ID J9IAM8_9SPIT Unreviewed; 2070 AA.
AC J9IAM8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OXYTRI_01007 {ECO:0000313|EMBL:EJY77362.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY77362.1};
RN [1] {ECO:0000313|EMBL:EJY77362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY77362.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY77362.1}.
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DR EMBL; AMCR01010584; EJY77362.1; -; Genomic_DNA.
DR EnsemblProtists; EJY77362; EJY77362; OXYTRI_01007.
DR OrthoDB; 1222064at2759; -.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EJY77362.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EJY77362.1}.
FT DOMAIN 459..721
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1901..2067
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 101..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1849..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1515..1542
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..858
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1981
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2070 AA; 240060 MW; B4D50710D9068284 CRC64;
MQLQVDRTFD QDFKLEGSKN RLQNNTLINI INKASRTLNE VQSSNGNRNL QNNLDFNIFD
CESEEEKVFD QFQNSNAQQI QIQPRNTEER KVDSNTAFIN NNNAENQYKQ QKSRSNQPNQ
RKNKKRMQLG HIQIQHAQER ETIRENPLQN DSIANFSLNR EQFSHTSSEA FQVNLSQLQS
NQEQSSSLNN TTTTCLNIIK ITNNKASNSS MTSLSQDQFD NTNTKVRKFF NFLNIDMDLN
EYCNVLDFWN FKQTGKIEAQ VSIYERQQHY KTFAKIVGFN KKRKLIVDSL TKFQRQVKNK
DQKGAANEHM GHKPSTELKQ NQFSNLYDDL VYILKNREIT FKDTNHIFDI YSVEKEQDRS
HFKNLSGAKN ENFFKRTDSK KSKVNNNNNR NRRNSRFSAH KTEEPVNPQP GKKIYSISIS
PITWEGKDSL LITVKDITHE KVINQKQLMD KLRNMIFKSF SHELKTPLNG IIMSVDTSKF
ISKALIQKLQ KERQRGLLQL DDAIQQSNQL KLQIKVMESC SYVLKNIMHD FFDYHQLQTN
ELTMNVKEFE VHSFIRDIQR IVKQQMKFDK VQFKCFIEYD NPGGFAQNNS LTIKNSTMMK
ADKERLQQIL LNLLMNSIKF TNIGSIELKV LIQLHTAPQS IIFKVQDTGT GIEQDRLPLI
FNLFEKDENS SLNDYLNLNH KSARMGLPIS QNLCQLMGGQ IRVRSKINEG SIFSFKLPLN
PQDDFEKMLA IQSQKINNIL ENTKSDFSLF TSRAQDPKKV QHRSLPHINE NQIQDKNSQI
LVSPSNNINS LNLQSYQDQV RIILPKHEKQ EDKKLMGRKS EEESKSDEEE YCCGLEDEEQ
SSDTYDSFDE DEFEEDVDEL PPNSRHRGDN NDFLFQMQNK LGQFEFVFIS GERKSGQLSS
GEIRLDGNLT PQLRRSSEKF KNQLPVAKSS FKKQEQTRFK SSTPKEDVNT FSAQWNRIDQ
QQKELDKMKE LLIQDSDCQS RKSFSSNESN IKQQKDQVEN QINLQKQIEN QSSIQSARRK
PTNQAIPKKF QGDQLLQPAN GKSKMMKQAS FRQITLKNKN IDESSARGSN YSRNNSNLNT
NSNLNYNFSF QKKVLPNSII TAPPNLTYSK SHQIQANVKS KQTSNSSQIK QMNNNNNRIL
NNSEYWQQQN EELANQSLQK LKFEEEKSYS NEIQSNLETP QNKYLNKIKD QFNYHRQYSD
CQKNKTDFLV QIKKQSTNSA LTRNYGIYEG SSGNNSKKQA LNKNFAHLQK QNQALEKHQI
ECSLDTPQSA MSPCSLPNLN GGESPSIIKD DVFTLNPFQN LLPSKFQNMN LNLKLNQRSK
SMIPQKQINS QTISVNQNLT AKQVTQKYIN VNQIKPLHSY LRLSNQLSQS NQSQDNKSQF
NNYLGKSFEL DAASNEVNMM QKRAVKQSTK TLIEYLKFNI DKPIQEKQDV KNQELLFKNK
NEESDYRFVD EEFKDFDNTS EELVESERLS DIQYDSRQLN LKAGRTLFLN SSNFLENEQL
QLHMRSFSQN PNVYSNTLTN QLHNYKQQNQ TKNQQKQDLV QQRNFSSDQY DKIKVSQFQL
NLKESGFMSK VGSQININSE ANQFHIQQQP ATMPIQEYMT TPRGTQIWQN TLGNDQIFIE
ESVDISLPDR INVSYDEFTN ILYDQRMHSD NKKKQRNQNL RIPQIETSSF RSSCQQNYSI
KSASLSPSQS ENNKKLRQSK DKSPSGVQQH YTLISFAGSN SAQQFQNSKN QYIASQEEIK
FQEDYDSKQS IVSCSKKPAA FTFQQDSIRN CGNLNQQNRR KSTFLSPQKL QQQLQSIRNQ
KNQSQNASSN LSQNASLNLS QNTSPNQQIK KKQYFDFSGQ VNQTSKLEAI QSKSEIEKQR
RRSHNPGKKI KLDLKIDSNY NSEDSYSDKN KESLRESKCP QILVVDDVQM NRYAVEQMLS
LIFNIKVLQA ENGQNAIDTL IEHYQVSSDI AESMKETGNL FPHRNCCNQE TCKGIQLILM
DIEMPIMDGI TASRKLKQIM KKQDKNVGWI PDIPIVALTA YMDEKDNCIK SGMSDFSKYN
SFIILIIYIV TKPTSKVELQ EILYKYKVLT
//
