ID A0A7K4YZR1_BUCAB Unreviewed; 1191 AA.
AC A0A7K4YZR1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, 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};
DE Flags: Fragment;
GN Name=Rc3h2 {ECO:0000313|EMBL:NWR64613.1};
GN ORFNames=BUCABY_R08120 {ECO:0000313|EMBL:NWR64613.1};
OS Bucorvus abyssinicus (Northern ground-hornbill) (Abyssinian
OS ground-hornbill).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Bucerotiformes; Bucorvidae; Bucorvus.
OX NCBI_TaxID=153643 {ECO:0000313|EMBL:NWR64613.1, ECO:0000313|Proteomes:UP000551127};
RN [1] {ECO:0000313|EMBL:NWR64613.1, ECO:0000313|Proteomes:UP000551127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-012-80 {ECO:0000313|EMBL:NWR64613.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
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:NWR64613.1}.
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DR EMBL; VYZL01004834; NWR64613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K4YZR1; -.
DR OrthoDB; 10067217at2759; -.
DR Proteomes; UP000551127; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:TreeGrafter.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:TreeGrafter.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR GO; GO:0035613; F:RNA stem-loop 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:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:TreeGrafter.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR CDD; cd16782; mRING-HC-C3HC3D_Roquin2; 1.
DR FunFam; 1.20.120.1790:FF:000001; roquin-1 isoform X1; 1.
DR FunFam; 4.10.1000.10:FF:000004; roquin-1 isoform X2; 1.
DR FunFam; 3.30.40.10:FF:000047; Roquin-2 isoform 1; 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; IPR052249; Roquin_domain.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000551127};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
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..579
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 1095..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWR64613.1"
FT NON_TER 1191
FT /evidence="ECO:0000313|EMBL:NWR64613.1"
SQ SEQUENCE 1191 AA; 131460 MW; 8EAD8DE76F33A955 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 NKVGVNTTVS TTTGNVISVI
GSPEAAGKMV PSTNGIANLE SGVPQLIPRC ADTSLRALEN TKKGGKTGAN GQNVSASPTE
SLPENKIGSP PKTPVSQAAA TSAGPPNIGT EVNSVPPKSS PFVPRVPVYP PHSDNVQYFQ
DPRTQLSYEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA SVPYADHYST
FPPRDRLNSP YQPPPPQPYG PVPPVPSGMY APVYDSRRIW RPQMYPRDDI IRSNSLPPMD
VMHSSVYQTS LRERYNSLDG YYSVACQPPN EQRTVPLPRE PCGHLKTGYD EQLRRKPEQW
AQYHTQKTPL VSSTLPIATP SPTPPSPLFS VDFSTEFSES VGDLSGTKFE EDHLSHYSPW
SCGTIGSCIN AIDSEPKDVI ANSNAVLMDL DSGDVKRRVH LFETQRRAKE EDPIIPFSDG
PIISKWGAIS RSSRTGYHTT DPIQATASQG SATKPISVSD YVPYVNAVDS RWSAYGSDSN
SSARYAERDR FIVTDLSGHR KHSSTGDLLS IELQQAKSNS LLLQREANAL AMQQKWNCLD
EGSRLTLNLL SKEIDLRNGE TDYTEDCADT KPDRDIELEL SALDTDEPDG QGEQIEEILD
IQLGISSQDD QLLNGTTVEN GHPLKQHQKE SMEQKRQSLG EDLVILEEQK TILPVTSCFS
QPITTSVSSA SCLPISTSVS VGSLILKTAH IMSEDKNDFL KPVANGRMVN S
//
