ID A0AA35PLD3_9SAUR Unreviewed; 882 AA.
AC A0AA35PLD3;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PODLI_1B036003 {ECO:0000313|EMBL:CAI5792399.1};
OS Podarcis lilfordi (Lilford's wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=74358 {ECO:0000313|EMBL:CAI5792399.1, ECO:0000313|Proteomes:UP001178461};
RN [1] {ECO:0000313|EMBL:CAI5792399.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (DEC-2022) 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}.
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DR EMBL; OX395139; CAI5792399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA35PLD3; -.
DR Proteomes; UP001178461; Chromosome 14.
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:UP001178461};
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 18..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 301..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..344
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97663 MW; 970275EC6054CF12 CRC64;
MAASPRPEPR GSETPSSCVL CCGELEVVAL GRCEHPICYR CSVRMRALCG VRYCAVCREE
LAQVVFGKKL ASFSTIALNQ LQHEKKYDIY FTDGKVYALY RKLLQHECPL CPEAKPFATI
VDLEQHMRKQ HELFCCRLCV KHLKIFTYER KWYSRKDLAR HRIHGDPDDT SHRGHPLCKF
CDERYLDNDE LLKHLRRDHY FCHFCDSDGA QEYYSDYEYL REHFREKHFL CEEGRCSTEQ
FTHAFRTEID YKAHKTACHS KNRAEARQNR QIDLQFNYAL RHQRRNEGVV GGEDYEEVDR
YNRQVRGGRS GPRGGQQNRR GSWRYKREEE DRDIAAAVRA SVAAKRQEEK KRGEDKEDGS
RAKKEDAKDL DLSTSKRGPK PPADVPAPKE TAVKAVLSQD DFPAINSTAV GSVQSSAQPA
SVKLDEEDFP SLSASSSTAP TVSSAMSLTY TATARRSAFQ EEDFPALVSK VQPNIKAAST
LTSAWNCGSG KSMVKAVPTS NSSASQPARK AAPSSSGKGG RKNKAALCSD DQESGSGLTS
QEIRSAPTMV DVSSLLAASN SQTFVKVGKK KKVGAEKPRA ASPSILQEAP APIPSAEKAP
EAEQVPTLPA DADVPAVVNG HSEKCVGTCN ASKEPPGLKK PPVASQTLLP QEDFPALGNS
GPPRMPPPPG FNSVVLLNSP PPPPGLSVSL SKPPPGFTPI PPTSISESAP APVKEPKPCQ
GPYLILDNFQ QRNIHLIQSI KEFLQEDESQ FNKFKTYSGQ FRQGLISAAQ YYKSCQELLG
ENFKKIFNEL LVLLPDTAKQ QELLAAHNDL KARLGSSASP IGRSRKNRKS AWQTDLGSDL
DCCVCPTCQQ VLTQQDLLSH KALHMEEEEE FPSLQAISRI IS
//
