Phytochrome-like protein cph2 - Synechocystis sp. (strain PCC 6803 / Kazusa)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Phytochrome-like protein cph2

Alternative name(s):
Bacteriophytochrome cph2

Gene names

Name:	cph2
Ordered Locus Names:	sll0821

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length	1276 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region.
Domain	Both bilin lyase domains bind with the bilin tetrapyrrole chromophore precursor. The domain 1 shows red, far-red light photoreversibility. The domain 2 is photochemically inactive. Ref.4
Post-translational modification	Contains two covalently linked tetrapyrrole chromophores.
Sequence similarities	Belongs to the phytochrome family. Contains 1 EAL domain. Contains 2 GAF domains. Contains 2 GGDEF domains.

Ontologies

Keywords
Biological process	Sensory transduction
Domain	Repeat
Ligand	Chromophore
Molecular function	Photoreceptor protein Receptor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cyclic nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro detection of visible light Inferred from electronic annotation. Source: InterPro intracellular signal transduction Inferred from electronic annotation. Source: InterPro protein-chromophore linkage Traceable author statement PubMed 15641769. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Molecular_function	phosphorus-oxygen lyase activity Inferred from electronic annotation. Source: InterPro red or far-red light photoreceptor activity Traceable author statement PubMed 15641769. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1276

1276

Phytochrome-like protein cph2

PRO_0000172002

Regions

Domain

23 – 186

164

GAF 1

Domain

461 – 598

138

GGDEF 1

Domain

607 – 861

255

EAL

Domain

939 – 1080

142

GAF 2

Domain

1130 – 1266

137

GGDEF 2

Region

1 – 197

197

Bilin lyase domain 1

Region

939 – 1075

137

Bilin lyase domain 2

Sites

Binding site

129

1

Tetrapyrrole chromophore 1 (covalent; via 1 link) Probable

Binding site

1022

1

Tetrapyrrole chromophore 2 (covalent; via 1 link) Potential

Experimental info

Mutagenesis

129

1

C → S: Holoprotein exhibits no photochromic activity. Ref.3

Mutagenesis

130

1

H → F: Chromophore ligating activity (in vitro) is 30-40% lower than wild-type. Ref.3

Mutagenesis

130

1

H → Q: Chromophore ligating activity (in vitro) is about 10% more efficient than wild-type. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q55434 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 318CF3A73962D99E
Show »

FASTA

1,276

144,687

        10         20         30         40         50         60 
MNPNRSLEDF LRNVINKFHR ALTLRETLQV IVEEARIFLG VDRVKIYKFA SDGSGEVLAE 

        70         80         90        100        110        120 
AVNRAALPSL LGLHFPVEDI PPQAREELGN QRKMIAVDVA HRRKKSHELS GRISPTEHSN 

       130        140        150        160        170        180 
GHYTTVDSCH IQYLLAMGVL SSLTVPVMQD QQLWGIMAVH HSKPRRFTEQ EWETMALLSK 

       190        200        210        220        230        240 
EVSLAITQSQ LSRQVHQQQV QEALVQRLET TVAQYGDRPE TWQYALETVG QAVEADGAVL 

       250        260        270        280        290        300 
YIAPDLTGSV AQHYQWNLRF DWGNWLETSL WQELMRGQPS AAMEPMAAVQ STWEKPRPFT 

       310        320        330        340        350        360 
SVAPLPPTNC VPHGYTLGEL EQRSDWIAPP ESLSAENFQS FLIVPLAADQ QWVGSLILLR 

       370        380        390        400        410        420 
KEKSLVKHWA GKRGIDRRNI LPRLSFEAWE ETQKLVPTWN RSERKLAQVA STQLYMAITQ 

       430        440        450        460        470        480 
QFVTRLITQQ TAYDPLTQLP NWIIFNRQLT LALLDALYEG KMVGVLVIAM DRFKRINESF 

       490        500        510        520        530        540 
GHKTGDGLLQ EVADRLNQKL SPLAAYSPLL SRWHGDGFTI LLTQISDNQE MIPLCERLLS 

       550        560        570        580        590        600 
TFQEPFFLQG QPIYLTASMG ISTAPYDGET AESLLKFAEI ALTRAKCQGK NTYQFYRPQD 

       610        620        630        640        650        660 
SAPMLDRLTL ESDLRQALTN QEFVLYFQPQ VALDTGKLLG VEALVRWQHP RLGQVAPDVF 

       670        680        690        700        710        720 
IPLAEELGLI NHLGQWVLET ACATHQHFFR ETGRRLRMAV NISARQFQDE KWLNSVLECL 

       730        740        750        760        770        780 
KRTGMPPEDL ELEITESLMM EDIKGTVVLL HRLREEGVQV AIDDFGTGYS SLSILKQLPI 

       790        800        810        820        830        840 
HRLKIDKSFV NDLLNEGADT AIIQYVIDLA NGLNLETVAE GIESEAQLQR LQKMGCHLGQ 

       850        860        870        880        890        900 
GYFLTRPLPA EAMMTYLYYP QILDFGPTPP LPKVALPETE TEAGQGNVGD RPLPNSLNRE 

       910        920        930        940        950        960 
NPWTEKLHDY VLLKERLQQR NVKEKLVLKI ANKIRASLNI NDILYSTVTE VRQFLNTDRV 

       970        980        990       1000       1010       1020 
VLFKFNSQWS GQVVTESHND FCRSIINDEI DDPCFKGHYL RLYREGRVRA VSDIEKADLA 

      1030       1040       1050       1060       1070       1080 
DCHKELLRHY QVKANLVVPV VFNENLWGLL IAHECKTPRY WQEEDLQLLM ELATQVAIAI 

      1090       1100       1110       1120       1130       1140 
HQGELYEQLE TANIRLQQIS SLDALTQVGN RYLFDSTLER EWQRLQRIRE PLALLLCDVD 

      1150       1160       1170       1180       1190       1200 
FFKGFNDNYG HPAGDRCLKK IADAMAKVAK RPTDLVARYG GEEFAIILSE TSLEGAINVT 

      1210       1220       1230       1240       1250       1260 
EALQVEVANL AIPHTVSGTG HVTLSIGIAV YTPERHINPN ALVKAADLAL YEAKAKGRNQ 

      1270 
WLAYEGSQLP HVDGEV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[3]	"A second photochromic bacteriophytochrome from Synechocystis sp. PCC 6803: spectral analysis and down-regulation by light." Park C.-M., Kim J.-I., Yang S.-S., Kang J.-G., Kang J.-H., Shim J.-Y., Chung Y.-H., Park Y.-M., Song P.-S. Biochemistry 39:10840-10847(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOPHORE 1 BINDING, MUTAGENESIS OF CYS-129 AND HIS-130.
[4]	"Defining the bilin lyase domain: lessons from the extended phytochrome superfamily." Wu S.-H., Lagarias J.C. Biochemistry 39:13487-13495(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF TWO BILIN LYASE DOMAINS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA10536.1.
PIR	S75801.
RefSeq	NP_442466.1. NC_000911.1. YP_005652527.1. NC_017277.1. YP_007452342.1. NC_020286.1.
3D structure databases
ProteinModelPortal	Q55434.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48801N.
IntAct	Q55434. 11 interactions.
STRING	1148.sll0821.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA10536; BAA10536; BAA10536.
GeneID	12253839. 14618023. 952361.
KEGG	syn:sll0821. syy:SYNGTS_2574.
PATRIC	23842638. VBISynSp132158_2858.
Phylogenomic databases
eggNOG	COG2203.
KO	K02488.
OMA	AIHQGEL.
ProtClustDB	CLSK2393495.
Family and domain databases
Gene3D	3.20.20.450. 1 hit.
InterPro	IPR001054. A/G_cyclase. IPR001633. Diguanylate_PEstase_EAL_dom. IPR003018. GAF. IPR000160. GGDEF_dom. IPR016132. Phyto_chromo_attachment. IPR001294. Phytochrome. IPR013515. Phytochrome_cen-reg. [Graphical view]
Pfam	PF00563. EAL. 1 hit. PF01590. GAF. 2 hits. PF00990. GGDEF. 2 hits. PF00360. PHY. 1 hit. [Graphical view]
PRINTS	PR01033. PHYTOCHROME.
SMART	SM00052. EAL. 1 hit. SM00065. GAF. 3 hits. SM00267. GGDEF. 2 hits. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 2 hits. SSF141868. SSF141868. 1 hit.
TIGRFAMs	TIGR00254. GGDEF. 2 hits.
PROSITE	PS50883. EAL. 1 hit. PS50887. GGDEF. 2 hits. PS00245. PHYTOCHROME_1. False negative. PS50046. PHYTOCHROME_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHY2_SYNY3

Accession

Primary (citable) accession number: Q55434

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents