ID G0RSQ3_HYPJQ Unreviewed; 1302 AA.
AC G0RSQ3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR45720.1};
GN ORFNames=TRIREDRAFT_81014 {ECO:0000313|EMBL:EGR45720.1};
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:EGR45720.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR45720.1,
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; GL985077; EGR45720.1; -; Genomic_DNA.
DR RefSeq; XP_006968345.1; XM_006968283.1.
DR STRING; 431241.G0RSQ3; -.
DR EnsemblFungi; EGR45720; EGR45720; TRIREDRAFT_81014.
DR GeneID; 18489267; -.
DR KEGG; tre:TRIREDRAFT_81014; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_81014; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_000022_2_17_1; -.
DR OrthoDB; 3305653at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT DOMAIN 541..618
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 140525 MW; 3D959393CE4840D4 CRC64;
MSIIDTTKDL AALFELQAQA TPDAIALEDE KRSLTYAELD SLTWSLADRL RRYGVGRDDL
VGVLMGRSAD NVIASLAALR AGGAFLVLEL AYPTSLLHDV IDDAKPTVII TQKAHAASIK
SGVATIIIDQ PEPDDAPVDG HAAPVVVETR EPLPASDDLD RLAFVSYSSG TTGKPKGIAN
PHRAPVLSYD LRFRTSDLQP GDRVACNVFF VWEMLRPLIR GATTVAVPDS ISYDPIGLVD
FLAERRITDT LMTPTLLTTV LSRHPKLGER LPELRSLWLN GEVVTTDLVR RACDALPNTR
LLNVYSASET HEIAVGDIKT FVDYEARVCP VGPPVDPEHI YILDEAGNRL EPGVSGELFV
GGDLLAREYL NLPETTAAAF QMDPFVKNKE GARMYRTGDM ARMLPSGLLE ITGRVGGMIK
TRGYTVQPGA VETTIVKHLA VRDCAVVAHG EGLQKQLVAY IVPDVDNVQG RTIVVIDESG
HSPVARRALS AHLAHYMIPP LWVELKELPT HAVSGKTNLK ALPPPPRPRT PEQVAAAKPE
RNVTIKMDTI VKMWSAALNV PVTSITPKHD FFDLGGHSLI LADLASRLSK AFGFPVPLGP
LAGNPTLEGH LEAVKAARDG HTEQVQADLP AVLRADAQLP EDIQPHVASP RMKRLSDAET
ILLTGSTGYL GAFLLKALLE HTSAHILCMV RFTEPTEDCR PAGTARIRKN LIDLGIWSDS
MLDRMEIVPG NLARSRLGLS PEAFEELASR VQVIVHAAAT VNLVYPYAAL RSANVGGTRE
MLRLASRGGA TVHHISTNGV LPPSREGWPE DAMIDYDDVP TRLQDGYGQT KWVAEKLVVE
ASRRGIPARI YRPGTISGHS VTGAANTYDL LNALIIESLQ LGQAPDVPDW VVEMTPVDVV
TGAIVALADH TDGQQLVYHL GDSRPVTSAS LFDSLAELGY ETGRLPWDEW VALWNEKRGA
RGGGDDPFTV DILRGGMPTV DGLQGAIVLR DDATRPLLER YGVRRIDVDS ALLETYTRHF
FARGWLPHPP RRLTTNGTNG SAVTMMKKKR GRLSGKVAVV TGASSGIGAA VAFALAKEGA
SIALAARRTD ALEKLKSRIT SSSSSSSATT KVLIHKTDIT DKAQVDALVQ ETERALGPVD
ILVCCAGVMY YTMMANVRTD EWERTVDVNC KGLLHCLSAT IPGMLARKAG HVVAISSDAG
RKVFPGLGVY SASKFFVEAT LQSLRLETAG TGLRVTSVQP GNTATELLGM STDDEAIKKY
GEPSGAKILE PEDVAGAILY AVCQPEHVAV NEVLIEPRDE PI
//
