ID A0A3Q7PGD8_CALUR Unreviewed; 915 AA.
AC A0A3Q7PGD8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC112828217 {ECO:0000313|RefSeq:XP_025732920.1};
OS Callorhinus ursinus (Northern fur seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Otariidae;
OC Callorhinus.
OX NCBI_TaxID=34884 {ECO:0000313|Proteomes:UP000286641, ECO:0000313|RefSeq:XP_025732920.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025732920.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025732920.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_025732920.1; XM_025877135.1.
DR AlphaFoldDB; A0A3Q7PGD8; -.
DR CTD; 90850; -.
DR InParanoid; A0A3Q7PGD8; -.
DR Proteomes; UP000286641; 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; IPR056437; Znf-C2H2_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; PF23230; zf-C2H2_13; 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:UP000286641};
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 34..74
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 299..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..508
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..549
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..597
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 99383 MW; EFBB20B71ECD4335 CRC64;
MAAAAAAVTV AAGAEGRRAA LEAAAVPERG GGSCVLCCGD LEATALGRCD HPVCYRCSTK
MRVLCEQRYC AVCREELRQV VFGKKLPAFA TIPLHQLQHE KKYDIYFADG KVFALYRQLL
QHECPQCPEL PPFGLFGDLE QHMRKQHELF CCKLCLKHLK IFTYERKWYS RKDLARHRMQ
GDPDDTSHRG HPLCKFCDER YLDNDELLKH LRRDHYFCHF CDSDGAQDYY SDYAYLREHF
REKHFLCEEG RCSTEQFTHA FRTEIDLKAH RTACHSRSRA EARQNRQIDL QFSYAPRHSR
RSEGVVGGED YEEVDRYNRQ GRAGRASGRG AQQSRRGSWR YKREEEDREV AAAIRASVAV
PQLQQETRRS EDREEGGRAK KEEAGLRVLE ELRGPRRLPR TQGEGAGLKE ASPNGPVSPE
GLPATGQATG ATPPSTLPPP TSKLKDEDFP SLCASASSSA SCSAAAALGP VGLALAYPIP
ARGRSTFQED DFPALVSSAS KPSAAPTSLI SAWNSSGSKK VVHPTSGAQA AGGSGQPPRK
AGKAGKGSKK GAPPPSEEEE EEEAGRAGLT AQELRSVPTT VAVSSLLALA STQTLPKVGK
KKKVGLEKPA ATSPPPQPPD KDGPPGAEQA PTTTAGRAEG PVALIVNGHT EGPAPARSTP
KEPPGLPRPL GPPACPTPQE DFPALGVPCP PRMPPPPGFN AVVLLKGTPP PPPPGLVPPV
SKPPPGFSGL LPSPHPACVP STATATKAPR LTPAPQVYLV PENFRERNLQ LIQSIKDFLQ
SDEARFGKFK SHSGEFRQGV ISAAQYYKSC RDLLGENFQK IFNELLVLLP DTAKQQELLS
AHTHFRGRER PPGTKAKKNR KSAWQASTRP AGLDCCVCPT CQQVLAHGDV SGHQALHAAQ
DNDFPSLQAI ARILT
//
