GenomeNet

Database: UniProt
Entry: A0YJ38_LYNSP
LinkDB: A0YJ38_LYNSP
Original site: A0YJ38_LYNSP 
ID   A0YJ38_LYNSP            Unreviewed;       967 AA.
AC   A0YJ38;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=L8106_01952 {ECO:0000313|EMBL:EAW39039.1};
OS   Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW39039.1, ECO:0000313|Proteomes:UP000000737};
RN   [1] {ECO:0000313|EMBL:EAW39039.1, ECO:0000313|Proteomes:UP000000737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA   Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:EAW39039.1}.
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; AAVU01000002; EAW39039.1; -; Genomic_DNA.
DR   RefSeq; WP_009782494.1; NZ_AAVU01000002.1.
DR   AlphaFoldDB; A0YJ38; -.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 9814202at2; -.
DR   Proteomes; UP000000737; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 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; 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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAW39039.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW   Transferase {ECO:0000313|EMBL:EAW39039.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          543..616
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          617..669
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          710..967
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          653..701
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   967 AA;  110614 MW;  F22F21A060AC841C CRC64;
     MNSKQLQRLL IFYSAIGIFT ISVLVAVLSI FPLYQQLRKS EERNLQSALK TRKLAVEEFL
     SGVKDITAQI ASSTQAKQLL EIYNQNPNDR KSAATNVTLF LTDALNQTEY LAGITRLDQN
     NQFMAQVGLS IPKSFWKFSA VNSQDTQISN PIRLNDKFYL IVIQPIFDLK QEQIGTDLVL
     FEMDRLKEII VTDYTGLGKA EQVFLGTLED QKVKLLLSSN NENETLLKPI IEALEKTVVS
     QESGFTVVKG KFWNHAQVII FEPLSEFNWG LVIKIDRQEL YAPVNRQLMT IGMVTIIFSL
     LGAGGMVLLL RPLAGRAIIQ TDELEKQLQE KSLTLRELNY TQEQLLLEIR DRKFAQTELQ
     KRAEQLRNHN TVLIGIAQQR AVNQGDLLTA AQAITEATAK ILEVDRVGVW LYNEDKTHLK
     CFDLYQKKLN KHEREGVIRH NDYPAYFDAI NIQDSIAASD ARNDPRTCEF LSNYFIPNNI
     FSLLDSTIRI GGKIVGVICI EQCNQIQNWT PEDEIFVRSI GNIISLAIEA RNHQKAEIAL
     QESERMFRQL AESIDSVFWI SDPDGKEIYY VSPAYERVWG RPCRQVYEQP QSFLESIHSE
     DREGVILALT KQVSGGYEEE YRIVKPNGEI RWIYDRGFPI KNDQGKIDRV TGIATDITER
     KQAENALRES EAQLREQKQQ LQQTLKELQR TQAQMIQNEK MSSLGQMVAG IAHEINNPVN
     FIHGNIVHAA DYIRDLLSLI QLYQQYYPHP HPDIEIEIEA IELDFLQEDI KKLLKSMQVG
     TERIREIVKS LRIFSRLDES EIKEVDLHEG LESTLMILHN RFKAKSIYPG IKVIKEYDKI
     PRITCYSGHL NQVFMNILSN AIDAIEDAQS FQSPEEIQHN PGCIRIKTQQ IAPNWIQILI
     ADNGQGMSEE VRTRLFDPFF TTKPIGKGTG LGLSISYQVI IEKHKGNIEC DSILGQGTEF
     RIQIPIR
//
DBGET integrated database retrieval system