ID   A0A0V1I182_9BILA        Unreviewed;      1072 AA.
AC   A0A0V1I182;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Ubiquitin conjugation factor E4 B {ECO:0000313|EMBL:KRZ16183.1};
DE   Flags: Fragment;
GN   Name=Ube4b {ECO:0000313|EMBL:KRZ16183.1};
GN   ORFNames=T11_4350 {ECO:0000313|EMBL:KRZ16183.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ16183.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ16183.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ16183.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
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}.
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:KRZ16183.1}.
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DR   EMBL; JYDP01000013; KRZ16183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1I182; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000055024; 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; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          988..1061
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ16183.1"
SQ   SEQUENCE   1072 AA;  123074 MW;  77A5FB04F86C5314 CRC64;
     LTLLLDDFVI IRFRMPHNQE ENNAAMESNP FALLTENVEQ EAELCTMNAE IAEDTSESSS
     PVKMDDYDPC SHSVIENENI CGDLMCEICS LLNVSKGSNS EFAFVLQPLE TLRDEACQNL
     AQWENACELV FCDLMFCLRK ENFAELLAPE ETLAPNVADE QRACREVFAH VWPESNTFES
     RIFNYSIICF NNIVAHMNAS VDHSKSCFVI PFRKIFFSLL ISLLSGNMFA QINLDEFRLV
     MIKSLLVESH DAFWSQLIAE VIQQSSENDS LMSEKFDKIF HPIISLLLTA NGAGKLTKSG
     MFAQALKAMS YLCQIKVGSS RPICSSLSRR ADFINTPYTT AVGREIALLS SVGQWFDFDS
     IEETHEFVEE QLQHSEESMS ESRKEVVYKI VRDRLDTCRY HCCKILKNLL TNAKSREAAI
     TYSYNVVLHN IRRGNIMVEH MTTAPDGFFL NFLYTFYQLS HKVILDKIDP MFILHPKCRK
     ISSRECAINM SEEELNTYIN NLHEEWSDPK FSTECFFLTV YIQHLSVVPG LRMHKRRLRN
     VQEAQRLLAQ VRAKRNTVPN TSSSEEAENH AKSIVSEIET IVQGLCTAYM LSEATFFDPN
     LLRNVLTFVN VQLSFIMKIL CLNGMDGLTP VKVPELFKTL PEFFVEDVMD LLIFLLSEKP
     ELIVHCSCDT LAHGLLTLVC NADQFKNPYL VAKVVEVIFY TCPHLRPAAH SLHMAILNHP
     LAPANFFRSL VKFYSDVESM GSSTEFFDKF TIRFHIQAVF KSMWQNAQHK LVIIDFCNEA
     DSSFIRFVNM LINDTTFLLD ESLEGLKRLN EAQRLMDDMT QWNTVQEEER ERILSQMQQD
     ERVVRSSLQL AHVIVDMFDF MTEDIKEPFL SAELGDRLAA MLNFNLAQLC GPKCRHLRVK
     NPQRFNWDPR ALLDQLTQIY LHLDNDKFAA AIANDERSYS KQLFEDVVGR IVRHKIKAVS
     QVEQFKLLAE RVEQIWEMKR EQEVILCDIP EEFTDPLMGT IMRNPVLLPS GNITDVSSIR
     RHLLNKPTDP FTRQQLDESM LIPATELKNK IDAWIAEKLK ESKAASVAKK TD
//