ID I3J7Y3_ORENI Unreviewed; 914 AA.
AC I3J7Y3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 63.
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:ENSONIP00000004973.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000004973.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000004973.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; I3J7Y3; -.
DR Ensembl; ENSONIT00000004976.2; ENSONIP00000004973.2; ENSONIG00000003945.2.
DR GeneTree; ENSGT00940000157685; -.
DR HOGENOM; CLU_004948_0_0_1; -.
DR Proteomes; UP000005207; Linkage group LG7.
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 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:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 101192 MW; 01A725D2DF5AE5F3 CRC64;
MPVQAAQWTE FLSCPICYNE FDSSGHQPIS LGCSHTVCKT CLHKLHRKAC PFDQTPISTD
IDLLPVNCAL LQLVGAQVPD VQPVSLSSAA EVKHYEVCRM CVEELALYLK PISGAKGVAN
LSPSVLSRPM QRKLVTLVNC QLVEEEGRVR AVRAGRSLGE RTVTELILQH QNPQQLSANL
WAAVRARGCQ FLGPAMQEDA LKLVLLALED GSALSRKVLV LFVVQKLEAR FPQASKTSIG
HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RTYEALRREH DAQIVHIAME AGLRISPEQW
SSLLYGDLVH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLTSL RPHLELLANI
DHNPDASAPS WEELESVMLA VKLVVHGLVE FIQNFSKKSH ETPQPQANSK YKTSMCRDLR
QQGGCPRGTS CTFAHTQDEL EKFRLRNKKS SSVGRGFPLA QGGMNKTFTM EGSIHSDVSG
GVGQGLKGNG DSTATMAEGV PSLNHPQLIS RGLDVMEESK RAVPNGTSGP NPLSPPRTPV
SHSSVMSPLT TVGRSDGGAP IPKHGQFILR PSHPSQASEV YYQEPHSTYD TAHYQPASGS
YYPSSLHPPH KPCMARFLRS SNVPESSLPP SIDRMGPPTF HAHPGHPLGP AHGVYAPLYD
SRRVWRPQLY HREDARSNSL PPEVLHSSVY QPPLRERFNS LDSNYCSGAE HRAGLHRDYG
RVALGYEDLF RRKQEQWAHH HHHHSANRPS QSSPIFTIDF GTEVSKQIRK IIFGCVQMCV
ISLKCARVFP TQELDSNESG GGGVGDSGVG KRWLHSLDNY RRLKDEDPII PFSEGPIISK
WGAISRASRT GYHTTDPVQA TACQGSASTT PINFKDYNAH LDHSDYRWSS RGSDSSSHSS
FLERYSIYIQ TLSF
//
