ID A0A0D1X4N1_9EURO Unreviewed; 459 AA.
AC A0A0D1X4N1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU365081};
DE Short=PPIase {ECO:0000256|RuleBase:RU365081};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU365081};
GN ORFNames=PV11_04643 {ECO:0000313|EMBL:KIV82541.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV82541.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV82541.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV82541.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU365081}.
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 ECO:0000256|RuleBase:RU365081};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily. {ECO:0000256|ARBA:ARBA00010739,
CC ECO:0000256|RuleBase:RU365081}.
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DR EMBL; KN846952; KIV82541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1X4N1; -.
DR STRING; 1016849.A0A0D1X4N1; -.
DR HOGENOM; CLU_018791_2_1_1; -.
DR OrthoDB; 169228at2759; -.
DR Proteomes; UP000053599; 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-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR CDD; cd12235; RRM_PPIL4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45843; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR PANTHER; PTHR45843:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365081};
KW Nucleus {ECO:0000256|RuleBase:RU365081};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU365081};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU365081}.
FT DOMAIN 6..171
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 248..326
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 339..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 51764 MW; 915556389799248A CRC64;
MSVLLETSLG EVVIDLLVDS APKCCENFLK LCKVKYYNFS PVHSVQKGFS CQTGDPLGPD
SAESDGGSSI WGLLSGASNK SFVAEIDPKV KHTQRGTVSM ATVPSPNDSD ERLAGSQFII
TLGDDIDYLD GKAAPFGMVV EGFDTLEKIN DTFTDSNGRP LKDIRIRHTI ILEDPYDDPP
GLAIPDSSPA PTKAQLATVR IADDEELDQD MDEAAMDKLR REREARAQAL TLEMVGDLPF
AEVKPPENVL FVCKLNPVTH DEDLELIFSR FGKILSCEVI RDKRTGDSLQ YAFIEFENQK
DCEQAYFKMQ GVLIDDHRIH VDFSQSVSKL SDVWRNSTNN KRARHSGGFG GIADLEKKRH
YRDQDGGGRN GRGYRMVFDK DDIRRKGDSD LAKDFRRSRS RSPQPDVKSP THGGRRDRDR
DGGRYQDRTF RNSDRDNGRD SVRHRDRDRD RDYLGDRYR
//
