ID A0A493U0G8_ANAPP Unreviewed; 1139 AA.
AC A0A493U0G8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RC3H2 {ECO:0000313|Ensembl:ENSAPLP00000031616.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000031616.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000031616.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000031616.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
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DR AlphaFoldDB; A0A493U0G8; -.
DR Ensembl; ENSAPLT00000022596.1; ENSAPLP00000031616.1; ENSAPLG00000013920.2.
DR GeneTree; ENSGT00940000157685; -.
DR Proteomes; UP000016666; Chromosome 18.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16782; mRING-HC-C3HC3D_Roquin2; 1.
DR Gene3D; 1.20.120.1790; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041523; ROQ_II.
DR InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13139:SF2; ROQUIN-2; 1.
DR Pfam; PF18386; ROQ_II; 1.
DR Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 14..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 410..438
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 410..438
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 520..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 125953 MW; C31DF9706A900830 CRC64;
MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
IDVLPVNFAL LQLVGAQVPD HQTVKLSNVG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS
LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL
WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG
HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI
DPNPDAASPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR
QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI SATVRTFPLL NKVGVNSTVS TTTGNVISVI
GSPEATGKMV PSSNGIANLE SGVPQLIPRC ADTSLRALEN SKKGGKTGAN GQNVSGSPTE
SLPENKIGSP PKTPVSQAAA TSAGPPNIGT EVNSVPPKSS QFVPRVPVYP PHSDNVQYFQ
DPRTQLSYEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA SVPYADHYST
FPPRDRLNSP YQPPPPQPYG PVPPVPSGMY APVYDSRRIW RPQMYPRDDM IRSNSLPPMD
VMHSSVYQTS LRERYNSLDG YYSVACQPPN EQRTVPLPRE PCGHLKTGYD EQLRRKPEQW
AQYHTQKTPL VSSALHMATP SPTPPSPLFS VDFSTEDLDS GDVKRRVHLF ETQRRAKEED
PIIPFSDGPI ISKWGAISRS SRTGYHTTDP IQATASQGSA TKPISVSDYV PYVNAVDSRW
SSYGSDSTSS ARYAERDRFI VTDLSGHRKH SSTGDLLSIE LQQAKSNSLL LQREANALAM
QQKWNSLDEG SRLTLNLLSK EIDLRNGETD YTEDCADAKP DRDIELELSA LDTDEPDGQG
EQIEEILDIQ LGISSQDDQL LNGTTVENGH PLKQHQKESM EQKRQSLGED LVILEEQKTI
LPVTSCFSQP ITTSVSNASC LPISTSVSVG SLILKTAHIM SEDKNDFLKP VANGRMVNS
//
