ID A0A8C5TWS1_9PASS Unreviewed; 882 AA.
AC A0A8C5TWS1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Malurus cyaneus samueli.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Meliphagoidea; Maluridae; Malurus.
OX NCBI_TaxID=2593467 {ECO:0000313|Ensembl:ENSMCSP00000013021.1, ECO:0000313|Proteomes:UP000694560};
RN [1] {ECO:0000313|Ensembl:ENSMCSP00000013021.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMCSP00000013021.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A8C5TWS1; -.
DR Ensembl; ENSMCST00000013360.1; ENSMCSP00000013021.1; ENSMCSG00000009233.1.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000694560; Unplaced.
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:UP000694560};
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 24..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 306..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..326
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..350
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 98259 MW; 1C65D72D89FF043B CRC64;
MAAMAGAGPG SGSSSSSGST EGPCVLCCGE LDVVALGRCE HPICYRCSVR MRALCGVRYC
AVCREELRQV VFGRKLPSFS SIALHQLQHE KKYDIYFMDA EVHALYRKLL QHECPLCPDA
KPFNTFADLE QHMRKQHELF CCKLCVKHLK IFTYERKWYS RKDLARHRIH GDPDDTSHRG
HPLCKFCDER YLDNDELLKH LRRDHYFCHF CDSEGAQEYY SDYEYLREHF REKHFLCEEG
RCSTEQFTHA FRTEIDYKAH KSACHSKNRA EARQNRHIDL QFTYTPRHPR RTDGVVGAED
YEEVDRFNRQ GRASRLSSRG SQQNRRGSWR YKREEEDRDV AAAVRASVAA KRQEEKKRVE
DKEDGSSSSR GKKEDLRDSD VLGSKRVPKS SNDVTEAAAN GVLSQEDFPA IGSAAGPLQG
SAQPALVKLK EEDFPSLSSS AAPTISSGMS LAYTATAKKA AFQEEDFPAL VSKVRPTNKT
VTHITSAWNN CSSKNVVKAM SSPCVNQPAK KPSLNTSKGS KKSNKLCESD DEDGGGGLTT
QEIRNTPTMF DVSSLLAAST SQTFTKVGKK KKQGVEKQNQ SSPRPSQETL LPRPATEKPP
EAEQPAKVFP AAHGPDRATA VVNGHSDKSS AACGAPKEPP GLKKPPVTNK SPLPQEDFPA
LGSSGSARMP PPPGFNSVVL LKNPPPPPGL SVPVSKPPPG FGVIPSSTIS DPVTTALKEP
KSCHGSYLIP ENFQQRNIQL IQSIKEFLQS DESKFNKFKT HSGQFRQGLI SAAQYYKSCR
ELLGENFKKI FKELLVLLPD TAKQQELLSA HNDFRIKEKQ SSNKSKKNKK NVWQTDSPTD
LDCSICPTCR QVLTQQDLVT HKALHIEDEE FPSLQAISRI IS
//
