ID A0A367LGI5_9HYPO Unreviewed; 427 AA.
AC A0A367LGI5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE Flags: Fragment;
GN ORFNames=L249_5460 {ECO:0000313|EMBL:RCI13528.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13528.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13528.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13528.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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 -!- 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:RCI13528.1}.
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DR EMBL; LKCN02000006; RCI13528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LGI5; -.
DR STRING; 1330021.A0A367LGI5; -.
DR Proteomes; UP000253664; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR005651; Trm112-like.
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 Pfam; PF03966; Trm112p; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 95..253
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 257..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RCI13528.1"
SQ SEQUENCE 427 AA; 46661 MW; A452A07F1DD6E171 CRC64;
PVQVVSGTVP QVQGGGKRYI VLYNPGRCPF FPPFFRPSSQ DISFQLSPNI QQLEITMLNL
KGLLTTAALV LGITLVLFSQ VAEAAKGPKI THKVTFHMKH GDDDIGSIVM GLYGKTVPKT
AENFFQLSKK KAGEGYLDST FHRIIPQFMI QGGDFTKGDG TGGKSIYGEK FPDENFKLKH
TKPGILSMAN SGKDTNGSQF FITTVITSWL DGRHVVFGEV LEGMDVVTKI EKVPTDQRTN
KPEKPVRVAK VDTEELAEGA APGEDEPATP PAQDEGSAGW SSLQKLIVLG VFVGAVAIYL
RSRNHLNFLT CAVKACKSSS ASYPLHPRDA ELVQDDIEIN PEMLINLLPR LDWAALRETA
SELGFSELPE QPPAREQLQA DEGMLRDLHH LLLETQISEG KLVCGNCGHE YAVKEGIANF
LLPSHLV
//
