A3FQA7 (A3FQA7_CRYPI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493
EC=5.2.1.8 RuleBase RU000493

Gene names

ORF Names:

cgd2_4120 EMBL EAZ51416.1

Organism

Cryptosporidium parvum (strain Iowa II) [Complete proteome] EMBL EAZ51416.1

Taxonomic identifier

353152 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Conoidasida › Coccidia › Eucoccidiorida › Eimeriorina › Cryptosporidiidae › Cryptosporidium › Cryptosporidium parvum

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins By similarity. RuleBase RU000493 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493 SAAS SAAS020892
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420 SAAS SAAS020892
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAZ51416.1

Ontologies

Keywords
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Technical term	3D-structure PDB 2PLU PDB 2POY Complete proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A3FQA7 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 709330D5E8C8AAC8	FASTA	172	18,544
	10 20 30 40 50 60 MPNPVVYFDI SIGQTPAGRI TMELFADKVP ITAENFRALC TGEKGMGQSG KPLCYTGSFF 70 80 90 100 110 120 HRIIPQFMIQ GGDFTRGDGT GGESIYGSKF RDENFVYTHD APFLLSMANA GPNTNGSQFF 130 140 150 160 170 ITTVPCPWLD GKHVVFGKVL EGMEVVKSIE KCGSQNGKPT KSVCITASGV LS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the apicomplexan, Cryptosporidium parvum." Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G., Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P., Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L., Anantharaman V., Aravind L., Kapur V. Science 304:441-445(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Iowa II.
[2]	"Cryptosporidium Parvum Cyclophilin Type Peptidyl-Prolyl Cis-Trans Isomerase Cgd2_4120 in Complex with Cyclosporin A." Wernimont A.K., Lew J., Hills T., Kozieradzki I., Lin Y.H., Hassanali A., Zhao Y., Schapira M., Arrowsmith C.H., Edwards A.M., Weigelt J., Sundstrom M., Bochkarev A., Hui R., Artz J.D., Xiao T. Submitted (APR-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-170.
[3]	"Crystal structure of Cryptosporidium parvum cyclophilin type peptidyl-prolyl cis-trans isomerase cgd2_4120." Wernimont A.K., Lew J., Hills T., Kozieradzki I., Lin Y.H., Hassanali A., Zhao Y., Schapira M., Arrowsmith C.H., Edwards A.M., Weigelt J., Sundstrom M., Bochkarev A., Hui R., Artz J.D., Xiao T. Submitted (APR-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 3-170.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AAEE01000005 Genomic DNA. Translation: EAZ51416.1.

RefSeq

XP_001388243.1. XM_001388206.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PLU	X-ray	1.82	A	3-170	[»]
2POY	X-ray	1.80	A/B/C	3-170	[»]

ProteinModelPortal

A3FQA7.

SMR

A3FQA7. Positions 3-170.

ModBase

Search...

Protein-protein interaction databases

STRING

5807.cgd2_4120.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3373663.

KEGG

cpv:cgd2_4120.

Organism-specific databases

EuPathDB

CryptoDB:cgd2_4120.

Phylogenomic databases

HOGENOM

HOG000065981.

KO

K01802.

ProtClustDB

CLSZ2501168.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

A3FQA7.

Entry information

Entry name

A3FQA7_CRYPI

Accession

Primary (citable) accession number: A3FQA7

Entry history

Integrated into UniProtKB/TrEMBL:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	May 29, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)