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InterPro: IPR006262 Cytidine deaminase, homotetrameric

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UniProtKB

Matches:

1127 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006262 Cyt_deam_tetra

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11644:SF2	Cyt_deam_tetra	1040
TIGRFAMs	TIGR01354	cyt_deam_tetra	980
Signatures in BioMart

InterPro Relationships Help

Contains

IPR002125 CMP/dCMP deaminase, zinc-binding
IPR016193 Cytidine deaminase-like

GO Term annotation Help

Process

GO:0046087 cytidine metabolic process

Function

GO:0004126 cytidine deaminase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family represents the small homotetrameric form cytidine deaminase, which is a zinc metalloprotein. It is found in humans and most bacteria. A related homodimeric form, IPR006263, with a much larger subunit is found in Escherichia coli [1] and in Arabidopsis thaliana (Mouse-ear cress). Both types may act on deoxycytidine as well as cytidine.

Structural links Help

PDB - click here

SCOP: c.97.1.1

CATH: 3.40.140.10

Database links Help

Enzyme: EC:3.5.4.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006262

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P19079 Cytidine deaminase

P32320 Cytidine deaminase

P56389 Cytidine deaminase

Q06549 Cytidine deaminase

Q09190 Putative cytidine deaminase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002125	CMP/dCMP deaminase, zinc-binding
IPR016193	Cytidine deaminase-like
IPR016192	APOBEC/CMP deaminase, zinc-binding
IPR006262	Cytidine deaminase, homotetrameric
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Carlow DC, Carter CW Jr, Mejlhede N, Neuhard J, Wolfenden R. Cytidine deaminases from B. subtilis and E. coli: compensating effects of changing zinc coordination and quaternary structure. Biochemistry 38 12258-65 1999 [PubMed: 10493793] http://dx.doi.org/10.1021/bi990819t

Additional Reading Open in usermanual
	Chung SJ, Fromme JC, Verdine GL. Structure of human cytidine deaminase bound to a potent inhibitor. J. Med. Chem. 48 2005 658-60 [PubMed: 15689149] http://dx.doi.org/10.1021/jm0496279
	Teh AH, Kimura M, Yamamoto M, Tanaka N, Yamaguchi I, Kumasaka T. The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse. Biochemistry 45 2006 7825-33 [PubMed: 16784234] http://dx.doi.org/10.1021/bi060345f
	Johansson E, Neuhard J, Willemoes M, Larsen S. Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase. Biochemistry 43 2004 6020-9 [PubMed: 15147186] http://dx.doi.org/10.1021/bi035893x
	Xie K, Sowden MP, Dance GS, Torelli AT, Smith HC, Wedekind JE. The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1. Proc. Natl. Acad. Sci. U.S.A. 101 2004 8114-9 [PubMed: 15148397] http://dx.doi.org/10.1073/pnas.0400493101
	Johansson E, Mejlhede N, Neuhard J, Larsen S. Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution. Biochemistry 41 2002 2563-70 [PubMed: 11851403] http://dx.doi.org/10.1021/bi011849a

InterPro 23.1