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
//