ID A0A1V6PQS2_9EURO Unreviewed; 545 AA.
AC A0A1V6PQS2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=PENANT_c052G04018 {ECO:0000313|EMBL:OQD79390.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD79390.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC subfamily. {ECO:0000256|ARBA:ARBA00038509}.
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:OQD79390.1}.
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DR EMBL; MDYN01000052; OQD79390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PQS2; -.
DR STRING; 416450.A0A1V6PQS2; -.
DR OrthoDB; 1328057at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 18..184
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 193..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 60171 MW; 01A248C1FCA4BCE3 CRC64;
MSSQYASEPN PTASATLNTT VGPIQIALFA NQTPLTCKNF LQHCKDNYYA GTIFHRVAPD
FVIQGGDPTG TGSGGTSIYE YPEFEYDPEA RDPNERVVLR DELHSRLRFN RRGLLGMAKS
EDGTYGSQFF ITLANTEREM NGQCTIFGRL EGDSIYNVLK IADAELVEGT ERPVYPIKVT
SCEVGELGPL EGKLKDRQAI SSTSKPEKQA PKKKKKAPKG GKTLLSFGDD EGDDGMPMRP
AKPKFNTQLV ADVPGAQTDA PKPKTSSDAQ SQPRKRQRSP SPRRLASPER KKRIKTPEPE
TQLPVQDPES PIRSPTPEAP KESKLSKTNA QIASLMASMR REVDTGPKDT GRKKSALEAM
IPETSIRGRR RPPPGSANGS SRNGTGPSNA AEREALQLFN AFKAKLEGAK PEPTPASQTK
TNGKESVQNK DADEDEEAQL CDLHFIANCQ SCQSWDDPSA DAGDDPAQEG DWLSHELRFG
KDTLGKDLEW KKKNQEADSL MVIDPREKEK EVVGSSSGKK RGFQRDRERE RKRERAGDLE
WERGR
//
