ID A0A7L0L7V3_9SYLV Unreviewed; 1076 AA.
AC A0A7L0L7V3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=Ube4a {ECO:0000313|EMBL:NXK63922.1};
GN ORFNames=SYLVIR_R13539 {ECO:0000313|EMBL:NXK63922.1};
OS Sylvietta virens (Green crombec).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Sylvietta.
OX NCBI_TaxID=208069 {ECO:0000313|EMBL:NXK63922.1, ECO:0000313|Proteomes:UP000567822};
RN [1] {ECO:0000313|EMBL:NXK63922.1, ECO:0000313|Proteomes:UP000567822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-009-59 {ECO:0000313|EMBL:NXK63922.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXK63922.1};
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. Mediates
CC 'Lys-48'-linked polyubiquitination of substrates.
CC {ECO:0000256|ARBA:ARBA00037624}.
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 -!- 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:NXK63922.1}.
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DR EMBL; VXAN01000149; NXK63922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0L7V3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000567822; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
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; cd16657; RING-Ubox_UBE4A; 1.
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; IPR016024; ARM-type_fold.
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:SF16; UBIQUITIN CONJUGATION FACTOR E4 A; 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; SSF48371; ARM repeat; 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 Reference proteome {ECO:0000313|Proteomes:UP000567822};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 992..1066
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXK63922.1"
FT NON_TER 1076
FT /evidence="ECO:0000313|EMBL:NXK63922.1"
SQ SEQUENCE 1076 AA; 123740 MW; AD96575EC95EE34A CRC64;
MTDQENNNSI SSNPFAALFG SVAAAKHFAA VQKQQQLRQL AGEETSISQD DSDNSVSESL
DDCDYSVAEI SRSFRSQREL CEQLNINHMI QRIFLITLDN SDPSMKSGNG IPARCVYLEE
MAADLDDQDW LDMDNVEQAL FTRLLLPEPG SHLIHMTSAS TQNLSADRDA GERQILRYLY
ACFRRAREEI TKVPENLLPF AVRCRNLTVS NTRTVFLTPE IYVNQNVYEQ LVDLMLETLR
GAQFEDMTEF LEEVIEALTM DEEVRTFGEV MVPVFDILLG RIKDLDLCQI LLYTYLDVLL
YFTKQKDIAK VFVGYIQPKD HSNGQMYQKT LLGAVLNISC LLKTPGVVEN HGYFLNPSRS
SPQEIKVQES NIHQFMAQFH EKIYQMLKNL LQLSPETKHR ILSWLGNCLH ANAGRTKIWA
NQMPEIFFQM YTSDAFFLNL GAALLKLCQP FCKPRSPKLL TFNPTYCALK ELNEEERRSR
NVHMKGLEKE TCLIPPLSDQ EPQFANSYNL VTENLVLTQY TLHLGFHRLH DQMVKINQSL
HRLQVAWREA QQSSSPAADS LREQFERLMT IYLSTKTAMT EPQMLQNCLN LQVSMAVLLV
QLAVGNRGTE LLELTFPLPE VEHSALAYVP EFFADNLGDF FIFLRRFADD ILETSADSLE
HILHFVTVFM GDVERMKNPH LRAKLAEVLE AVMPHLDQAQ NPLVSSVFHR KRVFCSYQHA
AHLAEALIKV FVDIEFTGDP HQFEQKFNYR RPMYPILRYM WDTDSYQDSI KALADYASEN
LEAMNPPLFL RFLNLLMNDA IFLLDEAIQY LSKIKIQQIE KDRGEWDSLS PEARREKESS
LQMFGQLARF HNIMSNETIG TLAFLTSEIK SLFVHPFLAE RIISMLNYFL QHLVGPKMGA
LKVKDFSEFD FKPQQLVSDI CTIYLNLGDE ENFCATVPKD GRSYSPTLFA QTVRVLKKIN
KPGNMIVSFS NLAERIKSLA DRQQQEEETY ADACDEFLDP IMSTLMSDPV ILPSSRVTVD
RSTIARHLLS DQTDPFNRSP LTMDQIRPNT ELKEKIQRWL AERKKQKEEE LEDTLN
//
