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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene
N/A
Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by cyclosporin A (CsA).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
Cyclophilin B
Rotamase B
S-cyclophilin
OrganismiSchistosoma japonicum (Blood fluke)
Taxonomic identifieri6182 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000002548324 – 213Peptidyl-prolyl cis-trans isomerase BAdd BLAST190

Proteomic databases

PRIDEiQ27774.

Structurei

3D structure databases

ProteinModelPortaliQ27774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 197PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST163

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi210 – 213Prevents secretion from ERBy similarity4

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q27774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLRVLCGL LLVSILFLGF VLSEGNGPKV TEKVFFDIEV DEQPLGRIII
60 70 80 90 100
GLFGKTVPKT VENFKQLSIG TTLKDGRTAA YKGSTFHRVI KSFMIQGGDF
110 120 130 140 150
TNHDGTGGFS IYGERFPDEN FKLKHVGAGW LSMANAGPNT NGAQFFITTT
160 170 180 190 200
QNPWLDGKHV VFGKVVEGMS VVRQIENMQT DSRDRPVKSV KIANCGHIPV
210
DVPFSVSNTD AAE
Length:213
Mass (Da):23,238
Last modified:November 1, 1996 - v1
Checksum:iD4986CDF7EDB8368
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50389 mRNA. Translation: AAC47316.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50389 mRNA. Translation: AAC47316.1.

3D structure databases

ProteinModelPortaliQ27774.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ27774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIB_SCHJA
AccessioniPrimary (citable) accession number: Q27774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.