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Database: UniProt
Entry: E1IFJ6_9CHLR
LinkDB: E1IFJ6_9CHLR
Original site: E1IFJ6_9CHLR 
ID   E1IFJ6_9CHLR            Unreviewed;       848 AA.
AC   E1IFJ6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Cyclic nucleotide-binding protein {ECO:0000313|EMBL:EFO80012.1};
GN   ORFNames=OSCT_2097 {ECO:0000313|EMBL:EFO80012.1};
OS   Oscillochloris trichoides DG-6.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Oscillochloris.
OX   NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO80012.1, ECO:0000313|Proteomes:UP000054010};
RN   [1] {ECO:0000313|EMBL:EFO80012.1, ECO:0000313|Proteomes:UP000054010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-6 {ECO:0000313|EMBL:EFO80012.1,
RC   ECO:0000313|Proteomes:UP000054010};
RX   PubMed=21037015; DOI=10.1128/JB.00931-10;
RA   Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA   Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA   Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT   "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT   Oscillochloris trichoides subsp. DG-6.";
RL   J. Bacteriol. 193:321-322(2011).
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:EFO80012.1}.
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DR   EMBL; ADVR01000092; EFO80012.1; -; Genomic_DNA.
DR   RefSeq; WP_006562659.1; NZ_GL501404.1.
DR   AlphaFoldDB; E1IFJ6; -.
DR   STRING; 765420.OSCT_2097; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_336116_0_0_0; -.
DR   OrthoDB; 151598at2; -.
DR   Proteomes; UP000054010; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR46438; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR46438:SF7; ALPHA_BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000054010};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          167..283
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          539..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          496..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        546..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   848 AA;  94914 MW;  B6DE779649B91340 CRC64;
     MDTPVNPPNP GTEHPAAAMQ TIRHELRTPV NHIIGFSEML LEEASDLGIE QDYAPLKQVV
     TAGRHILAAV TEILSKDDVI VREADFIALH QRIEPHLLNI SAICTQLISA AQHEGQTQFA
     HDLSKIMGAV GQLDQISSGR LPASDAPDII PSPPDDAQAQ GADLRGHLLL VDDNDMNREM
     LSRRLERMDY QVTQVNDGYP ALDALHSHSF DLVLLDIMMP GLDGYAVLRA MRDDVDLRHV
     PVIVLSALDD IASVVQAIEL GADDYLPKPA DQVLLKARIG ACLFKHQVYQ RELEYVRRIQ
     HEKQRADELL HVVIPIGVAL STEKDFNHLL ERIVTEAQKL CHADGATLYL RTEDEKLRFM
     IVRTRSLNIA MGGVSGKDIP YPPLRLYDER SGQPQRNYVV VETTLSGEPI LIPDAYGPVD
     FDLSGTHDFD RRTGYRSISL LSMPLKDGAG YVIGVLQLIN AQDEQGTVIA FDEVAVQMVQ
     SLGRLAAAAL TAYTREQQLR QEINELRIEI DQVKKQREVE QITTSSYFGQ LQSRAQQMRS
     GADIGESSTR RSDKTDKGQE LQKRVYTVAG QEIHVHEQGP PGRQTILLIH GWSSSWYALS
     PLLPVLSERN RCVVVDLPGY GDSPPLRQRA TIIAYVDLLA QLIKQISPNQ QVILIGHSMG
     GMISVTMALR HTPLIERMVL ICPTISGKLS FWINVFISPI TMLERFRLAN RVVAMLEPYM
     LRATDRLMRP ASFADRTMIS EQDYIRLRAD ARRPGQGRVR AECFWAMRAN DLSEKLSLVT
     TPALVIWGME DNTVPLRDAS LVDDLLGGSE LQVLPRAGHW PQFESPERTR RLIRSFLGKP
     LKLLRVQL
//
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