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Database: UniProt
Entry: A0A1G4AWT6_9PEZI
LinkDB: A0A1G4AWT6_9PEZI
Original site: A0A1G4AWT6_9PEZI 
ID   A0A1G4AWT6_9PEZI        Unreviewed;      1077 AA.
AC   A0A1G4AWT6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ubiquitin elongating factor core {ECO:0000313|EMBL:OHE93553.1};
GN   ORFNames=CORC01_11150 {ECO:0000313|EMBL:OHE93553.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE93553.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHE93553.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE93553.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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:OHE93553.1}.
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DR   EMBL; MJBS01000117; OHE93553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4AWT6; -.
DR   STRING; 1209926.A0A1G4AWT6; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000176998; 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   CDD; cd16658; RING-Ubox_UBE4B; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT   DOMAIN          988..1061
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          532..559
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1077 AA;  121166 MW;  28410410A4B1C0B6 CRC64;
     MDTNEGNQAS DAPDVKKMND IRLRRLAKLG SSTRSPKPEG ESSADVETLN SATSEGKATK
     ASADTTLSST PKPVASNPFT QLGVRSASGA SSPAPSNAPD SNKRVASDRT PAPAPAKKAY
     TEESLDDFSD RTLSHVFRIT VDPERVVDAH GHKLTFLPEA SQELQENGSP LKLTTSILDS
     ALLEAVTAIP AEKPLLGYLL PSFKRIVRTN ILKETVDKRE VLEEAKRLCV SNSLFALTIP
     DLFGRSRPES LVTYLLKGHE QDDGVCLDFL REAVKRFPED DQFPVAFAEA MHTLSTKLST
     LTMEDDYKPY ISALMSYTKF PPLLNALAQH PNFMTTQTLG AHIERETILG PFFRISPLQS
     EVTMTYFPNP RGLDRTRAAP SQDALRAILR VHQDELFTIA NAFIRADTDT RSRVLDWFAS
     AINGNHKRRA LQVDPKEVSS DGFMMNLTVV LDRFCSPFMD TTFSKVDRIE VEYFRRSPRV
     NIKEETKLNA DQSASDAFYA TKSEGNSNFI SEVFFLTLAA HHYGSEATNS KLKSLERDIK
     WYEKHLAAME AERVKVQNQP QQLAMFELTL KRHTTVLEKA IAMKFAIEGV FLDEKMQELS
     LRFMRYVAVW LLRLASQSHY TPDKDLQLPL PAQAPEAFAC LPEYALQDVV DNFKFVYRYL
     PQIMPSAVGS EMIALCIAFL RSSEYIKNPY LKSSLVTLLF SGTWPFMHFK KGVLGDQLYG
     SKFANDNLLH ALMKFYIEAE STGANTQFYD KFNIRYEIFQ VIKCVWGNDV YKQQLTRESK
     VNRQFFVQFV NLLLNDATYV LDEALTKFPK IHTLQQELEF GNALSTQDRE KKQEELTQLE
     GQAGSYMQLA NETLAMMKLF TSALASAFTM PEIVQRLASM LNYNLETLAG PKMGQLKVNN
     PTKYHFQPRV LLSDFVDIYL NLGSSQAFID AVASDGRSYK PEIFDKASYI LSKRSMKEAN
     ELERLDTLKA KFLESKQIAD QAELDLGDIP AEFEDPIMGD LMKDPVILPS KHIVDRGTIV
     QHLLSDPKDP FTRQPMTVDD AIPHTELKEK IQKWREGKIA AAKARAAGDD AMDTTEG
//
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