UniProt: A0A3Q3BKY5

Database: UniProt
Entry: A0A3Q3BKY5_KRYMA

LinkDB:  A0A3Q3BKY5_KRYMA 
Original site:  A0A3Q3BKY5_KRYMA

All links

Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (17)   
   InterPro (8)   
   Pfam (5)   
   PROSITE (2)   
   SMART (2)   
All databases (27)   

Download RDF

ID   A0A3Q3BKY5_KRYMA        Unreviewed;      1689 AA.
AC   A0A3Q3BKY5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   10-JUN-2026, entry version 29.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000025719.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000025719.1}
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}.
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   RefSeq; XP_017275398.1; XM_017419909.3.
DR   Ensembl; ENSKMAT00000026043.1; ENSKMAP00000025719.1; ENSKMAG00000018992.1.
DR   GeneID; 108238071; -.
DR   CTD; 7267; -.
DR   GeneTree; ENSGT00940000154465; -.
DR   OrthoDB; 8062037at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000264800; Unplaced.
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; 5.
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:UP000264800};
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          217..250
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          525..558
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1629..1669
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          333..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1494..1523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1314..1377
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1455..1489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        375..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..984
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1689 AA;  192662 MW;  53927BCE7A2E8798 CRC64;
     MFCSKLVFED LNKMSDSDSD GEWENSRYQK YKRGEAFAKF YLSDETYSQW NSIPVKTRRD
     AAQRMKVCVF WLPTVLQPDD SKTFDWALEI GFIGSRDSEE LQLEHMFKIQ IVESILFDLE
     MGTLKKEAPR HVFYLANLLN LQFCPESLEK AVHFLEKTGD RCIRSNLTLL GDFPTCLSTI
     SFIFSEYAKF IQEMSTNLGK TLVALMAKPD ECYIAQSERM KAIGNDQFRL QRYEEAVKYY
     SKAIKFFPDN HILYGNRALC YIRSEKYLKA AADGKRAVLI QPLWAKGHYR YCEALFNMHQ
     TNLALEANNT AILLCQDNLE GLVDLVQQRQ KMEEELTKMP KPAQSFKAGP SQRRPQATKN
     ASRSDRAKST APKVTETKMD KKTVKTENSV QSEGRSRDST PSKSEKRELG TPTKKKPKNR
     DVQESQKTAA RSKADVCMEL RSLVQDAHAA LYDLRSRNAE QAFSQALSLL ETVTPKELGL
     STVDVLLLLF GRVSALTEIG QPEELAESQK LLDKMKSYES RTFQSLVFFA IGRVFLRENR
     FAVALQQFSD SLQMVKNQIT PGKLTWPLTK EIVKETQPEY FKEILDRSIE LCKFPPPPDA
     VCRLEKCLCP LKAEIFLTDP DFKGFVEIRC CHSCRVEFHV SCWKSLKTTK FFERNEKDFL
     HEKCLTPDCI GRICSIKIFC PTGLVKCKFE AAIAKPQTPK KPKVNQKCTS LKKLKSKEEH
     KLKKKQYKQS FQDIKTINDE ILQKKDDSGT QKQQKAWLVY RDPVLLQINQ NSALLREEKG
     LLVSALAGSL KPWLELDSSR GNQIAARLLN WQQEPLLALG QAVELLLERK NRVWARVFIQ
     QLSSCVDINP KLSSWASQLN NAGLNAARTF IDRHAEHLEQ QDLTLLLHFE PLKEMILEKL
     SAIPEFFSST GLTVTEYLKQ APTQDMRLFI WTLEEYQDDY VSCHAILDEY FDMMDGHGSV
     LKKSDENENN SMKAKSRGRK KKQREPKGLI VFPGMRGGTR ELDQDVFEED SLSFLHPGNP
     FSVPPHLREQ VAEFEEQYGN SRSRSPFINI LDNNPDPTKE SLYDYFAQIL EEHGPLVVED
     PLLVGELQHF PAAARQKMEE AGGFEAFLLE SLRFIKMGRC IGLAKHAVAL QQAGHAASLD
     DLDEITDTDC NASPDLYTAS VFPSYLKNYT EIPPVFPNPY LCDASPHWTD RNFDQASNLL
     PNSYGETHLD ALDTNFSFSE PDLTSEKAVF MPKDETFLQR HAAAQTCPKA VSSVAVNTEL
     YEPFESYQGD LNKKEKGNIN LEQMIKKIKN CVKVNDREDI VLLEKDIKTV TINIQETLRE
     QATLQQKLEE EVEKDQKEKK ANQEELKALK TETEQLVEEQ TRLSQNIREK KSSYEKKLRD
     SLELRNQSAA EKMSLEDEIK RCKTLLASSA RRSHKAQLSV VESSRDQGLY GLYRELTDAK
     ALLSKLDEAV HRNPNQDLEG IVKTCRAKVE EMEKKISSAE RRFQEELDQL SGEFVPQASG
     DSAPPAAEAP LKQQKPVSRK PEAPLGAVRD KVMESLTAMF PDYKRPDLMK YIQEFCLSRG
     GSLSSVALQD VVGGVTQRIL DHQERLNSFR ASIVEWSGPG PYVAQSPVWQ AVTAHRFQTS
     KALNVEDPCI ICHEDMSPDE TCVLECRHGF HEECIRSWLK EQSTCPTCRT HALMPDDFPA
     LLGRRRQAP
//

DBGET integrated database retrieval system