ID A0A1Y2DY33_9PEZI Unreviewed; 1003 AA.
AC A0A1Y2DY33;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ubiquitin elongating factor core-domain-containing protein {ECO:0000313|EMBL:ORY64119.1};
GN ORFNames=BCR38DRAFT_343225 {ECO:0000313|EMBL:ORY64119.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY64119.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY64119.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY64119.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORY64119.1}.
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DR EMBL; MCFJ01000007; ORY64119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DY33; -.
DR STRING; 1141098.A0A1Y2DY33; -.
DR InParanoid; A0A1Y2DY33; -.
DR OrthoDB; 1554at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193689; 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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT DOMAIN 915..988
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 113102 MW; BC06018350475008 CRC64;
METGITRPLK RHPHTRTCAD EEASPAAAPP AKKIHVKDEK IDDWSDRVLS DVFRVTLDVT
RALDSRGARL AYLPNLKDEI ERSGEPTKLT ALNIDQAILE AASAVPASRP LFSYLLPCFK
RVVRAASTSR RPTPEKQAVL DEAKRLCMSH CIFALTMPDL YGREPNASHD TLAPYLLRHH
ENDDGVCLDF FNEAVSRMKE DEQIAPIFTE AMVQISNKLA TMSMNDDYRP YVNCLVTYSR
YPALLDALAQ HDHFLVTPTP GMTKEQIAVS SEVDSILGPF FRISPLQPEV TKSYFANPRT
IDPGHIKTSQ SALQMTLKTH QGDLTSIINA FVRSGQTARN RVLDWFAFIV NTNHKRRALQ
LNPTHVASDG FMVNVTATLD QLCEPFMDAS FSKISKIDID YLRRNPRVNI SDETKLNADQ
SSSDEFYDKK VEGTSNFISE VFFLNLAAHH YGSEAANSKL KDLDKDIKHF QRAEKEMSEN
MKKLPNNSPQ MFAAKLQYDK IINVLEKSMA LRFSIEGVLT DKSMQTLSLQ FMRYVTVWLL
RVASGSAYVP GQSLKLPLSK DSPQEFNCLP EYALQDVVDN FKFVMRFMPQ IMMSAVGDEI
AALCITFLRS SEYVKNPYLK SSLVTLLFSG TFPMYHLSRG ILGDILVGSQ FANEHLLHAL
MKFYIECESS GVSTAFYDRF NIRYEIFQVM KTIWQNSVYK EQLSKESKVN RQFFVQFVNL
LLNDATYLLD EALSKLAKIH DYQKQLLDQS LSPEDREKVQ SDMEQAEQQC QSWMSLVNET
MAMMKLFTEA LKDAFTMPEI VGRLASMLDY NLETLVGPKR GNLKVEDAKK YNFDAKTLLS
GFIDIYLNLG SQEAFIDAVA ADGRSYKPAN FDAASKILSG KGLKTPEELA KWATLKQKVA
KAKEIADQAE VDLGEVPSEF EDPIMGILME DPVLLPSKAI VDRSTIVQHL LSDARDPFNR
NPMTIEDVIP VDELRRQVQA WKAERVAIAE AKLAGDAMDT TAG
//
