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Database: UniProt
Entry: A0A195EDT2_9HYME
LinkDB: A0A195EDT2_9HYME
Original site: A0A195EDT2_9HYME 
ID   A0A195EDT2_9HYME        Unreviewed;      1398 AA.
AC   A0A195EDT2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=ALC57_04139 {ECO:0000313|EMBL:KYN23266.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN23266.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN23266.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN23266.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN23266.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ979039; KYN23266.1; -; Genomic_DNA.
DR   STRING; 471704.A0A195EDT2; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd06373; PBP1_NPR-like; 1.
DR   CDD; cd14042; PK_GC-A_B; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF494; GUANYLATE CYCLASE; 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.
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, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KYN23266.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1398
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008270775"
FT   TRANSMEM        511..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        626..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          670..944
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1020..1150
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1229..1286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1298..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1398 AA;  156355 MW;  E4CBAA68484E6E23 CRC64;
     MASRTRKRWC GNGGVLVRLT LTLSGLCAGQ CTNIGLMTMT TTTMTRTSTT ETGTTMTMTA
     GGSRECIGGV RTMSEGEVKL AVIAPGDPHH EQSLQRVLPA VLLAVKYVSS PRGPLPGWNI
     KVDYRDSYCS STYGPLAAFE FYINQTADAF LGPVCDYVIA PVARYAGVWG IPVLTAGAQA
     EAFRHKGQHY PTLTRMMGSH RLVGEALRHI LRSFGWKICG LLFHNHEMAS SKGNSECHFT
     LSAVYTALNQ TPAHKSFNQE TADTDEYKNL LSFIAKSARI IVMCANSTTI REILLAAEEL
     GMVDSGEYVF FSIELSSSDN DSKEPWRVDG DTDERNKKAR KAYQALLTVT ARTPDNLEYL
     NFSREVKSLA QSKYNFIFGN SSVSTFVTAF YDAVLLYALA LKESLPEKPG EVNLDGGNLT
     RQMWGKSFKG ITGDVNIDEN GDRIADYSLL DMDPKTSRFE IVANYYGANK TLEYIPGKQI
     HWAGGRLEPP PDTPTCGFDG SLCPDNSLPG YAILSMVLSS IVVVLVVGSV FIYRRFKLEA
     EIVSMTWKVH WDDVIVIPNA KTRGSMYSLI ANKFRGSELV RYSVDAFLII SLHSVKKQKR
     KRPFLNLFVL FSYTTNKRKN RKKISFFPYS LNFTFIYKAC RSFLFNDRIF DQFSLSRFNL
     IEMSSQQYFF PHVKQLSAKN IFQMKEITLS FNNSIDNSKV AIKLIPRNKV EISRPLLLEL
     KRMKDLQHDH LVRFYGACLE PPHCCLLTEY CPKGSLQDIL ENEQIKLDRV FRGSLTHDIV
     RGMAYLHASE VKSHGNLKSS NCVVDSRFVL KIADFGLHEL RRNADVDSDG DKNSYAYWRK
     QLWTAPELLR MERQLPEGTQ KGDVYSFAII VHEIVMRQGP FYLGDNNELS PKEIIEGVRR
     GGGSPLRPII DDASVEEEVA TLMRRCWAQE AADRPDFPAL KQTIRKINKD YESSNILDNL
     LSRMEQYATN LETLVEERTA DYLEEKRKCE ELLYQLLPKS VASQLILGQS VIAETYDQVT
     IYFSDIVGFT SLSAESTPLQ VVDLLNDLYT CFDSIIENFD VYKVETIGDA YMVVSGLPVR
     NGMNHAREIA RMSLALRDTV MTFSIRHRPT EQLKLRIGMH SGPCVAGVVG LKMPRYCLFG
     DTVNTASRME SNGEALKIHV SPKTKEILDT FGTFELVCRG EVILKGKGPM TTYWLMGEIP
     TNNNVQQANP TTTVSQISIL QDQPPITTQI QTTQTKQQEQ RALSSVNQQH KFQGQSEQPY
     PTQQSIQSRS QEPRQQGHPG QQRPQELQHQ GLMTVQSRCQ AVQTNPSSTT NQIQGQRSAT
     VNPACVTGNG APKSVIASRT VVATPIGNSS PSRNRTSGPP SANNSMHQVY PTAENMPNHT
     ESGPNAPLLL PAGAIPRV
//
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