ID A0A091DWC4_FUKDA Unreviewed; 856 AA.
AC A0A091DWC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE SubName: Full=Zinc finger protein 598 {ECO:0000313|EMBL:KFO34718.1};
GN ORFNames=H920_03746 {ECO:0000313|EMBL:KFO34718.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34718.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO34718.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO34718.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN121905; KFO34718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DWC4; -.
DR STRING; 885580.ENSFDAP00000020089; -.
DR eggNOG; KOG2231; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; IPR056437; Znf-C2H2_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; 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; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 130..151
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 267..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..311
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..493
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 93952 MW; 8CE9FF6D395C4E19 CRC64;
MAAMGASLAQ VSSEEVVFGR KLPAFATIPI HQLQHEKKYD IYFADGKVFA LYRQLLQHEC
PQCPQLPPFG LFGDLEQHMR KQHELFCCKL CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD
DTSHRGHPLC KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQDYYSDYA YLREHFREKH
FLCEEGRCNT EQFTHAFRTE IDLKAHRMAC HSRSRAEARQ NRQIDLQFSF TPRHSRRSEG
PRTVTGCVLT TGVISGEDYE EVDRYNRQGR AGRASGRGAQ QSRRGSWRYK REEEDREVAA
AIQASVAAPQ QDETRRSEDH EEGSKPKKEE TAARGSEEPR GPRRLPRTQG EGPGPKEASG
NDPVGQETSS APGSSTAAVP PSALLPPTPK LKDEDFPSLH ASASSCCPVT APGPVGLTLA
YPGPARGRNA FQEEDFPALV SSASKPSTTT RSLISAWNSS CGKKGALPTP GAQAASGGSQ
PPKKPGKGIR GCRKGGSAPM EEEEGGGLIV QELRTTPTTV AVSTLLGSAP THTSTKVSKK
KKVGSEKPGA MPSPPVPPEH TPNPPVAEQA LDIPVSRAEG PVPVVVNGHT EGPALTRSAP
KEPPGLPRPL GPLPCPAPQE DFPALGGPCL PRMPPPPGFN AVVLLKGTPP PPPPGLVPPI
SKPPPGFSNL LPGPHPACIP SPNTTTVKTP RLTPSSRSYL VPENFRERNL QLIQSIKDFL
QSNEARFSKF KSHSGEFRQG MISAAQYYRS CRDLLGENFQ RIFRELLVLL PDTAKQQELL
SAHTDFCSRE KPPVAKSKKN KKNAWQASTQ QMGLDCCVCP TCQQVLAHGD VSSHQALHAA
RDDDFPSLQA IARIIT
//