ID A0A852AFH2_CALOR Unreviewed; 897 AA.
AC A0A852AFH2;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
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:NXE70369.1};
GN ORFNames=CALORN_R09947 {ECO:0000313|EMBL:NXE70369.1};
OS Calcarius ornatus (Chestnut-collared longspur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Fringillidae; Emberizinae; Emberizini;
OC Calcarius.
OX NCBI_TaxID=198940 {ECO:0000313|EMBL:NXE70369.1, ECO:0000313|Proteomes:UP000603627};
RN [1] {ECO:0000313|EMBL:NXE70369.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-015-28 {ECO:0000313|EMBL:NXE70369.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXE70369.1};
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:NXE70369.1}.
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DR EMBL; WBNL01001544; NXE70369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A852AFH2; -.
DR Proteomes; UP000603627; 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:NXE70369.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000603627};
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 268..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..326
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..350
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXE70369.1"
FT NON_TER 897
FT /evidence="ECO:0000313|EMBL:NXE70369.1"
SQ SEQUENCE 897 AA; 100272 MW; F6A21D93C2F5D132 CRC64;
AEAAMAAMAG AGPGPAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
EELRQVVFGR KLPSFSSIAL QQLQHEKKYD IYFMDAEVYA LYRKLLQHEC SLCPDAKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQDSVLSLP SDYEYLREHF REKHFLCEEG
RCSTEQFTHA FRTEIDYKAH KSACHSKSRA EARQNRHIDL QFTYAPRHPR RNDGVVGGDD
YEEVDRFNRQ GRASRLSSRG SQQNRRGSWR YKREEEDRDV AAAVRASVAA KRQEEKKRVE
DKEEGSSSRG RKEDSRDPDV LGSKRVPKSS NDPLLWNEWV WVENNVFALS VPVPKEAAAN
GVLSQEDFPA IGSAAGPLQG SAQPALVKLK EEDFPSLSSS AAPSISSGMS LMYTATARKA
AFQEEDFPAL VSKVKPTNRT VTHITSAWNN GSSKNVVKAM CSPCVNQPAK KPSLNTSKGN
KKSNKLCESD DEDGSGGLTT QEIRNTPTMF DVSSLLAAST SQTFTKVGKK KKMGVEKQSP
SSPRPPQEPP LPRPGTEKPP EAEQPCRAFP AAHGPLVNGH TEKPSAGCAA PKEPPGLKKP
PVTNKCPLPQ EDFPALGSSG SARMPPPPGF NSVVLLKNPP PPPGLSVPVS KPPPGFAVIP
SSTISEPVTT ALKEPKSCHG SYLIPENFQQ RNIQLIQSIK EFLQSDESKF NKFKTHSGQF
RQGLISAAQY YKSCRELLGE NFKKIFKELL VLLPDTAKQQ ELLSAHNDFR IKEKQSSNKP
KKNKKNVWQT DSPADLDCYI CPTCRQVLTQ QDVVTHKALH LEDEEFPSLQ AISRIIS
//
