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Database: UniProt
Entry: K1R877_CRAGI
LinkDB: K1R877_CRAGI
Original site: K1R877_CRAGI 
ID   K1R877_CRAGI            Unreviewed;      1372 AA.
AC   K1R877;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=CGI_10004768 {ECO:0000313|EMBL:EKC30171.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC30171.1};
RN   [1] {ECO:0000313|EMBL:EKC30171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC30171.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
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|RuleBase:RU003431};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; JH818178; EKC30171.1; -; Genomic_DNA.
DR   HOGENOM; CLU_256222_0_0_1; -.
DR   InParanoid; K1R877; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 1.20.80.60; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000313|EMBL:EKC30171.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   1372 AA;  154081 MW;  2409EF4A43501534 CRC64;
     MNRDVELQKL VKVTVVTIDG NENQVTVPVV GDEQISVTDI YAKACDCLGL QKTSSKWFSL
     FCGGETIRRL KPDTFTHSSA KEVSLRKWCF NGRIEANMIK DDPVACHLVY LEAKAAIEKG
     LLSVTNEQRE KLEEYEDPAF KLEKDYILLA QTLEGYFSVL IQNCIITDQE PIESTLQVVN
     PSESFFYSSM ISTNEEGSTS YENVLYRGPC DGVDDEGRYN GNSIWRLDEQ LNVTLFANLS
     FIPRGMAVHP RTNELYVCGV ERDGSRDDLL SLNRRHLIAR FSADGTFISD ITISPHDPHR
     LGLMNEDKVC FSDYGKNNKR QLVVMDKMGT VLCVYEGRHE LENPFYPLGT QVDQYENIIV
     ADWNNDCVHL LDKNGEFSQF LVDQESDIER PCSLGLDTDG HLWETTTLIS LRQKYVVSTN
     HHHSMICVCH GAILASQCWD SFHIYREERN VVAFRPGSAE SRVLSVGRQI ANVTINSTTS
     KVNKKPNSVK LMEMKHQNCC AFVGACIDPG RILLLWEYCH KGSLQDVIWN QNIKLDRMFM
     FALSQDIAKG LDFVHKSSIH YHGNLKSSNC VVDSRWTCKL ADFGVPSLRH SDKCHKEDEN
     PDKLQWTAPE LLRLEKSIDK QKVDIFSLGI ILKEIFTRSG PYTEYPFLRI HELIDKVRYP
     VCGAPPFRPK LSVEVQQTPE LHALIDECWN ESVFVRPSAG RILKTLARIN PSKMTMIDNM
     IAILEKHANH LEELVAERTS ELDAEKKKTE NLLYRMLPQS VADDLKKGKP IEAEHFDETT
     IYFSDIVGFT TICAGSTPIQ VVNLLNSLYT LFDDIITRYD VYKVETIGDA YMLVSGLPKR
     NGNRHSKEIA DCAMDIMASI GTFCIPHQPN AKVKIRIGIH SGPAVAGVVG LAMPRYCLFG
     DTVNTASRME STGLPLKIHL SSMTRDQLET FGCYHILYRG ETNVKGKGIM KTYFLNGRDG
     FTKELPSISE EGMCLKFSPS ATSDLHYMGV ATSPGTPKTS VTAIGEGLNI ERKEMPSVKE
     TLQGLSGEDS KKKCASDVMS LTLGDVLPDS VKETVERFRK TGLSCFPQDT NEKGISRRHS
     YNDAPKKNCF IPASHDAVPI YEDASYDIRK KLSTGSEAAD SGRGSFRRTG SSSSSLNDVI
     TSSLKNITCL DEINVNCLMN RNVKSFPDIM NSTPRENGRL HKRKFSTGDV IDSIQSYRNG
     YSAGKLKIRK LSAESFFEGY CISKKTPKQE ETRGRKYSIE SFIRGLLGNK TKLNKSQSTV
     KEPCMIKSID KHIKDSHPMH SCSLTENCHE NLAFQDDQNE LHDHDEATVQ EIVNELHEMA
     TDPNNMAPGV LPADKLPISL GHIFPRHRVL TKSDSGYGTP ENLSIASATT FL
//
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