ID A0A8C3SG29_CHESE Unreviewed; 876 AA.
AC A0A8C3SG29;
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 Chelydra serpentina (Snapping turtle) (Testudo serpentina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelydroidea; Chelydridae; Chelydra.
OX NCBI_TaxID=8475 {ECO:0000313|Ensembl:ENSCSRP00000014377.1, ECO:0000313|Proteomes:UP000694403};
RN [1] {ECO:0000313|Ensembl:ENSCSRP00000014377.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCSRP00000014377.1}
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; A0A8C3SG29; -.
DR Ensembl; ENSCSRT00000014990.1; ENSCSRP00000014377.1; ENSCSRG00000011021.1.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000694403; 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:UP000694403};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ SEQUENCE 876 AA; 97571 MW; 4D1DEDD0E4FD2D6D CRC64;
MAASPSPAAG PPDGLCVLCC GELEVVALGR CDHPICYRCS VRMRALCGVR YCAVCREELG
QVVFGRKLAS FSTIPINQLQ HEKKYDICFA DGKVFALYRK LLQHECPLCP DVRPFNTVVD
LEQHMRKQHE LFCCKLCVKH LKIFTHERKW YSRKDLARHR IHGDPDDTSH RGHPLCKFCD
ERYLDNDELL KHLRRDHYFC HFCDSDGAQE YYSDYEYLRE HFREKHFLCE EGQCSTEQFT
HAFRTEIDYK AHKTACHSKN RAEARQNRQI DLQFNYASRH QRRNEGVVGG EDFEEVDRYN
RQGRAGRSGL RGGQQNRRGS WRYKREEEDR DIAAAVRASV AAKRQEEKKQ VEDKEDGSRG
KKEELRDPEV SSTKRVPKPS NEATVPKEAA ANGALSQDDF PAIGSAAGPL QRSAQPASVK
LKEEDFPSLS SSAAPTIASG VSLTYTVAAK KTAFQEEDFP ALVSKMRPNA RTVSNITSAW
SNSSNKSAVK AITSLSSSSN RLAKKPAPSN SNKGSRKSSK LSLSDDEDSG SGLTTQEIRN
TPTMFDVSSL LAASTSQTFT KVSKKKKMGV EKQRASSPQL PEETLPPASA LEKLAEAEQT
PSAPANLHLS DRSADVMNGH LEKSVAICNA SKEPPGLKKP PVTSQCPLSQ EDFPALGSSG
PSRIPPPGFI SVALLKSPPP PPGLSVPASK PPPGFTVIPS TNVSDPVTTS LNEPKPCRGS
YLIPEHFQQR NIQLIQSIKE FLQSDESRFN QFKTHSGQFR QGLISAAEYY QSCRELLGEN
FTKIFNELLL LLPDAAKQQE LLSAHNDFRI KEKQGANKPQ KNKKNVWQMD SASDLDCCIC
PTCQQVLTPQ DIASHKALHI EDEEFPSLQA ISRIIS
//