPKAVKRVHE IFENPTFMKD VKGSDIKQGG
LGDCWLMSSL TALASVEDGV PRCCVAYDTK IGIYGFLFYR DGEWVYSIVD DKLYLKSPCW
DSPSMQRDLL QQIDREDVET VYRKTYQTGS KALFFAQCKD QNETWVPLLE KAYAKAHGDY
ASLSGGWIGE GLEDLSGGVT TELLTSDILD LDAFWENEMS KVNKEFMFGC STGLLDYGYG
QRDGISEAHA YVVVDARTLK SGQRLVKLRN PWGEIRKGLW EGPWSDGSKE WTTEVQEELG
HKFGSDSVFW ISFEDLIRKY THFDRTRLFR NDDDWRCCQR WIGVDVPWKA DYHEKFRVKL
TRDSPFILVL AQLDGRYFKG LQGQYSFRLH FRLHHEDRPD AEDYIVRSHG NYFMKRSVSV
ELPDLPAGNY TVYLKVTGQR DSKQPSVEEV VKREAKDRVE NEKLAQVGYA YDLAHSKAWE
HMEKVAKIRK QRDQQKASAC RQEERRRQWE RRHISRDITK KQKKKNTEKK ERKKEAKQAA
RR
//
