ID A0A0B7FB05_THACB Unreviewed; 560 AA.
AC A0A0B7FB05;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000313|EMBL:CEL53398.1};
DE EC=5.2.1.8 {ECO:0000313|EMBL:CEL53398.1};
GN ORFNames=RSOLAG1IB_11330 {ECO:0000313|EMBL:CEL53398.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL53398.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL53398.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL53398.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May catalyze the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides thereby assisting the folding of
CC proteins. May also function as a chaperone, playing a role in
CC intracellular transport of proteins. May also have a protein ubiquitin
CC ligase activity acting as an E3 ubiquitin protein ligase or as a
CC ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on
CC proteins. {ECO:0000256|ARBA:ARBA00003697}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000256|ARBA:ARBA00007930}.
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DR EMBL; LN679220; CEL53398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7FB05; -.
DR STRING; 1108050.A0A0B7FB05; -.
DR Proteomes; UP000059188; 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 GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd01923; cyclophilin_RING; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF1; RING-TYPE E3 UBIQUITIN-PROTEIN LIGASE PPIL2; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:CEL53398.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 61..139
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 323..469
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 205..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61259 MW; 4482E7C85A3073C3 CRC64;
MASDGTEWFG DGLRRSCLRY TTMGHGSNDK LYITHNEHSA GLHSASSRGF RAKQEGPHPG
SRTPFDCCAL SFQAFEFPVC ARNADGTGTV FDLTNIIPWL KEHNNTHPHT NEPLKPADLI
KLHYGKNSSG ALIDPITMKP LSEHSHIVAI ATTGNVFLAD SVSKFAGGRD LVADVAFKKE
DVITLQDPHR ITTLSIAAPV INAPKTTEDS KDKEPAKADA AKPSKSEVTA KPKKDLTEKP
QAAAVVNLKA KERAYNVSPF ASGYTGASLT STSLDPMTKS DAAMFDEEEL MFDDISKERS
QKAQKKNLAS RRAYVRMVTN LGGSLNLELF CEKAPKTCYN FIMLAKSGKY DNCPFHRLIP
GFMIQGGDPT GTGSGGESHW GTPFRDEFDM PKAEKHDSRG VLSMANKGLN SNGSQFFITF
KPTPHLDGKH TVFGKLVGGE DVLDAMESIP RAPGTEKPAK DIRITEVIVY QDPFEEYKAR
LARKLEHQSQ SGDPNKKRRA ETLEDSMTWF GQKVGEEQKG GAGQGGVGKY LKLEAPVTTA
RSADEGKKKR KTGFGNFDNW
//
