ID T1J6T7_STRMM Unreviewed; 1761 AA.
AC T1J6T7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:SMAR009363-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:SMAR009363-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; JH431887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 126957.T1J6T7; -.
DR EnsemblMetazoa; SMAR009363-RA; SMAR009363-PA; SMAR009363.
DR eggNOG; KOG3619; Eukaryota.
DR HOGENOM; CLU_239095_0_0_1; -.
DR OrthoDB; 3686360at2759; -.
DR PhylomeDB; T1J6T7; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
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; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF26; ADENYLATE CYCLASE TYPE 1; 1.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
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:UP000014500};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..240
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 673..817
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 974..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1761 AA; 195800 MW; 192964926CCBF85F CRC64;
MIANGAVFLS ANVAGLFVHS LMEHAQRKAF LDTRNCIGAR LEMEDENEKL GFEIGLLLNL
MAMVVLKKFV FLQERLLLSV LPQHVAMEMK EDIIAPREQQ FHKIYIQKHE NVSILFADIV
GFTVLASQCT AQELVRLLNE LFGRFDQLAN DNHCLRIKIL GDCYYCVSGL PEPRSDHAHC
AVEMGLDMID AIASVVEATD VQLNMRVGIH TGRVLCGVLG LLKWQYDVWS NDVTLANHME
AGGIAGRVHI TQDTLDFLHG EYEVEPGNGA DRDAYLREHN PLLFNTLQVR SAIGSTTRRK
LSFKNVSNVV VQLLHSIKYS VEVPFSNMAM QPTINDKPGS TKKTKVTDKF KRPFKKRHSS
VYHQPTNRVN KYLAQAIEAR SVDHEKSSHV SVITLCFRDK KREKLYHDDV DHSFASGMLC
ALILLILLGT VQVIILPKTV ILMVLFITAF VWISVLLMLL LSSRLKCISW DLSRSFLLRL
SITIFSLILI YTVAQVNVFT CSMEKGCNKT VSDAADSLHH RSCPLPQYIM LSCVISYLAI
SIFLRLPVVI KLILAVSMAI VYILVIVLLH IDLFLCYDHL VTSDIPVYIV EVVVIIHFML
AILIHGRQVE WTARLDFLWQ VQANEEKLDM DALQRSNQRI LFNLLPSHVA THFLDNQFRN
NMDLYHQSYS KVGVMFVSIP NFHEFYIELD GNNQGVECLR LLNEIIADFD ELLDDERFKS
VDKIKTVGST YMAAVGLIPD MRIEDEVEES GGRCLSTLVE LVFAMKERLI IINENSYNNF
MLRVGINVGP VVAGVIGARK PQYDIWGNTV NVASRMDSTG LPNHTQVTEE VYQTLKNYPY
DFQCRGKVKV KGKGEMTTYF LVSRKQTAME PSSETANGPT SGLPRTVVPG GVPTPLSFVA
QIKKGHGGNN VSSSLSGNET PYKGRKAALH HHDGGAVIDI DEKIHNNHRH SSGSRTNNQE
KTILNQFGVQ LRPTAQDKHS HSHKHNGTSR SSADRPPALP PHGPGWQLNQ ELVPARTTQS
QSRASKPVKQ TNEIPTQYTP PPWMDKTGNS DDKNNLPVTR AQLQSRTPPR SYSHSRPSKY
ITPPRDIMAA AKALPPFGRL NLQLADERLH HKSKTRHRSD ESLPGAVLSR DLQAAARHSS
ADEISSLNRS PSSSSVESFP QTDRLRMDQS PVRSRRATVH CDSKWLYPVD GFPSQTNNSA
TRAMLVPVAA GSSSGDSLAK ITGLTPQEGG AKSFPHVGRS PSTQRWRNDL DARQLGNELD
SATDSDHRTS SDNAESLDNQ LLARILNDPR TRSIPGMGNY NNSRGNAASR SRAPNRDLDA
SAHSSPSLGS GSGSRKRSLD RSSKETLSSL PSSPDEVPCK KSISEACREL IEANNTLAAD
SEENAMDGTD RSDKSGAVDN DALINLTKDI PPPPHADATS NGEANGQPEV QFDEKKASEL
IEPLWGERDE LPGGLTLEEL ENVNQVLAEL GQASLRVQDD SKLKDHINNN PVVLRAATET
ASKIPGQQLY KTPDKMDKMD KMDKIGLHYD PVERRMLLKF PLLAEDAKHD AKNKPFGFRF
PLDIPDVGRK VKRNPSQRST NKDQSEYENL DSDFDKTPGR SKGAAEFGET ESSEDEAHEE
EPLLEEEPGY AIDDPTLDNA SMLNEAGLTD AEGALSDLNS IFNDPGHDGD MDDTSMSSRA
SSRIFDSDQL LSADSLNAMY DSEYDNCRAG MVSDEDLFHA EPSDIDIDYF DDIHVENLRT
LSDSIARNFG QPVEENQSDA G
//
