PHY2_SYNY3
ID PHY2_SYNY3 Reviewed; 1276 AA.
AC Q55434;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Phytochrome-like protein cph2;
DE AltName: Full=Bacteriophytochrome cph2;
GN Name=cph2; OrderedLocusNames=sll0821;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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 CHROMOPHORE 1 BINDING, AND MUTAGENESIS OF CYS-129 AND HIS-130.
RX PubMed=10978170; DOI=10.1021/bi992831r;
RA Park C.-M., Kim J.-I., Yang S.-S., Kang J.-G., Kang J.-H., Shim J.-Y.,
RA Chung Y.-H., Park Y.-M., Song P.-S.;
RT "A second photochromic bacteriophytochrome from Synechocystis sp. PCC 6803:
RT spectral analysis and down-regulation by light.";
RL Biochemistry 39:10840-10847(2000).
RN [4]
RP IDENTIFICATION OF TWO BILIN LYASE DOMAINS.
RX PubMed=11063585; DOI=10.1021/bi001123z;
RA Wu S.-H., Lagarias J.C.;
RT "Defining the bilin lyase domain: lessons from the extended phytochrome
RT superfamily.";
RL Biochemistry 39:13487-13495(2000).
CC -!- FUNCTION: Photoreceptor which exists in two forms that are reversibly
CC interconvertible by light: the R form that absorbs maximally in the red
CC region of the spectrum and the FR form that absorbs maximally in the
CC far-red region.
CC -!- DOMAIN: Both bilin lyase domains bind with the bilin tetrapyrrole
CC chromophore precursor. The domain 1 shows red, far-red light
CC photoreversibility. The domain 2 is photochemically inactive.
CC -!- PTM: Contains two covalently linked tetrapyrrole chromophores.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10536.1; -; Genomic_DNA.
DR PIR; S75801; S75801.
DR PDB; 4BWI; X-ray; 2.60 A; A/B=2-424.
DR PDBsum; 4BWI; -.
DR AlphaFoldDB; Q55434; -.
DR SMR; Q55434; -.
DR DIP; DIP-48801N; -.
DR IntAct; Q55434; 12.
DR STRING; 1148.1673324; -.
DR PaxDb; Q55434; -.
DR EnsemblBacteria; BAA10536; BAA10536; BAA10536.
DR KEGG; syn:sll0821; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR eggNOG; COG5001; Bacteria.
DR InParanoid; Q55434; -.
DR OMA; AIHQGEL; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0009883; F:red or far-red light photoreceptor activity; TAS:UniProtKB.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; TAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 2.
DR Gene3D; 3.20.20.450; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00990; GGDEF; 2.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00267; GGDEF; 2.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF55073; SSF55073; 2.
DR TIGRFAMs; TIGR00254; GGDEF; 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromophore; Photoreceptor protein; Receptor;
KW Reference proteome; Repeat; Sensory transduction.
FT CHAIN 1..1276
FT /note="Phytochrome-like protein cph2"
FT /id="PRO_0000172002"
FT DOMAIN 23..186
FT /note="GAF 1"
FT DOMAIN 461..598
FT /note="GGDEF 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 607..861
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT DOMAIN 939..1080
FT /note="GAF 2"
FT DOMAIN 1130..1266
FT /note="GGDEF 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT REGION 1..197
FT /note="Bilin lyase domain 1"
FT REGION 879..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1075
FT /note="Bilin lyase domain 2"
FT BINDING 129
FT /ligand="a tetrapyrrole"
FT /ligand_id="ChEBI:CHEBI:26932"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000305"
FT BINDING 1022
FT /ligand="a tetrapyrrole"
FT /ligand_id="ChEBI:CHEBI:26932"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000255"
FT MUTAGEN 129
FT /note="C->S: Holoprotein exhibits no photochromic
FT activity."
FT /evidence="ECO:0000269|PubMed:10978170"
FT MUTAGEN 130
FT /note="H->F: Chromophore ligating activity (in vitro) is
FT 30-40% lower than wild-type."
FT /evidence="ECO:0000269|PubMed:10978170"
FT MUTAGEN 130
FT /note="H->Q: Chromophore ligating activity (in vitro) is
FT about 10% more efficient than wild-type."
FT /evidence="ECO:0000269|PubMed:10978170"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4BWI"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 152..163
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 169..215
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:4BWI"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:4BWI"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:4BWI"
FT HELIX 401..418
FT /evidence="ECO:0007829|PDB:4BWI"
SQ SEQUENCE 1276 AA; 144687 MW; 318CF3A73962D99E CRC64;
MNPNRSLEDF LRNVINKFHR ALTLRETLQV IVEEARIFLG VDRVKIYKFA SDGSGEVLAE
AVNRAALPSL LGLHFPVEDI PPQAREELGN QRKMIAVDVA HRRKKSHELS GRISPTEHSN
GHYTTVDSCH IQYLLAMGVL SSLTVPVMQD QQLWGIMAVH HSKPRRFTEQ EWETMALLSK
EVSLAITQSQ LSRQVHQQQV QEALVQRLET TVAQYGDRPE TWQYALETVG QAVEADGAVL
YIAPDLTGSV AQHYQWNLRF DWGNWLETSL WQELMRGQPS AAMEPMAAVQ STWEKPRPFT
SVAPLPPTNC VPHGYTLGEL EQRSDWIAPP ESLSAENFQS FLIVPLAADQ QWVGSLILLR
KEKSLVKHWA GKRGIDRRNI LPRLSFEAWE ETQKLVPTWN RSERKLAQVA STQLYMAITQ
QFVTRLITQQ TAYDPLTQLP NWIIFNRQLT LALLDALYEG KMVGVLVIAM DRFKRINESF
GHKTGDGLLQ EVADRLNQKL SPLAAYSPLL SRWHGDGFTI LLTQISDNQE MIPLCERLLS
TFQEPFFLQG QPIYLTASMG ISTAPYDGET AESLLKFAEI ALTRAKCQGK NTYQFYRPQD
SAPMLDRLTL ESDLRQALTN QEFVLYFQPQ VALDTGKLLG VEALVRWQHP RLGQVAPDVF
IPLAEELGLI NHLGQWVLET ACATHQHFFR ETGRRLRMAV NISARQFQDE KWLNSVLECL
KRTGMPPEDL ELEITESLMM EDIKGTVVLL HRLREEGVQV AIDDFGTGYS SLSILKQLPI
HRLKIDKSFV NDLLNEGADT AIIQYVIDLA NGLNLETVAE GIESEAQLQR LQKMGCHLGQ
GYFLTRPLPA EAMMTYLYYP QILDFGPTPP LPKVALPETE TEAGQGNVGD RPLPNSLNRE
NPWTEKLHDY VLLKERLQQR NVKEKLVLKI ANKIRASLNI NDILYSTVTE VRQFLNTDRV
VLFKFNSQWS GQVVTESHND FCRSIINDEI DDPCFKGHYL RLYREGRVRA VSDIEKADLA
DCHKELLRHY QVKANLVVPV VFNENLWGLL IAHECKTPRY WQEEDLQLLM ELATQVAIAI
HQGELYEQLE TANIRLQQIS SLDALTQVGN RYLFDSTLER EWQRLQRIRE PLALLLCDVD
FFKGFNDNYG HPAGDRCLKK IADAMAKVAK RPTDLVARYG GEEFAIILSE TSLEGAINVT
EALQVEVANL AIPHTVSGTG HVTLSIGIAV YTPERHINPN ALVKAADLAL YEAKAKGRNQ
WLAYEGSQLP HVDGEV
