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Database: UniProt
Entry: T1IKH0_STRMM
LinkDB: T1IKH0_STRMM
Original site: T1IKH0_STRMM 
ID   T1IKH0_STRMM            Unreviewed;      1770 AA.
AC   T1IKH0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR001419-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR001419-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
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}.
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DR   EMBL; JH430530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 126957.T1IKH0; -.
DR   EnsemblMetazoa; SMAR001419-RA; SMAR001419-PA; SMAR001419.
DR   eggNOG; KOG3619; Eukaryota.
DR   eggNOG; KOG4209; Eukaryota.
DR   HOGENOM; CLU_238847_0_0_1; -.
DR   OrthoDB; 3087296at2759; -.
DR   PhylomeDB; T1IKH0; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd15039; 7tmB3_Methuselah-like; 1.
DR   CDD; cd07302; CHD; 2.
DR   CDD; cd12306; RRM_II_PABPs; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR032628; AC_N.
DR   InterPro; IPR009398; Adcy_conserved_dom.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF1; ADENYLATE CYCLASE TYPE 8; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF16214; AC_N; 1.
DR   Pfam; PF06327; Adcy_cons_dom; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00044; CYCc; 2.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; 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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1770
FT                   /note="adenylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004579272"
FT   TRANSMEM        187..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        750..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        781..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        806..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        834..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        859..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1265..1286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1292..1314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1335..1353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1396..1414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1421..1439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1459..1477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          184..402
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   DOMAIN          507..584
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          961..1088
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          1540..1676
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1770 AA;  202902 MW;  A80A2E5F9DE2DE8A CRC64;
     MSCSSFTMSF PLSIILTTLN LLFHRVICQQ QQQQPCSNGA VYPSLNRCLF ECRNDEYNNN
     ASHPDEKHEY KVLVLSVNDF SITTNGFLVA DLPIPELPTN LYVIHNFTAR ICYPLDQNFI
     SCDKWSLESD EFVLSNDSHH LWTIPDNKIY TLGQFYMFMI DNESLPVVCI SQKAIEHHKN
     IVAVDKWFLG LHIVSATSLI IAFVCCVRFP ALNVRHNYNL LCHMCVMSVA YWTLVIEYFM
     RQWKTTPDAC LVVAFIKQFA FLATFFWINV QAIDLFLRFN NLSINSTPGS NTRRFVYYSG
     YAWGCPFAVS CITLIVAKSD VELRYRPNWQ QFCWFDYKYK LTGLIYFYAP IAIILVVNSG
     LFGLTMWKLY TVGKMVSNVN KRIHQQLLQL CVKLLVITGL CWSMEVIGWA VGEYKNNMFN
     AKKIEHIEEF DNDDDEFGFG RILREMDEEE KQNHEQNLKI EQFHNLNSDK ILNEVEIEIQ
     VQPSPHVDNN TIFISCKEEE KQEIHSRSIH VGNIAFTATP EDLKQHFNAC GSIKRVTIVY
     DKVTGRSRGF AYIEFTDEDA VNNAVALNNS LFRDRNIKVH LCRQVFCDEN GRSFAKKRFN
     DHNENDLTRY KKRKFNPVSP RSQWVRAFGR IKARGRVCST GRGSDSGLSQ LSITDPHPHL
     DGGNVFTIDK PDRSCASVPV HLADRVRRGL VLPCNNAFSN KHLELAYQRY SSRQKQKSLI
     VVNLVDFFVK LLLLASEILQ KRESISPLNI SFSACWMFFN LVVCVLCFWR CFANNYLRQS
     AVFTWLVLNI QGFSALSVGF KCDKMHQYGG IETSWYIIFI VFVTHAMLPL PLEWSVTAGS
     LTAVVHLLLS TIWNSADVTF YKLIFGNVLL YLCLNLAGIY GKYLMERAQR KAFVETRRSM
     ETRYKTEKET ERQEKLLLSM LPRFVAAEMI NDIIAQEEAE KKAFQPSQFH KIYIHRYENV
     SILFADIKRF TELASRCTAQ ELVTLLNQLF ARFDRLANET HCLRIKLLGD CYYCVSGLPE
     PRVDHAKCCV EMGLHMIKAI GSVREQTNVN VDMRIGIHSG SVLCGVLGLR KWQFDVWSND
     VTMANHMESG GIPGRIHISK ATLDCLGDHY RVEPGCGHER DVYLKHHGVP TFLIVATEPK
     RWTKLKRRER TRLWSLDEGL RLSAAATTRS DWMPEIPFEN FEMGQHVNVE GFDDNSDLEN
     GGVAFAAGGE SMSDRVDDLI DNSIEIESNL RMRREHVNRF TLTFKDEHME TQFCRSADDV
     FKSNMLTAFF IWIIGTSTHC IVMHELIIWR LIISATATTL LFVGFALVMA EEFVSMPASL
     RRLSAHLTRN RNARNAFTCI FVSIICLASS IGMCLCSKHS DEPLASDCHN VSVYRTTHCF
     LPNVFGHVTV CHFPQYYIYL WALSMVACAS FLQLPYLVKS SLLGAMMCLY CVLLLTVYQH
     VLSSNTHCDT IDCLFDDPIV LQLFMFFYVL MYQCRLVEIT CRLDFLWKRQ TEQEASEIRL
     LRHHNEHMLK NMLPVHVLVH FLSDDRNVDQ LYYQSIDSVG VLFASIPNFA EFFSEDVNRG
     VECIRLLNEI IADFDELMEQ PRFKCIEKIK TIGSTYMAAS GLNPKQSDEE HAHICTLVDY
     ALAIKGALKE VNRHSFNDFF LRIGISHGPL VGGVIGAKKP VFDIFGNTVN EASRMDSTGI
     VDAIQVPKNT ADILGRCGYQ VEFRGSVAVK GKGHMDTYLV AGKRSPKTVA FNRQASRQPS
     FAFVVYGMVQ ARRRQTSVKK SFVRRKPVDQ
//
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