ID D8EZS0_9DELT Unreviewed; 1023 AA.
AC D8EZS0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Adenylate and Guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EFK11009.1};
GN ORFNames=NPH_4997 {ECO:0000313|EMBL:EFK11009.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK11009.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK11009.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK11009.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
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:EFK11009.1}.
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DR EMBL; ADZZ01000144; EFK11009.1; -; Genomic_DNA.
DR AlphaFoldDB; D8EZS0; -.
DR OrthoDB; 9806735at2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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; IPR007890; CHASE2.
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; PF05226; CHASE2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM01080; CHASE2; 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 Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 606..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 718..877
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1023 AA; 115968 MW; 4587D9194EA7988B CRC64;
MLKKAVIVLL IGLSVFAVMH FISSKTRLFL GIERNLLNGL FFLREPEVHE TNPLVSQEVI
LLGFDEDAIA SIGKWPWKRD VHARMLNNLE KFSPRTVMFD VVFVKNETIP PFLSKKLTPE
PKLLLKVEKA FNEMDQAFAE ALKEYNNVFL DVQLVENPRP DLPKAYLNRI FFNEQILKDY
SLPLKNNQSL LVFHSLEPVL SEFISSAHPA IVNVLADDDD VTRMFPLYYT YKMSDGTVRN
LFTATLLLVK QYYRVHNEDI SITPDRIVLS NAKIPILDPL THQLHVFEKD FNWVKHKILN
PVAPEGYPYN QNLFRLLLNR LKMKIAFDKK PAPFPIHVLK GTGGFEILEG WEVFDAAREG
KAETVQFVVY EKGTIEINTP VPGFSYINYA GTEKRYIMDE KTGVPKIYTT VPTKSYGNVH
AMASLPEIPL LNASGRIEAD YETRPLEKWY MAFCEKRSYT AYHQAAGDLG DDVQDDVRLK
DYLNRNSEIG KYFFYSYYFS NADAPAGMLR ALIEQYPGFG TEIGQDPADF LTDERVVQDL
MATYMDQFQL YYHKFVFAGA TARILGDIQQ TPYGAMNGIN TLINAFNTII TQNQLTFSAH
VPNLDLLLLL GLCLFCSFAY GFTSIRFSSV IFILLVLGTL TISFALFSIK NLVLTTTPLV
FSNVLIFGGI IVLKVLTEQK DKKFLKTTFS SYLAPEIIDE MYRNKTMPTL GGEARPITAY
FTDIQGFSTF SEKLTADQLV ELINEYLSAM TDILIGNMGT LDKYEGDAII AFFGAPMDVP
DHALRACRVA VSMQGKLAEL RRKWAKEKQD SHEPNRNTKG LAAHEWKTGD KWPLIVHSMK
MRIGINTGEI VVGNMGSAMR MNYTMMGDPV NLAARLEEAG KQYGVFILVS EDTLKCEIAD
DRGTLKQVFD MVEVRFIDTI AVVGKSEPVR VYELCAMKGG LTANEKELIA VFDRAMGHYL
KMNWNGAIRD FEKASNMERI PDGKTTPSTT PSRVYMDRCR TYKENPPVAP GEVWDGVCRL
TKK
//