ID A0A0Q3XB46_AMAAE Unreviewed; 887 AA.
AC A0A0Q3XB46;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AAES_12360 {ECO:0000313|EMBL:KQL61383.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL61383.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL61383.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL61383.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:KQL61383.1}.
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DR EMBL; LMAW01000001; KQL61383.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3XB46; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 272..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..338
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 99250 MW; 0464C297189432E7 CRC64;
MAASAGPADG PCVLCCGELD VVALGRCDHP ICYRCSVRMR ALCGVRYCAV CREELAQVVF
GRKLTSFSTI ALSQLQHEKK YDIYFTDGDV YALYRKLLQH KCSLCPDVKP FNTFADLEQH
MRKQHELFCC KLCVKHXKIF TYERKWYSRK DLARHRIHGD PDDTSHRGHP LCKFCDERYL
DNDELLKHLR RDHYFCHFCD SDGAQEYYSD YEYLREHFRE KHFLCEEGRC STEQFTHAFR
TEIDYKAHKT ACHSKNRAEA RQNRQIDLQF NYAPRHQRRN EGVVSGEDYE EVDRYNRQGR
SARLGGRGSQ QNRRGSWRYK REEEDRDVAA AVRASVAAKR QEEKKRVEDK EDGSSRGRKE
DMRDSEVLSS KRVPKSSNDA TVNGFELKMS LFVPVPKEAA ANGALSRDDF PAIGSAAGPL
QGSCQPAVVK LKEEDFPSLS SSAAPTISSG MSLTYTTTAK KTAFQEEDFP ALVSKMRPNS
KTVTNITSAW NNGTSKSVVK AISNPCVNQP AKKPSSSLNS TKGSKKSNKL SQSDDEDSGS
GLTTQEIRNT PTMFDVSSLL AASTSQTFTK VSKKKKVGAE KQRPSSPRLS QETAFPRAST
EKLPEAEQTS NASSSALHSP DRPTAVMNGH SEKLLVVCST PKEPPGLKKP TVTNKCPLPQ
EDFPALGSSG SARMPPPPGF NTVVLLKNPP PPPGLSVPVS KPPPGFAVIP STTISEPVTT
SLKEPKPCPG SYLIPENFQQ RNMQLIQSIK EFLQSXESKF NKFKTHSGQF RQGLISAAQX
YGSCRELLGE NFRKIFKELL VLLPDTAKQQ ELLSAHNDFR LKEKQSSSKP XKNKRNVWQT
DSSSELDCSI CPTCKQVLTQ QXVGTHKALH MEDEEFPSLQ AISRIIS
//
