ID A0A078A084_STYLE Unreviewed; 1640 AA.
AC A0A078A084;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=Contig9892.g10578 {ECO:0000313|EMBL:CDW75560.1};
GN ORFNames=STYLEM_4550 {ECO:0000313|EMBL:CDW75560.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW75560.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW75560.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW75560.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCKQ01004404; CDW75560.1; -; Genomic_DNA.
DR EnsemblProtists; CDW75560; CDW75560; STYLEM_4550.
DR InParanoid; A0A078A084; -.
DR OMA; FRSEINQ; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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 Pfam; PF00072; Response_reg; 1.
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:CDW75560.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Transferase {ECO:0000313|EMBL:CDW75560.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 516..687
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1493..1632
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 335..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 796..823
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1550
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1640 AA; 191020 MW; EB89CA68A8793B51 CRC64;
MNGNCSTTTQ EPFIHLKDGF QKLKTGLYNN SYLTLSLSSL LIAVSQIPSR ADLCYLDWIF
ALSISLFQIF TVCKLKDFLF KEEYLPFFRD FLLTSLLMMM NHIYQIYDSS HKIALSMMII
GLIPSNIEND LNQQCNQKNS SSEELYYFKE EMPTLRQSEL QRNIKILFLI YFNKESLTIC
LIAIFYLLNM EYRLLHDQQI IRELNQNLIS SKISLNQEVQ KWRGLIEKFP QGLIIINKSQ
CLYSNQMLSK QLHAYSENEA VGKVLQWCVK GEPYEKKVQV NQKYSLNVIR NNDFTPRVSH
DYRRSLNKIE QNENSKQLFS SKFSNFNFVN EFKKESKPTL RNENSPENEK SGDNFFDNSN
QFNNIDIMSN ELNIDYSKAF IQLQQAFSRN NQPIYFSKSA MKVPTSRNNS CLDLTPLNRK
TNDINSLFKP SNHDYPRQSL LNESFSANYS NIAAENQLEK KEFEIQTSLV QWGEEDTILL
VIKDITDTQN FRKIKLQNKY KSKALCTLSH ELRTPDYSLI EQNRLFIEVC YFNVRDIIIE
VTEAFEYQAR LKQLNFQIYF DQKLPQTINS DPNRIKQIMF NLIQNAIKFT SKGFIKIYIY
LEMVKKRGKV KNFVNFEVED TGIGIRQPEI PYLYELFGIN KINKEKKNVG LGLSISYQLS
KKLGRALNVE SKYGSGTIMG FKVKNKCEEY ANEGSLIQDE IMSQVEEEKS FDVESPAKLN
LFILPDSQRG SRRTSNLLNR EKTMNSRHIR KINSECVIEY DCILFESIRN DKIQEKQLFE
NQRKIKVVLR YQTNQNQDLS KLIREKQLNM EQLQKRGETQ QQQLITTAKE NQEMPNSNRY
TRGIKNNNTI KNQNLSYNLT GTEFTLNKLT KQNTNQNEKG GQAWRQSSFI VRSPKKGNNK
SGSIEISKDN EDSNNIDDQD QLSKQLKNQR SRTLISNQME KSNLAFLNPQ NINISKKRTF
NAKAKQLRNI SDQQNLNLTS YQHSSDFQSS MIRVNSPIEN KKSSTKNVTF SKYDMKSIRE
DIINHKGIST SNQIDRTQII ALRQKLQSQQ SNNLFLSIKN RSPRQSNEEN KEQHREYKQM
FSFHKNNMNT TNCNPQQQRE LFNQYIEHGI IQQNNIVISG SSSNNNNMNS LYMNNNVRDS
FNPIEREFNQ RNSQVYQSLI KHQNQKLIQI QDQSDQKQNL EFYNQPQMAL VNTDTDLNIT
EFNDDEKNAK FTNFELINKA SIDDASQSFI KRQNNNMAKL DGLFMQSDSI DHQPQNNQRF
IPPILILPAN DSDSGEQVNM NPDSILQESS ELINMGNDLR LQPEIHIDQV YPQQPITQSG
VNFPQGFYEQ LLLEQQLRNN LKNHSSSNSQ QNNILTNISP QFGGKPFNFI PVDHYSYGFN
PQIGQINTQQ QIFTNMTLKN LNFKRGNTQI NYQTDRYGLR DFQSVEDSPT NNKINMCIAI
EENSKLNSDN YVDKDQGFTV EELEILQKQQ LKEEITTFAL RIREMRKECQ CPSILIVEDD
EFIKVMTKYT LMQVKFELHD VGNGQLAVEA VEEQNSKCNK CQGYLIILMD YDMPVMNGVE
VFQPLISQLI QATLKIKKLQ QEGKIEDIPI VAVSAFVASQ EIERCLNSGM CDYSNQIQFH
LFQQPSHLIH RGYSMCFLNG
//
