ID A0A2G5TGN5_9PELO Unreviewed; 948 AA.
AC A0A2G5TGN5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN Name=Cni-gcy-33 {ECO:0000313|EMBL:PIC26437.1};
GN Synonyms=Cnig_chr_V.g19012 {ECO:0000313|EMBL:PIC26437.1};
GN ORFNames=B9Z55_019012 {ECO:0000313|EMBL:PIC26437.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC26437.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001436};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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:PIC26437.1}.
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DR EMBL; PDUG01000005; PIC26437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TGN5; -.
DR STRING; 1611254.A0A2G5TGN5; -.
DR Proteomes; UP000230233; Chromosome v.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 6.10.250.780; -; 1.
DR Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR PANTHER; PTHR45655:SF8; SOLUBLE GUANYLATE CYCLASE GCY-33; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 437..567
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 619..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 107092 MW; C5F39204FB7B5EDB CRC64;
MYGLVIEGVR FMIQENWGPQ ILLQVQKLTS LSEKSVSTHD QYSEHVVPQM FKAIHEITGT
PYEQIGVLAG RFFVQFLIRN GYGDLMNVMG RRFSDFIKGL DNIHEYFRFS YPKLRAPSFY
CKSESEDGLV LHYRSRRTGY LSYVIGQLVE LARVFYQLDI GIQVLKKKEK GRFTFVVLKI
SFDNVGLGHD LKLKERVKNL NEYLPVDTKS FLQMFPFHIA FNKKLEILMA GQGLLNLMPN
IQGLLMTDVF DLQRPCIKFT AEGILVHQNC VFQIESLHPV LKQSEENITV QINDIVEDKV
SLEKKTVMDN EYESLPYVTL RGPIIVLKAS DTFLLLATCV VDTLDTMFKM GLYLNDFGES
DCNREIIMAT IQKSDTLKTM LENEKRRSEI LTEMTKEISE AKKTARGLLT QMMPYEVAQT
MMRSGSVEHC EAFECVSIGF IRVCDFAKIS LFIEAFEVVN LLNTIYSHLD EIVDTHGVYK
VETIGESYMI SAGCPYRDEH DAEMVADCCL EMVAHIKSFE YQSHDAVKKV LIKCGIFTGP
VVGGVVGVRT PRYCLFGDTV NTASRMESSN QTAMTIQVGQ RTKDRVEKQA SGSFRIKPKG
NIFVKGKGDM RVYEIEKKKG RPRYKKAEPL RKKMVAEKKE AEEMLDEDNE GHRSSTLSRM
SLGESIDSSS SRRGSLSGSQ LELNKTIAHT IEVTSKASEA LDLNMQDENN RPPTWSETHA
QDIRRPRKTE SKITLHSRLS SSDLAGSRSE TSKDLENETP RPTSSELKEV NRIRAEARAQ
EEEEARKATE EMKIAEEGKE EDRASEAATS LVDNESVISQ NNITFSEMPS DSIPHEDRAS
LPSAEPSEAG DAIKPKKKLE QKDSNSSMSS LEDITTVSAK PVPTRRLLGE RGSKDEKKRS
SMASSSVTSS SAHSHSTKSR RDTRDKSRCK CEDIRADNKL KTKVCSIM
//
