ID PHY1_SYNY3 Reviewed; 748 AA. AC Q55168; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=Phytochrome-like protein Cph1; DE EC=2.7.13.3; DE AltName: Full=Bacteriophytochrome Cph1; DE AltName: Full=Light-regulated histidine kinase 1; GN Name=cph1; OrderedLocusNames=slr0473; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [3] RP CHARACTERIZATION. RX PubMed=9109482; DOI=10.1038/386663a0; RA Hughes J., Lamparter T., Mittmann F., Hartmann E., Gartner W., Wilde A., RA Borner T.; RT "A prokaryotic phytochrome."; RL Nature 386:663-663(1997). RN [4] RP CHARACTERIZATION, PHOSPHORYLATION AT HIS-538, AND MUTAGENESIS OF HIS-538. RX PubMed=9278513; DOI=10.1126/science.277.5331.1505; RA Yeh K.-C., Wu S.-H., Murphy J.T., Lagarias J.C.; RT "A cyanobacterial phytochrome two-component light sensory system."; RL Science 277:1505-1508(1997). RN [5] RP CHARACTERIZATION. RX PubMed=10828948; DOI=10.1021/bi992916s; RA Park C.-M., Shim J.-Y., Yang S.-S., Kang J.-G., Kim J.-I., Luka Z., RA Song P.-S.; RT "Chromophore-apoprotein interactions in Synechocystis sp. PCC6803 RT phytochrome Cph1."; RL Biochemistry 39:6349-6356(2000). RN [6] RP REVIEW. RX PubMed=10594094; DOI=10.1104/pp.121.4.1059; RA Hughes J., Lamparter T.; RT "Prokaryotes and phytochrome. The connection to chromophores and RT signaling."; RL Plant Physiol. 121:1059-1068(1999). CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are CC reversibly interconvertible by light: the R form that absorbs maximally CC in the red region of the spectrum and the FR form that absorbs CC maximally in the far-red region. Has also a slight blue shift for the CC far-red maximum. Forms a two-component system with the Rrcp1 response CC regulator. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC Q55168; Q55168: cph1; NbExp=8; IntAct=EBI-594457, EBI-594457; CC Q55168; Q55169: rcp1; NbExp=2; IntAct=EBI-594457, EBI-766949; CC -!- PTM: Contains one covalently linked tetrapyrrole chromophore. CC {ECO:0000250}. CC -!- MISCELLANEOUS: The R form exhibits both ATP-dependent CC autophosphorylation and phosphotransfer to Rcp1 activities. Unlike the CC higher plants where Pfr is thought to be the active form. CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome CC family. {ECO:0000305}. 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; BA000022; BAA10307.1; -; Genomic_DNA. DR PIR; S74389; S74389. DR PDB; 2VEA; X-ray; 2.21 A; A=1-514. DR PDB; 3ZQ5; X-ray; 1.95 A; A=1-514. DR PDBsum; 2VEA; -. DR PDBsum; 3ZQ5; -. DR AlphaFoldDB; Q55168; -. DR SMR; Q55168; -. DR DIP; DIP-34651N; -. DR IntAct; Q55168; 10. DR MINT; Q55168; -. DR STRING; 1148.gene:10499807; -. DR iPTMnet; Q55168; -. DR PaxDb; 1148-1001165; -. DR EnsemblBacteria; BAA10307; BAA10307; BAA10307. DR KEGG; syn:slr0473; -. DR eggNOG; COG4251; Bacteria. DR InParanoid; Q55168; -. DR PhylomeDB; Q55168; -. DR BRENDA; 2.7.13.3; 382. DR EvolutionaryTrace; Q55168; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB. DR GO; GO:0009883; F:red or far-red light photoreceptor activity; IDA:UniProtKB. DR GO; GO:0009584; P:detection of visible light; IEA:InterPro. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0009585; P:red, far-red light phototransduction; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR GO; GO:0009639; P:response to red or far red light; IDA:UniProtKB. DR CDD; cd16921; HATPase_FilI-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.450.270; -; 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; 1. 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; IPR000014; PAS. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013654; PAS_2. DR InterPro; IPR016132; Phyto_chromo_attachment. DR InterPro; IPR001294; Phytochrome. DR InterPro; IPR013515; Phytochrome_cen-reg. DR InterPro; IPR043150; Phytochrome_PHY_sf. DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1. DR Pfam; PF01590; GAF; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF08446; PAS_2; 1. DR Pfam; PF00360; PHY; 1. DR PRINTS; PR01033; PHYTOCHROME. DR SMART; SM00065; GAF; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 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; 2. 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; PS50046; PHYTOCHROME_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chromophore; Kinase; Nucleotide-binding; KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome; KW Sensory transduction; Transferase. FT CHAIN 1..748 FT /note="Phytochrome-like protein Cph1" FT /id="PRO_0000172001" FT DOMAIN 19..86 FT /note="PAS" FT DOMAIN 152..320 FT /note="GAF" FT DOMAIN 535..748 FT /note="Histidine kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT REGION 87..510 FT /note="Chromophore binding domain" FT BINDING 259 FT /ligand="a tetrapyrrole" FT /ligand_id="ChEBI:CHEBI:26932" FT /note="covalent" FT /evidence="ECO:0000250" FT MOD_RES 538 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107, FT ECO:0000269|PubMed:9278513" FT MUTAGEN 538 FT /note="H->K: No autophosphorylation; no phosphotransfer to FT Rcp1." FT /evidence="ECO:0000269|PubMed:9278513" FT HELIX 9..16 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 30..36 FT /evidence="ECO:0007829|PDB:3ZQ5" FT TURN 37..40 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 49..53 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 83..88 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 90..98 FT /evidence="ECO:0007829|PDB:3ZQ5" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 102..112 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 118..124 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 136..149 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 153..168 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 210..218 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 221..225 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:2VEA" FT STRAND 232..238 FT /evidence="ECO:0007829|PDB:3ZQ5" FT TURN 240..242 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 258..266 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 270..279 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 282..293 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 299..344 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 348..353 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 356..361 FT /evidence="ECO:0007829|PDB:3ZQ5" FT TURN 362..364 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 366..372 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 385..397 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 409..411 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 414..419 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 420..423 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 424..431 FT /evidence="ECO:0007829|PDB:3ZQ5" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 446..452 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 458..463 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 466..470 FT /evidence="ECO:0007829|PDB:3ZQ5" FT STRAND 478..482 FT /evidence="ECO:0007829|PDB:3ZQ5" FT HELIX 491..514 FT /evidence="ECO:0007829|PDB:3ZQ5" SQ SEQUENCE 748 AA; 84233 MW; A9ECA6D8D5B3C88A CRC64; MATTVQLSDQ SLRQLETLAI HTAHLIQPHG LVVVLQEPDL TISQISANCT GILGRSPEDL LGRTLGEVFD SFQIDPIQSR LTAGQISSLN PSKLWARVMG DDFVIFDGVF HRNSDGLLVC ELEPAYTSDN LPFLGFYHMA NAALNRLRQQ ANLRDFYDVI VEEVRRMTGF DRVMLYRFDE NNHGDVIAED KRDDMEPYLG LHYPESDIPQ PARRLFIHNP IRVIPDVYGV AVPLTPAVNP STNRAVDLTE SILRSAYHCH LTYLKNMGVG ASLTISLIKD GHLWGLIACH HQTPKVIPFE LRKACEFFGR VVFSNISAQE DTETFDYRVQ LAEHEAVLLD KMTTAADFVE GLTNHPDRLL GLTGSQGAAI CFGEKLILVG ETPDEKAVQY LLQWLENREV QDVFFTSSLS QIYPDAVNFK SVASGLLAIP IARHNFLLWF RPEVLQTVNW GGDPNHAYEA TQEDGKIELH PRQSFDLWKE IVRLQSLPWQ SVEIQSALAL KKAIVNLILR QAEELAQLAR NLERSNADLK KFAYIASHDL QEPLNQVSNY VQLLEMRYSE ALDEDAKDFI DFAVTGVSLM QTLIDDILTY AKVDTQYAQL TFTDVQEVVD KALANLKQRI EESGAEIEVG SMPAVMADQI QLMQVFQNLI ANGIKFAGDK SPKIKIWGDR QEDAWVFAVQ DNGIGIDPQF FERIFVIFQR LHTRDEYKGT GMGLAICKKI IEGHQGQIWL ESNPGEGSTF YFSIPIGN //