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Database: UniProt
Entry: A0A2A2LFU5_9BILA
LinkDB: A0A2A2LFU5_9BILA
Original site: A0A2A2LFU5_9BILA 
ID   A0A2A2LFU5_9BILA        Unreviewed;       794 AA.
AC   A0A2A2LFU5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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   ORFNames=WR25_04471 {ECO:0000313|EMBL:PAV85020.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV85020.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV85020.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV85020.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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   -!- 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:PAV85020.1}.
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DR   EMBL; LIAE01006806; PAV85020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LFU5; -.
DR   STRING; 2018661.A0A2A2LFU5; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF355; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-10-RELATED; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00220; S_TKc; 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; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          217..497
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          568..698
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          752..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  89423 MW;  43C7CDCFDAC070DE CRC64;
     MLNTQENPVL NLQKYMSINE EADNVNELID NVAKDIEVTS QVLVIGSDFV DLYGVLQKLD
     LHKISTRNFI TVLVAPTGVL KITANDALRR YLNSAGVYVL APIINISENF TIKISTSINA
     TGPILDLDQI EEPALLYSAC YAFCVARKKY DSDTVDNYYK TLAGQEYTND LGTFKFDQNG
     VVLRDYQFMY LRNDKRGNDT VIMTVKAQYA ETCGPHYQCF TVRGPGGKTT KPSSHETLTS
     KRRTITSYAL MGTVKAEFLF YRQFKRIRWT KPELRYLTEL KALNHDNITK FIGLSCNDSA
     DVYILYGLVE RATLEDFIYD SDFSLDFTFK SAFARDILRG LQYIHKSSIV AHGMLSVQTC
     MIDANWVLKL TNFGVSSLIH NFMTDGTLQC TTSIALEELL REIAHCATAS VPRGTQKGDI
     YSLGMVLYQM VYRMQPFPKS SSAQELIVGI IDRRMKPERL EASAEENKLV DCIMLCFNEP
     EKRPKAREIA NAVSTVYTAA KGNLVDQMIR MNEKYALNLE KLVKERTDLL VAAQEQTDRL
     LNEILPKSVA QVLKLGGVIP PRSYDSATVL FAQLCDFPLL VGKSGPDDVI NFLNDVFDKF
     DNIIRKHDAY KVETTGETYM VVSGVPTENE GQHVFEIAEI SLEIRETAMN YVVEHCPSFK
     VRTRIGFHAG PIAAGVIGIR SPRYCLFGDT VNFASRMQSN CPPSQIQTSE VTANILMKSE
     EYSLVQRGIV HVKGKGNVNC YWLNEHIHDL SNEEPEGNIH KSDNENRPKT TQQKLEDQNA
     TPLPKSLIQN NNQS
//
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