ID   PPIH_ASPOR              Reviewed;         181 AA.
AC   Q2TZ33;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase H;
GN   Name=cyp3; ORFNames=AO090103000002;
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP007174; BAE65490.1; -; Genomic_DNA.
DR   RefSeq; XP_001826623.1; XM_001826571.2.
DR   AlphaFoldDB; Q2TZ33; -.
DR   SMR; Q2TZ33; -.
DR   STRING; 510516.Q2TZ33; -.
DR   EnsemblFungi; BAE65490; BAE65490; AO090103000002.
DR   GeneID; 5998745; -.
DR   KEGG; aor:AO090103000002; -.
DR   VEuPathDB; FungiDB:AO090103000002; -.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   OMA; RHPNNPV; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..181
FT                   /note="Peptidyl-prolyl cis-trans isomerase H"
FT                   /id="PRO_0000232954"
FT   DOMAIN          17..180
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   181 AA;  20110 MW;  F0AB50731ED1F45B CRC64;
     MDSQVTSSAK TPNPVVFFDI TLGGESLGRI KMELFTSITP RTAENFRQFC TGESKSPQGR
     PQGYKNSKFH RVIKDFMIQG GDFVNGDGTG SRTIYGTPRF QDENFILKHD QPGLLSMANS
     GPNTNGCQFF ITTTATPFLN NKHVVFGQVV EGMDVVRMIE NTRTTRDKPN QDVTIIQCGE
     M