ID A0A6I9YEW8_9SAUR Unreviewed; 736 AA.
AC A0A6I9YEW8;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Zinc finger protein 598-like {ECO:0000313|RefSeq:XP_013922712.1};
GN Name=LOC106549546 {ECO:0000313|RefSeq:XP_013922712.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013922712.1};
RN [1] {ECO:0000313|RefSeq:XP_013922712.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_013922712.1; XM_014067237.1.
DR AlphaFoldDB; A0A6I9YEW8; -.
DR GeneID; 106549546; -.
DR KEGG; tsr:106549546; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000504617; Unplaced.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
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; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000504617}.
FT DOMAIN 35..56
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 133..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..201
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..677
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_013922712.1"
SQ SEQUENCE 736 AA; 81617 MW; 78291E49466C0239 CRC64;
KIFTYERKWY SRKDLARHRI HGDPDDTSHR GHPLCKFCDE RYLDNDELLK HLRRDHYFCH
FCDSDGAQEY YSDYEYLREH FREKHFLCEE GRCSTEQFTH AFRTEIDYKA HKTACHSKNR
AEARQNRQID LQFNYAPRHQ RRNEGVVSGE DYDEVDRYNR QMRGSRSGSR GGQQNRRGSW
RYKREEEDRD VAAAVRASVA AKRQEEKNRV EDKGDSCRPK KEDAKDPEPT VSKRGVKPSS
EEPVPKEAVP KAALSQDDFP AIGSPNMNSV PSSSQLAPVK LDEEDFPRLS FSSAPPVVSA
SLPLSYMATA QKTGFQEEDF PALVSKVRPS SKTVSTLASA WSGGSSKNMA RAMTATASQP
ARKGPPPGSS KASKKSKVAI PGNFQDGSGS VSTQEIRSAP TMVDVSSLLA ASNSQTFAKV
GKKKKVGTEK LRTVLQEVPA APHSLEKVDD AEQSSPVTAG PDLLSTSATL VNGHSEKPPL
PCRAPKEPPG LKKPSGGGQC LLPQEDFPAL GNTGPPRMPP PPGFNSVVLL NSPPPPPGLS
VPPSKPPPGF TPIPTTGTSE NAPASVKEPK LCQGPYLILE NFQQRNIQLI QSIREFLQED
ESQFNKFKMY SGQFRQGLIS AEQYYKSCQE LLGENFNKIF NELLVLLPDT AKQQELLSAY
QDLKVKAPAG SSSPSSTRSK KNRKGVWHTE PPSDLDCCVC PTCQQVLTQQ DLVSHQALHL
EEEEFPSLQA ISRIIS
//