ID A0YP74_LYNSP Unreviewed; 1044 AA.
AC A0YP74;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Signal transduction histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=L8106_11487 {ECO:0000313|EMBL:EAW37296.1};
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:EAW37296.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW37296.1, 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 -!- 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:EAW37296.1}.
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DR EMBL; AAVU01000012; EAW37296.1; -; Genomic_DNA.
DR RefSeq; WP_009784276.1; NZ_AAVU01000012.1.
DR AlphaFoldDB; A0YP74; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3920; Bacteria.
DR OrthoDB; 9758522at2; -.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737}.
FT DOMAIN 102..165
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 384..457
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 459..511
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 512..594
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 585..637
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 845..1039
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 184..218
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 335..394
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 628..673
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1044 AA; 120059 MW; F23C9FAF6AEA13C9 CRC64;
MSFNPFYFHV PSLDQIIVPV SLSLTPSQTV LEAVNLMSQM TNSTTRSSDK PGENQQGDSG
LRHRCILVIE ADQWMGILGE HHIIQAIASG KNLASLSVAE VMTTPNISLN LDDDLSNNLQ
TILSLLQHYQ LDQLPVLNAQ GKIQGIITAH SILHHLQPIH SPHPTETEVL SVEEQKPSVE
NPPENQLKRE LAEYKTQLNT ANQRIQQAIN QRQLIQRIDH KLRSSQQEIR AFLAALSDVM
LIIYLRENTV EIQETPPNPF YPTHSEIIAE TIQQLSQHSL SEHLIHPIRQ ALKSQEVVSF
EYSLNTKEGM FWFSAKISPL VDNSVIWVAQ DITKRKQAEQ ALQQLTNVLE SRVTERTNEL
QKVNTNLRQV LHERELAEQQ LRDSEQKFRQ LAESIREVFF IWSLDAFNLL YVSPAFEHIW
GISPVSLYEN PRLWIEMIHP EDQKQIEDTL LAEFSRGNFD QEFRIIRPDG EIRWILTRTF
PVENDSEIVY RIVGLAEDVT ERRRVEKALQ EREGQLATLA DISPVGIFHT DIAGYYLYVN
ERTSEIVGQP FREFMGQHWM LMVHPSDRPY VEKAWFMTRN HDQPLELEYK INRSDQIITW
VFAQIIPDFD DWGIVKGFVG TLTNISERKQ IETELQQLNQ QLETIVEQRT AQLQQTNEKL
RHEINQRQQV QDQIAAKANQ QAIIANLGQK ALSGIDYNQL IQQVGVQVSR CLGVESVQVL
NVPIQDPSLL RLLTEIQPNN SQLNPSEALN QTRSEDLKID LVEQAISFSQ VDSNSNLYGL
SIAIESRTTC FGILSAYTRQ QRVFNRDDVY FIQSVAHILA TVIERNETES QLKTSLQQKE
VLLKEIHHRV KNNLLVVSNI LEFQTDYTEN PEVIKILQES QRRIESMALI HEKLYESTGL
DKIDFGDYIQ DLVSQLRESY DFNSQLIELE LDVEGIALNL ETAHPCGLIV NELVSNAFQH
AFPDHRSGKI WVKFHQNSDG IVTLTVRDNG IGFPQNIDFR QIDSLGMELV CTLINQLEGE
IELIRDQGTT FSLTFKELQY RQRY
//
