Q55F68 (CYAD_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylate cyclase, terminal-differentiation specific
EC=4.6.1.1

Alternative name(s):
ACB
ATP pyrophosphate-lyase
Adenylyl cyclase

Gene names

Name:	acrA
Synonyms:	acb
ORF Names:	DDB_G0267376

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	2123 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Through the production of cAMP, activates cAMP-dependent protein kinases (PKAs), triggering terminal differential and the production of spores. Ref.1 Ref.3 Ref.4 Ref.5
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Inhibited by high osmolarity. Inhibited by caffeine and 2',5'-dideoxyadenosine (DDA). Ref.6
Subunit structure	Homodimer Probable. Ref.1
Subcellular location	Membrane; Multi-pass membrane protein Potential.
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. Ref.4 Ref.5
Disruption phenotype	Cells cannot complete sporulation and have abnormally long, thin stalks, though able to aggregate and form normal slugs. Ref.1
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 1 guanylate cyclase domain. Contains 1 histidine kinase domain. Contains 2 response regulatory domains.

Ontologies

Keywords
Biological process	Sporulation cAMP biosynthesis
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro sorocarp development Inferred from mutant phenotype. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.1. Source: dictyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW soluble fraction Inferred from direct assay Ref.1. Source: dictyBase
Molecular function	ATP binding Inferred from sequence or structural similarity Ref.1. Source: dictyBase adenylate cyclase activity Inferred from direct assay Ref.1. Source: dictyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2123	2123	Adenylate cyclase, terminal-differentiation specific		PRO_0000328240
Regions
	Transmembrane	246 – 266	21	Helical; Potential
	Transmembrane	279 – 299	21	Helical; Potential
	Transmembrane	305 – 325	21	Helical; Potential
	Transmembrane	328 – 348	21	Helical; Potential
	Transmembrane	403 – 423	21	Helical; Potential
	Transmembrane	502 – 522	21	Helical; Potential
	Transmembrane	572 – 592	21	Helical; Potential
	Domain	654 – 928	275	Histidine kinase
	Domain	954 – 1076	123	Response regulatory 1
	Domain	1125 – 1239	115	Response regulatory 2
	Domain	1583 – 1712	130	Guanylate cyclase
	Compositional bias	20 – 26	7	Poly-Glu
	Compositional bias	75 – 102	28	Poly-Asn
	Compositional bias	201 – 216	16	Poly-Gln
	Compositional bias	363 – 377	15	Poly-Gln
	Compositional bias	438 – 457	20	Poly-Asn
	Compositional bias	830 – 841	12	Poly-Gln
	Compositional bias	1215 – 1257	43	Poly-Asn
	Compositional bias	1443 – 1453	11	Poly-Gln
	Compositional bias	1843 – 1848	6	Poly-Gln
	Compositional bias	1852 – 1902	51	Poly-Gln
	Compositional bias	1916 – 1971	56	Poly-Gln
	Compositional bias	1975 – 2045	71	Poly-Gln
	Compositional bias	2052 – 2090	39	Poly-Gln
Sites
	Metal binding	1588	1	Magnesium 1 By similarity
	Metal binding	1588	1	Magnesium 2 By similarity
	Metal binding	1589	1	Magnesium 2; via carbonyl oxygen By similarity
	Metal binding	1632	1	Magnesium 1 By similarity
	Metal binding	1632	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	1010	1	4-aspartylphosphate By similarity
	Modified residue	1174	1	4-aspartylphosphate By similarity
Experimental info
	Sequence conflict	1936	1	Q → R in AAD50121. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q55F68 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: D99245C5D8C2902B	FASTA	2,123	243,012
	10 20 30 40 50 60 MTNNRLKNRK KPNQIHTISE EEEEEEPLFN NEDLQTQHLN SPSSDSISTS SSSSLSSVGG 70 80 90 100 110 120 SVVGNNNSNS NGIDNNNSNN NNNNNNNNNN NNNNNNSNNN NNYTGNSIGG NDFKNKASSS 130 140 150 160 170 180 SSTPTTSTGI GSSKFPNIKR KNSFSNRYDS GGGGSGSSRS NSFGGSNSSG GASKEFFYFD 190 200 210 220 230 240 NDDMIQDDDL IPMLMQDQEH QLQTQYQNQQ QVQQQQNIIN SFINHENLKF PFSIIYTNKL 250 260 270 280 290 300 HIWLSYFLFT FVLIFCCLAV GPLLWIELPP NSGCMWCRIF KLEWVISFMS LISAMFHYTI 310 320 330 340 350 360 RRDMFPLYLS IIGFYHVLTY SEPFLEPFRV NNFFSLILTV ICIFIAFYPK NKLRRQQASN 370 380 390 400 410 420 HHQQQQQQQQ QQRQRQQNNN RQPEKSIIKR IIQNEWFHSL IQILIVLGIV VLLFFSIFIL 430 440 450 460 470 480 ALFMKDDKTF SGDVIDGNIN SNNNNNNNNN NNINNNNIDN NNNNIKNNNK GFIEEIEQGE 490 500 510 520 530 540 EQLELYLENA YHIFKELVFK KFISSSVVYL ILITLLFCIS LVYHWEVRKP YTLMALASMI 550 560 570 580 590 600 PQLTQALYKV ELTLTGVMDK GTMSHNVTPL GGGIFYILNV ISYTSFYCGL AIDVVVASGE 610 620 630 640 650 660 KYKRLKKRGE KYHRRLSTQI NEQNAFVNKI YASGTAQLLQ KVEFMQKFVD KILFSTLEIS 670 680 690 700 710 720 NRLQRLESSD QDIPSSLVDQ LNDIQYQTNR SLLLLNDTKL ILAIESGVIS REDVSVNLFD 730 740 750 760 770 780 FLEDVLERTS KDIKFNNIEL VYKIDKDVPL NIILDPTALT QICFQLLSNA IKYTEEGEIG 790 800 810 820 830 840 ILIKRILRND YEYQQEQQQP QQDNELPPFG TISEEDEEYN SNNPPPPLNQ QQQQRQQQQQ 850 860 870 880 890 900 QEPKQIYLEI SIFDSGPGMD DDELDICNQF QPFPDIGDED DIEIKKKGSG LGLLICNKVL 910 920 930 940 950 960 KSIGGDLIVE RYLETGGCIF KCCIPVLVDP QPKENFTFQI PLSQETNELL SDLSVLVIDD 970 980 990 1000 1010 1020 NPYARDSVGF IFSSVFNSAI VKSANSSVEG VRDLKYAIAT DSNFKLLLVD YHMPGCDGIE 1030 1040 1050 1060 1070 1080 AIQMIVDNPA FSDIKIILMI LPSDSFAHMN EKTKNITTLI KPVTPTNLFN AISKTFKLKE 1090 1100 1110 1120 1130 1140 FSSVVDLVDL NAPDTSTQIP LKRNRLKFKI DFPFRLPETG KPIMRVLIGE SDKSTQSKIQ 1150 1160 1170 1180 1190 1200 KVIESFGYFS TFVTDGTALI SLSKKNYYDL VIVDLELQST DGFECAQIIR DTHGEIFSNT 1210 1220 1230 1240 1250 1260 IFVPKPISTN SNDDNNNNNN NNNNNNNNDN NNNNNNNNNN NNNNNNNNNN NNNNNNNSIL 1270 1280 1290 1300 1310 1320 TSSVDTDGNH IVSSSTSTSS SFPTRRSSIG SFQTASPSMT EISHRRRVKL PIIGIWHHSD 1330 1340 1350 1360 1370 1380 IIPDDIIKKI KRVGFDGYCS FDNLEFYLQE FLLEFDRKRK SNILSPIRLF PNGSPSTNIY 1390 1400 1410 1420 1430 1440 DYSSIISNLN QASGNNNNSS PISGILNENV ISSPISLDLD LNSVSSIQSQ SSSSSSSFQH 1450 1460 1470 1480 1490 1500 NNQQQQQQQH QHQLTPTQQS IGGGNNGINQ LSFSSQQSTP IFNQSQIQHQ IISNRSKHSS 1510 1520 1530 1540 1550 1560 LSSSTSSNGS GGSGGKSRFS IPMLPSSTNR DSSPHSSSKM ALKRVQDLES VISKFVPIEF 1570 1580 1590 1600 1610 1620 QQLIAPSGME NVYLGDAICK SITIFFSDIR DFTSTTEKML VDDVIDFLNT YLAFALPSIT 1630 1640 1650 1660 1670 1680 DSGGFIDKFI GDAIMAIFPN SDMKLQAINA VKAAIRMMRS LDFMSISGFR FSSVETGVGI 1690 1700 1710 1720 1730 1740 NTGKTIIGIV GTENRMEPTA LGDAVNLASR TEQLCKEYQS RILITQFTME AIGTSIDEFV 1750 1760 1770 1780 1790 1800 IRLVDSVTVK GKSEAVNIYE VIDGEREDKR VLKMKILPWY QNGMDLYKRH CYEEALSYFQ 1810 1820 1830 1840 1850 1860 LCTEIMPNDK PTLIYIQRCI QNIKTLELQQ IQLQQLQRQQ LLQQQQQQLL LQQQLQQQQQ 1870 1880 1890 1900 1910 1920 QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ SQNIQQPQSQ QSQYVQQPQQ 1930 1940 1950 1960 1970 1980 QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQPQQQQQL QQQQQHQQQK QPSPQQQQQP 1990 2000 2010 2020 2030 2040 QQPQQQQQQQ IQNQYQHQLQ YQRQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 2050 2060 2070 2080 2090 2100 QQQQQHHHHH HQQQQFQQQS QQSQQQSQQQ QQQQQQQSQQ QSQQQSQQIQ KKSQHPHSQQ 2110 2120 IQSQRHQSQP QNVDTNVKTK PQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An adenylyl cyclase that functions during late development of Dictyostelium." Soederbom F., Anjard C., Iranfar N., Fuller D., Loomis W.F. Development 126:5463-5471(1999) [PubMed: 10556070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, FUNCTION, DISRUPTION PHENOTYPE. Strain: AX4.
[2]	"The genome of the social amoeba Dictyostelium discoideum." 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. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"A novel adenylyl cyclase detected in rapidly developing mutants of Dictyostelium." Kim H.-J., Chang W.-T., Meima M., Gross J.D., Schaap P. J. Biol. Chem. 273:30859-30862(1998) [PubMed: 9812977] [Abstract] Cited for: FUNCTION AS AN ADENYLYL CYCLASE ACTIVITY. Strain: AX2.
[4]	"Fingerprinting of adenylyl cyclase activities during Dictyostelium development indicates a dominant role for adenylyl cyclase B in terminal differentiation." Meima M.E., Schaap P. Dev. Biol. 212:182-190(1999) [PubMed: 10419694] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE. Strain: NC-4.
[5]	"Requirements for the adenylyl cyclases in the development of Dictyostelium." Anjard C., Soederbom F., Loomis W.F. Development 128:3649-3654(2001) [PubMed: 11566867] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE. Strain: AX4.
[6]	"Pharmacological profiling of the Dictyostelium adenylate cyclases ACA, ACB and ACG." Alvarez-Curto E., Weening K.E., Schaap P. Biochem. J. 401:309-316(2007) [PubMed: 16952277] [Abstract] Cited for: ENZYME REGULATION. Strain: NC-4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF153362 Genomic DNA. Translation: AAD50121.1. AAFI02000003 Genomic DNA. Translation: EAL73140.1.
RefSeq	XP_647665.1. XM_642573.1.
3D structure databases
HSSP	HSSP built from PDB template 1WC3 based on UniProtKB O32393.
ProteinModelPortal	Q55F68.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191294; DDB0191294; DDB_G0267376.
GeneID	8616482.
GenomeReviews	Gene locus acrA in contig CM000150_GR.
KEGG	ddi:DDB_G0267376.
Organism-specific databases
dictyBase	DDB_G0267376. acrA.
Phylogenomic databases
eggNOG	euNOG12860.
GeneTree	EPrGT00050000000552.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR003594. ATPase-like_ATP-bd. IPR011006. CheY-like_superfamily. IPR004358. Sig_transdc_His_kin-like_C. IPR005467. Sig_transdc_His_kinase_core. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 1 hit. G3DSA:3.30.565.10. ATP_bd_ATPase. 2 hits.
Pfam	PF00211. Guanylate_cyc. 1 hit. PF02518. HATPase_c. 1 hit. PF00072. Response_reg. 2 hits. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00044. CYCc. 1 hit. SM00387. HATPase_c. 1 hit. SM00448. REC. 2 hits. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 1 hit. SSF55874. ATP_bd_ATPase. 1 hit. SSF52172. CheY_like. 2 hits.
PROSITE	PS00452. GUANYLATE_CYCLASE_1. False negative. PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50109. HIS_KIN. 1 hit. PS50110. RESPONSE_REGULATORY. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYAD_DICDI

Accession

Primary (citable) accession number: Q55F68
Secondary accession number(s): Q9U9S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)