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Database: UniProt
Entry: A0A443SF91_9ACAR
LinkDB: A0A443SF91_9ACAR
Original site: A0A443SF91_9ACAR 
ID   A0A443SF91_9ACAR        Unreviewed;      1001 AA.
AC   A0A443SF91;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-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=B4U80_00317 {ECO:0000313|EMBL:RWS26175.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS26175.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS26175.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS26175.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
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}.
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:RWS26175.1}.
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DR   EMBL; NCKV01002987; RWS26175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443SF91; -.
DR   STRING; 299467.A0A443SF91; -.
DR   EnsemblMetazoa; LDEU005865-RA; LDEU005865-PA; LDEU005865.
DR   VEuPathDB; VectorBase:LDEU005865; -.
DR   Proteomes; UP000288716; 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; cd14042; PK_GC-A_B; 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; 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:SF501; 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};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          328..609
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          677..807
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1001 AA;  113598 MW;  54B64CD9430B71F3 CRC64;
     MLTHYFVYVL LSETDVLVDF ARLLVSGDFN DVIDIKDYVI ISVEDDDVYN PNNTEQFMVH
     QYGDHEIYEI PESLVAFQAV LLLAPSAPSN PYFYEFQNDV YERGHLPPFS IPKNEMIERQ
     IPIVAGLAYD AVMVYAIAAT SALERGENLA DGEKLLDHIK GLQYESILGF SVTIDNNGDA
     EGNYTLLALL QTERGSNKSM KPVGTFTHQN NSSLPLLHIE HPIQWIAGKP PVSEPQCGFY
     GELCTLKPNW LLISVCSLTG LLMLIASSFA FRHYRYEHKL ACLLWKVDIR EIKSLRRKCD
     YPIECSKSNI NLIEREKLHV KDRRSSPSPV SVRLEKGEEN EIEGNTICSD ENVGRYKGNL
     VFVRRVNKKN IDLTRTIRKE LIQMRDLRHE NINPFIGASV DAPNILILTL YCGRGSLQDV
     LKNEDLDLDN MFMASLVADL IKGMMYLHDS EIVSHGNLKS SNCLVDSRWV LQIADFGLHE
     FKAGQEKCGL EQEKQRYSSL WRAPELLRQE YPPAQGTQKG DVYSFAIVLH EIMTRAGPWG
     GCGDTVDEIR DKVTNPSNYG NSIHRPPVRG LKCADYIISC MIECWHENPE SRPDFKCVNE
     KLKRMQTGLK ANIFDNMIAL MEKYSSNLEA VVQERTTQLV GEKKKTEQLL LRMLPKSVAE
     QLKRGVQVEA ESFDCVTIYF SDIVGFTALS AESTPLQVVN LLNDLYTLFD EIIENYEVYK
     VETIGDAYMV VSGLPIRNGN THAGHIASMA IHLLTAIQNF EIKHKSNERL KLRIGIHSGQ
     CVAGVVGLKM PRYCLFGDTV NTASRMESTG EALKIHVSED CKNILDKLGG YILEERGLTF
     VKGKGEMRTY WLLGKCTNNG YCQSRRLRKD YNICLCRNEK ETSESRLSLQ SHTDTTSIGT
     IEDNTIAYND ADGTVVNIRK EKLNSKCYGE NNLNSYLKNE DSCIEKRYSD VSLPESSGYS
     SCLNLFQEYG KHILRDFHNN SFKFNRHKNE QKTKVTHNYL S
//
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