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Database: UniProt
Entry: A0AA97MKW1_9PASS
LinkDB: A0AA97MKW1_9PASS
Original site: A0AA97MKW1_9PASS 
ID   A0AA97MKW1_9PASS        Unreviewed;       890 AA.
AC   A0AA97MKW1;
DT   27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT   27-MAR-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};
DE   Flags: Fragment;
GN   Name=Znf598 {ECO:0000313|EMBL:NXE94044.1};
GN   ORFNames=MENNOV_R12781 {ECO:0000313|EMBL:NXE94044.1};
OS   Menura novaehollandiae (superb lyrebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Menuridae; Menura.
OX   NCBI_TaxID=47692 {ECO:0000313|EMBL:NXE94044.1};
RN   [1] {ECO:0000313|EMBL:NXE94044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10K-CU-030-46 {ECO:0000313|EMBL:NXE94044.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXE94044.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
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}.
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:NXE94044.1}.
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DR   EMBL; VWPS01000228; NXE94044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AA97MKW1; -.
DR   Proteomes; UP000521578; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   Ligase {ECO:0000313|EMBL:NXE94044.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000521578};
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          20..60
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          303..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..660
FT                   /note="Disordered"
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        587..600
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXE94044.1"
FT   NON_TER         890
FT                   /evidence="ECO:0000313|EMBL:NXE94044.1"
SQ   SEQUENCE   890 AA;  99482 MW;  086C7FE6056C363E CRC64;
     AEAAMAAMAG AGPGPAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
     EELRQVVFGR KLPSFSSIDL HQLQHEKKYD IYFMDGEVYA LYRKLLQHEC SLCPDAKPFN
     TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
     KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQEYYSDYE YLREHFREKH FLCEEGRCSS
     EQFTHAFRTE IDYKAHKSSC HSKSRAEARQ NRHIDLQFTY TPRHPRRSDG VVGAEDFEEV
     DRYNRQGRAG RLSSRGNQQN RRGSWRYKRE EEDRDVAAAV RASVAAKRQE EKKRVEDKED
     GSSSRGKKED LRDPDVLSSK RVPKSSNDFG LKTFLCSFFT VPKEAAANGA LSQDDFPAIG
     SAAGPLQGSA QPALVKLKEE DFPSLSSSAA PTISSGMSLT YTATAKRTAF QEEDFPALVS
     KMKPTNKTVP HITSAWNNGS SKNVVKAIST PCVNQPAKKP SLNTSKGSKK SNKLCESDDE
     DGGGGLTSQE IRNTPTMFDV SSLLAASTSQ TFTKVSKKKK MGVEKQSPSS SRPSQDTSFP
     RPSTEKPLEA EQPSKVFPAP HGPDRATAVV NGHSDKPSAA CGTPKEPPGL KKPPVTNKCP
     LPQEDFPALG SSGSARMPPP PGFNSVVLLK NPPPPPGLTV PVSKPPPGFA VIPATNSSDP
     VTTALKEPKS CHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE SKFNKFKTHS GQFRQGLISA
     AQYYKSCREL LGENFKKIFK ELLVLLPDTA KQQELLSAHN DFRIKEKQSS NKSKKNKKNV
     WQTDPPADLD CSICPTCRQV LTQQDVLTHK ALHIEDEEFP SLQAISRIIS
//
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