ID L1JDJ5_GUITC Unreviewed; 2293 AA.
AC L1JDJ5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=GUITHDRAFT_45786 {ECO:0000313|EMBL:EKX46591.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX46591.1};
RN [1] {ECO:0000313|EMBL:EKX46591.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX46591.1,
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:EKX46591}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR EMBL; JH992993; EKX46591.1; -; Genomic_DNA.
DR RefSeq; XP_005833571.1; XM_005833514.1.
DR STRING; 905079.L1JDJ5; -.
DR PaxDb; 55529-EKX46591; -.
DR EnsemblProtists; EKX46591; EKX46591; GUITHDRAFT_45786.
DR GeneID; 17303466; -.
DR KEGG; gtt:GUITHDRAFT_45786; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_001110_0_0_1; -.
DR OMA; DVNETMC; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 15.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 15.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 15.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 14.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 15.
DR SMART; SM00091; PAS; 15.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 15.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 15.
DR PROSITE; PS50112; PAS; 15.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011087}.
FT DOMAIN 1..36
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 59..112
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 113..184
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 187..239
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 240..311
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 314..366
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 367..438
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 441..494
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 495..566
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 569..621
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 622..693
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 696..748
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 749..820
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 823..875
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 876..947
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 950..1002
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1003..1074
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1077..1129
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1130..1201
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1204..1256
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1257..1328
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1331..1383
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1384..1459
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1458..1510
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1511..1582
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1585..1637
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1638..1709
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1712..1764
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1765..1836
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1839..1891
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1908..2129
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2177..2293
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 2226
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKX46591.1"
FT NON_TER 2293
FT /evidence="ECO:0000313|EMBL:EKX46591.1"
SQ SEQUENCE 2293 AA; 255998 MW; D2C8830F74561E1D CRC64;
FSIDLHDRLR DWNAISQRQM GWKKGDVVGK SIYEFLVADV LKSKIQQGIE HAKSKRESVS
LEFSASKPDG SVIFLSLRGI PIVQDDAKSC EEVLFVGQDI TDRKQYEQEM VRKAQELRSF
IDTVNAPIFG TDVSYNINEW NDQAEEVSGF KRNQVLGKNF IEFFIAHENQ VSVRDLLNDA
LNGNNRTNFE LPLLDAKKQR LLVLLNVTAR KNIDGEVIGI MGVGQDITDR KRFQDERARV
AQELQNFIDT ANAPIFGIDH MGLVNEWNLK AAEITQFSRE EVIGKNLVEI YITDEFRSSV
KLVLDNALKG FEAANFEFAL YTKDHRRVDV LLNATPRRDV EGNVIGVIGV GQDITERKMA
EMEKARVAQE LQTFIDTANA PIFGIDDQGL VNEWNMKAAE LTGFSKQEVL GQNLVEVYIG
EKFRNTVNGV LQNALCGMET SNIEFPLYTK EEKRRVEVLV NATARRDING NIIGVIAVGQ
DITERKRVEG EKTRVAKELQ TFIDTANAPI FGIDAKGLVN EWNNKAAEIT GFSREEVLGQ
DLVEVYISEE FRQSVREVLD NALQQKATAN FEFPLYTKDE RRVDVLLNAT PRLDANGNVV
GVIGVGQDIT ARKLFEEEKT RVAKELQTFI DTANAPIFGI DANGLVNEWN NKAAEITGFS
KDQVLNRNLV EDFISPDYRV SVSQVLTNAL KGRGTANFEF PLFTVDKRRV EVLLNATPRK
DISGNVVGVI GVGQDITDRK QVEVEKTRVA EELQNFIDTA NAPIFGIDAN GFVNEWNNKA
AEITGFSKEE VLGKDLVEVY ITDEYRSSVK EVLDNALQGH ETANFEFPLF TKNQRRVEVL
LNATTRRDES GKAVGVIGVG QDITERKQVE SEKFRVAQEL QAFIDSANAP IFGIDAKGRI
NEWNNKAAEI TNFSSMEVLG RELVKDFITE EYRETVKEVL DNALRGVEAS NFEFPLYTKD
QRRVEVLLNA TTRRDVSGRV VGVLGVGQDI TQRKRVEIEM TRIARELQTF IDTANAPIFG
IDDQGLVNEW NNKAAEITGY SKAEVLGKNL VEVYITEEFR ASVKEVLDKA LKGAETANFE
FPLFTKDMRR VDVLLNATTR LGDGGRVVGV IGVGQDITER KRAEEEKTRV AKELQNFIDT
ANAPIFGIDA EGLVNEWNNK AAEITGFSSE DVLGRNLVQD FITEEYRVTV KEVLDNALLG
IETSDFEFPL YTVDKRRVEV LLNATSRRNT AGKIVGVIGV GQDITERKRV EEEKARVAQE
LQTFIDTANA PIFGIDANGL VNEWNNKAAE ITGFSREQVI GRSLVKDFIT EEYRVSVRDV
LDKALKGVGT ANFEFPLYTV DGQRVEVLLN ATTRRDAHGN VTGVVGVGQD ITDIKRSQEE
MTRVANELQT FIDTANAPIF GIDAKGLVNE WNNKAAEITG FSREEVLGQD LVEVYISEEF
RQSVRKICDL ALQKVATANF EFPLYTKDER RVDVLLNATP RLDANGNVVG VIGVGQDITA
RKLFEEEKTR VAKELQTFID TANAPIFGID DKGLVNEWNN KAAEITGFSR EEVLGQDLVE
VYISADFRST VSEVLENALK GRGTANFEFP LYTKDGRRVE VLLNATPRRN MARQVVGVIG
VGQDITERKE VEIEKTRVAQ ELQTFIDTAN APIFGIDDKG LINEWNNKAA EITGFSRQMV
FGQNLVEKYI TEEYREQVKM VLDNALEGEE TANFEFPLFT NTGRRVDVLL NATTRRDVTG
RPIGVIGVGQ DITERKQVEE EKTRVAQELQ TFIDTANAPI FGIDANGLVN EWNNKAAEIT
GYSKAEVLGR NLVEVYITQE FRPSVKKVLD DALLGKEKSN FEFPLFTKDK RRVEVLLNAT
TRRDVTGAIV GVIGVGQDIT EMRRLMEQEA LLFQAQAAND AKSQFLATMS HEMRTPLNVI
MGMNDLILET SLLDEQRKFA EQIKSSSESL LVLINDILDL TKIEAGKLEL VSVDFDLRQV
IEDTVDSVAS KALGKGLEIC CYMSPNTPTV VNGDPDRLRQ ILLNLLSNGI KFTNSGQVYL
LAEMEEETPT HQAFRFKVYD SGIGISEEGQ KKLFNRFSQV DSSTTRTYGG TGLGLAISKQ
FAELMNGSMG VQSNLGKGSL FWFNAVFKKI NTAVQPTFSL PSASNKAPPS AAQSSVVAAP
APAPAAVQPK KESKAARILI VEDHWANRKL LEAMLLQKGH ELHCVENGVE AVNITAVVEF
DLVLMDCNMP IMDGWQATEK IRQRAGLNQT TPIIAVTANA MKGDRDKCIA AGMDDYISKP
VERKRLYEII AKW
//
