ID A0A0T6AQT1_9BACT Unreviewed; 500 AA.
AC A0A0T6AQT1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
GN ORFNames=XU14_C0014G0005 {ECO:0000313|EMBL:KRT77353.1};
OS Armatimonadetes bacterium CSP1-3.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT77353.1, ECO:0000313|Proteomes:UP000051026};
RN [1] {ECO:0000313|EMBL:KRT77353.1, ECO:0000313|Proteomes:UP000051026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT77353.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT77353.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDXQ01000014; KRT77353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AQT1; -.
DR PATRIC; fig|1640515.3.peg.739; -.
DR Proteomes; UP000051026; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11635:SF168; CAMP PROTEIN KINASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 366..486
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 500 AA; 55244 MW; 6DBA8766F9E89C9C CRC64;
MAAEMAAAGT RFGFGARAPF KMPDGATRLV PVFYWKGEPY PVILPSIRDP RLHFAAIIWG
LQIMGQVWLR FETTPALIIS TIFVAAIFEI YLFAETQKVI QFPSSAMQAA NSLTWFVKTN
GTRWGDWFSM NGFGFLWLGA FIAIGQKYII KLRGEQVFNP SALAIFTLLV LFPRHVHPTP
LTWGVSWGGQ LFLVLYLAIG VYYVLRSFRL TLIPFTFLAA FAPAAFVTSQ IATGALGAGA
REGLLYWLAV LFSPEFMLFS FAFITDPKVA PRSERGRMVY GGLNGVLWAL AMLFVLFTPG
EAGYAQFGAL NLSLRDQYII ETIFIGNLLF IQLFLRRWMD ARWPARRPMD PVELIWGDSG
GFIQETFKGF SEQQARVLAA KFAREAVPAG QVIVHQGDAA TRFYILTKGE AEVVVAEEGG
QERKVASLAP GNYFGEIAIL EDTARTATVR AVTECTLIAL DAETFKAAVA QSVAAGEDIR
KELQRRVTEA GLVLAPAPQA
//
