ID G0RC65_HYPJQ Unreviewed; 1559 AA.
AC G0RC65;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR51171.1};
GN ORFNames=TRIREDRAFT_104359 {ECO:0000313|EMBL:EGR51171.1};
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:EGR51171.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR51171.1,
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; GL985058; EGR51171.1; -; Genomic_DNA.
DR RefSeq; XP_006962711.1; XM_006962649.1.
DR STRING; 431241.G0RC65; -.
DR EnsemblFungi; EGR51171; EGR51171; TRIREDRAFT_104359.
DR GeneID; 18480825; -.
DR KEGG; tre:TRIREDRAFT_104359; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_104359; -.
DR eggNOG; KOG0266; Eukaryota.
DR HOGENOM; CLU_000288_6_16_1; -.
DR OrthoDB; 2517632at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR031359; NACHT_N.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10039; AMELOGENIN; 1.
DR PANTHER; PTHR10039:SF14; NACHT AND TPR DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_7G06670); 1.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17100; NACHT_N; 2.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50837; NACHT; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 432..584
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REPEAT 1184..1225
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1226..1267
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 175577 MW; A0F21F9DB0EE3098 CRC64;
MPRRSISAFF KGLQSRNGKG KGRAEKSSSG SKDEKLSRRS VSRDSQLSTP RNVPVVLPPD
ALSSLSVSRE PELPTPGSGV PVPPAEASTL TAEPQTTEEK KKAASCAQEL WDEAYDELKN
EETKLLQAYE VILSNRLSDP SFSSGGTDVN IIGSGDERRA QLLLVIEAAQ KKTHTEAKIK
ENIGEGMKVV NSVRGVISAA VQAAPQAALP WSLVTMSLDV GISPAQCAVE FELTFGGKIL
QNPLKQHQRQ TEGISYTAKR MEWYWSLSNE LFDRAGTANP SITPTMRDAL LSRLRELYKK
IILFQVKSIC SYYRNRGLQL LREFAMLDDW EESMKEIRVL EQEVQNDCNA YMGLERTSLS
HHIKECLENL LALQVKDLEQ QDRDCLRDLY ITNPRNDRKR LLEAKGGLLP DSFKWVMKSA
TFQQWHREKQ TNLLWIKGDP GKGKTMIICG VSEELESMGP YPDLVSYFFC QGTDPNFNSA
TAVLRGLIYL LAIQRPSLIS HLQEEYKNVG SRALFDGVNA WITLSSIFRS MLEDPALESA
CLVLDALDEC DSGRKFLLDL IVESTSLAPH IKWVLSSRNS PDIEAKLVNC PTAVVIDLES
NDRHVTDSVD AYVRARIQQL NLIQDNEELH TKLHRAIIEK SNGTFLWAAL VFKELEELRT
YDDDAEILEL LQEIPSGLIA LYDRMVDQIE RLSRNDQQRC RNLLAVMATA YQPLDLGATP
IMAGLKDRLA RSEPLKTLIK TCGSFLTVRD NVVYFVHQSA KDYLVGEGYH RIFQHGTEAV
HRDLFYRSMD ALQKPGRLRP NIYSLPYPGV NVHEVSIPQP DPLADIQYCC VAWLRHFCDG
FFGAHSTKKD DLLEGIEKAL NFLKIHFLHW IESLSLLRNI QVGVVFLRSL VKHLSGRLEP
DDSYEFFQDA ARFMFYNRYI LETAPLQTYV SALIFSPSRS QVRLHFKDTL SWIKTSPKVD
DDWISSCVNT LYASGVQTVA FSNDSLRLTA SFVDGRGRSW DIATGDLVCV YDFDSVDFDA
PAFSENHNFL FVSSATKNTV WDIEVGKLIQ ELDVGFLLFL MPKALFSADD RLLALIFEEH
LGIWDLSTGR LVRKILCSSS RRAVAISRDF ELLATESYRR EATREWIAMQ VSDIATSEVL
YELETEVSVF DDIMAISRDF RYLVSAGKHL QVLHIPSGAE SITVKDYDKN ISSIAFSDDS
TLLALGLKDG GVEVWSLETK VKIGSYEGHT DDVQFMVFSR DDKLLATASA DETIKVWAID
LSNPVDDSPD AIANNCIFNH VALSEDRNHV VYNSDGGNIN VWHRHENRQL PGIRQSRPLP
DKNAEGVKLW EWQGAPAISK GSRLIAFECV YSAGQLCDRL HQIEVWDINL RPIAQIPLEK
RIDSQADLAF LPDGDLLAAA HHRDELTIVT VWRAETGELI SEFDTSGPVR FCVYQANLYL
ATETGCYSID RSDVGNPCLI HFRPIATDSF PGFGYYLKSS EDTYNGDWVA WNGKRIIWLP
VNYRPRGGVS FCAAASEVVI GTARRDFVTM EFEEPPHTAY DQKEFLLQSQ ASPDTNDHP
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