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Database: UniProt
Entry: A0A6J3R387_TURTR
LinkDB: A0A6J3R387_TURTR
Original site: A0A6J3R387_TURTR 
ID   A0A6J3R387_TURTR        Unreviewed;       421 AA.
AC   A0A6J3R387;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=RNF14 {ECO:0000313|RefSeq:XP_033709240.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033709240.1};
RN   [1] {ECO:0000313|RefSeq:XP_033709240.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_033709240.1};
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00044508}.
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DR   RefSeq; XP_019780165.1; XM_019924606.1.
DR   RefSeq; XP_033709240.1; XM_033853349.1.
DR   AlphaFoldDB; A0A6J3R387; -.
DR   GeneID; 101339880; -.
DR   Proteomes; UP000245320; Chromosome 3.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20341; BRcat_RBR_RNF14; 1.
DR   CDD; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd16628; RING-HC_RBR_RNF14; 1.
DR   CDD; cd23820; RWD_RNF14; 1.
DR   FunFam; 1.20.120.1750:FF:000011; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 2.20.25.20:FF:000007; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000186; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR031128; RNF14_RING-HC_Zfn.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          163..404
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          167..212
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   421 AA;  48036 MW;  C37DEAD68A5C8BB0 CRC64;
     MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFL SALCKHLDNL
     WEEHRGSVVL FAWMQFLKEE TLAYLNIVSP FELKMGSQKK VQRRMAQASS NTELDFGGAA
     GSDVDQAEVV DERAVQDVES LSSLIQEILD FDQAQQIKCF NSKLFLCNIC FCEKLGSECM
     YFLECRHVYC KACLKDYFEI QIRDGQVQCL NCPEPKCPSV ATPGQVKELV EAELFARYDR
     LLLQSTLDLM ADVVYCPRPS CQLPVMQEPG CTMGICSSCN FAFCTLCRLT YHGVSPCKVT
     AEKLMDLRNE YLQADEANKR FLEQRYGKRV IQKALEEMES KEWLEKNSKS CPCCGTPIEK
     LDGCNKMTCT GCMQYFCWIC MGSLSRANPY KHFTDPVSPC FNRLFHAVDV NGVIWEDEFE
     D
//
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