ID S7PX44_MYOBR Unreviewed; 1066 AA.
AC S7PX44;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=D623_10031241 {ECO:0000313|EMBL:EPQ13127.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ13127.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 EMBL; KE163671; EPQ13127.1; -; Genomic_DNA.
DR AlphaFoldDB; S7PX44; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 3.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF12; ADENYLATE CYCLASE TYPE 3; 1.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF00211; Guanylate_cyc; 3.
DR SMART; SM00044; CYCc; 3.
DR SUPFAM; SSF55073; Nucleotide cyclase; 3.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 3.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 3.
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:UP000052978};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..362
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 471..598
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 658..785
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 237..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116882 MW; FB9D62EBE6BFAF49 CRC64;
MPLSSGDTVH TSEQAGAEGL CMAPPLSPPA TLSLLQTYFK RQRHETLLVL VVFAALFDCH
VVVLCAVVFS ADKLAPLAVA GVGLALDILL FVLCRKGLLP SRVTRKVVPY LLWLLITAQI
FSYLGLSFPG AHAASDTVGW QAFFVFSFFI TLPLSLGPIV VISVVSCVAH TLIVGVTVAQ
QQQDRLKGMQ LLREILANVF LYLCAIVVGI MSYYMADRKH RKAFLEARQS LEVKMNLEEQ
SQQQASDHPA AQQIPVPGRG DPSPGGQEAE HPALGRRDFS LGAFAPYCIC GLPDYREDHA
VCSILMGLAM VEAISYVREK TKTGVDMRVG VHTGTVLGGV LGQKRWQYDV WSTDVTVANK
MEAGGIPGRV HISQSTLDCL KGEFDVEPGE GGSRCDYLEE KGIETYLIIA SKPEVKKTAS
QNGLNSSENL MLSILPKHVA DEMLKDMKKD ESQKDQQQFN TMYMYRHENV SILFADIVGF
TQLSSTCSAQ ELVKLLNELF ARFDKLAAKY HQLRIKILGD CYYCICGLPD YREDHAVCSI
LMGLAMVEAI SYVREKTKTG VDMRVGVHTG TVLGGVLGQK RWQYDVWSTD VTVANKMEAG
GIPGQDTVNV AVSQENLMLS ILPKHVADEM LKDMKKDESQ KDQQQFNTMY MYRHENVSIL
FADIVGFTQL SSTCSAQELV KLLNELFARF DKLAAKYHQL RIKILGDCYY CICGLPDYRE
DHAVCSILMG LAMVEAISYV REKTKTGVDM RVGVHTGTVL GGVLGQKRWQ YDVWSTDVTV
ANKMEAGGIP GSPALIETKE SNGSVHTSGS TSEEPEEQDA QADNPSFPNP HRRLRLQDLA
DRVVDASEDE HELNQLLNEA LLERESAQVR VHISQSTLDC LKGEFDVEPG EGGSRCDYLE
EKGIETYLII ASKPEVKKTA SQNGLNSSHP CTGGREGGAG GGVAEDWARP GGGMSCEVQV
GITAMPSPAE QVAGGLRSEG QLVPAGGDCP VRRWERVWCS ERLGCREGPC REEAVEATGV
TWMPRRGAEG GREEAVGAPP YSPRPPPGPR PALHSLFIFV HVRVKL
//
