ID A0A1U7S8B7_ALLSI Unreviewed; 616 AA.
AC A0A1U7S8B7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=ADCY9 {ECO:0000313|RefSeq:XP_006036635.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006036635.2};
RN [1] {ECO:0000313|RefSeq:XP_006036635.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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 RefSeq; XP_006036635.2; XM_006036573.3.
DR AlphaFoldDB; A0A1U7S8B7; -.
DR KEGG; asn:102373860; -.
DR eggNOG; KOG3618; Eukaryota.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF8; ADENYLATE CYCLASE TYPE 9; 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:UP000189705};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT DOMAIN 399..526
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 69800 MW; 4AF097A09D151932 CRC64;
MASPPHQQLL HHHSTEVSCD PSGDSNSVTV RINPKQHQGC ISAKHCKYSI SSSCSSSGES
AGPRRAAGGG ASGGSGLRRQ KKVPQLFERA SSKWWNPKFD SNNLEEACME RCFPQTQRRF
RYALFYIGVA CLVWGIYFSI HMQEKLMVFT VPALGFLLVC IAFFMFTFTQ TYARHYVWTS
LILTLLVFTL TLAPQFQALT TLSGRDDVSN HTSLVRAADA SLSQVGSFSM CIEVLLLLYT
VMHLPLYLSL FLGLLYSVLF ETFGYHFRVE YNFTPIEANA AYWEQLMSKT LLHICIHAIG
IHLFIMSEVR SRSTFLKVGQ SIMHGKDLEV EKALKERMIH SVMPRIIADD LMKQGDDESE
NSVKRHSTSS PKSRKKKPSI QKTPIIFRPF KMQQIEQVSI LFADIVGFTK MSANKSAHAL
VGLLNDLFGR FDRLCEDTKC EKISTLGDCY YCVAGCPEPR ADHAYCCIEM GLGMIKAIEQ
FCQEKKEMVN MRVGVHTGTV LCGILGMRRF KFDVWSNDVN LANLMEQLGV AGKVHISEAT
AKYLDDRYEM EDGKVIERVG QSVVADQLKE TLPLRPELII KDGWQDYKKC LRRFRETAGK
RKGDIQQRNW WGQNRS
//