(data stored in ACNUC2731 zone)

HOGENOM: SCHMA_100_PE13

ID   SCHMA_100_PE13                       STANDARD;      PRT;   213 AA.
AC   SCHMA_100_PE13; Q26551;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B; Short=PPIase B;
DE   EC=5.2.1 8;AltName: Full=Cyclophilin B;AltName: Full=Rotamase B;AltName:
DE   Full=S-cyclophilin;Flags: Precursor; (SCHMA_100.PE13).
GN   Name=CYP;
OS   SCHISTOSOMA MANSONI.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Acoelomata; Platyhelminthes;
OC   Trematoda; Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae;
OC   Schistosoma.
OX   NCBI_TaxID=6183;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHMA_100.PE13.
CC       Schistosoma mansoni scaffold Smp_scaff000100 sma_v3.1  sequence
CC       1..1567898 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PPIB_SCHMA
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by cyclosporin A (CsA).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- DEVELOPMENTAL STAGE: This soluble protein is present in abundance
CC       in the adult worm as well as in the schistosomula and the eggs.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       B subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- GENE_FAMILY: HOG000065981 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schistosoma_mansoni;SMP_040790;SMP_040790__MRNA;SMP_040790__MRNA.
DR   EMBL; FN357391; - ;
DR   EMBL; U30874; - ;
DR   UniProtKB/Swiss-Prot; Q26551; -.
DR   EMBL; U30874; AAC46985.1; -; mRNA.
DR   ProteinModelPortal; Q26551; -.
DR   SMR; Q26551; 27-206.
DR   EnsemblMetazoa; Smp_040790__mRNA; Smp_040790__mRNA; Smp_040790.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR015891; Cyclophilin-like.
DR   InterPro; IPR020892; Pep-Pro_Isoase_cyclophilin_CS.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; CSA_PPIase; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   HOGENOMDNA; SCHMA_100.PE13; -.
KW   Smp_04079010037236820036002503210000011;
KW   Q26551; C4Q8B8; FN357391; U30874;
KW   Cyclosporin; Endoplasmic reticulum; Isomerase; Rotamase; Signal.
SQ   SEQUENCE   213 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAVLKLLCPL LLLSIICFGL IRSEANGPKV TDKVFFDIEV DGKPLGRIII GLFGKTVPKT
     VENFKQLSIG TQLKDGRTAS YKGSTFHRVI KSFMIQGGDF TNHDGTGGFS IYGDRFPDEN
     FKLRHVGAGW LSMANAGPDT NGSQFFITTV KTSWLDGKHV VFGKVVEGMN IVRQIESETT
     DSRDRPVKSI KIASCGHIPV EIPFSVTNSD AVE
//

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