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Database: UniProt
Entry: C3ZJ65_BRAFL
LinkDB: C3ZJ65_BRAFL
Original site: C3ZJ65_BRAFL 
ID   C3ZJ65_BRAFL            Unreviewed;       639 AA.
AC   C3ZJ65;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM71 {ECO:0000256|ARBA:ARBA00040205};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=Protein lin-41 homolog {ECO:0000256|ARBA:ARBA00043228};
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000256|ARBA:ARBA00041679};
DE   AltName: Full=Tripartite motif-containing protein 71 {ECO:0000256|ARBA:ARBA00042007};
GN   ORFNames=BRAFLDRAFT_86892 {ECO:0000313|EMBL:EEN47396.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN47396.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN47396.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN47396.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   EMBL; GG666631; EEN47396.1; -; Genomic_DNA.
DR   RefSeq; XP_002591385.1; XM_002591339.1.
DR   AlphaFoldDB; C3ZJ65; -.
DR   STRING; 7739.C3ZJ65; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; C3ZJ65; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05819; NHL; 1.
DR   CDD; cd16609; RING-HC_TRIM65_C-IV; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR   PANTHER; PTHR24104:SF48; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01436; NHL; 3.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51125; NHL; 3.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   TRANSMEM        304..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          99..140
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          340..380
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          492..534
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          539..582
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ   SEQUENCE   639 AA;  71422 MW;  C56A8A7D9ED821E7 CRC64;
     MAAAPSSLGD QICEELSCSI CLELFTRPKV LPCQHTFCQD CLQDHAGKGG AFQCPNCRLK
     FKLPPQGVAG LPNNHLVTSL CERLQNQASL SGETREQPQS GNWCSFHPSE EVKLYCKQCN
     VPVCNECLDE MHSDHETISL KKALRERKAP IEVLITEGRK ILEVYCGFLK SLREKEKTSD
     EQKQETDNSI IQAYNLEVQR ATEKRDHLLL QEEEKYKNNK EARKEERGRM LADVSKLSAA
     CNLTEQEMEQ GGVKALSLET VLAELVEKYR GKLQNAAPEH PQPDAQDVQP QSVHAVFQPP
     STPVLSMVTV AGILVVAFAV LLYSPLYRQT VQPLPKTITF GGEGSGTGQL RLPFGVAVSD
     EGEIFVADNL NQRIQVFTLQ GTFVRQFPTV VSGEERMHPH DVALDGEGNL WVVGEQWVVG
     TDLEFEPEFA VHVQYNKQGR VLRKFKLQKA AAGWLRARGV AVDTWWNRIL ITQITEDQDN
     KHGEVLVFRP DGTLVRTVGQ QQGMKYPWYV TVDGEGNILV SDRENHCVYI VYNENGQFLF
     QFGGWGSGEG QLKLPHGICT DRAGNIIVAD YGNHRVEMFD KTGRFLKHIT TETILLHTVK
     VVLMLDLKPL GPWGVAIGPQ GQLVVTDVSE DTVHIIPSY
//
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