ID A0A444UBE3_ACIRT Unreviewed; 905 AA.
AC A0A444UBE3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EOD39_0248 {ECO:0000313|EMBL:RXM32494.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM32494.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM32494.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM32494.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM32494.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) 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:RXM32494.1}.
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DR EMBL; SCEB01214897; RXM32494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444UBE3; -.
DR Proteomes; UP000289886; 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:UP000289886};
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 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 296..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..346
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..390
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 101293 MW; 808AC42888459046 CRC64;
MASKSLKDTE RSCVLCCQEI EIFALGKCDH PVCYRCSTKM RVLCEQKYCA VCREELDKVL
FVKKRDPFST IATQHFQCEK KHDIYFSDAD IHTQFRRILQ HECPQCPELR VFTKFEELEQ
HMRKQHELFC CKLCAKHLQI FTHEREWYNR KELARHRTQG DLDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DSDGAQEYYS DYDYLREHFR EKHYLCEEGR CSAEQFTHAF
RTEIDYKAHK AACHSKTRAE ARQNRHIDLQ FNYASRHPRR SEGVVGGEDY EEVDRFNRHS
RAGRGGGGGG GGGGRGGQQN KRGSWRYNRE EEDREVAAAV RASVAARRQE EKRPAQEREI
PKPKEEATEA EDFRHARAPA KPASEAAGAK DAAKPVKSNG PLKGEEFPAL GVMAAPIPST
NTAAAVKLKE EDFPSLLSKS VSSPMTPAYT AQPRKPSAFQ EEDFPALVSK IRAPKQCGST
TSAWSTSSNK NAGKPSPAAS PFPSFNTPTP SSSASTQPRK KPLPASSNKS NPRNKLSPAS
DEDDDRGGKT TQEIRSVPTM LDISSLLTGR SAPLASASQT VSKVGKRKKM GMEKQSPAFT
ASLTPPVGMT TNVAQKENVP ETKQPPPNIT QPASNAASKT NLLINGHSEQ PAENNSPLVK
KEPPGLKKQL TLEPCPLPEE EFPALLPKKS PPGFNTEFPM KGGHSSLPPP PPPGLAAPPS
KPPPGFTGIA LNANVLEPTI PTVNEPSFTT GTYLVPENFQ LRNMELIQSI KNFLLDEESK
FNQFKTFSGQ FRQGHMSAVQ YHQSCRELLG ENFKRIFNEL LVLLPDTSKQ QELPAAHNHC
QASSKPKKNK KNAWQTGNNN NPELDCRICP SCRQVLTEKD FIAHKSQHRQ DDDFPSLQAI
SKIIS
//
