ID A0A3P7IB59_ANGCS Unreviewed; 1081 AA.
AC A0A3P7IB59;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN ORFNames=ACOC_LOCUS12384 {ECO:0000313|EMBL:VDM63969.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|EMBL:VDM63969.1, ECO:0000313|Proteomes:UP000267027};
RN [1] {ECO:0000313|EMBL:VDM63969.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM63969.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 ECO:0000256|RuleBase:RU003431};
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYYA01005014; VDM63969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P7IB59; -.
DR STRING; 334426.A0A3P7IB59; -.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 506..805
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 874..980
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 814..845
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1081 AA; 124684 MW; 037D0F3F096F2521 CRC64;
MIDYCYYCLQ ILFIFLFIFR VNVTFFCVIR TQYAPRVSST LVINSVGVSI ATMPNLEFAR
DEINANPDLL PDHRLSYIFD NTCGKERQST QYFMEHWKMG ARVFIGPEMN CRTEATMAAA
QNLPIISYKC KDQTVSDKKK YNTFARTVPA ETDIVKAFIA LCREYKWKKF TVIYEEHPAH
EELYQALQNV SKVVRFSEVQ SEKLIDSVIE QTKDITRCEC LAKSVIALYV TFGNVRLFRK
ILMSMGKLGL TDSQQYLLIY LDADYNWLNV YHAMNNHFFR NTMIDLQSSW DVSNSSDHRI
IGYSRAALAI IPTPVELNSE RFKKFWEQAV KDLVNFGITK HEHTWSIKVN RFACYLYDAI
YLYARALNEL IEETSEQQAH GYDPTRDGAA IIRKILNRKY SSMQGFDMRI NANGDAKGNY
TLLAWQKVEP VRTKDDGNYY PLDHALDITA MFVDEGDGQN NMPKLVFHKP IIWLDGPTRD
QPYCGFHGEL CRDYGGYISV ISFMLFAVVL IGGAISAGFI YRSRKFEKEL AMIWKIEVRE
VQHLMEDNSS TISLFPDGND MVDHPWYTGT DGEKKGSGLR GVAYYKGTLV VLKELTFSRK
PRELTRQAKI EMRVMRQLTH PNINSFMGII LCPYSICIVR EFCAKGSLMD ILRNREFKLD
HLYIASFVED LINGMVYLHD SELKVHGNLK STNCLITSRW ALQVADFGYH EIREGRTQKG
DVYAFGIILH EIFTRQGPFQ IFAKNEVQIS EIVARVAGGT CTRPSLSCIE GQDYVTDTMR
LCWSEYPENR PDFKNGIKHK LKPMFAGIYK RNIMDHMMVM MEKYQNQLED LVDERTAELR
EEQKRSQHLL QRISVAQQLL DGQDVVPESF PSVTIYFSDI VGFTRISGES TPMQVVTFLN
KLYTKFDRII QKYDVYKEIA LMALRLLRAV RNFKIPHRSS EQLMLRIGIH TGSCVAGVVG
KTMPRYCLFG DTVNTASRME SNGERKRYLT LKIHCSQPTR DVLTTITGFV LEERGTLTIK
GKGQMTTYWL LDAEGYEFSD DEDYEEEEPT LAPEIFPRNS TFRAMRGSGF GPFFFLTALF
M
//