ID A0A139WRD3_9CYAN Unreviewed; 965 AA.
AC A0A139WRD3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=WA1_09620 {ECO:0000313|EMBL:KYC34992.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC34992.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC34992.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC34992.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:KYC34992.1}.
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DR EMBL; ANNX02000053; KYC34992.1; -; Genomic_DNA.
DR RefSeq; WP_017743782.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139WRD3; -.
DR STRING; 128403.WA1_09620; -.
DR OrthoDB; 415806at2; -.
DR Proteomes; UP000076925; 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:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.30.450.40; -; 1.
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; 3.
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; 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; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
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|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 6..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 157..306
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 341..385
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 417..469
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 509..571
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 584..636
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 773..965
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 300..344
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 471..519
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 965 AA; 111014 MW; CD1670009D72CB5A CRC64;
MDSQRTIFII DDCEEDRMVY RRFLERDTRY TYKILEFELA AEAIESCKSC IPDLILVDFM
LPDATGLEFL EELKLSTDKN RLPVIMLTGQ GDESVAVQAM KSGAQDYLVK GKLTDDTFYR
ASYTVMERVR LMQQVEQQQE QQRLIAAIAL RIRLSLSLEI VLNTAVEEIR DFLKADRVIV
YQFHPDKSGT IVAESVVPGW KSCLNVRFED NCFQGVRGSY HRSRAGAVND TRQAALSDCY
VELLEHYQVR ANLYVPIFSG IQPVEADRCL LRNEPPVWGL LVAHQCGNPR QWQQWEMDLL
EQLSVQLAIA IQQAELYENL QSLNAQLEAK VEERTAELQQ SERKFRAIFE QTFQLIGLLT
PKGAILELNQ ASLEFFGAES DELRGLFFWE LSCYKISPTV HDSLQKAIAQ ASVGNFVRYE
VTLPNAQGVQ RTIDFSIKPI FNEMGKVVLL LPEGRDITER KQAEEALCDL NEELEARVQQ
RTQDLEQANL NLRSEIGERQ RVENELRRSE EKFRQLAEKI REVFFIFNHD LSETIYISPA
YEEIWGKSCS SIYQNSLSWL NLVHPEDKDN VILSLDQYKY IEGFKQEYRI IRDDGDIRWL
RAQSFLVRDS AGVTQRIVGL AEDITERKQA ELELLRNRDL REAIFNESAD AIFIVDEDTR
RIIDCNRRAI KLFEASNKQA LINDDNHTLQ HYPLTFQELE KLTEEVKAKG FWSREIEYIT
LKGNSFWGNL AVKQINVAGT VRNLVRVTDI SDRKQAVDQL EHSLEEKETL LKEIHHRVKN
NLQIISSLLR MQSRRARDES TMMLFQESQN RVQSMALIHE HLYQSPEISQ IDFGEYIRSL
TDNLFRCYGI SQKAIVLKIE TGGIKLNLDT AIPCGLLINE LVSNSLKYAF PKGRRGEIAI
CLVSSTDNTI TLTVSDTGIG IPESLDWSNT NSLGLRIVHN LTRQLKGTLT LDRNHGTAFS
ITFSR
//
