ID A0A7L3ZNC5_9AVES Unreviewed; 1346 AA.
AC A0A7L3ZNC5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=Ubiquitin conjugation factor E4 B {ECO:0000256|ARBA:ARBA00072779};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 B {ECO:0000256|ARBA:ARBA00083610};
DE AltName: Full=Ubiquitin fusion degradation protein 2 {ECO:0000256|ARBA:ARBA00081821};
DE Flags: Fragment;
GN Name=Ube4b {ECO:0000313|EMBL:NXW14511.1};
GN ORFNames=CIRPEC_R13577 {ECO:0000313|EMBL:NXW14511.1};
OS Circaetus pectoralis (black-chested snake-eagle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Circaetus.
OX NCBI_TaxID=321084 {ECO:0000313|EMBL:NXW14511.1, ECO:0000313|Proteomes:UP000562238};
RN [1] {ECO:0000313|EMBL:NXW14511.1, ECO:0000313|Proteomes:UP000562238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-010-60 {ECO:0000313|EMBL:NXW14511.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXW14511.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. May also
CC function as an E4 ligase mediating the assembly of polyubiquitin chains
CC on substrates ubiquitinated by another E3 ubiquitin ligase. May
CC regulate myosin assembly in striated muscles together with STUB1 and
CC VCP/p97 by targeting myosin chaperone UNC45B for proteasomal
CC degradation. {ECO:0000256|ARBA:ARBA00056267}.
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}.
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:NXW14511.1}.
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DR EMBL; VZZV01000072; NXW14511.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000562238; 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: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 CDD; cd16658; RING-Ubox_UBE4B; 1.
DR FunFam; 3.30.40.10:FF:000060; ubiquitin conjugation factor E4 B; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000562238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1270..1344
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 11..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..96
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXW14511.1"
FT NON_TER 1346
FT /evidence="ECO:0000313|EMBL:NXW14511.1"
SQ SEQUENCE 1346 AA; 151226 MW; 3C5BE1F9CB24FC97 CRC64;
ISFVQIRRRR LARLAGGPSS QPTTPLTSPQ RETPPGPPVV APAPGPSHSL GLNVHSMTPA
TSPIGASGVA HRSQSSEGVS SLSSSPSNSL ETQSQSLSRS QSMDIDSVSC EKSMSQVDVD
SGIENMEVDE NDRREKRSLT DKEPLSGSEV SEEQALQLVC KIFRVSWKDR DRDVIFLNSL
SAQFKQNPKE VFSDFKDLIG QILMEVLMMS TQSRDENPFA SLTATSQPIA AAARSPDRSL
ILNMGSNPGS SPMFCNVGSF GSSSLSSLYG TSPAPTTNFT SYVPMTGSSL TPPASSVATT
SVPSITVSPH LTATSLSGMQ PSSPRYRPYT VAHSGGFSAS SSPRSLNISI PSSSPSPPAM
AASPPAMPVI TSRQRPTTMG PPLFTASPST LRRRSSLLNR IPSSIYDNPF SLLLLAVSDV
SEDSSDEENE DDDFSCVQFG SSVGGSGSSS VSDSCSDHFT IENCKETEML NYLIECFDRV
GIEERKAPKM CSQPTVSQLL SNIRSQCISH AALVLQGSLT QPRSLQQQSL LVPYMLCRNL
PFGFIQELVR TTYQDEEVFK QIFIPILQGL AVASKECSLD SDNFKYPLMA LCELCEIKFG
KTHPMCSLVV SLPLWLPKSL STGAGRELQR LSYLGAFFSL SVFAEDDSKV VEKYFSGPAI
TLENTRVVSQ SLQHYLELAR QELFKILHSI LLNGETREAA LNYMAAIVNA NMKKAQMQTD
DRLVSTDGFM LNFLWVLQQL STKIKLETVD PMYIFHPRCR IDLPTDETRV KATMEDVTAW
IAELYRDPSP FSEPKFPTEC FFLTLHAHHL SILPSCRRYI RRLRAIRELN RTVEDLKNNE
SQWKDSPLAT RHREMLKRCK TQLKKLVRCK ACADAGLLDE NFLRRCLNFY GMVIQLMLRI
LDPAYPNIKL PLTPEVPKVF AALPEFYVED VAEFLFFIVQ YAPQVLYEPC TQDIVMFLVV
MLCNQNYIRN PYLVAKLVEV MFMTNPAVQP RTQKFFEMIE NHPLSTKLLV PSLMKFYTDV
EHTGATSEFY DKFTIRYHIS TIFKSLWQNI AHHGTFMEEF NSGKQFVRYI NMLINDTTFL
LDESLESLKR IHEVQEEMKN KEQWDLLPRD QQQARQSQLA QDERVSRSYL ALATETVDMF
HILTKQVQKP FLRPELGPRL AAMLNFNLQQ LCGPKCRDLK VENPEKYGFE PKKLLDQLTD
IYLQLDCARF AKAIADDQRS YSKELFEEVI SKMKKAGIKS TIAIEKFKLL AEKVEEIVAK
NARAEIDYSD APDEFRPLMD TLMTDPVRLP SGTIMDRSII LRHLLNSSTD PFNRQTLTEN
MLEPGILPEL KEQIQAWMRD KQNADH
//
