GenomeNet

Database: UniProt
Entry: A0A2J7RQ84_9NEOP
LinkDB: A0A2J7RQ84_9NEOP
Original site: A0A2J7RQ84_9NEOP 
ID   A0A2J7RQ84_9NEOP        Unreviewed;       588 AA.
AC   A0A2J7RQ84;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=B7P43_G09584 {ECO:0000313|EMBL:PNF42986.1};
OS   Cryptotermes secundus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX   NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF42986.1, ECO:0000313|Proteomes:UP000235965};
RN   [1] {ECO:0000313|EMBL:PNF42986.1, ECO:0000313|Proteomes:UP000235965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:PNF42986.1};
RA   Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA   Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA   Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA   Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA   Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA   Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA   Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA   Bornberg-Bauer E.;
RT   "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001593};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PNF42986.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NEVH01001345; PNF42986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J7RQ84; -.
DR   Proteomes; UP000235965; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009975; F:cyclase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 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; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF23; AT30656P-RELATED; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235965};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          351..498
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          556..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  68060 MW;  973EFF93A8BB6D44 CRC64;
     MDDNLYKYQQ TLKKADEQMA EAIKNMHVGV YDRWCLRENI NPVCLTFENI QWELPFLKQP
     DPLFKFYVGC ALLVLLGMLI IQCLGLQSSH WMPWAGFGVS LGVILVLLPL TWTHYIWNKL
     KDPHEEQDYI PEPTNKLLNL LYQASLKVVW SVSTRTVLYL IICISLTICT MLEMVECDLK
     SEDTEVKSNN VTGGDMLEVL TDCLAPWHIT QICSLTLIMS FLFLRIHFQL KLILGIFTVV
     IYSCGVWILF PKVFQYGETW NPQMETRIAH IMNVTFLTVT LHLMDRQTEY MSRLDYKWKC
     QLAQEQEESS TVHMINKMLL QNILPVHVAD WFLNTNRDHE ELYHEEYDTV AVMFASLTEY
     ALWDDNGLDD ANELSSIRLL NQIICDFDKL LFHANSLRVE KIKVAGWTYM AACGLDPGRR
     DSVNSVNRDS YSDHVVLVLT RFAANMMGVL QKINKEFLQN FKLRVGISHG KVTAGVIGAQ
     KPHYDIWGHS VNMASRMEST GEPEKIQVTE NTARVLQQLG IHCECRGAIK VKSMTNLVTT
     YFVHFDEKFQ LKHAEGVQDS DHDSVLEENE VRDYEKRYRE ERQNNTTP
//
DBGET integrated database retrieval system