Q03101 (CYAG_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylate cyclase, germination specific
EC=4.6.1.1

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

Gene names

Name:	acgA
Synonyms:	acg
ORF Names:	DDB_G0274569

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	858 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Has a large extracellular domain which may be involved in the recognition of an extracellular signal present during germination, leading to activation or inhibition of cAMP synthesis by the cytoplasmic domain.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Enzyme regulation	Insensitive to guanine nucleotides.
Subcellular location	Membrane; Single-pass type II membrane protein.
Developmental stage	After fruiting bodies have been formed and during germination.
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 1 CHASE domain. Contains 1 guanylate cyclase domain.

Ontologies

Keywords
Biological process	Germination cAMP biosynthesis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro regulation of protein kinase activity Traceable author statement. Source: dictyBase response to osmotic stress Inferred from genetic interaction. Source: dictyBase spore germination Inferred from mutant phenotype. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype. Source: dictyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: dictyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from mutant phenotype. Source: dictyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from direct assay. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 858

858

Adenylate cyclase, germination specific

PRO_0000195715

Regions

Topological domain

1 – 18

18

Cytoplasmic Potential

Transmembrane

19 – 41

23

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

42 – 858

817

Extracellular Potential

Domain

86 – 317

232

CHASE

Domain

396 – 526

131

Guanylate cyclase

Compositional bias

738 – 848

111

Asn-rich

Compositional bias

835 – 848

14

Poly-Asn

Sites

Metal binding

401

1

Magnesium 1 By similarity

Metal binding

401

1

Magnesium 2 By similarity

Metal binding

402

1

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

445

1

Magnesium 1 By similarity

Metal binding

445

1

Magnesium 2 By similarity

Experimental info

Sequence conflict

755

1

L → F in AAA33164. Ref.1

Secondary structure

1

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858

Helix Strand Turn

Details...

Beta strand

391 – 398

8

Helix

403 – 408

6

Helix

415 – 432

18

Beta strand

439 – 443

5

Beta strand

446 – 451

6

Helix

462 – 473

12

Beta strand

475 – 478

4

Turn

479 – 482

4

Beta strand

495 – 500

6

Beta strand

506 – 509

4

Helix

517 – 527

11

Beta strand

531 – 534

4

Helix

538 – 542

5

Sequences

	Sequence		Length	Mass (Da)
	Q03101 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: B409D387D8A96453	FASTA	858	98,380
	10 20 30 40 50 60 MKKTFVKILS KSYVEGYPVG FFIGLIILAI FGSMVCIFSF MHYSEEENSN IQMDLERSSK 70 80 90 100 110 120 QIIHNIQMNA MYLLSSIDTL KALYYVNPNF DRNDFNVFLN TTLKNSEFQY LFWIKKINNN 130 140 150 160 170 180 DRNCFEEKFS KEIKDTFQIY SFDENTNSIH VAKNKSSYFP ILHAFPDINK DIIGLDINST 190 200 210 220 230 240 DYMNETIKKS IFNKKPTVHL NKKVLLSKRN IDILIVSPII VTKTLESTNE TMEDMSHISS 250 260 270 280 290 300 GLFLMEKNVQ ASRIEVENGN DFTIFLSTTN GEIVYQENYL NFKTLYQVHE SGLFEDRLKY 310 320 330 340 350 360 ESSLKIADCV LKLWIFTTEE YENNSKTYLP LLVSIISAVI LVLLITYSVD QRKQKSLIAK 370 380 390 400 410 420 IMREKNNLIN KILPLEVSVK LENGEDVVAE RSNNACVFFL DIAGFTRFSS IHSPEQVIQV 430 440 450 460 470 480 LIKIFNSMDL LCAKHGIEKI KTIGDAYMAT CGIFPKCDDI RHNTYKMLGF AMDVLEFIPK 490 500 510 520 530 540 EMSFHLGLQV RVGIHCGPVI SGVISGYAKP HFDVWGDTVN VASRMESTGI AGQIHVSDRV 550 560 570 580 590 600 YQLGKEDFNF SERCDIIHVK GKGRMKTWYL MGKKSSDFSL KKDFSRSRVQ PSLFNRKQSH 610 620 630 640 650 660 VHCIYPEFPS GLQALNIENN LNNTDAGCEN CSKILKKTYA YSPDHSTSNY YYHGDDNSPP 670 680 690 700 710 720 PPSLNSNDLI DGSEYHDDPF PSDSNVGYHD TSKDIKEDEN EQNETLLFNQ EQLKKKQIEN 730 740 750 760 770 780 IQRDLSLNDS IEAIKILNNN NNNNINDNNI NNTNLNNNNN DININNSDNV NNYENNNNFS 790 800 810 820 830 840 DKIENNDGDN NNINDNNYKS TNENNIKSKT LFKDSKSLIN DIKMAKENCD NNDDNNNNNN 850 NNNNNNNNDE NVESKKNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structurally distinct and stage-specific adenylyl cyclase genes play different roles in Dictyostelium development." Pitt G.S., Milona N., Borleis J., Lin K.C., Reed R.R., Devreotes P.N. Cell 69:305-315(1992) [PubMed: 1348970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"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.
[4]	"Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis." Liu Y., Ruoho A.E., Rao V.D., Hurley J.H. Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997) [PubMed: 9391039] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 387-543.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M87278 Genomic DNA. Translation: AAA33164.1.
AAFI02000012 Genomic DNA. Translation: EAL70177.1.

PIR

A42239.

RefSeq

XP_643956.1. XM_638864.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AWM	model	-	A/B	387-543	[»]

ProteinModelPortal

Q03101.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblProtists

DDB0185013; DDB0185013; DDB_G0274569.

GeneID

8619384.

GenomeReviews

Gene locus acgA in contig CM000151_GR.

KEGG

ddi:DDB_G0274569.

Organism-specific databases

dictyBase

DDB_G0274569. acgA.

Phylogenomic databases

eggNOG

KOG1023.

GeneTree

EPrGT00050000001678.

Family and domain databases

InterPro

IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR006189. CHASE.
[Graphical view]

Gene3D

G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.

Pfam

PF03924. CHASE. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
[Graphical view]

SMART

SM01079. CHASE. 1 hit.
SM00044. CYCc. 1 hit.
[Graphical view]

SUPFAM

SSF55073. A/G_cyclase. 1 hit.

PROSITE

PS50839. CHASE. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CYAG_DICDI

Accession

Primary (citable) accession number: Q03101
Secondary accession number(s): Q555V4, Q86A89

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)