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
//