NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Rowbotham-Bradford;
DOI=10.1126/science.1101485; PubMed=15486256 [NCBI, ExPASy, EBI, Israel, Japan]
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M.;
"The 1.2-megabase genome sequence of Mimivirus.";
Science 306:1344-1350(2004).

[2]

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
DOI=10.1128/JVI.00940-06; PubMed=16971431 [NCBI, ExPASy, EBI, Israel, Japan]
Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H., Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
"Mimivirus giant particles incorporate a large fraction of anonymous and unique gene products.";
J. Virol. 80:11678-11685(2006).

Comments

FUNCTION: May catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in the 6 collagen-like proteins of Mimivirus (Potential).
CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O₂ = procollagen trans-4-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
SUBCELLULAR LOCATION: Virion.
SIMILARITY: Belongs to the P4HA family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.

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

AY653733; AAV50856.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_142947.1; -.

3D structure databases

ModBase

Q5UP57.

Ontologies

GO:0004656;	Molecular function: procollagen-proline 4-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR006620; Pro_4_hyd_alph.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

SMART

SM00702; P4Hc; 1.
SMART graphical view of domain structure.

BLOCKS

Q5UP57.

Genome annotation databases

GeneID

3162420; -.

Other

ProtoNet

Q5UP57.

UniRef

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

Keywords

Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Virion; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 242`	`242`		`Putative prolyl 4-hydroxylase.`	`PRO_0000206660`

Sequence information

Length: 242 AA [This is the length of the unprocessed precursor]

Molecular weight: 27901 Da [This is the MW of the unprocessed precursor]

CRC64: EF3D0F965EC41C2A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTVTIITII VVIIVVILII MVLSKSCVSH FRNVGSLNSR DVNLKDDFSY ANIDDPYNKP 

        70         80         90        100        110        120 
FVLNNLINPT KCQEIMQFAN GKLFDSQVLS GTDKNIRNSQ QMWISKNNPM VKPIFENICR 

       130        140        150        160        170        180 
QFNVPFDNAE DLQVVRYLPN QYYNEHHDSC CDSSKQCSEF IERGGQRILT VLIYLNNEFS 

       190        200        210        220        230        240 
DGHTYFPNLN QKFKPKTGDA LVFYPLANNS NKCHPYSLHA GMPVTSGEKW IANLWFRERK 


FS

Q5UP57 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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