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Database: UniProt
Entry: A0A0N4ZS00_PARTI
LinkDB: A0A0N4ZS00_PARTI
Original site: A0A0N4ZS00_PARTI 
ID   A0A0N4ZS00_PARTI        Unreviewed;      1136 AA.
AC   A0A0N4ZS00;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001128200.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001128200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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};
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DR   AlphaFoldDB; A0A0N4ZS00; -.
DR   STRING; 131310.A0A0N4ZS00; -.
DR   WBParaSite; PTRK_0001128200.1; PTRK_0001128200.1; PTRK_0001128200.
DR   Proteomes; UP000038045; Unplaced.
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; 3.40.50.2300; -; 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; 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   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF485; RECEPTOR-TYPE GUANYLATE CYCLASE DAF-11; 1.
DR   Pfam; PF01094; ANF_receptor; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          514..867
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          937..1067
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          874..901
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1136 AA;  128956 MW;  3BFC770CDC178BB7 CRC64;
     MINCNLCRRY INIFLLYIIL YYSYGVILAQ TILEAPSVGK PLSMNVGVIY DNVWTDNVKT
     FVTNSINNIY NENSTLLFKI NPIFADDIPS CKETIGVGEG AYLLSKIYFN NKNTNSGNPG
     VQTFIGPTCS NDLQISSRIS KQLKLLEFNI WNEYEDEAFD NEIVQMSTES GTNIAANLYT
     VLNVLNWKKI AIIYCNECIS RFKGNGVSNE IDLTLQTITD ILEVNSIEVR ETIKLNSAQI
     NDMTFMINIL KNMKTKARIF VPILGTKLSN YEVYMKALVA NDMKTSSFMT IIFRLFEYPL
     LNDPWVLANG SYDESILQLY DRTIVLQNNY YSPEEVVSFK SKYSLTINDN SILFYFQLFE
     TAYTYMYMLT GAYIHTSNNI SLFSSTDYSV YLIQYMRNNK IEGPYGSIYF DNSNQRVSPF
     TVEVIENSPR KKGLNSLISV NIDELCVYEG TNINDNKNCL ALTGVITNMD ASILEDLPQD
     MPSCGFDGEL CDQTGTIIII VAVIITVILV IVVFIFVRRM RNGESANMPW AIEPESLEIL
     ENDCQMYGSS GGIQSNLSIH SIHQQFESKV KLREMLRNWQ LGNIDGTGYV LVEPYILKEK
     MVYDKQDMQV LFNLRQTIHD NLNPFIGICV DNKANEFCFL WQHAMRGNLA SMLFNQQNKM
     IKDVETTKDF TRAFVRDILK ALDYIHSSSL SYHGGLTTSN CWVDSHWILK VGGCCTTRML
     LKWKSLGIIS GKNDLPIILN SDLHYFAPEI RKAIKNNIHA NKGERLEVSN NDGQKQDMYS
     FGIILYEMLF KKRVVEIDDS YGITKNDYDP GIFNVQAEAL IPLYPVIPEE HKEVHPDLIS
     LMHKCYNGNA SLRPDSNMAR KITDATLKMP GSLVDQMIKN LEQYTNNLEN LVAERTGELE
     KEQKHAEQIL LELIPKSVAE DIKHGRPVEA KSFKYCTIMN SDIVGFTSLC SGILPMEVVE
     LLAGLARNFD RIITDNKCFK IETVGDAYVV SCGVPEPSRY NHVKNIANMT LQMREFLLGY
     KVPHRPEKHL QCRFGFNSGP VFSGVIGLKA PRFCLFGQTA SVASKMEQNG VPDHIQMTLK
     SYQLLSEKFP EFICTPRGGV RIEGIGTLLT YFLDSKDPSK ARTDLVSWDD TDIGDE
//
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