ID G9NCE7_HYPVG Unreviewed; 1380 AA.
AC G9NCE7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-MAY-2023, entry version 58.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHK15371.1};
GN ORFNames=TRIVIDRAFT_196232 {ECO:0000313|EMBL:EHK15371.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK15371.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK15371.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK15371.1}.
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DR EMBL; ABDF02000092; EHK15371.1; -; Genomic_DNA.
DR RefSeq; XP_013949572.1; XM_014094097.1.
DR STRING; 413071.G9NCE7; -.
DR EnsemblFungi; EHK15371; EHK15371; TRIVIDRAFT_196232.
DR GeneID; 25789940; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_196232; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_002022_1_0_1; -.
DR InParanoid; G9NCE7; -.
DR OMA; FENGMEM; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17947; DEADc_DDX27; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR019236; APP1_cat.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR28208; PHOSPHATIDATE PHOSPHATASE APP1; 1.
DR PANTHER; PTHR28208:SF3; PHOSPHATIDATE PHOSPHATASE APP1; 1.
DR Pfam; PF09949; APP1_cat; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 243..271
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 274..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 409..578
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 577..617
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 243..271
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 152330 MW; 3A93B1555DDC227E CRC64;
MAPSQKRSIE DDFIHTLSDN DDQIAENEEV AVQPPKKKAK TNKKSAKKSK DEEPQPEENE
GVWGQKDEND GAMDSDFEFM VDDAGDLGED EFEGWGFEGA KKGMAVEKAG VDLDEIIRRR
REKKNQKAGK EEDISPDDEA EIDMDDDEDG VLADDAFGMN VDSDAEESGE DADANSDKED
DGDKDEDEDD DAASDNDSVA TPVGHPDDMS DDDDEEDAEE KAKRDAFFAP EEKPKPGQKV
DVSSFQAMSL SRPILRGITT VGFSKPTPIQ AKTIPIALMG KDLVGGAVTG SGKTAAFVLP
ILERLLYRPK KIPTTRVVIL TPTRELAIQC HAVATKLAAH TDIKFTLAVG GLSLKAQEVE
LRLRPDVIIA TPGRFIDHMR NSASFSVDTV EILVLDEADR MLEDGFADEL NEILTTLPKS
RQTMLFSATM TSTVDRLIKV GLNKPVRVMV DSQKKTAGTL TQEFVRLRPG REEKRMGYLR
IASVESFRDG KVCYLLATDL ASRGLDIKGV DTVINYEAPQ SVEIYVHRVG RTARAGRHGT
SVTLAAEPDR KVVKAAVKAG KAQGSKIISR VIEVKDADKW QAEIDEMDDE IAEIEKEEKE
ERQLAQVEMQ IKKGENIIEH EAEIKSRPKR TWFETQQDKK NAKQAGRDEL NGPRAAKKKG
GNVKLSNKDK KKLDAKAERV DKSMGWKKDR YRERLFDFHL DTLPKLKYRI QSRIYRYILG
RQSKRRALSG IPVPRADQNQ GAVPLNPNDE LREQEKIAQE AAMIERRGRE EKRIANSGAY
SEQPREDTSF GGPAYPLPRP LPARGDSRTP DSLSGSPKLP TRQNSSVANE LTEAELATAN
ANLMARIAPF MTNPLVALPI TIFFYNESKS QSRNVLTDDA GHFAIRAPLD FVPTHVKILV
NEGLSTTQEV KYIEPYGVSL ISDIDDTVKM SNISAGAREI FRNTFVRELA DLTIEGTKEW
YGKMQDLGVS VHYCSNSPWQ LFPMLATFFK VSGLPLGSLH LKQYSGMLQG IFEPVAERKK
NTLVRLLRDF PQRKFLLVGD SGEADLEVYT ELALAYPERI LAVFIRDVTT PETAGYFDSS
FEMTRRTMSG LTLNSNSGPA NNRPATRQNS APGSVSDSKP PTGPVMGTLI DFSDEPEEAK
IDDVAVLEQI KRSRPGPSAS VSATDLLARK PPPPPRPAKP AALASTPAIP TARKGSVGLG
ISGAATNNSS EPPPPPPRKP VGQSGNQPVH PLAQIQNSSQ QTIESTKTAD KPPPPPPRRS
TKNLSPRMVA YFRGPSSNSD VDFDPLPPSL APVPAATGLS FYRPNSRSGN TSPSGSPTMG
AVNKKLELWR RRLARAHDQL DHLGVALYTW RKGQDVEAEA VGIIKRYMEE LEKEKRMRRS
//
