ID A0A5J5MW21_MUNRE Unreviewed; 841 AA.
AC A0A5J5MW21;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
GN ORFNames=FD755_006447 {ECO:0000313|EMBL:KAB0384530.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0384530.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0384530.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0384530.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0384530.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:KAB0384530.1}.
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DR EMBL; VCEB01000002; KAB0384530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5MW21; -.
DR Proteomes; UP000326062; Chromosome 2.
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:UP000326062}.
FT DOMAIN 129..150
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 254..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..440
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..471
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..481
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..527
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 92037 MW; 233285AFEC8A6C00 CRC64;
MSPGCAGLVS ELRQVVFGKT LPAFATIPLH QLQHEKKYDI YFMDGRVFAL YRQLLQHECP
RCPERPPFTL FGDLEQHMRK QHELFCCKLC LRHLQIFTHE RKWYSRKDLA RHRMQGDPDD
TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDADG AQDYYSDYAY LREHFREKHF
LCEEGRCSTE QFTHAFRTEI DLKAHRTACH SRSRAEARQN RQIDLQFSYA PRHSRRSEGV
IGGEDYEELD RYNRQGRMGR ASGRGAQQSR RGSWRYKREE EDREVAAAIR ASVAAQQQQE
THRTEDREEG GRPKKEESGL RGPEEARGPR RPARTPGEGP GPKEASANGP VNQDTFSTTG
PAAGATLPNA LPPPTSKLKD EDFPSLCASA LSSSSAAAAP GPVGLALAYP VPARGRTTFQ
EEDFPALVPS VSKPSSVPTS LISAWNSGAS KKVAHPAPGS QSTSGGSQPP RKSGKGVKGG
KKGGPPPAEE AEEDGRAGLT AQELRSVPTT VVVSSLLAGA ATQTFTKAGK KKKVGSEKSG
AASPPPPDRE GPPGAEVAPT APPGRTEGTP AVIVNGHSEG PAPARSTPKE PPGLPRPLGP
PPCPTPQEDF PALCGPCPPR MPPPPGFNAV VLLKGTPPPP GLAPPVSKPP PGFSGLPSSP
HPACVPSTTT TTKAPRPTPV PRAYLVPENF RERNLQLIQS IRDFLQSDEA RFSKFRSYSG
EFRQGVISAA QYYKSCRDLL GENFEKIFNE LLVLLPDTAK QQELLLAHTD FRGREKPPGT
KAKKNRKSAW QASTRQVGLD CCVCPTCQQV LAHGDVGSHQ ALHAARDDDF PSLQALARIL
T
//
