ID D0SVH2_ACILW Unreviewed; 481 AA.
AC D0SVH2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EEY89879.1};
GN ORFNames=HMPREF0017_01296 {ECO:0000313|EMBL:EEY89879.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY89879.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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DR EMBL; GG705059; EEY89879.1; -; Genomic_DNA.
DR RefSeq; WP_004279823.1; NZ_GG705059.1.
DR AlphaFoldDB; D0SVH2; -.
DR eggNOG; COG2114; Bacteria.
DR HOGENOM; CLU_047397_0_0_6; -.
DR Proteomes; UP000018425; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 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 20..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..362
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 481 AA; 56334 MW; ABD19C66AC4EE242 CRC64;
MQLDDWIQKE PHQFEYFHRM MGYIMLSVVL VVFHYTEPDT QYQLFVPFFL FLVLLITPKL
SRWLIYRHDY HIRRNILFLI DVIVISVVLA GVHLDLVLSL LGLVAVLYTA ISNKISFMMA
SLTSLIGITL FYLANILVFG FNNYFEPTSS ELTVLGFICL ITYFGVGSFY QSGRVQYMTQ
KKDHYFEQMN RYMEFANQLS RYAPVQLWQS IMKGESEAKI EYKRKKLTIF FSDIQGFTEL
SETLIPDDLA FLLNDYLRHM TEIAKNYEAT VDKFMGDAIL IFFGDPNSEG VEQDAKNCME
MALAMRQQMK LLRERWIKMG YPPLHIRMGI STGYCHVGNY GATHRMAYTI VGRDANLAAR
LQSAAEVDEI LISEDTHNLI KDDYLCAPKK PIFLKGIKAP VRTWQVMEKY ASQKVEYQRW
FDYEYKGFHL LLNLDEVQNF EYPELIHVLE KMIKRIETQQ KMTNSQGIVK LKLEDEVIEH
I
//
