ID A0A553NDJ2_TIGCA Unreviewed; 986 AA.
AC A0A553NDJ2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 08-OCT-2025, entry version 22.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=TCAL_16641 {ECO:0000313|EMBL:TRY63510.1};
OS Tigriopus californicus (Marine copepod).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX NCBI_TaxID=6832 {ECO:0000313|EMBL:TRY63510.1, ECO:0000313|Proteomes:UP000318571};
RN [1] {ECO:0000313|EMBL:TRY63510.1, ECO:0000313|Proteomes:UP000318571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Diego {ECO:0000313|EMBL:TRY63510.1,
RC ECO:0000313|Proteomes:UP000318571};
RX PubMed=29988158; DOI=.1038/s41559-018-0588-1;
RA Barreto F.S., Watson E.T., Lima T.G., Willett C.S., Edmands S., Li W.,
RA Burton R.S.;
RT "Genomic signatures of mitonuclear coevolution across populations of
RT Tigriopus californicus.";
RL Nat. Ecol. Evol. 2:1250-1257(2018).
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}.
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:TRY63510.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VCGU01000458; TRY63510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553NDJ2; -.
DR STRING; 6832.A0A553NDJ2; -.
DR OMA; KNCTFAH; -.
DR Proteomes; UP000318571; Chromosome 10.
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; cd16638; mRING-HC-C3HC3D_Roquin; 1.
DR FunFam; 1.20.120.1790:FF:000001; roquin-1 isoform X1; 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:SF54; RING-TYPE E3 UBIQUITIN TRANSFERASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000318571};
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 407..435
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 407..435
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 642..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 876..944
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 652..661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 108367 MW; A0C29632FA86A58E CRC64;
MPVQSPQWTE YLSCPVCENG FELRNRLPIS LGCGHTICQT CLAQLRRRAC PFDQGQIRLP
LNQLPVNTSL VLLIDADASL EQYRIKIEDE SVTPHYVAAT VQLEKLAQFL RVLSRPPLSR
PMQRKLVTLI NCQLLEEEGR ARVVRAARSL GERSVTELIL QHQNPQQLSA NLWAAVRARG
CQFLGPAMQE EVLKLVLLAL EDGSALSRKV LVMFVVQRLE PHFPQASKTS IGHVVQLLYR
ASCFKVTKRD GDSSLMQLKE EFRTYDTLRR EHDAQIVQIA TEAGLRIAPD QWSSLLYGDG
AHKSHMQSII DKLQTPQSFL QSVQELIIAL QRTGDPGNLG QLRPHLDFLA ALDPNPESDN
PDWETLNSSL CSVYEVVQGL QAFIEQQTQS RKGSDGLNAN PSAPNARYKT SMCRDLTSHG
SCPRGKNCTF AHSQSEMEQF RTSRKPKFVG KPPPVVGSVP PIVNSARGPV LGAKKDPMGM
GSPLTIPPVA QVAPLQRGFV APTHLSTPVE PTIGHGMAQV MPMDEAYVNE VLHSNPGPIG
SFPSRDGVGM TSNEHGESAY HQTHTVMSVQ PMTGGNLIKG SEHDSNFDRY PLRCESRNSH
LDIPEMTMAT KSLGALKSRK EEIIDYLEDL VGKEETQTIT KKASITIGNG NGPSSSQSPS
SLTVEKPQLR QSKSAPSQSN YSIWTSRSIA TLPSPCENTQ SEGKVATVAP NFIEDIAADV
CTSPSEFDLM EDGEKVPMGE VNIDTWHVGK SCLDEDEEMI PFSDTPQICR FGPISRKTGT
LLQLASPSQT QALMNDEPTP TAVVRHSKQL TRQVPSLASL YHQNGTRTTL QPVAIGANGE
ISYVAVPESS YPTTDVTLQQ IQHNSALLSN VAPASQQSLF AESERMKHEL EMLQKKISDL
NMAHIERQST GSDPNSRYGV SSERDDLTRE LQMIESTIRD RELEISANRL RIETGENTII
PLSSSFGAFA ASHGKLLALA DVPSQA
//
