ID A0A0R2TQT9_9RHOB Unreviewed; 438 AA.
AC A0A0R2TQT9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Guanylate cyclase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABR89_05285 {ECO:0000313|EMBL:KRO89214.1};
OS Rhodobacter sp. BACL10 MAG-120910-bin24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1655597 {ECO:0000313|EMBL:KRO89214.1, ECO:0000313|Proteomes:UP000051243};
RN [1] {ECO:0000313|EMBL:KRO89214.1, ECO:0000313|Proteomes:UP000051243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-120910-bin24 {ECO:0000313|EMBL:KRO89214.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO89214.1}.
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DR EMBL; LICH01000033; KRO89214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TQT9; -.
DR Proteomes; UP000051243; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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 CDD; cd00207; fer2; 1.
DR CDD; cd03467; Rieske; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00355; Rieske; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 119..250
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 319..434
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 438 AA; 49049 MW; 9D67A75FFFCD892F CRC64;
MKISFKPDNI STEISTDESI LTAALRNGIN HLHACGGSAR CSTCRIQVVS GLENCNPRNE
LELKLADTHN FSDDVRLACQ TTITGNVDIR RLLVDIEDLK FSTLNHKKLG PIGSHRKVAI
LFADIQGFTP MSERMQSYDV MYVLNKYFDF AGKIINANGG EINNYIGDAF LAIFGLDDAG
DEVFRAIKSG LEIQDNLITF AKTIEVNFNE EFKVRIGIHY GDAIIGMLGS RGTERLSVIG
DTVNTAARVE AANKESDTFM LVSETAYEEV RDRVEVHDYI RVKLKGTSER SSLYEISKVI
GDTNALKNLK TRVLEGTVWH RSFKSAEVLD KDKKVIQLFD KDLLIFRFGG ELKVVQNNCP
HMNLPLDAGQ ITDNGTILCP FHDSEFCIHT GEVKRWVENL PPMIPEKQAE LMKGIKPVPI
QLFQAQEIDG YIWISEPT
//