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Database: UniProt
Entry: J9ESM5_WUCBA
LinkDB: J9ESM5_WUCBA
Original site: J9ESM5_WUCBA 
ID   J9ESM5_WUCBA            Unreviewed;      1218 AA.
AC   J9ESM5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=WUBG_03901 {ECO:0000313|EMBL:EJW85188.1};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW85188.1, ECO:0000313|Proteomes:UP000004810};
RN   [1] {ECO:0000313|Proteomes:UP000004810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Wuchereria bancrofti.";
RL   Submitted (AUG-2012) 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   -!- 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:EJW85188.1}.
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DR   EMBL; ADBV01001271; EJW85188.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9ESM5; -.
DR   Proteomes; UP000004810; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
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; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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   Kinase {ECO:0000313|EMBL:EJW85188.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transferase {ECO:0000313|EMBL:EJW85188.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          564..869
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          941..1072
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          878..909
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1218 AA;  139227 MW;  146BC9392BD66060 CRC64;
     MNGILNNSKL MLEKAADEKL NSDRSILISY LAAISQFPKN LFDSLKLLSE ANNIETTAER
     DKNYGYLSKC FRTDFEGSMI SGALQVAVDD VNADPELLPN HKLVLDFFMQ HWAQGAKVFI
     GPEMNCRTEA TMAAAQNLPI LSYKCKDEMM SDKSKYPTFA RTVPTETEIT AALIALFKHF
     EWRKFSVIYE RNVANEELFR SIKSTIEKQN VDLEVSDTQY VIINVSIVPH PFSEIERSNI
     KQIISDTYAS TRIYLTFGNV RLFRRILLEM GAQGLMESGD YALIYLDPDY NWLNTYHAMN
     NHFFRDTLLS VKQSWNDLNS QDRKVVNFSK FALAIIPTPV QLNAPEFIAF WRKANHYLSL
     FGVKQSNTAT SIKANRFACY LYDAVKLYAS ALTIVLNETA NEQLSVGYDP ISDGKRIIGH
     ILGRVYRSIQ GFDMHINSNG DAQGNYTLLS LQEIEPVLDM DNPDYYPLNY GLDISADFVH
     DFTGDLPLLR FKRDIQWPTG FAPRDEPICG FHGKMCKKGT FFNIHLIIHL VLLRYILDRY
     FRLVVNSFPD SSHCILSYKF EKELSNVWKI DQREIEKIVQ CCESAASLYV VENNQILLQN
     DEECNQEKRW PGLCGVALYK GAVVSIDEIT YPRKVKELTR AAKLEMRIMR QLHHDNINSF
     RGIVIGSSSI CVVREFCARS SLMDILRNHD LKLDHLFIAS FVEDLVKGMI YLHESDLGVH
     GNLKSTNCLI TSRWTLQIAD FGLHEIRDGQ EWESDDFMWE NFLWTSPELL RKSGCVHAVK
     GTQKGDAYSF GIILHEIITR QGPFMMLRNS DLTAEEVVLN VLNNVDYRPS CDGLPAASYV
     INVMTLSWSA IPANRPDFRT IRHKLKPMLE PIYKRNIMDH MMVMMEKYQN QLEDLVDERT
     TELREEKRRT ENLLQRMLPV SVAQQLLAGL DVVPESFSSV TIYFSDIVDF TKISGISTPL
     QVVEFLNKLY TLFDHIIKQY DVYKVETIGD AYMVVSGMPE ARPVEVHAEQ IGMMALHLLA
     AVRNFKIPHL PQEQLRLRIG IHTGPCVAGV VGKTMPRYCL FGDTVNTASR MESNGCPLKI
     HCSEQTQDVL ARIDGFELKK RGTLQIKGKG LMTTYWLTSR RNVTFAIKDE CELLLDEKLA
     QNIFPRMSVR HRRLSTSAIS KGSSISLAGK EPSLLRRIIE RATFLRNDNL EFCSGYIHES
     SSVNSNRPQM TCSILPYR
//
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