ID   A0A3B4T8I5_SERDU        Unreviewed;       815 AA.
AC   A0A3B4T8I5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000002272.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000002272.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   STRING; 41447.ENSSDUP00000002272; -.
DR   Ensembl; ENSSDUT00000002334.1; ENSSDUP00000002272.1; ENSSDUG00000001764.1.
DR   Ensembl; ENSSDUT00000002372.1; ENSSDUP00000002307.1; ENSSDUG00000001764.1.
DR   GeneTree; ENSGT00940000163785; -.
DR   OMA; ACCERFD; -.
DR   OrthoDB; 2898719at2759; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR038158; H-NOX_domain_sf.
DR   InterPro; IPR011644; Heme_NO-bd.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR042463; HNOB_dom_associated_sf.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR45655:SF10; SOLUBLE GUANYLATE CYCLASE 88E; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}.
FT   DOMAIN          491..619
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          289..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..454
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        289..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  93082 MW;  50C98BAA92125F22 CRC64;
     MYGLYLEAVN DYINESYGED VWRLIENRAE IPHLKFVRHQ MYNDNLILRL AKAAGEVLGK
     THDELMYAFG VYMVKRIGNY GYERILKVLG RNVRDFINEL DNLHEYFRFS FPKVQPPSFC
     VEEECETSLT LHYRSTRKGF TQFVKGQLSQ VGRQFYNTDI EVEILSKEET EKMTYVVYKM
     NFDNAAFKHR MPQQKTAPSY EKLPMKRGIF FDMFPFSVIF RRDMTMYRIG DGLKEVFSDL
     QGKKVNEEFT LVRPMLEFSW DNIYTHLNNV FELLSKAVVE SKQKVNIPKL SKEEPEEKEE
     SEKAKREEER EPKAVEEMKG TDQEYSSALT QYNSSANSGG EDIELLAFQT VTGKCSETIF
     EDMREPPKKP LHLKGQMKYV PQWDSLIFLG TPIIETVEDM IKMGVYVNDL NLHDSSRELI
     LAGTQQSAEL QLALDQEQQK YAQLQEIIKK LDEEKKRGDS LLYAMIPKAV ADRLRKGITA
     LETCQVFPDV TILFSDVVKF NEICIHITPM QVVDMLNEIY IVFDTLSEKH NVYKVETIRD
     AYMVVAGVPN KTTFHAHHIC DMALDMLSSI DHLKDPSTGD NIQIRVGIHS GMVVAGVVGL
     KMPRYCLFGD TVNTASRMES NGVGMQIHIS QTTKDHLEHE PYIIEERGKI FVKGKGYMKT
     YWLKGKKDLS FKTPAELRYS SEQKDSEDKS SNGSTSTNAK RMASNLHITG SDEQAEGKPS
     PSDLPLDTLP QPEATNEPPT ISTEPQEKEK AKKTKNNKGA KLDVPPGNTM PEYSPPADGL
     ENPGPLLNSK RNSFRQQYAK LPANLPIRSA SCSIL
//