ID A0A3B5B049_9TELE Unreviewed; 1136 AA.
AC A0A3B5B049;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RC3H1 {ECO:0000313|Ensembl:ENSSPAP00000019132.1};
GN Synonyms=rc3h1 {ECO:0000313|RefSeq:XP_008290739.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000019132.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000019132.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008290739.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_008290739.1; XM_008292517.1.
DR AlphaFoldDB; A0A3B5B049; -.
DR STRING; 144197.ENSSPAP00000019132; -.
DR Ensembl; ENSSPAT00000019422.1; ENSSPAP00000019132.1; ENSSPAG00000014400.1.
DR GeneID; 103365157; -.
DR CTD; 558213; -.
DR GeneTree; ENSGT00940000157143; -.
DR OrthoDB; 2909513at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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; cd16781; mRING-HC-C3HC3D_Roquin1; 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:SF6; ROQUIN-1; 1.
DR Pfam; PF18386; ROQ_II; 1.
DR Pfam; PF21206; Roquin_1_2-like_ROQ; 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:UP000694891};
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 413..441
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 413..441
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 511..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 124631 MW; 34619F3EC39DCA9A CRC64;
MPVQAPQWTE FLLCPICTQT FEETVRRPIS LGCGHTVCKM CLNKLHRKAC PFDQTAISTD
IEQLPVNTAL LQLVGGQVPK AQPVALITSP EDSQHYEEAR QCVEELALYL KPLSNTRGVG
LSSTAQSMLS RPMQRKLVTL VHCQLVEEEG RVRAMRAARS LGERTVTELI LQHQNPQQLS
SNLWAAVRAR GCQFLGPAMQ EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT
SIGHVVQLLY RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEGGLRIAP
DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL NRLRPHLELL
ANIDPSPDAP PPTWEQLEKG LVAVKTVVHG LVDFIQNHSK KGADPQQPPQ HSKYKTYMCR
DMKQKGGCPR GASCTFAHSQ EELEKYRKMN KRLAARLPGA GGLLSDDGLP LDVAVTRKPS
PLTNGSGAPS LPQLIARGTD TVSYELLRKP VKMDGGSPSA PGSPPDVLDP VPKPGMPLPP
HAMAHPRMPA DHLSGVKHMP VVPRGSPVYP QPPLPEMCYD TRPPPSASQY EPPQYPTGYP
YQQPPQYVTR DYIRNAPPPS ESGPPYQDPY SGYGPPERPY QAPHSGPPFS YPHPSHYDRG
RHGTYTGPPP PPQPYPSQRD GLVRMSPAPL DVPPPSAGQA NSLYHQDPNP RDRYPPDAYY
PPGAQPPPMR TYVRGPSYGG SQPSLDYLHR RRQELLSQLE ERKVISPPPF AASPTLPHPF
PSDYPPEYGE ESSKTMVKCR EPDYAGQYSP WSCETIGSYI GTKDAKPKDV MVPGAMEMMN
VEAKSLREPS LEAPRRGAEV KDDDPIIPFG PQPTVSRFGA ISRTSKTGYQ TTGPVQAMVA
NPQNPNSKHM AMPAEYTYGS HGGWGGASYP SHQTASSSQG HFTERLPMAA PDREQLKIEL
QQVNQQITQQ TQMHSMEAAS NSLLLQREAS ALAGQPVQPS QGQAAVAPQQ QQPKWPAGGA
SATAVSSEQL SLELHQVERE IGKRTREMAM ENQVAHDVQQ YKMKSAENGQ PEHKTQLEEI
ALARGEVSNG SSSLQESAVG GSMLTLTNKT SALGLCSDPG ATGSEMQKNG VVHSCS
//
