NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/emboj/19.21.5916; PubMed=11060042 [NCBI, ExPASy, EBI, Israel, Japan]
Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.;
"Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms.";
EMBO J. 19:5916-5929(2000).

Comments

FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins (By similarity).
CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H₂O = formate + methionyl peptide.
COFACTOR: Binds 1 Fe(2+) ion (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (Potential).
SIMILARITY: Belongs to the polypeptide deformylase family.

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

AF271258; AAG33981.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Les.2897

3D structure databases

HSSP

P27251; 1G2A. [HSSP ENTRY / PDB]

SMR

Q9FUZ0; 88-275.

ModBase

Q9FUZ0.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0042586;	Molecular function: peptide deformylase activity (inferred from electronic annotation from InterPro).
GO:0006412;	Biological process: translation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000181; Fmet_deformylase.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.45.10; Fmet_deformylase; 1.

PANTHER

PTHR10458; Fmet_deformylase; 1.

Pfam

PF01327; Pep_deformylase; 1.
Pfam graphical view of domain structure.

PRINTS

PR01576; PDEFORMYLASE.

ProDom

PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00079; pept_deformyl; 1.

ProtoNet

Q9FUZ0.

Other

UniRef

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

Keywords

Hydrolase; Iron; Metal-binding; Mitochondrion; Protein biosynthesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 277`		`Peptide deformylase, mitochondrial.`	`PRO_0000006731`
`ACT_SITE`	`239 239`		`By similarity.`
`METAL`	`196 196`		`Iron (By similarity).`
`METAL`	`238 238`		`Iron (By similarity).`
`METAL`	`242 242`		`Iron (By similarity).`

Sequence information

Length: 277 AA [This is the length of the unprocessed precursor]

Molecular weight: 30986 Da [This is the MW of the unprocessed precursor]

CRC64: 5E8DB2C695AEBE52 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMERFPRLAQ RVLSVPFTPK YLKSCKKTNP LTSHLMQLRG SQRPIFIQWN LQGRPSVCTD 

        70         80         90        100        110        120 
LISKKNYSSA TARAGWFLGL GEKKKQAMPD IVKAGDPVLH EPSQDIPLEE IGSERIQKII 

       130        140        150        160        170        180 
EEMVKVMRNA PGVGLAAPQI GIPLKIIVLE DTNEYISYAP KDETKAQDRR PFGLLVIINP 

       190        200        210        220        230        240 
KLKKKGNKTA LFFEGCLSVD GFRAVVERHL EVEVTGLDRN GKAIKVDASG WQARILQHEY 

       250        260        270 
DHLDGTLYVD KMAPRTFRTV ENLDLPLAAG CPKLGVC

Q9FUZ0 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