ID A0A0B2WX90_METAS Unreviewed; 586 AA.
AC A0A0B2WX90;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 08-NOV-2023, entry version 42.
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 ORFNames=MAM_01635 {ECO:0000313|EMBL:KHO00857.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO00857.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHO00857.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO00857.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
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:KHO00857.1}.
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DR EMBL; AZHE01000002; KHO00857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WX90; -.
DR STRING; 1081103.A0A0B2WX90; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR OrthoDB; 7846at2759; -.
DR Proteomes; UP000030816; 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:KHO00857.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 34..108
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 334..481
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 194..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 63620 MW; EF25765F97B62B96 CRC64;
MPITHSEWSS SDAYSASAGA KSSPLNASGA APFRRLPFNY CAASLQPFKN PVCTPDGTIF
DVEVIGAWLE KHPNQNPVNG EPLHKKDLIR LNFARNASSE PLSSGPSGDA KGDLIDPVTY
KVLTDNTHIV AIRHGTYANA FAWETVERMN IKPKLWQDLV DDQPFGRADI ITLQDPRNAA
SRNLEQFKYL KDGQGAQLTK EQEEEQRNAS GINASALGSM GDKVLKAKAA VEKARKAREA
GGDVNRSSGA LANPSAAAAA STGQSTATAA SQRVVTKDKK LAANAAAYTT GKAAASFTST
GLTPETSGER ALLTDEEFML RPRRVKAKGY ARMETNLGDL TVELHTDTAP RAVWNFIRLA
QTGYYKGVAF HRNMANFMIQ GGDPSGTGKG GSSIWGKYFN DEFDGPLTHN SRGILSMANK
GKNTNSSQFF ITYKATPHLD RKHTIFGLVV DGKDVLSKME AVQTDGSHRP LNKIFIKDIV
VFVDPFAEFQ TQRKEQERLE REREEVRRRG GTDDDRTTWT GKRIRGDGTV VSAEAKDSVG
KYLNKSAVSS MASDGAGAID STTGGWEEPV RKKTKGNGGF GNFDSW
//
