ID B8FM24_DESAL Unreviewed; 884 AA.
AC B8FM24;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cyclic nucleotide-binding protein {ECO:0000313|EMBL:ACL05757.1};
GN OrderedLocusNames=Dalk_4072 {ECO:0000313|EMBL:ACL05757.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL05757.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL05757.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL05757.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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DR EMBL; CP001322; ACL05757.1; -; Genomic_DNA.
DR AlphaFoldDB; B8FM24; -.
DR KEGG; dal:Dalk_4072; -.
DR eggNOG; COG1235; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR HOGENOM; CLU_330324_0_0_7; -.
DR Proteomes; UP000000739; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd19920; REC_PA4781-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF1; TWO-COMPONENT RESPONSE REGULATOR ORR33; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000739}.
FT DOMAIN 7..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 642..744
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 884 AA; 99453 MW; CE2F1ED5A17ECC8A CRC64;
MDEDKAKILI VDDEKIHISV LTKFLSGDYD VSIALNGAEA LMRAKADPPP DLILLDVMMP
EMDGFEVCRR LKSDKSLKSI PVIFLTTKDD EENTARGFEL GAVDFIRKPF RPAVLSARIR
THLAMSNQKQ LLEQQVKERT AELVKSQKKL RDAMGNLLTI QVAPGVLWLQ VPEADLRILC
GCPGEVVKLL MLKGLNAPAF KDGVNFETGP NVILLSDLLV QNGQFANLSE FPVLQMLYRQ
GMMIPGHPNN TGVKPMLIGS AEQVRAQMEY IHHGNYGLLS KEEIMAAGID EELAESMMRV
KLKFAFGKIK KPYEFLDTLE IDDTLQEIRN GVFVRRIGFN QFRFHYRERF ADIDLNLPKD
AHYPSPYPLG RHRLQRHYFS VLHTGEGDGW NTKKPSMSSV LMFQGRIYLV DAPPSVMNGL
TALGIDISEV EGIFHTHSHD DHFAGLPDLV HTDRRLKYFA TPLVRTAVAK KFAALTSLPE
EKFEQFFDIH DLEFDTWNKI GGLEVKPLYS PHPVENNLFL FRALDWNGHR TYAHWADLTS
FEVLDKMTGE GPEDVPPDFA EAVKKSYMIP AAIKKLDIGG GMIHGVASDF MDDDSERLIL
AHLERDLTPE EMEIGSEASF GAVDVLIAGE QGHLQQKIFD YLREMFPESS EDEIRMLMNG
PIVDHNAGAI LTKKGQDADV VRMLLAGAVL FVDSELGISN QLGFGSFIGL KQVFEKDART
AGTYRAASHG SSLHIHRRLF RTFLKNNGIM EDFAERLKKI QFLRRTWLFG ENTSFSFLDR
LSKQVETTYL LDGAQIDLCS DAGLCLIEQG GVTVTNGAGG VKGELKAGDF FGEHFHTKEN
FENPVFSAKG DCALINIPRD EIFNAPIVHW KILETRRKRV RVLY
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