ID I3CD04_9GAMM Unreviewed; 1007 AA.
AC I3CD04;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=PAS domain S-box {ECO:0000313|EMBL:EIJ41497.1};
GN ORFNames=BegalDRAFT_0581 {ECO:0000313|EMBL:EIJ41497.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41497.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41497.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41497.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; JH600070; EIJ41497.1; -; Genomic_DNA.
DR AlphaFoldDB; I3CD04; -.
DR STRING; 395493.BegalDRAFT_0581; -.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_10_6; -.
DR OrthoDB; 6115136at2; -.
DR Proteomes; UP000005744; 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 CDD; cd06225; HAMP; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..385
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 750..880
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1007 AA; 113563 MW; FAEA03E86A2B9433 CRC64;
MVIMGEPFVF KNLKLKSKLL LSFFIVTCIS TISTTIVSIY YFTDKIEVEA LENMKKNMRV
AYLIYQNKVA EIEEMTHTLA ADRSLQVLVN FSIKNKINQY IGDTLKNKQL SQIIIVDPEK
KLIAQTTHQN YLALEKEHNF EKNALVDYVL SQHKTIAATE LVEVDNLQKF IAISVASPLF
KSEVVRSANA DIASKNQPEI VGIILTRYVL NQNTRVVSDI ENLLELTAAI YYNAEAISFT
TAHLENKPQI KAESYFKALR IRQNVQDMDV RYGGQLAEYK TINDINNNPI ALLGVSVSAD
KYVETTKQAV INLVVLMLLC IIVASIFGYL LARSILIPIY KLLNGVERVT SGDLSYEIIM
DLKDEFGILA HSFNSMSRQL QELFNTLEQR VQDATRKLQN TLAHMTAIID NMADGLLVTD
KEGKIIRYNP AFLAMFPERR DMLGKDCQEI FNDAEAAELA KKVMNSIGEV YGAEIRLVDN
RIGQAVATAI IQKDTLSDTS EYVGSKYIGS VILIRDITKE KEADRVLKNT VETLTRVGTA
LSGENSLVKL LELFVSEARS VTNADGGTLY ILEDEQLNFE IIQNKSLNLF LGGAYAQPIH
LPAINIQEQK YVAYSARTQQ ILTSKADFKE DFDPERDKDI YNLFKGYVIQ ELLVVPLLDR
MQNAVGVLQL INPIDPKTGD SIPFANNQIE IVFSLASQAA VAIENVRNYE KIEQKNIAFK
RFVPTEFLLR LGKKEIEDVV LGDASQENMS VLFSDIRSFT TLSETMTPED NFHFLNDYLD
FIGPNITENG GFIDKYIGDA IMALFSGSHV GVADDAVLAA VGMLNRLQEY NAYRQNNGEK
PLSIGVGIHT GALILGTIGF ESRMESTVIG DTVNLASRME GLTKQYGITI GITSPTYQQL
QNPERFLIRE IDTVQVKGKE EAITVYEVFD VDPQPLRDMK VTYLNKYMQA LECYKRYQWQ
EALEQFLELK TVLQGDKVIN IYIERCQHFI TTPPNESWRG VTRLDEK
//
