ID A0A135LAF8_PENPA Unreviewed; 302 AA.
AC A0A135LAF8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=PGRI_048130 {ECO:0000313|EMBL:KXG45957.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG45957.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG45957.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG45957.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388}.
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 Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000256|ARBA:ARBA00010898}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXG45957.1}.
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DR EMBL; LHQR01000069; KXG45957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LAF8; -.
DR STRING; 5078.A0A135LAF8; -.
DR OMA; EMEQNCN; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 1..103
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 239..272
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 302 AA; 33329 MW; 34F7DF8BCA89B8BD CRC64;
MIQGGDFTAF NGTGGESIYG EKFPDENFDL KHDRPFLLSM ANSGPGTNGS QFFVTTVPTP
HLDGKHVVFG EVINGKSVIR KIENLKTQSD KPIQDVTVVD CGELSGEDYE NATKRQQDAT
GDPYEDFTED HQGEQLTAPL CFKIASELKG FGNTAFKSGD LNLGLEKYQK GLRYLNEFPE
PDENDPKELG EQMKALRFTL HSNSALLGNK LQKFQQAQNW ASYALQVADA AKAKDADRAK
AYYRRAVAHE GLKEEDAALK DLREAEKLAP GDAGIINEIA KVKQTVKSRE AKEKAAAKKF
FS
//
