ID A0A0K0ENL6_STRER Unreviewed; 1101 AA.
AC A0A0K0ENL6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0001105300.1};
RN [1] {ECO:0000313|Proteomes:UP000035681}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SSTP_0001105300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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,
CC ECO:0000256|RuleBase:RU003431};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR AlphaFoldDB; A0A0K0ENL6; -.
DR STRING; 6248.A0A0K0ENL6; -.
DR WBParaSite; SSTP_0001105300.1; SSTP_0001105300.1; SSTP_0001105300.
DR Proteomes; UP000035681; 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 CDD; cd06352; PBP1_NPR_GC-like; 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; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF495; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-7; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1101
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005328370"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 550..807
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 879..1009
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1075..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 126695 MW; 5BDD91A6D746A238 CRC64;
MKVSNLFFLI ILSPLIKSQK NINLGFIFVK TDSEDGGVLG FTLAVGIVPV AIKRIMDEQL
LPEYNFTFKY YFDNCIEANS SGSTHKLIVH DKVDVIFGPS CSRSAIRSAN VAQFYQKPLF
IWGQVGTTQF ANINRFPNVY SATPVFYSLA LTVLDILKTF NWEKFVFLIV SRNSQRCSLM
FDDFVNVSNA YEGFKPAMVS SFKPSTPPLD IEYDAFINET IKRARIILTC FDSRIWKRNF
LLKMFDRGLN SPEYVHINME YAGRAFDSSR LDSNDKPIPF YIDSNEINDG RDNDAFEMAK
RMFILDTVRY NYDNLSFDRE IIKNVKDWPF YCNECNITNK SSLNKYSKYL GDSIYMWGIL
LNKSLNKYSN DVFNDPTLLR KDCMMNRESF TGKMHFDQNC IRLPLIQFTG LDSFGNQIPW
FSYSFSSINN FERKNTVSSD QFDKTIFENW NNSIPLTEPV CGYLHNHCPI NFFKVYLKEV
IIVGVIMIIL LILIIIGIIW YICKIRAQKE EELLKWKIPL SKLIKTSEKK DDTGSIHSSI
SKMTSNTNKY SIHEKIDTEN YSFYLYYDES VVGRKYKVIF NLIKNDYIEL NEMLSIDHQN
INKFFGMCAD ECLPMSIWRY CKRGSLHEIL QTEIPNFDSY FMMSLIKDIC NGLLYIHSSF
INFHGTLTSK ICLVSDRWQV KISNFSPKNL SRYEDISKEN LLWRAPEHLN DDFSIGSKEG
DIYSFAIILS EVISKGNFWN LNQREEGIDE LIYLVKRGDS PPIRPEIVVA PNIEVNPSLI
TLTKDCWNDS SKNRPTIKQV ESVLKAFNKD GPKNLMDHVF KTLEEYASTL QDEVNERTKE
VVEEQKKSDL LLKKMLPGEI VNKLKLGKVI EPENFDQVTV FFADIVKFTI LASKCSPFQV
VTLVNDLFVL FDNLIETLDI YKVETIGDGY LCVSGLPTRN GNMHAKEIAE LAIGFNKICR
NFFIPYLPNE KIMVRVGCNS GPCVAGVVGL SMPRYCLFGD TVNTASRMES NGKPGKIHIT
ENCSKLLNTI GGYIIEPRGE VIIKGKGVMN TFWLIGRVGE SNNNLINDND NEVRHEKNLS
NDKKNTETKE GMYREFNQND N
//