ID A0A1B8GW67_9PEZI Unreviewed; 576 AA.
AC A0A1B8GW67;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 08-NOV-2023, entry version 32.
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:OBU00093.1};
GN ORFNames=VE01_01835 {ECO:0000313|EMBL:OBU00093.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBU00093.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBU00093.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBU00093.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV460210; OBU00093.1; -; Genomic_DNA.
DR RefSeq; XP_018133825.1; XM_018271350.1.
DR AlphaFoldDB; A0A1B8GW67; -.
DR STRING; 342668.A0A1B8GW67; -.
DR GeneID; 28835221; -.
DR OrthoDB; 7846at2759; -.
DR Proteomes; UP000091956; 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-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 Pfam; PF04564; U-box; 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:OBU00093.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 39..112
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 323..470
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63711 MW; A78370CFA007ED05 CRC64;
MGKGTDKLYI THSEWSSSDQ FSASAGSNVN ARSAPGSFKR LPFNFCAASL QPFHHPVCTP
SGTIFDIEVI STWLATHTTN PVTGAPLKSS ELIKLNFARN GDTDAGAAEG RKEALGEMVD
PVTFKVFTDN THIVAIRHGG EANVFAWETV ERLNVKARMW RDLVDDREFS RKDIITLQDP
QNVESRDLSQ FKFLKEGESV LTKREEEERK GGSVNVAALG RVGEKVLKAK EAVEKARRER
EANGDVNRTK AVAKASAPVM RPQMHTQKKE VYNAAQYTTG KAAASFTSTG LTPSTSGERA
LLTEEEYMLR PKRVKNKGYA RLETNYGSLN LELYPETAPR AVWNFIQLAK KGYYKGVIFH
RSIRNFMLQG GDPTGTGKGG TSCWGKNFQD EFDGPLTHDA RGIVSMANKG KNTNSSQFFI
LYRPQKHLDR KHTIFARVVG GMDVLARIEA VPVDSGDRPT EEVVIEDVVV FVDPFEEFQA
ERREREGKER EREEVERMGG KEDDRTTWTG KRVRGDGTVV QSEEAGGVGR YLKAAIEEGK
GGGDGGEREG EGGGWEEEPV KKKVKAAGGF GNFDGW
//