ID G0RG78_HYPJQ Unreviewed; 401 AA.
AC G0RG78;
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=Chitin biosynthesis protein {ECO:0000313|EMBL:EGR49997.1};
GN ORFNames=TRIREDRAFT_59346 {ECO:0000313|EMBL:EGR49997.1};
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:EGR49997.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR49997.1,
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; GL985061; EGR49997.1; -; Genomic_DNA.
DR RefSeq; XP_006964320.1; XM_006964258.1.
DR AlphaFoldDB; G0RG78; -.
DR STRING; 431241.G0RG78; -.
DR EnsemblFungi; EGR49997; EGR49997; TRIREDRAFT_59346.
DR GeneID; 18486454; -.
DR KEGG; tre:TRIREDRAFT_59346; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_59346; -.
DR eggNOG; ENOG502QRF7; Eukaryota.
DR HOGENOM; CLU_019904_0_0_1; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd17742; BRCT_CHS5_like; 1.
DR CDD; cd13945; Chs5_N; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 6.20.120.50; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT DOMAIN 75..165
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 163..251
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 254..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43079 MW; D473A6D7CFD64C8C CRC64;
MLVSLTVGKV DAGVTVLLTP DKRLIEFPSI LLPPNISSGS IVDITVGRNV SKEAAAEEEF
RALQDRIYQS FGASEPAAPV LRCRNATQTS VVLEWDPIEL ATADLISLSL YRNGQKAGNI
PRPLEMHSTK ISGLAVDTEY SFHLVLRTSA GTRASEKVVV RTHKMTDLSG ITITTGILPA
TTRENLTRAV ERIGAKIVDG VRIDTTHFVT TEGRGTAWEK AVENNIPVVR PEWVTACEQN
GRILGVTKFY LDVMRPGPPS DDQLPPPPAK DVPPKDTPPR ASPPAAQDSA HDKARDSKAA
PADGKKDQEA EGEASTKADS DSNSPEKEED GEGEASEPKA KTGGQAEQKV RLEDVQEQKV
ALRPVESQTA LVEQVEDSDG GEDESKPASP PDGASFQEVE L
//