ID L1J551_GUITC Unreviewed; 1453 AA.
AC L1J551;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKX43663.1, ECO:0000313|EnsemblProtists:EKX43663};
GN ORFNames=GUITHDRAFT_140409 {ECO:0000313|EMBL:EKX43663.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX43663.1};
RN [1] {ECO:0000313|EMBL:EKX43663.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX43663.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX43663}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH993009; EKX43663.1; -; Genomic_DNA.
DR RefSeq; XP_005830643.1; XM_005830586.1.
DR STRING; 905079.L1J551; -.
DR PaxDb; 55529-EKX43663; -.
DR EnsemblProtists; EKX43663; EKX43663; GUITHDRAFT_140409.
DR GeneID; 17300264; -.
DR KEGG; gtt:GUITHDRAFT_140409; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_4_0_1; -.
DR OMA; WLKFKAT; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR CDD; cd14291; UBA1_NUB1_like; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00165; UBA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011087}.
FT DOMAIN 403..443
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 465..565
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 678..845
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 904..1078
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1453 AA; 160474 MW; F42E8036EABA33C3 CRC64;
MSTTAKPVSK SKINKLPQNK AKRGIFSNAN AGSSGGPEVD VKAWKAAQKA AASGSKGAEE
EEEKKKQERT KRFAVASEVA AACESSAKQA LKAVEGVGGK KEEVVKGYVN QGAKKGAQGA
ESTTKQQGAE SVEGVAGVTK IRDTTKKPRQ LLSEFCQKQK LGKPSIVTLQ DKNGFKAKFI
LHKDGGDPQV RVTDRSYATA QEAQEAAAVW GLYCTAGDRR MDRIMGAEYA ALWKEVEAAE
AESKRRAEMA AKRKENEKKR ENSASKDKFM PLYISSALLT KLENVLRSAV SSFFPSQGSG
KGGCGEEERS KVLALGFAQE QVDRAMRACG EGGAELMIDW LCLHEDEGKL PEGLRTKGGN
MPFEIIDFSK DRKSQKGEEE VGKGGKGREE ERRSGRSSAA VSWEDATDVE ILISLGFHEE
ASQSALQACD GEVQNALNHL LWEQQQGGGG GGEGEAESIA EEAEEEAQAL SSIFGENFFA
ENGEWRVKVD GALGGRIEGL ELSISLLGSS YPHSPPRRIL VRGPTTPRAH QVWMSKELFD
LSSRSVGGPV VFDLVSWLQS DEPLAILPAR QEELSSLLSC RRSQQEADDL SEVSTEGSAE
GSRGGSSTSV VKVKSSSGPS RSSAQRGGRE QALNAEQVKQ VSLLMKEQEE KKKSSPAWCK
LQDKRRSLPA WKAREEIIEK LSKNQVLIIS GETGCGKTTQ VPQFILDDLI ERGGGGGANI
ICTQPRRISA LGVAERVAQE RCEDVGGSIG YQIRLESKRS RQTRMLFCTT GILLRRMAED
RELSGVSHVM VDEVHERSVD SDFLLILLRR LIRKRKDIKI ILMSATLDAH KFCKYFDDAP
AFTFQASLSL WKSFSSRIVS ASPASSSAVV SEPADERPYD PNGRLTDVEI SMLNVDESKI
NYEMIELLLL HISSSSAKDS KQDGSVLVFL PGMGEIQRAH DTLVDSSRLR QVGKFWFIPL
HSSLPSLDQL KVFERPPPGV RKVILATNIA ETSITIDDCS YVIDCGRSKQ VAFDAETGLS
RLLEDWISRA AAQQRRGRAG RVREGVCYRL FSRRLFHRMP EQQQPEIHRV PLTGLCLQIM
EMQLGSAAAF LREALDPPSS KSIEHAMDTL YGVGAIQGGE KGKWLEQGAL WRLTHMGEHL
AKVPADVRLA RMLMFGAVFG CVDPILTVAA TMTSKSPFLV PFDKREEAMK RKQSFAHPRD
KSDHLLFIRV FDEWTKARRR GAKEERLFCQ TNFLSSSSLN TISDLREQFR ELLSDAGFIH
SRANSRVRNM LTYQLDASCN SNSDNVRLLR AVIAAGLYPH VIRVQLPETK FVEQAAGAIA
RAATAKELKL YTEKDGRVFL HPSSINFSEG DFLSPWLVYH DKQATSKVFI RDSSMVTPYA
LVLFGTDLRI LHAAGHVYVD DWIKFRAPAR LSVFLKYLRR LLQEALDDKL RNPEADISDH
PAVSLLMDFL EFE
//
