ID F0UH00_AJEC8 Unreviewed; 586 AA.
AC F0UH00;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000256|ARBA:ARBA00020592};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=Cyclophilin-60 {ECO:0000256|ARBA:ARBA00030661};
DE AltName: Full=Cyclophilin-like protein Cyp-60 {ECO:0000256|ARBA:ARBA00030942};
DE AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000256|ARBA:ARBA00033051};
GN Name=CYP8 {ECO:0000313|EMBL:QSS55179.1};
GN ORFNames=HCEG_03614 {ECO:0000313|EMBL:EGC44399.1}, I7I53_02989
GN {ECO:0000313|EMBL:QSS55179.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|EMBL:EGC44399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|EMBL:EGC44399.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QSS55179.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS55179.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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: 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; DS990638; EGC44399.1; -; Genomic_DNA.
DR EMBL; CP069105; QSS55179.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UH00; -.
DR STRING; 544711.F0UH00; -.
DR VEuPathDB; FungiDB:I7I53_02989; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR OMA; NFIKHCA; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR Proteomes; UP000663419; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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 CDD; cd16663; RING-Ubox_PPIL2; 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; IPR026951; PPIL2_U-box_dom.
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:EGC44399.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 41..114
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 315..466
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 220..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 63948 MW; 2F52C5D3385CD1C7 CRC64;
MGKGTDKLYI THSEWASEDA YSASAGSGVR SKAGTVHSSF KRLPFNFCSL SLQPFSHPVC
TLSGTLFDLT NIIPWIKKHG TNPVDGTPLR SSDLIKLNFA KNDEGEYVDP VTYKAFTDNT
HIVALKPSGN VFAWDTLDKL NVKAKMWRDL VTDEEFGRKD IITLQDPQNI QSRDLSSFKF
LIDGESGLSD EQLREQRSTV NMNAMGSSAR ILKAKEAVSK ARAEREQKAH ATALEKSKGK
DTTVLGKNSS TKASMNQNKK PTPYNAAKHT TGLAAASFTS TGITPHTSAD LALLTDEQYM
LRRGRVNIKG YARISTTMGD LNLELHTEHA PKAVWNFIQL AKKGYYNDVT FHRNIKGFMI
QGGDPTGTGR GGESIWGKNF EDEIEGPFKH DARGTVSMAN KGKNTNSSQF FIAYRALPHL
NLKHTIFARL IDDPSPSSTT LNALEISPVD STNKPITPIR IINVTIFVDP FEEFLSQKRA
EEEAQTGAGP DPSNDSRSRD GQSDDQLTWT GKRVRTGGVA SSAASGGNMG VGRYLKAATA
AAAAAQAKTS EDEIAEFIDE EPDLEHARKK IKAANGGGGF GNFDSW
//
