ID   A0A667Y0B7_9TELE        Unreviewed;      1296 AA.
AC   A0A667Y0B7;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   10-JUN-2026, 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};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005017704.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005017704.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMMDP00005017704.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   Ensembl; ENSMMDT00005018141.1; ENSMMDP00005017704.1; ENSMMDG00005008879.1.
DR   GeneTree; ENSGT00940000154465; -.
DR   InParanoid; A0A667Y0B7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000472263; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16481; RING-H2_TTC3; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   InterPro; IPR056872; TTC3/DZIP3-like_helical.
DR   InterPro; IPR056870; TTC3/DZIP3/RBM44-like_helical.
DR   InterPro; IPR043866; TTC3/DZIP3_dom.
DR   InterPro; IPR056871; WH_TTC3.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR17550; E3 UBIQUITIN-PROTEIN LIGASE TTC3; 1.
DR   PANTHER; PTHR17550:SF8; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF24525; TTC3; 1.
DR   Pfam; PF24905; TTC3_9th; 1.
DR   Pfam; PF19179; TTC3_DZIP3_dom; 1.
DR   Pfam; PF24812; WHD_TTC3; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          136..169
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          385..418
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1231..1271
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          1010..1122
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1296 AA;  148570 MW;  371F1B4A57625EC0 CRC64;
     MHVFRRDQPV VTHCPSETTY EAWINIPIDK KLEAGQLLRI CAFWDPILLE RHESHGTTRW
     ARHVGFISSL DSDDLSLKQL NKIETLEAIL RAMEKGCVSW LLSASVFVQM FPSLLSHICT
     LFQILAVFHV PLLQKCEEMK NKGNEKFQKN KYEEAVEFYS KAINFYPGNH LIYGNRALCY
     IRCKKYLNAV GDGKRATLLK PVWAKGHYRY CEALFCLGEF IRAIEANKQA QILCKDSQEG
     IKDLEQQYQR FISVFPEIKG TCTAMLRRAD QMFLFIYCHQ AGDLSYCICP SPSYQKVAAS
     STGVCQALRS AVQDGHSALV DLRSRSAEQA FRKALAILET STPKTLLVKK IKCGVNVCFF
     LTQELTEAQN VLEKIKLFEE RTFECLVYYG IGKVYLKENR YPYALRQFSD ALQMVKNQIT
     PGKLTWPMTK EIVKETQLDY FKELLFNVID LCKFPPTPQA ICRLENCLGP LKAEIYFTDP
     DFKGFIRIGC CQSCIVEYHI TCWKALKSVS FSDKNEKDFL QEPCFTPDCG GQICCIKIFG
     STGLIKCKVR KIFGGEADQK KLKSKEERKL RRMQHRLSSY SCCFNLVSVM SAWLLYRDRV
     LLQISQNMEV LRVEKNVHVE DLASSLKPWL ELDLSRGNQL AERMLSWQQQ PEQTLDQAVE
     MILERKNRVW ARVFLQCLSN SLDINPKLLD WARHLNDAGL NAAKSFIERH AGHLEELDLA
     LLLKFGPLQD LILEKLGTRP EVFTKIGLTV TDYLKQAPSQ DMRLFIWTLE EHRDQYVSCH
     NILDEYFEMM GKSKNRGRKK KKESKGVIVL SGMRGATPRD EWDQDFFDED DSLSVLHPGD
     PFSVPSHLRE HVADFEEQYN ATNHRSLYKK ILDNNPDPAK ENLYDYFAQI LEEHGPLCAQ
     DPLLVGELDN FPAVAQEKIQ EAGGFESFLL ESLRFIKMGQ RIGLAKHAVC LQQAGHGSSL
     DDLDDITDAD ISSSAPSMYA CHDVFTNYLQ DYSSMENDYE KINLRRKEAI TSLEEDLQRI
     STNIQVTNTE LALFQQKLEE EVKKDQKEKK GNQEALKSLK TEIEQLVEEQ ESLTRNIRQK
     NMKYQTQLND FLELSNQSAA KRMSLEDEIK RCKDLCTKAK RRSQTAQVGP ISAEISLKKS
     LLHSHQDAVE LFWLLFVCFH VCIYLMMFIQ DLRSANGGSL SSMALQDVVN GVTQLILDQQ
     VGKPMNPAIS DPNCVCACVC VVLQLNMEDP CIICHDDMSP DDVCVLECRH SFHRECIKSW
     LKEQSTCPTC REHALLPEDF PMLPGRRRRA HNPAAV
//