ID A0A093I4M5_STRCA Unreviewed; 887 AA.
AC A0A093I4M5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Adenylate cyclase type 5 {ECO:0000256|ARBA:ARBA00040910};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase 5 {ECO:0000256|ARBA:ARBA00042065};
DE AltName: Full=Adenylate cyclase type V {ECO:0000256|ARBA:ARBA00042046};
DE AltName: Full=Adenylyl cyclase 5 {ECO:0000256|ARBA:ARBA00041988};
DE Flags: Fragment;
GN ORFNames=N308_15953 {ECO:0000313|EMBL:KFV86795.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV86795.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV86795.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV86795.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; KL206896; KFV86795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093I4M5; -.
DR STRING; 441894.ENSSCUP00000018150; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
DR CDD; cd07556; Nucleotidyl_cyc_III; 1.
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:SF7; ADENYLATE CYCLASE TYPE 5; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..887
FT /note="Adenylate cyclase type 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001887383"
FT TRANSMEM 388..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..223
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 697..836
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV86795.1"
FT NON_TER 887
FT /evidence="ECO:0000313|EMBL:KFV86795.1"
SQ SEQUENCE 887 AA; 100643 MW; 6D14C2FD787B80C9 CRC64;
FPLLQLVSNV LIFSCTNIVG VCTHYPAEVS QRQAFQETRE CIQARLHSQR ENQQQERLLL
SVLPRHVAME MKADINAKQE DMMFHKIYIQ KHDNVSILFA DIEGFTSLAS QCTAQELVMT
LNELFARFDK LAAENHCLRI KILGDCYYCV SGLPEARADH AHCCVEMGMD MIEAISLVRE
VTGVNVNMRV GIHSGRVHCG VLGLRKWQFD VWSNDVTLAN HMEAGGKAGR IHITKATLNY
LNGDYEVELG FGGERNAYLK EHSIETFLIV RCSQKRKDEK ATIAKMNRQR TNSISHNPPH
WGVDRPFYNH LGAHQVSKEM KRMGFEDPKD KNTQESMNPE DEVDEFLGRA IDARSIDRLR
SEHVRKFLLT FREPDLEKKY SKQVDDRFGA YVACASLVFL FICFVQIVIM PHSTFMLGFY
LTCFLILTTV VFVSVIYSCV KLFPAPLQTL SRKIVQSRTN STLVGVFAII LVFLSAFVNM
FMCSTVDLAS CMAAEYNVTR DRMDICLISN LTSNYSLGTL QRFCDSPLPS CNFPEYFTYS
VLLSLLACSV FLQISCIGKL ILMLIIEFIY VLIVEVPGVN LFDNADLLVT ANTYVSANAT
LPCTPAMTRV ALKIVTPVII TVFVLALYLH AQQVESTARL DFLWKLQATE EKEEMEELQA
YNRRLLHNIL PKDVAAHFLA QERRNDELYY QSCECVAVMF ASISNFSEFY VELEANNEGV
ECLRLLNEII ADFDEIISED QFRQLEKIKT IGSTYMAASG LNDSTYDKEG KTHIKALADF
AMRLMDQMKY INEHSFNNFQ MKIGLNIGPV VAGVIGARKP QYDIWGNTVN VASRMDSTGV
PDRIQVTTDM YQVLAANNYQ LEYRGIIKVK GKGEMTTYFL NEGPPIS
//
