Reviewed, UniProtKB/Swiss-Prot Q99280 (CY43_TRYBB)

Names and origin

Protein names

Recommended name:
    Receptor-type adenylate cyclase GRESAG 4.3
    EC=4.6.1.1
Alternative name(s):
    ATP pyrophosphate-lyase
    Adenylyl cyclase

Gene names

Name:

GRESAG 4.3

Organism

Trypanosoma brucei brucei

Taxonomic identifier

5702 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	1229 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could act as a receptor for a unknown ligand.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase Receptor
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1229

1229

Receptor-type adenylate cyclase GRESAG 4.3

PRO_0000195739

Regions

Topological domain

1 – 24

24

Cytoplasmic Potential

Transmembrane

25 – 45

21

Potential

Topological domain

46 – 845

800

Extracellular Potential

Transmembrane

846 – 866

21

Potential

Topological domain

867 – 1229

363

Cytoplasmic Potential

Domain

889 – 1043

155

Guanylate cyclase

Sites

Metal binding

894

1

Magnesium

Metal binding

937

1

Magnesium

Amino acid modifications

Glycosylation

77

1

N-linked (GlcNAc...) Potential

Glycosylation

84

1

N-linked (GlcNAc...) Potential

Glycosylation

626

1

N-linked (GlcNAc...) Potential

Glycosylation

693

1

N-linked (GlcNAc...) Potential

Glycosylation

768

1

N-linked (GlcNAc...) Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1229

Helix Strand Turn

Details...

Beta strand

888 – 895

8

Helix

898 – 904

7

Turn

906 – 908

3

Helix

909 – 926

18

Beta strand

930 – 935

6

Beta strand

938 – 944

7

Helix

946 – 962

17

Helix

969 – 984

16

Beta strand

985 – 987

3

Helix

997 – 1003

7

Beta strand

1009 – 1016

8

Beta strand

1019 – 1022

4

Turn

1024 – 1026

3

Beta strand

1029 – 1033

5

Helix

1034 – 1045

12

Beta strand

1051 – 1054

4

Helix

1055 – 1060

6

Helix

1063 – 1067

5

Beta strand

1071 – 1077

7

Beta strand

1086 – 1091

6

Sequences

	Sequence		Length	Mass (Da)
	Q99280-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 2B2AA575C62AC288	FASTA	1,229	136,142
	10 20 30 40 50 60 MIARVCRLTK HSKPPHLPIT LTTPTLFLVV LVLLQLHPIC VLVNVDDGGG VTVKAISLLY 70 80 90 100 110 120 SRKWNVKVIN AVNAGLNASL AARNWTVAPG VNVEVVRPPS YDIDPAQFLD VYLKVLNDDK 130 140 150 160 170 180 SLLVVLGPMG NDDAEKLYDT LEENRLVGFG PMTVSTRHEG YMPHLYFLRP EATGESYCPS 190 200 210 220 230 240 TLCGESLRVL RQGFMYLDGL LGGSEAYDHA VDFISRMGYS FCCVFTVEDK AGGQGGSSEE 250 260 270 280 290 300 FDAVWDEFAG GNPQAVIMFA TMKPDAKKFL VRLVSDPRTE DTFVLTPIFL QKSIVSIWKE 310 320 330 340 350 360 TLEEANVPLH PHRVIQTGSN PLAKEDYIDA IKRFQTEMRN YLTEYKEWSG FNDADHFLKN 370 380 390 400 410 420 DADGELMVNG WIAGEVLRRA LRSHGWMNTA TAFLESLYEQ RRYVIDDIVV GDFGGECDSF 430 440 450 460 470 480 TSANGATCRC NRGGKNVYMR EIAEDYRLQP LVGGHIMTTP LQCHIDPSIL RPPLTGLTVD 490 500 510 520 530 540 MEDHEELLRG STQFETGVST TTSSGKAGEM NSFFLQKVVT DTQKVSNELN TLRQERIVTA 550 560 570 580 590 600 VFGIVTKAVL GLPGLTFIDP ITPTPHLNSF SRNVIHLSPT LEQQLYVLVN YLSSIRADFP 610 620 630 640 650 660 NCVIRGGEAP AIIDALRKTL VTFGLNLSST VVLTPGDTVG EHLPKSGITF IIGLAVDDIV 670 680 690 700 710 720 VIEEHLRIHT KARVLVQFSD IALLYNEFVQ AFNNSDGAKH LLFATSLPHW ADVDTTSETV 730 740 750 760 770 780 RRFHEAVREV EKWTPLSLLG FTTGRLIQEN LQNMERVTSD LLVDLFFNQT VITIDDMHYG 790 800 810 820 830 840 PYKHYDCIIN GVVTADDCMA NFGATDISVW SMARALRSDE PLLQNPMSPS LVYTVPNGNA 850 860 870 880 890 900 LTPAQLAGVV GGSLFVVALA ICLSVLACFT LRGTRDNDSA PKEPTGPVTL IFTDIESSTA 910 920 930 940 950 960 LWAAHPDLMP DAVATHHRLI RSLITRYECY EVKTVGDSFM IASKSPFAAV QLAQELQLRF 970 980 990 1000 1010 1020 LRLDWETNAL DESYREFEEQ RAEGECEYTP PTAHMDPEVY SRLWNGLRVR VGIHTGLCDI 1030 1040 1050 1060 1070 1080 RYDEVTKGYD YYGRTSNMAA RTESVANGGQ VLMTHAAYMS LSGEDRNQLD VTTLGATVLR 1090 1100 1110 1120 1130 1140 GVPEPVRMYQ LNAVPGRNFA ALRLDRELFN DGEDETTTSC SDHSSLRAEL SIAAQTIAAS 1150 1160 1170 1180 1190 1200 LQSLLGTFTP AQRQKALTPF CERCGVTLPR KMGHVWDNDS CQEVIRRIAA KVGHVVDRHA 1210 1220 AETRERSVCT LSSGSVIIIS NDLSDMIRV

References

[1]	"Differential expression of a family of putative adenylate/guanylate cyclase genes in Trypanosoma brucei." Alexandre S., Paindavione P., Tebabi P., Pays A., Halleux S., Steinert M., Pays E. Mol. Biochem. Parasitol. 43:279-288(1990) [PubMed: 1982555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: EATRO 1125.
[2]	"Structural analysis of adenylate cyclases from Trypanosoma brucei in their monomeric state." Bieger B., Essen L.-O. EMBO J. 20:433-445(2001) [PubMed: 11157750] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]	Erratum Bieger B., Essen L.-O. EMBO J. 20:5302-5302(2001)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52121 mRNA. Translation: CAA36366.1.

PIR

S14199.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FX4	X-ray	1.90	A	876-1106	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.6.1.1. 74165.

Family and domain databases

InterPro

IPR001054. A/G_cyclase.
[Graphical view]

Gene3D

G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.

Pfam

PF00211. Guanylate_cyc. 1 hit.
[Graphical view]

SMART

SM00044. CYCc. 1 hit.
[Graphical view]

PROSITE

PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CY43_TRYBB

Accession

Primary (citable) accession number: Q99280

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)