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Database: UniProt
Entry: A0A0S8F6Z7_9GAMM
LinkDB: A0A0S8F6Z7_9GAMM
Original site: A0A0S8F6Z7_9GAMM 
ID   A0A0S8F6Z7_9GAMM        Unreviewed;       586 AA.
AC   A0A0S8F6Z7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN   ORFNames=AMJ59_22145 {ECO:0000313|EMBL:KPK56512.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK56512.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK56512.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK56512.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK56512.1}.
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DR   EMBL; LJTI01000116; KPK56512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8F6Z7; -.
DR   PATRIC; fig|1703405.3.peg.5129; -.
DR   Proteomes; UP000051321; Unassembled WGS sequence.
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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.40.50.10070; TolB, N-terminal domain; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF52964; TolB, N-terminal domain; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   4: Predicted;
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          7..121
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REPEAT          454..487
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          491..524
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          168..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  64609 MW;  75CF603E306CEB45 CRC64;
     MERRLAAILT ADAVGYTQMM ARDEVATLET LDAYRSIMGG LIKQHGGRVV DAVGDNLLAE
     FPSAVDAVQC AIEIQRQLAE NNAERPEDRQ MRFRIGINVG DLIVIGDRIV GDGVNVAARI
     EAEATPGSVA ISRAVLDQVD GKLPLNLRDK GEFSLKNVPR PVRIYEIEHK PDDEERDPDD
     SRAGIEPQVP GFGGRSAIAV LPFRNLSADP NQEYFADGLA EDLITSLAAL RVYPIISRNS
     SFAYKDKPTD PRQAGKDLGA HYIVTGSVRK VGDRIRVNAE LVDSGDGRQV WSGRYDREIS
     DIFEVQDEIT ASIAGAVGPA LFQSEMLHAI RRAPKNADAW DCVHRGMWHL YRYTREGVAK
     ARAWAARALE LQPDSATAYC VIAFSHMYEV IYQWVDSREE PLRAAMQAAE HAVAADRDDP
     MSLTALGFAC SLCGHRDRAV AVLERAVQAN PSSALAFWSL GATLTTAGRP DEGIPMVEKA
     MRLSPQDPLM NEFLFTIGSA HFMAERYDEA IQFAQRSLDI KSDQPGAWRI IAAASALLGK
     LDEARRALGQ MIRLAPDLTE ERLRVFLRET DVERYVRGLR LAGWSG
//
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