ID G0RFF2_HYPJQ Unreviewed; 1851 AA.
AC G0RFF2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR50462.1};
GN ORFNames=TRIREDRAFT_76515 {ECO:0000313|EMBL:EGR50462.1};
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:EGR50462.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR50462.1,
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 STXBP/unc-18/SEC1 family.
CC {ECO:0000256|ARBA:ARBA00009884}.
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DR EMBL; GL985060; EGR50462.1; -; Genomic_DNA.
DR RefSeq; XP_006963941.1; XM_006963879.1.
DR STRING; 431241.G0RFF2; -.
DR EnsemblFungi; EGR50462; EGR50462; TRIREDRAFT_76515.
DR GeneID; 18488626; -.
DR KEGG; tre:TRIREDRAFT_76515; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_76515; -.
DR eggNOG; KOG0029; Eukaryota.
DR eggNOG; KOG1302; Eukaryota.
DR HOGENOM; CLU_002666_0_0_1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd00084; HMG-box_SF; 1.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR043155; VPS33_dom3b.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11679:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33B; 1.
DR PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00995; Sec1; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT DOMAIN 967..1061
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 1714..1790
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1714..1790
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 770..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1851 AA; 204616 MW; CB3E79D502B90A78 CRC64;
MAPRAEFSTE QVRGKARKDL LYLLEGVRGK KNLVFDRSLV GPIGTIVKVA TLQEYGVDKF
FILENNNVDA SQRNVVFVAR GECGRHAEAI AAQIKRIQRE SQTTHDFHIF WVPRRTLVSD
QLLEEAGVLG DINISELPLL FFPLEDDVLS LELEDSFKDL YLSKDITPNF LMAKALMEVQ
QNHGLFPRII GKGDNAKRVA DLLVRMRQER LAGDDGSDVK TALTPSTTNE SVIIIDREVD
FVTPLLTQLT YEGLIDEIFE IQNNQAKVDT TIVGAPAQSS TATSQSRKRT VQLDSSDKLY
EQLRNANFAI VGGLLNKVAR RLQKVQSDYE SKHKTKTIAE LKEFVSQLPG YQQEHQSARI
HTGLAEEIIK HTRTDLFKGL LEVQQNLAAG ADPSSQFDGI EELIAREAPL RETLRLLCIY
SCISGGIKPK DLEQFKRLIL QGYGYQHLLT LNNLEKLQLF LSRSSPLAGM IPMTANSGAD
GTKTNYAYLR KQLRLIVDEV QEDDPNDIAY VYSGYAPLSI RLVQCILQKQ YLLSITKGNG
AANASSVAPG AGTQGWHGFD EAVKHVRGQT FYELQKGEDK AVKARALLSG SGQKQTVFVV
FVGGVTFTEI AALRFIAKQE ESRRKIVICT TSIISGNRMM DAAIEKEAFA RKEPTKIQSA
APLKSVYYHL KACSAARESL IPARPAVASQ PYGLCPVRYA PEPVNPPDDL SCRLQTHSWV
QVLYTPRVRA NPVRLADNPD KTGGSHGRFP HHMMRLPSVM LYGLPIGPTF SHPTQDTDSS
SSISSLAAES VAKSQSQVTA SPKSVLSSRR VSGLGSSDES SEVAPEIVVW TEDMESEDMD
LSSGLSNHDT EESSSMHLDT DDEKLQHGDD IPLPAEPTED AIAQSFTSSH SSLSDLSEVL
SSPSIVSSKA TTPIETEIPS RPQIGGITQT FSASSSYRHD IERLTFNVRP KSSIPTDIPS
YQYASECIAA AESSRLNPYA LHPEEYQFLR HHISHSQVTT YLNIRNGILR MWMKQPSVGV
TRQEAVGCAN ARWFDAASVC YDWLVRRGYI NYGCVQLPEP QPDFRGNEPP TKKRKTIAVI
GAGISGLSCA RQLDGLFKQH ASHFYSRGEE LPKVVILEGR GRVGGRVYSR EFKTRPATSE
PEFKGKRYTA EMGGMIITGF DRGNPLNVIV RGQLGIPYHA LTAETTIYDS NGKPVDPVRD
LLVEKLYNDC LDRVSEFKYK YQPSKVIEGN RDLLDEGRDS LGDGSKTIIQ AEEATAALPD
APSVSQQNVP ETVNMVPVSA DKLTGRVHTE PGVPGTIKAS EKAKLMGWNI KAGAADKANL
DLTQATALEG ATLGSVLDYA ITQYKNIVDL NAQDHRLINW HIANLEYSNA TNLHNLSLGL
WDIDAGNEWE GHHTMVVGGY QSVARGLLQC PSPLEVKTKF AVQKITYHGE GFDGPASIES
EDGTVVEADA VVCTIPLGVL KQGTIQFEPP LPSEKAEAVR RLGFGILNKV VLLYDRVFWD
SDRHIFGVLR DAPNRHSTSQ QDYSTNRGRF FQWFNVTNTT GLPCLIALMA GDAGFDTEHT
SNDSLVAEAT DILRSVFGKD VPYPIETVVT RWGSDRFARG SYSSAAPDMQ PDDYNVMAQP
AGNLFFAGEH TIGTHPATVH GAYLSGLRAA SEVLESMIGP IEVPTPLVLP RDSLLLRKRK
EAAKDPRQAR LEAYEIEVWE HVLSKIGERP LRPNKVAGSA YILFSKAHFE AAKKRCEESR
KPGRGRSIPN EVRIMTSRMW KEATPEQKRP YEEQVAEQKK RYLEAMQEYN ELAEKWDRQA
MALRAAYEEE HPSVPGPEEE GGPEDASSTM AQKRRAKNVS YAEGGDTDAD A
//
