NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CXM1-105;
DOI=10.1007/s004380051052; PubMed=10485295 [NCBI, ExPASy, EBI, Israel, Japan]
Sharypova L.A., Yurgel S.N., Keller M., Simarov B.V., Puehler A., Becker A.;
"The eff-482 locus of Sinorhizobium meliloti CXM1-105 that influences symbiotic effectiveness consists of three genes encoding an endoglycanase, a transcriptional regulator and an adenylate cyclase.";
Mol. Gen. Genet. 261:1032-1044(1999).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294798; PubMed=11481432 [NCBI, ExPASy, EBI, Israel, Japan]
Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid.";
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).

Comments

CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
SIMILARITY: Contains 1 guanylate cyclase domain.
SIMILARITY: Contains 5 TPR repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ225896; CAB38103.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006469; AAK65519.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E95369; E95369.

RefSeq

NP_436107.2; -.

3D structure databases

ModBase

Q9Z3Q0.

Enzyme and pathway databases

BioCyc

SMEL266834:SMA1583-MON; -.

Ontologies

GO:0004016;	Molecular function: adenylate cyclase activity (inferred from electronic annotation from EC).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006171;	Biological process: cAMP biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001054; A/G_cyclase.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.1230; A/G_cyclase; 1.
G3DSA:1.25.40.10; TPR-like_helical; 1.

Pfam

PF00515; TPR_1; 4.
Pfam graphical view of domain structure.

SMART

SM00044; CYCc; 1.
SM00028; TPR; 4.
SMART graphical view of domain structure.

PROSITE

PS50125; GUANYLATE_CYCLASE_2; 1.
PS50005; TPR; 4.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9Z3Q0.

Genome annotation databases

6435284; -.

AE006469_GR; RA0861.

sme:SMa1583; -.

fig|266834.1.peg.861; -.

Phylogenomic databases

HOGENOM

Q9Z3Q0; -.

Genome annotation databases

CMR

Q9Z3Q0; RA0861.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

cAMP biosynthesis; Complete proteome; Lyase; Plasmid; Repeat; TPR repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 587`	`587`	`Putative adenylate cyclase 3.`	`PRO_0000195746`
`DOMAIN`	`12 127`	`116`	`Guanylate cyclase.`
`REPEAT`	`343 376`	`34`	`TPR 1.`
`REPEAT`	`421 454`	`34`	`TPR 2.`
`REPEAT`	`455 488`	`34`	`TPR 3.`
`REPEAT`	`490 522`	`33`	`TPR 4.`
`REPEAT`	`524 556`	`33`	`TPR 5.`
`CONFLICT`	`18 18`		`A -> T (in Ref. 1; CAB38103).`
`CONFLICT`	`178 178`		`R -> H (in Ref. 1; CAB38103).`
`CONFLICT`	`183 183`		`P -> L (in Ref. 1; CAB38103).`
`CONFLICT`	`196 197`		`KP -> S (in Ref. 1; CAB38103).`
`CONFLICT`	`251 251`		`D -> N (in Ref. 1; CAB38103).`
`CONFLICT`	`553 553`		`N -> D (in Ref. 1; CAB38103).`

Sequence information

Length: 587 AA [This is the length of the unprocessed precursor]

Molecular weight: 65307 Da [This is the MW of the unprocessed precursor]

CRC64: 4630AC9816FB615D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKESIRRRL AAILAADAVG YSRLMERDEK STHTLLMARW KEVLEPLVGI HQGRVFKRTG 

        70         80         90        100        110        120 
DGVLVEFGSA VNAVECAAAL QQAMAAANRD LPEDRAIVLR VGVNLGDIMV EDSDLFGDGV 

       130        140        150        160        170        180 
NVAARIEALA DPGGVAISDG IHEYVHGRTD IDFVDSGYHE VKNIERPVHI WTWSPKDRAR 

       190        200        210        220        230        240 
EPPNIAAEPP PQLPAKPSIA VLPFDNMSGD PEQGYFADGI TEDIITDLSK VSGLFVIARN 

       250        260        270        280        290        300 
SSFAYKGKTP DIRKVSRELG VRYVLEGSVR RAANRIRINA QMIDGTTGGH LWAERYDRGL 

       310        320        330        340        350        360 
EDIFAVQDEV TRTIVNALRV KLTAGEEERR ESRGKVDPEA YDLLVRSRQA ILQFNALSSM 

       370        380        390        400        410        420 
EARRMLHRVL EIDPGMAAAH ASLSIIALTD FINQWNGATP DNLTQALGLA QEAIDTDGSE 

       430        440        450        460        470        480 
PQGHYTLALA LSWMRRLDEA EHAAERAIEL DPNSANAYTA LGTIRDFQGR HEEALALYTR 

       490        500        510        520        530        540 
AHRLDPQFDL SLHFQGRALL NLGRFDEAEV AFKRRLLLAP RSDMTRFYLA CLYGRTGRHE 

       550        560        570        580 
EARGYWREVL GVNPSFSVDH LRRSLPYQDP HLMDRLVEGL REAGVSI

Q9Z3Q0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools