PPIL1_SCHPO
ID PPIL1_SCHPO Reviewed; 155 AA.
AC P87051;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase ppi1;
DE Short=PPIase ppi1;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin ppi1;
DE AltName: Full=Rotamase ppi1;
GN Name=ppi1; Synonyms=cyp2; ORFNames=SPAC57A10.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SNW1.
RX PubMed=11690648; DOI=10.1016/s0167-4781(01)00301-3;
RA Skruzny M., Ambrozkova M., Fukova I., Martinkova K., Blahuskova A.,
RA Hamplova L., Puta F., Folk P.;
RT "Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in
RT Dictyostelium discoideum and Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1521:146-151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Interacts with cwf13/snw1. {ECO:0000269|PubMed:11690648}.
CC -!- INTERACTION:
CC P87051; Q09882: prp45; NbExp=4; IntAct=EBI-1810686, EBI-457758;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF337536; AAK14383.1; -; mRNA.
DR EMBL; CU329670; CAB08166.1; -; Genomic_DNA.
DR PIR; T38930; T38930.
DR RefSeq; NP_593308.1; NM_001018738.2.
DR PDB; 3JB9; EM; 3.60 A; d=1-155.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; P87051; -.
DR SMR; P87051; -.
DR BioGRID; 279455; 11.
DR IntAct; P87051; 1.
DR STRING; 4896.SPAC57A10.03.1; -.
DR MaxQB; P87051; -.
DR PaxDb; P87051; -.
DR EnsemblFungi; SPAC57A10.03.1; SPAC57A10.03.1:pep; SPAC57A10.03.
DR GeneID; 2543019; -.
DR KEGG; spo:SPAC57A10.03; -.
DR PomBase; SPAC57A10.03; -.
DR VEuPathDB; FungiDB:SPAC57A10.03; -.
DR eggNOG; KOG0881; Eukaryota.
DR HOGENOM; CLU_012062_16_3_1; -.
DR OMA; ELYNDHA; -.
DR PhylomeDB; P87051; -.
DR PRO; PR:P87051; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:PomBase.
DR GO; GO:0006457; P:protein folding; IC:PomBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..155
FT /note="Peptidyl-prolyl cis-trans isomerase ppi1"
FT /id="PRO_0000064176"
FT DOMAIN 1..154
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 155 AA; 16864 MW; E3D1640E30486D21 CRC64;
MANVELQTSL GKILIELYTE HAPKTCQNFY TLAKEGYYDG VIFHRVIPDF VIQGGDPTGT
GRGGTSIYGD KFDDEIHSDL HHTGAGILSM ANAGPNTNSS QFFITLAPTP WLDGKHTIFG
RVVSGLSVCK RMGLIRTDSS DRPIEPLKII KAVAL
