ID A0A9Q0X8M2_9SAUR Unreviewed; 936 AA.
AC A0A9Q0X8M2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=JRQ81_010486 {ECO:0000313|EMBL:KAJ7306120.1};
OS Phrynocephalus forsythii.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Acrodonta; Agamidae; Agaminae; Phrynocephalus.
OX NCBI_TaxID=171643 {ECO:0000313|EMBL:KAJ7306120.1, ECO:0000313|Proteomes:UP001142489};
RN [1] {ECO:0000313|EMBL:KAJ7306120.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Muscle {ECO:0000313|EMBL:KAJ7306120.1};
RX PubMed=36882113;
RA Qi Y., Zhao W., Zhao Y., Niu C., Cao S., Zhang Y.;
RT "Chromosome-level genome assembly of Phrynocephalus forsythii using third-
RT generation DNA sequencing and Hi-C analysis.";
RL DNA Res. 0:0-0(2023).
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:KAJ7306120.1}.
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DR EMBL; JAPFRF010000021; KAJ7306120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q0X8M2; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP001142489; Unassembled WGS sequence.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001142489};
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 29..69
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..327
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..357
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..437
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..470
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..687
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 101347 MW; B13496B4813C6C11 CRC64;
MAAAAAASSS SEPRSPAGPS SPSPPSSSCV LCCGELEVVA LGRCEHPICY RCSVRMRALC
GVRYCAVCRE ELAQVVFGRK LTSFSTIALS QLQHEKKYDI YFTDGKVYAL YRKLLQHECP
LCPEARPFAT VADLEQHMRK QHELFCCKLC VKHLKIFTYE RKWYTRKDLA RHRIHGDPDD
TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDSDG AQEYYSDYEY LREHFREKHF
LCEEGRCSTE QFTHAFRTEI DYKAHKTACH SKNRAEARQN RQIDLQFNYA PRHQRRNEGV
VSGEDYEEVN RYHRQSRGGG GRAGLRGGQQ NRRGSWRYKR EEEDRDIAAA VRASMAAKRQ
EEKKHREEKE EGARAKREEA KDPDSNASKR GPKPPAEAPA PKEAASKPVL SPEDFPAIGS
AAAAAAALAQ GTSPAASVRL DEEDFPSLSS SSSSSFSSSA APASSAPAVS SAMALMYAAP
ARKGPFQEED FPALVSRVQP KTTSTLTSAW SCGSGKNMVK AMAASAATTT GSSSSSNTSQ
PAWKTAPAGS QKGGKKTRAA PPNDTNNSAT GTGLSIQGVR SAPAVVGVSS LLTAPNPQAF
VKVGKKKKVG AEKSRGASSP LPREAAAPAP PAEKAPEADP PPKGLAHAGV AEGAAGVVNG
HPEKATLPCT ASKEPPGLKK APSASPALLP PEDFPALGNS GLPRKPPPPG FNSVVLLNSA
PPPPGLSVPV GKPPPGFVPI PPTAVPETAP PAPAAASVKE SKPCQGPYLI LENFQQRNIQ
LIHSIKEFLQ EDESQFNKFK TYSGQFRQGL ISADQYYRSC QDLLGENFGK IFSELLVLLP
DTAKQRELLA THHDLKAKSG DAFSLSSSSS SAAALSRSRK TKGNAWQTGL GSDLDCCVCP
TCQQVLTQQD LAAHKALHRE EEEEFPSLQA ISRIIS
//
