PPIL1_ASPOR
ID PPIL1_ASPOR Reviewed; 161 AA.
AC Q2U6U0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN Name=cyp1; ORFNames=AO090120000099;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily. {ECO:0000305}.
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DR EMBL; AP007166; BAE62725.1; -; Genomic_DNA.
DR RefSeq; XP_001823858.1; XM_001823806.2.
DR AlphaFoldDB; Q2U6U0; -.
DR SMR; Q2U6U0; -.
DR STRING; 510516.Q2U6U0; -.
DR EnsemblFungi; BAE62725; BAE62725; AO090120000099.
DR GeneID; 5996117; -.
DR KEGG; aor:AO090120000099; -.
DR HOGENOM; CLU_012062_16_3_1; -.
DR OMA; ELYNDHA; -.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..161
FT /note="Peptidyl-prolyl cis-trans isomerase-like 1"
FT /id="PRO_0000232963"
FT DOMAIN 1..155
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 161 AA; 17689 MW; C7A7C5A8739303E4 CRC64;
MATDVAFDTS MGSFTVELYN SHAPKTCKNF ATLAQRGYYN NVIFHRIIPN FMVQTGDPTG
TGRGGSSIYG EKFEDEIRAD LKHTGAGILS MANSGPNTNG SQFFVTLAPT PWLDGKHTIF
GRVKSGMRVI QRMGLVKTNG EDRPVDEVKI IRARVVEEGE E