ID A0A0Q3PRQ9_AMAAE Unreviewed; 1065 AA.
AC A0A0Q3PRQ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AAES_112114 {ECO:0000313|EMBL:KQK78716.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK78716.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK78716.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK78716.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KQK78716.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMAW01002639; KQK78716.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3PRQ9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000051836; 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; cd16657; RING-Ubox_UBE4A; 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: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; 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:UP000051836}.
FT DOMAIN 982..1056
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 122058 MW; F96BD3AB20EA6954 CRC64;
MTDQENNNSI SSNPFAALFG SVAAAKHFAA VQKQQQLRQL TGDETSVSQD DSDNSVSESL
DDCDYSVAEI SRSFRSQREL CEQLNINHMI QRIFLITLDN SDPSMKSGNG IPARCVYLEE
MAADLDAQDW LDMDNVEQAL FARLLLQEPG SHLIHMTSSS TQNLSADRDA GERQILRYLY
ACFQRAREEM CIRDRPCAVR CRNLTVSNTR TVLLTPEIYV NQNVYEQLVD LMLEALRGAQ
FEDMTEFLEE VIEALTMDEE VRTFGEVMVP VFDILLGRIK DLDLCQILLY TYLDVLLYFT
KQKDIAKVFA GYIQPKDPSN GQMYQKTLLG TILNISCLLK TPGVVENHGY FLNPSRSSPQ
EIKVQESNIH QFMAQFHEKI YQMLKNLLQL SPETKHRILS WLGNCLHANA GRTKIWANQM
PEIFFQMYAS DAFFLNLGAA LLKLCQPFCK PKSARLLTFN PTYCALKELX EEERRSLEKE
TCLIPALSEQ EPEFANSYNL VTENLVLTQY TLHLGFHRLH DQMVKINQSL HRLQVAWREA
QQSSSPAADS LREQFERLMT IYLSTKTAVT EPQMLQNCLN LQVSMAVLLV QLAVGNCGTE
PLELTFPLPA VQDSALAYVP EFFADNLGDF FIFLRRFADD ILETSADSLE HILHFVTVFM
GDVERMKNPH LRAKLAEVLE AVMPHLDQAQ NPLVSSVFHR KRVFCSYQNA AHLAEALIRV
FVDIEFTGDP HQFEQKFNYR RPMYPILRYM WGTDSYRQSI KALADYASEN LEAMNPPLFL
RFLNLLMNDA IFLLDEAIQY LSKIKVQQIE KDRGEWDSLS PEARREKESS LQMFGQLARF
HNIMSXETIG TLAFLTSEIK SLFVHPFLAE RIISMLNYFL XHLVGPKMGA LKVKDFSEFD
FKPQQLVSDI CTIYLNLGDE ENFCATVPKD GRSYSPTLFA QTVRVLKKIN KPGNMIVSFS
NLAERIKSLA DRQQQEEETY ADACDEFLDP IMSTLMSDPV ILPSSRVTVD RSTIARHLLS
DQTDPFNRSP LTMDQIRPNT ELKEKIQRWL AERKKQKEEL DDTLN
//
