ID A0A433UJ93_ANAVA Unreviewed; 1392 AA.
AC A0A433UJ93;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DSM107003_41330 {ECO:0000313|EMBL:RUS93897.1};
OS Trichormus variabilis SAG 1403-4b.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS93897.1, ECO:0000313|Proteomes:UP000276103};
RN [1] {ECO:0000313|EMBL:RUS93897.1, ECO:0000313|Proteomes:UP000276103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS93897.1,
RC ECO:0000313|Proteomes:UP000276103};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:RUS93897.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RSCM01000016; RUS93897.1; -; Genomic_DNA.
DR OrthoDB; 434121at2; -.
DR Proteomes; UP000276103; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; 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; 2.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 4.
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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 3.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 4.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF55781; GAF domain-like; 4.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000276103};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 380..456
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 459..511
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 515..562
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 581..633
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1021..1239
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1261..1379
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 322..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 622..656
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1310
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1392 AA; 153029 MW; 50D5D64F5DF795B2 CRC64;
MTETTPKPAT TLPANEVERL EALRRYNILD TPPEAAFDRI TSLAARLFNM PITLVSLVDE
SRGWFKSTYG FDMREVPRDA TICNLVVLSD QVLVIPDTRQ DNRLACNPFV QNEPGLRFYA
GAPLLTQDGF NLGTLCLLDT QPRNALTDEQ KALLADLAAM VMDELELRLA VHKIAQIDAT
LQDVSQGVSA VTGEAFFLTL VQHLSKVLGV DYTYIGLVDK DNQEAIRTIA ACGKGQIIDN
FQYLLHDTPC QEVLQKRKLC CYANRVQALF PNAPLLEPLN VESYVAVPFF DTTGVPLGLL
GVMDGKALTN VQLAESLLTI FALRIATELE RQQTEAERQQ AQQELERLVA QRTAELSQAN
KLLQLEIAER QQAEVALQKE QELLRVLLDN VQAGIVACNA EGILTLFNRA AREFHGLPEQ
PLPADQWAEY YNLYLPDGKT RMSKNEIPLF RALQGQKVEN VEMVIAPKQG TAKTLLASGQ
AIADSQGKKQ GAVVVMHDIT ERKQAEAELL ISDVALQQMP NAILLTDLQG KIQRWLGNAE
QIFGYTAAEA IGRPMNFLHR SDIQATMTDQ IIESIQTTGE FYGEIPCLRK DGSIVPIEKT
AKTVYDKAGN PIFFIGINKD ITERQKSEAE RAQLLRQQVQ EQNARLEAES DQRRSAFLAE
ISTALASSLD YESTLASVAN VVVPFFADWC AIDLLQDNQF IHRVAVAHRD PTKVKLGWEV
HRQYPSRIDA TEGVAKVLRT GKTEMAAEIP DAALVMVAQD PEHLRILREL GLKSVIVSPL
IARGQILGAI SFVTAESERR YSEADLALAE DIAHQAAIAI DNARLYREAE QSAERITRLQ
SVTAAFSESL TPLQVADVII DQGIAALGAN FAMIALVNET GTELEVLRNV GCEPDQMNGW
QRFSLNEPVP LAEAVRTGQP IWAEPSQTRA IRYPHLAEQY QQQNFNAWIS IPLMVEGRAI
GGMSFGFIEP QQLDEEEETF ILSLAQQCAQ AIVRTRLYEA ERTARSAAEA ANRIKDEFLA
VLSHELRSPL NPILGWSKLL QNGKLDEATA KQALASIERN AKLQSELIED LLDISRILQG
KLSLAVSPLN LATTIRAASE TVRLAAEAKS ISIKANLDVE VGQVLGDSTR LQQVMWNLLS
NAVKFTPVGG HVEVRLEKDN NYAQVTVSDT GKGISPDFLP YVFDCFRQAD STTTRKFGGL
GLGLAIVRNL VELHGGTIQA ESLGEGLGAT FIVRLPLMPI QLTVNEEPQS LEPSCNLNGV
QVLVVDDDTD TRDLVAFLLE QAGAKVIAAA SGGEAFAALA QSQPDVILSD IGMPDMDGYM
LLRQIRALPP EQGGQIPAIA FTAYAAEFDQ QQALSAGFQK HIPKPVEPEV LVQAILQIIS
SAALSVSNEQ RH
//
