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Database: UniProt
Entry: A0A0D2JVD7_9EURO
LinkDB: A0A0D2JVD7_9EURO
Original site: A0A0D2JVD7_9EURO 
ID   A0A0D2JVD7_9EURO        Unreviewed;      1087 AA.
AC   A0A0D2JVD7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=Z520_09865 {ECO:0000313|EMBL:KIX94479.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX94479.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX94479.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX94479.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   EMBL; KN848087; KIX94479.1; -; Genomic_DNA.
DR   RefSeq; XP_016628602.1; XM_016780359.1.
DR   AlphaFoldDB; A0A0D2JVD7; -.
DR   STRING; 1442371.A0A0D2JVD7; -.
DR   GeneID; 27715611; -.
DR   VEuPathDB; FungiDB:Z520_09865; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16657; RING-Ubox_UBE4A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          987..1061
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1087 AA;  124333 MW;  7BA30895940166C3 CRC64;
     MADPSMDSDK IRNKRLAKLQ QSQPPPQSQD AVAAASSPSQ DGPDSTPSSR PETPQVDSPA
     LPTPTESATP SGTVTKEPSP PPTTRIRITP ANVTPQKREM DGLERPSSRQ SSRPNESIEQ
     WEDRTLRNIF RLSLNPEQTK DMHGQQLHVL AQLREELEAE GKPVLLSTDL LEQAIMEAGA
     DLGKLTPHDW LFGCWKRITR MSKAVKDRTP ENKKWTIISE ARRLCMSWCI LSVTTPDVFG
     AEYDGVAALA DHLLADPDED GGICGDFLTE VITRFDEDET IKGAFVGAVE NLSRRLAKLT
     MDSDYRRYTA MLRHLIRYKP VAIAITESKM FVDKSVPAAQ LEVATLLGPF FQLSPLQAEM
     TKQYFSGPKT MDPGRIRNSQ QSLQMSLRSH QTELFDIINT LVRASPEARE RVLDWFALVV
     NANHKRRAMR VDKATVSSDG FMINITTILD QLCEPFMDAQ FSKMDRVDID YLRRHPRVDI
     KEETKINADQ EHSDEFYKDQ LEGTNNFISE CFFLTVAAHY YGSEAARNML KDMDRDLKHM
     AKQIEMFETE RHKYVNNPAQ LAIFENALKK YKDQHDKGLS YKYAVQGVLL DEIAQTRSMQ
     FMRFVTVWIL RQVSPHRQFP KQNMTLPLPP EQPETFKNLP EYFLDVISSN FGFIMYNMPQ
     VISSTQSDEL IMLCITFLRN SEYIKNPYLK ASLVTILFRG TWSWRQGGRG ILADQYNSMP
     FATEHLLHSL MKFFIEAEFM GGHGQFFDKF NVRFEIFQII KCVWPNAVYR DNLLREAKVN
     MEFFVRFVNL LLNDVTFVLD ESFTAFHTIY DISKELSLAG TSLDQEQRKE KEEALEAAKS
     KAKSYMQLTN ETVAMLKLFT EALADAFTMP EIVQRLADML DYNLDAMVGP KSTTLKVENL
     QEYNFNPKAL LSEIVDVYLN LSERENFILA VARDGRSYKP ENFTNAGNIM RKFVLKAPEE
     LNRWQRLIEK FAKAKEEDEA ADADLGEVPD EFLDPLMFTL MEDPVRLPVS KIVIDRSTIR
     SHLLSDPHDP FNRVPLKIED VIPATDVKEQ IQKFKDERIG SRRKDFVETV KTETGGNADG
     EPMDLSQ
//
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