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Database: UniProt
Entry: A0A0J9VK48_FUSO4
LinkDB: A0A0J9VK48_FUSO4
Original site: A0A0J9VK48_FUSO4 
ID   A0A0J9VK48_FUSO4        Unreviewed;      1099 AA.
AC   A0A0J9VK48;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-JAN-2026, entry version 40.
DE   SubName: Full=Ubiquitin conjugation factor E4 B {ECO:0000313|EMBL:KNB11121.1};
GN   ORFNames=FOXG_11140 {ECO:0000313|EMBL:KNB11121.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB11121.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNB11121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB11121.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA   Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA   Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNB11121.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB11121.1};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   EMBL; DS231709; KNB11121.1; -; Genomic_DNA.
DR   RefSeq; XP_018249166.1; XM_018390656.1.
DR   AlphaFoldDB; A0A0J9VK48; -.
DR   GeneID; 28952565; -.
DR   KEGG; fox:FOXG_11140; -.
DR   VEuPathDB; FungiDB:FOXG_11140; -.
DR   OrthoDB; 20295at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0036503; P:ERAD pathway; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   FunFam; 3.30.40.10:FF:000055; Ubiquitin conjugation factor e4 a; 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   Isomerase {ECO:0000256|ARBA:ARBA00023110};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          1011..1084
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          545..572
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..90
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  124801 MW;  ECDC9F3A7367D9AD CRC64;
     MDPNEQPSWA GGDAPDKEKM EQIRARRLAK LGTSTPVSAK SDENKAPDSE SSNPSRTSTP
     KPQPQPQPAS AESRPKINVT SAAPPASSSP NPFDKLGVKA EPSSSTGTSS MNRKRLASEI
     DDVVPADRPS PKPSTTQPES DESYADRTLS QIFRITVDPH NMVNSSGQRL TFLPNLNEEL
     NESGEPLKLS VNTLDQALME AASSYPHDKP LMNYFLPCWK RAVKASLQFK GTEGPKFEVH
     EEAKRLCMSG CLFALSMPDL YGRSPNPKHD TLMPYLLKGV QDENGLCFNF IQEAIKRFDD
     DEAFPALFND AMVQISSKLG TISMDQDYKP YIQAMLTYTR FPPLIVNLAK HPTFTMAQSA
     AGIEKHTLLG PFFRISPLQN EVIKSYFPGA RGLDKGRIAN SQDALRMVLR THQDDLFAIT
     NAFIRAGQET RSRTLDWFAY IMNSNHKRRA LQVDPREVAS NGFMINVTTI LDRFCEPFMD
     MDFSKVNKID DNYFRKQPRI NISDETKLNA DQSYADSFYA NKIPGETNFI SEAFFLTLAA
     HHYGSEACNS QLKNLDRDIK YLEKRVKIME ADRIKFVNNP VQLQQYDKAV QRHVDALEKS
     IAVKLSIEGV LLDERMQSTS LRFMRIVAVW LLRLVTRSEY KPGQESKEIQ LPLPAEKSDV
     FSCLPEYTLQ NIVDNFKFIF RWLPKILPSA VGDEMIALCV TFLRSTEYIK NPYLKSSLVS
     LLFSATWPLM HLKRGVLGDQ LVGSQFANDH LLKGLMKFYI ECESTGADSA FYDKFNIRYE
     IFQVIKCVWV NDHYKRQLTR ESRVNKQFFV QFVNMLLNDA TYVLDEALTK FPKIRAIEKE
     LEDPSIPQED RQKKEEEMQQ LANQATSFMQ LANETLEMMK LFTEAMSEAF TMPEIVSRLA
     SMLNYNLETL AGKKAAAELS VSNRDKYHFR PIQIISDIVD IYLNLGNSPV FIDAVAADGR
     SYKPEVLERV SRILISKHQK DPADVARWDK LRVKFVDAKT LLDQAELDLG DIPAEFEDPI
     MGDLMKDPVL LPSKHIVDRS TIVQHLLSDP KDPFTRQAMT IDDAIPQTEL KERIEQWREE
     RVQAAKDKLK SDVMDTTEG
//
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