Q4QBH1 (Q4QBH1_LEIMA) 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

Name:	CYP11 EMBL CAJ03831.1
ORF Names:	LMJF_23_0050 EMBL CAJ03831.1

Organism

Leishmania major [Reference proteome]

Taxonomic identifier

5664 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania major species complex

Protein attributes

Sequence length	295 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

Ontologies

Keywords
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Technical term	3D-structure PDB 2HQJ Complete proteome Reference 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)
	Q4QBH1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 69AAC0FBD9533143	FASTA	295	31,497
	10 20 30 40 50 60 MSRTSVPPKV GQRPGIGVEK TTNPKVFFDI SIDNKAAGRI VMELYADTVP KTAENFRALC 70 80 90 100 110 120 TGEKGKGRSG KPLHYKSSVF HRVIPNFMIQ GGDFTRGNGT GGESIYGTTF RDESFSGKAG 130 140 150 160 170 180 RHTGLGCLSM ANAGPNTNGS QFFICTAATP WLDGKHVVFG RVIDGLDVVK KVERLGSSSG 190 200 210 220 230 240 KTRSRIVVSD CGEVAADKSK GQRPPQQQHQ PAKASADMKR AADKKAVAEK LLASSPAAEG 250 260 270 280 290 QKALSAKKET PPQVAAPSEA KKRMRAVDEE ETRLARLREK KAKLAALRSS AAGNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the kinetoplastid parasite, Leishmania major." Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G. , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G., Myler P.J. Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MHOM/IL/81/Friedlin.
[2]	"Cyclophilin from Leishmania major." Arakaki T.L., Merritt E.A. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-198.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

FR796419 Genomic DNA. Translation: CAJ03831.1.

RefSeq

XP_001683327.1. XM_001683275.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HQJ	X-ray	2.00	A	1-198	[»]

ProteinModelPortal

Q4QBH1.

SMR

Q4QBH1. Positions 22-199.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblProtists

LmjF.23.0050:mRNA; LmjF.23.0050:pep; LmjF.23.0050.

GeneID

5651954.

KEGG

lma:LMJF_23_0050.

Phylogenomic databases

HOGENOM

HOG000065980.

KO

K01802.

OMA

IYGTTFR.

ProtClustDB

CLSZ2456372.

Family and domain databases

InterPro

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

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

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

Q4QBH1.

Entry information

Entry name

Q4QBH1_LEIMA

Accession

Primary (citable) accession number: Q4QBH1

Entry history

Integrated into UniProtKB/TrEMBL:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)