ID H2L2D1_CAEEL Unreviewed; 947 AA.
AC H2L2D1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN Name=gcy-33 {ECO:0000313|EMBL:CCE71576.1,
GN ECO:0000313|WormBase:F57F5.2c};
GN ORFNames=CELE_F57F5.2 {ECO:0000313|EMBL:CCE71576.1}, F57F5.2
GN {ECO:0000313|WormBase:F57F5.2c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCE71576.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCE71576.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCE71576.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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}.
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DR EMBL; BX284605; CCE71576.1; -; Genomic_DNA.
DR RefSeq; NP_001256392.1; NM_001269463.1.
DR AlphaFoldDB; H2L2D1; -.
DR SMR; H2L2D1; -.
DR EnsemblMetazoa; F57F5.2c.1; F57F5.2c.1; WBGene00001553.
DR GeneID; 179644; -.
DR AGR; WB:WBGene00001553; -.
DR WormBase; F57F5.2c; CE20887; WBGene00001553; gcy-33.
DR OMA; YTAEKVR; -.
DR OrthoDB; 2898719at2759; -.
DR PhylomeDB; H2L2D1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001553; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; H2L2D1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070027; F:carbon monoxide sensor activity; IDA:WormBase.
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:0070026; F:nitric oxide binding; IDA:WormBase.
DR GO; GO:0019826; F:oxygen sensor activity; IDA:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0070482; P:response to oxygen levels; IMP:WormBase.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:H2L2D1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 439..569
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 641..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 106999 MW; 947968427B146D64 CRC64;
MYGLVIEGVR FMIQENWGPQ VLLQVQKLTS LSEKSVSTHD QYSEHVVPQM FKAIHEITGT
PYEQIGVLAG RFFVQFLIRN GYGDLMNVMG RRFSDFIKGL DNIHEYFRFS YPKLRAPSFY
CKSESEDGLI LHYRSRRTGY LSYVIGQLVE LARVFYQLDI GIQVLKKKEK GRFTFVVLKI
SFDNVGLGQD LKLKERVKNL NEYLPVDTKS FLQMFPFHIA FNKKLEILMA GQGLLNLMPN
IQGLLMTDVF DLQRPCIKFT AEGIMVHQNC VFQIESLHPV VKQTEENITV QINDITEDKV
SLEKKTVMDN EYGLESLPYV TLRGPITVLK SSETFLLLAT CVVDTLDTMF KMGLYLNDFG
ESDCNREIIM ATIQKSDTLK TMLENEKRRS EVLTEMTREI SEAKKTARTL LTQMMPYEVA
QTMMRSGSVD HCEAFECVSI GFIRVCDFSK ISLFIEAFEV VNLLNTIYSH LDSIVDTHGV
YKVETIGESY MISAGCPYRD DYDAEMVSDC CLEMVSHIKS FEYQSHDAVK KVLIKCGIFT
GPVVGGVVGV RTPRYCLFGD TVNTASRMES SNQTPMTIQI GQRTKDRVEK QASGAFRIKP
KGNVFVKGKG DMRVYEIEKK KGRARYKKSD PLRKKMVAEK KEAEELLDED NEGHRSSALS
RMSLGESIDS SSSRRGSLSG SQLELNKTIA QTIELTSKAS AALDLNMQDE NNRPPTWSAS
HSQDIRKPRK TESKITLNSR LSSSDLAVSR VETSKDSDGE TPRPTSSELK EVNRIREEAL
AQEKEEERTT KEENQKIEEV GEDHVSEATS LLDSEVSHGD NNISFSQMPS DSIPHEDRTS
LPSATPSEIG DAISKKKLEK EDSNSSMSSL DERTTVSAKP TTTRRLLNQK DLEKEKKRSS
MAGSSVTSSS AHSHSIRSKK DTRDKSRCKC EDIRADNKLK TKVCSIM
//
