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Database: UniProt
Entry: A0A401NHU3_SCYTO
LinkDB: A0A401NHU3_SCYTO
Original site: A0A401NHU3_SCYTO 
ID   A0A401NHU3_SCYTO        Unreviewed;      1108 AA.
AC   A0A401NHU3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN   ORFNames=scyTo_0014173 {ECO:0000313|EMBL:GCB60442.1};
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB60442.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB60442.1, ECO:0000313|Proteomes:UP000288216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCB60442.1}.
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DR   EMBL; BFAA01007507; GCB60442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401NHU3; -.
DR   STRING; 75743.A0A401NHU3; -.
DR   OMA; LYQGNHV; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; -; 2.
DR   Gene3D; 6.10.250.780; -; 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; IPR001170; ANPR/GUC.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF500; GUANYLATE CYCLASE 2G; 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   PRINTS; PR00255; NATPEPTIDER.
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.
PE   3: Inferred from homology;
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:UP000288216};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        326..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          863..993
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1072..1108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1108 AA;  123649 MW;  680C88ABBD435C37 CRC64;
     MQLAIETINS DPFFMLNCTL DFVYADSDCD PKVSINAFIS QVQKYNISAL FGPACSEAAE
     ITGLLASQWN IPIFGFVDQT PMLDNFLVYD TYMNLLSPPQ RMADVLTKTL QFFGWKYIAL
     IGGTARNSTW DKIDELWEMM VKMLETNFII TARAKYDTGN SALHQENLKQ IATVARIVIL
     ICTPKVARSI MLEAQQLGMT SGKYVFFILH MFEVTGEMDN FWTSALLDGK DEIALNAYNS
     AFLVALKFYS EYSHFNFLQE VYRRLKGAPF NSELSSETEV NSYSAYLHDA VMLYAMALQE
     MLKAGKNPFD GRALIKHLKG FGKGRFYGNT LVTVVAVLLV IAFVAAAFIV FLLVKKRKSQ
     NQGQDMWWKI KYEDITILKE SKKHVDALLG ATTSTKEVGS IESKTNVSSH QNYGSRDKLG
     NRVVYSTIGL YQGNYVAVVH LDGSTFPDMS KQSILQELQM MRELRHENLV TFFGVCTDLP
     HRCIISQYCK KGSLKGMVFL HDSPLKSHGN LQPKTCLVDS GMQVKISGFG LWEFRYGTKR
     KVVVTEEVNY EELYWTAPEL LRLKEYPLNG TQKGDGEFGE DGVFGEQGEF GAQDGFGEQG
     DFVEQGGFGE HGVFGEQGNF GELGVFGEHG EFGEQGEFGE QRDFGDQGVF GDQGDFGDQG
     DFGEQGEFGE QGEFGAQDGF GEQCGVGEKG VFGEQGEFSE QVRFAEQGGF GEQGWFGEQG
     EFGEQGEFGE QGGFGEQEII NRIINPETQL RPTLAAEKCN DQIFTLLQAC WDECADRRPN
     FRSIKQALRR ASPEGEVSIL DNMVDKLEKY ATHLEEVVQE RTNQLMVEKG KTDKLLSNLL
     PRFIAEQLMQ GNPVEPEFFE CVTIFFSDIV GFTNLCSSST PLQVVDMLND LYSLFDDIIM
     SYDVYKVETI GDAYMVASGL PIRNGIQHAG EIATMSLHFL SAIVRFKIRH IDNVQMKLRI
     GLNTGPVVAG VVGTMMPRYC LFGDTVNVAS RMESNGRPLK IHISHSTAEA LRALGGYDLV
     ERGTIKVKGK GNQATYWLKG KEGFKEPLPK LDYNVEEDLK DSLETDEELA AFAASGEPGN
     SASDPPEDTC TRPRGYSLEK NTVEDKTF
//
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