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Adenylate cyclase, terminal-differentiation specific (EC 4.6.1.1) (ACB) (ATP pyrophosphate-lyase) (Adenylyl cyclase)

 CYAD_DICDI              Reviewed;        2123 AA.
Q55F68; Q9U9S7;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
28-FEB-2018, entry version 88.
RecName: Full=Adenylate cyclase, terminal-differentiation specific;
EC=4.6.1.1;
AltName: Full=ACB;
AltName: Full=ATP pyrophosphate-lyase;
AltName: Full=Adenylyl cyclase;
Name=acrA; Synonyms=acb; ORFNames=DDB_G0267376;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=AX4;
PubMed=10556070;
Soederbom F., Anjard C., Iranfar N., Fuller D., Loomis W.F.;
"An adenylyl cyclase that functions during late development of
Dictyostelium.";
Development 126:5463-5471(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[3]
FUNCTION AS AN ADENYLYL CYCLASE ACTIVITY.
STRAIN=AX2;
PubMed=9812977; DOI=10.1074/jbc.273.47.30859;
Kim H.-J., Chang W.-T., Meima M., Gross J.D., Schaap P.;
"A novel adenylyl cyclase detected in rapidly developing mutants of
Dictyostelium.";
J. Biol. Chem. 273:30859-30862(1998).
[4]
FUNCTION, AND DEVELOPMENTAL STAGE.
STRAIN=NC-4;
PubMed=10419694; DOI=10.1006/dbio.1999.9352;
Meima M.E., Schaap P.;
"Fingerprinting of adenylyl cyclase activities during Dictyostelium
development indicates a dominant role for adenylyl cyclase B in
terminal differentiation.";
Dev. Biol. 212:182-190(1999).
[5]
FUNCTION, AND DEVELOPMENTAL STAGE.
STRAIN=AX4;
PubMed=11566867;
Anjard C., Soederbom F., Loomis W.F.;
"Requirements for the adenylyl cyclases in the development of
Dictyostelium.";
Development 128:3649-3654(2001).
[6]
ENZYME REGULATION.
STRAIN=NC-4;
PubMed=16952277; DOI=10.1042/BJ20060880;
Alvarez-Curto E., Weening K.E., Schaap P.;
"Pharmacological profiling of the Dictyostelium adenylate cyclases
ACA, ACB and ACG.";
Biochem. J. 401:309-316(2007).
-!- FUNCTION: Through the production of cAMP, activates cAMP-dependent
protein kinases (PKAs), triggering terminal differential and the
production of spores. {ECO:0000269|PubMed:10419694,
ECO:0000269|PubMed:10556070, ECO:0000269|PubMed:11566867,
ECO:0000269|PubMed:9812977}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by high osmolarity. Inhibited by
caffeine and 2',5'-dideoxyadenosine (DDA).
{ECO:0000269|PubMed:16952277}.
-!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:10556070}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Present at low levels in growing cells;
accumulates to high levels throughout development. Highly
expressed during early culmination and in fruiting bodies,
especially in the prestalk region. {ECO:0000269|PubMed:10419694,
ECO:0000269|PubMed:11566867}.
-!- DISRUPTION PHENOTYPE: Cells cannot complete sporulation and have
abnormally long, thin stalks, though able to aggregate and form
normal slugs. {ECO:0000269|PubMed:10556070}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-----------------------------------------------------------------------
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EMBL; AF153362; AAD50121.1; -; Genomic_DNA.
EMBL; AAFI02000003; EAL73140.1; -; Genomic_DNA.
RefSeq; XP_647665.1; XM_642573.1.
ProteinModelPortal; Q55F68; -.
STRING; 44689.DDB0191294; -.
PaxDb; Q55F68; -.
EnsemblProtists; EAL73140; EAL73140; DDB_G0267376.
GeneID; 8616482; -.
KEGG; ddi:DDB_G0267376; -.
dictyBase; DDB_G0267376; acrA.
eggNOG; ENOG410JF3E; Eukaryota.
eggNOG; COG2114; LUCA.
InParanoid; Q55F68; -.
OMA; ICKSITI; -.
PRO; PR:Q55F68; -.
Proteomes; UP000002195; Chromosome 1.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
GO; GO:0004016; F:adenylate cyclase activity; IDA:dictyBase.
GO; GO:0005524; F:ATP binding; IC:dictyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:dictyBase.
GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:dictyBase.
GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
GO; GO:0016310; P:phosphorylation; IEA:InterPro.
GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
GO; GO:0031000; P:response to caffeine; IDA:dictyBase.
GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
CDD; cd00075; HATPase_c; 1.
CDD; cd00156; REC; 2.
Gene3D; 3.30.70.1230; -; 1.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR029787; Nucleotide_cyclase.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
Pfam; PF00211; Guanylate_cyc; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00072; Response_reg; 2.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00044; CYCc; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00448; REC; 2.
SUPFAM; SSF52172; SSF52172; 2.
SUPFAM; SSF55073; SSF55073; 1.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 2.
1: Evidence at protein level;
ATP-binding; cAMP biosynthesis; Complete proteome; Lyase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Sporulation; Transmembrane;
Transmembrane helix.
CHAIN 1 2123 Adenylate cyclase, terminal-
differentiation specific.
/FTId=PRO_0000328240.
TRANSMEM 246 266 Helical. {ECO:0000255}.
TRANSMEM 279 299 Helical. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TRANSMEM 328 348 Helical. {ECO:0000255}.
TRANSMEM 403 423 Helical. {ECO:0000255}.
TRANSMEM 502 522 Helical. {ECO:0000255}.
TRANSMEM 572 592 Helical. {ECO:0000255}.
DOMAIN 654 928 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
DOMAIN 954 1076 Response regulatory 1.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 1125 1310 Response regulatory 2.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 1583 1712 Guanylate cyclase. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
COMPBIAS 20 26 Poly-Glu.
COMPBIAS 75 102 Poly-Asn.
COMPBIAS 201 216 Poly-Gln.
COMPBIAS 363 377 Poly-Gln.
COMPBIAS 438 457 Poly-Asn.
COMPBIAS 830 841 Poly-Gln.
COMPBIAS 1215 1257 Poly-Asn.
COMPBIAS 1443 1453 Poly-Gln.
COMPBIAS 1843 1848 Poly-Gln.
COMPBIAS 1852 1902 Poly-Gln.
COMPBIAS 1916 1971 Poly-Gln.
COMPBIAS 1975 2045 Poly-Gln.
COMPBIAS 2052 2090 Poly-Gln.
METAL 1588 1588 Magnesium 1. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 1588 1588 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 1589 1589 Magnesium 2; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 1632 1632 Magnesium 1. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 1632 1632 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
MOD_RES 1010 1010 4-aspartylphosphate.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
MOD_RES 1174 1174 4-aspartylphosphate.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
CONFLICT 1936 1936 Q -> R (in Ref. 1; AAD50121).
{ECO:0000305}.
SEQUENCE 2123 AA; 243012 MW; D99245C5D8C2902B CRC64;
MTNNRLKNRK KPNQIHTISE EEEEEEPLFN NEDLQTQHLN SPSSDSISTS SSSSLSSVGG
SVVGNNNSNS NGIDNNNSNN NNNNNNNNNN NNNNNNSNNN NNYTGNSIGG NDFKNKASSS
SSTPTTSTGI GSSKFPNIKR KNSFSNRYDS GGGGSGSSRS NSFGGSNSSG GASKEFFYFD
NDDMIQDDDL IPMLMQDQEH QLQTQYQNQQ QVQQQQNIIN SFINHENLKF PFSIIYTNKL
HIWLSYFLFT FVLIFCCLAV GPLLWIELPP NSGCMWCRIF KLEWVISFMS LISAMFHYTI
RRDMFPLYLS IIGFYHVLTY SEPFLEPFRV NNFFSLILTV ICIFIAFYPK NKLRRQQASN
HHQQQQQQQQ QQRQRQQNNN RQPEKSIIKR IIQNEWFHSL IQILIVLGIV VLLFFSIFIL
ALFMKDDKTF SGDVIDGNIN SNNNNNNNNN NNINNNNIDN NNNNIKNNNK GFIEEIEQGE
EQLELYLENA YHIFKELVFK KFISSSVVYL ILITLLFCIS LVYHWEVRKP YTLMALASMI
PQLTQALYKV ELTLTGVMDK GTMSHNVTPL GGGIFYILNV ISYTSFYCGL AIDVVVASGE
KYKRLKKRGE KYHRRLSTQI NEQNAFVNKI YASGTAQLLQ KVEFMQKFVD KILFSTLEIS
NRLQRLESSD QDIPSSLVDQ LNDIQYQTNR SLLLLNDTKL ILAIESGVIS REDVSVNLFD
FLEDVLERTS KDIKFNNIEL VYKIDKDVPL NIILDPTALT QICFQLLSNA IKYTEEGEIG
ILIKRILRND YEYQQEQQQP QQDNELPPFG TISEEDEEYN SNNPPPPLNQ QQQQRQQQQQ
QEPKQIYLEI SIFDSGPGMD DDELDICNQF QPFPDIGDED DIEIKKKGSG LGLLICNKVL
KSIGGDLIVE RYLETGGCIF KCCIPVLVDP QPKENFTFQI PLSQETNELL SDLSVLVIDD
NPYARDSVGF IFSSVFNSAI VKSANSSVEG VRDLKYAIAT DSNFKLLLVD YHMPGCDGIE
AIQMIVDNPA FSDIKIILMI LPSDSFAHMN EKTKNITTLI KPVTPTNLFN AISKTFKLKE
FSSVVDLVDL NAPDTSTQIP LKRNRLKFKI DFPFRLPETG KPIMRVLIGE SDKSTQSKIQ
KVIESFGYFS TFVTDGTALI SLSKKNYYDL VIVDLELQST DGFECAQIIR DTHGEIFSNT
IFVPKPISTN SNDDNNNNNN NNNNNNNNDN NNNNNNNNNN NNNNNNNNNN NNNNNNNSIL
TSSVDTDGNH IVSSSTSTSS SFPTRRSSIG SFQTASPSMT EISHRRRVKL PIIGIWHHSD
IIPDDIIKKI KRVGFDGYCS FDNLEFYLQE FLLEFDRKRK SNILSPIRLF PNGSPSTNIY
DYSSIISNLN QASGNNNNSS PISGILNENV ISSPISLDLD LNSVSSIQSQ SSSSSSSFQH
NNQQQQQQQH QHQLTPTQQS IGGGNNGINQ LSFSSQQSTP IFNQSQIQHQ IISNRSKHSS
LSSSTSSNGS GGSGGKSRFS IPMLPSSTNR DSSPHSSSKM ALKRVQDLES VISKFVPIEF
QQLIAPSGME NVYLGDAICK SITIFFSDIR DFTSTTEKML VDDVIDFLNT YLAFALPSIT
DSGGFIDKFI GDAIMAIFPN SDMKLQAINA VKAAIRMMRS LDFMSISGFR FSSVETGVGI
NTGKTIIGIV GTENRMEPTA LGDAVNLASR TEQLCKEYQS RILITQFTME AIGTSIDEFV
IRLVDSVTVK GKSEAVNIYE VIDGEREDKR VLKMKILPWY QNGMDLYKRH CYEEALSYFQ
LCTEIMPNDK PTLIYIQRCI QNIKTLELQQ IQLQQLQRQQ LLQQQQQQLL LQQQLQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ SQNIQQPQSQ QSQYVQQPQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQPQQQQQL QQQQQHQQQK QPSPQQQQQP
QQPQQQQQQQ IQNQYQHQLQ YQRQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQHHHHH HQQQQFQQQS QQSQQQSQQQ QQQQQQQSQQ QSQQQSQQIQ KKSQHPHSQQ
IQSQRHQSQP QNVDTNVKTK PQQ


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