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Database: UniProt
Entry: A0A851QTB2_TYCCO
LinkDB: A0A851QTB2_TYCCO
Original site: A0A851QTB2_TYCCO 
ID   A0A851QTB2_TYCCO        Unreviewed;       900 AA.
AC   A0A851QTB2;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 16.
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:NXC83465.1};
GN   ORFNames=CERCOR_R13219 {ECO:0000313|EMBL:NXC83465.1};
OS   Tychaedon coryphoeus (Karoo scrub-robin) (Erythropygia coryphaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Muscicapidae; Cercotrichas.
OX   NCBI_TaxID=614051 {ECO:0000313|EMBL:NXC83465.1, ECO:0000313|Proteomes:UP000631545};
RN   [1] {ECO:0000313|EMBL:NXC83465.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OUT-0024 {ECO:0000313|EMBL:NXC83465.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXC83465.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-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:NXC83465.1}.
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DR   EMBL; WBND01000201; NXC83465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A851QTB2; -.
DR   Proteomes; UP000631545; 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:NXC83465.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000631545};
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          309..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..353
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXC83465.1"
FT   NON_TER         900
FT                   /evidence="ECO:0000313|EMBL:NXC83465.1"
SQ   SEQUENCE   900 AA;  100562 MW;  279F4DE5428E974C CRC64;
     AEAAMAAMAG AGPGPAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
     EELRQVVFGR KLPSFSSIAL HQLQHEKKYD IYFMDAEVYG LYRKLLQHEC SLCPDAKPFN
     TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
     KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQEYYRQAH HWDGDYEYLR EHFREKHFLC
     EEGRCSSEQF THAFRTEIDY KAHKSACHSK SRAEARQNRH IDLQFTYTPR HPRRGDGVVG
     AEDYEEVDRF NRQGRAGRLS SRGNQQNRRG SWRYKREEED RDVAAAVRAS VAAKRQEEKK
     RVEDKEEGSR GRKEDLRDPD VLGSKRLPKS SNDVTGECWA RPAAAGHLWK VPSEAAANGA
     LSQDDFPAIG SAAGPLQGPA QPTLVKLKEE DFPSLSSSAA PTISSGMSLT YTATARKAAF
     QEEDFPALVS KVKPTNKTVT HITSAWNNGS SKNVVKAMSN PCVNQPAKKP SLNTSKGSKK
     SNKLCESDDE DGGGGLTTQE IRSTPTMFDV SSLLAASTSQ TFTKVGKKKK MGVEKQSPSS
     PRPSQEAPLP RPATEKPPEA EQPCKVFPAA HGPDRATAVV NGHSEKPAAG CAAPKEPPGL
     KKPPVTNKCP LPQEDFPALG SSGSARMPPP PGFNSVVLLK NPPPPPGLSV PVSKPPPGFA
     VIPSSTISEP VTTALKEPKS CHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE SKFNKFKTHS
     GQFRQGLISA AQYYKSCREL LGENFKKIFK ELLVLLPDTA KQQELLSAHN DFRIREKQSS
     NKPKKNKKNV WQTDSPAELD CYICPMCRQV LTQQDVVTHK ALHIEDEEFP SLQAISRIIS
//
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