ID D5BA42_ZUNPS Unreviewed; 348 AA.
AC D5BA42;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Putative diguanylate phosphodiesterase (EAL domain) with Response Regulator Receiver modulation {ECO:0000313|EMBL:ADF52340.1};
GN OrderedLocusNames=ZPR_2015 {ECO:0000313|EMBL:ADF52340.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF52340.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF52340.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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DR EMBL; CP001650; ADF52340.1; -; Genomic_DNA.
DR RefSeq; WP_013071443.1; NC_014041.1.
DR AlphaFoldDB; D5BA42; -.
DR STRING; 655815.ZPR_2015; -.
DR KEGG; zpr:ZPR_2015; -.
DR eggNOG; COG0664; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_70_2_10; -.
DR OrthoDB; 9127033at2; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF1; TWO-COMPONENT RESPONSE REGULATOR ORR33; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 1..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 160..242
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 273..342
FT /note="HTH crp-type"
FT /evidence="ECO:0000259|PROSITE:PS51063"
FT MOD_RES 50
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 348 AA; 39533 MW; 0115EEA02D2A3538 CRC64;
MILLIEDDMV LRENTAEILE LQDYEVITAP NGKIGIEKAI EHIPDIIICD IMMPEVDGYG
VLQSLSSNTK THHIPFIFLS AKTEHKEIRM GMNMGADDYL TKPFDENELV EVIETRLKKA
NLVSQVFVAE SSKKDPAEGD IRNLNELKNF FDDEGEVEEF KAKDSIFEVG DHSNYVYLIL
EGTIKTFQRD EEGKELVTGL YKPDDFLGFT SLAENYPHQE SAVAVKDTKL VKILKYKLKE
ILEQNRNVSL ELINMLTDNL SVIKQQLLIM AYSTVRKKTA QTILQFAEIL GKKSQEDIRI
TRSDLASVAG IAIETLIRTL SAFKKEGLIE IEGRVIRVLD LHRLELVD
//
