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Database: UniProt
Entry: C3YHI5_BRAFL
LinkDB: C3YHI5_BRAFL
Original site: C3YHI5_BRAFL 
ID   C3YHI5_BRAFL            Unreviewed;       631 AA.
AC   C3YHI5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
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_71751 {ECO:0000313|EMBL:EEN59972.1};
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:EEN59972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59972.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN59972.1};
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; GG666514; EEN59972.1; -; Genomic_DNA.
DR   RefSeq; XP_002603961.1; XM_002603915.1.
DR   AlphaFoldDB; C3YHI5; -.
DR   STRING; 7739.C3YHI5; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; C3YHI5; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
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   PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR   PANTHER; PTHR24104:SF48; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF17170; DUF5128; 1.
DR   Pfam; PF01436; NHL; 1.
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; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          39..80
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          121..162
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          363..403
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          502..544
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          549..591
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          333..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          194..269
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   631 AA;  69992 MW;  26FEBF1F0987076C CRC64;
     MDRWASGTVT LEGFVRHKVK KMAAAPTSLG AQIREELSCS ICLELFTRPK VLPCQHTFCL
     SPCLENLAGR GGTLKCAVCR QQVRLPPQGV AGLPDNHLVT SLCERLQNQA TLSGETREQP
     QSGNRCSFHR SEVLKVYCKP CQIPVCKPCL EEAHDGHGTT TIKKAAQERN STVQALINEG
     RNILESYLSF LRSLREDEKT LNEKKQQRDN YIIQTYNQMV QKLTQRKDQL LSESHQSNRE
     NLDRIQTERD RVLADINELS AACDQAEQEL QQGWVEFLSQ QTALTEVVEK YRGKAAPTPV
     QTQPAVFQPT DTPVPVLGHV TVQALPSAPI PAAHASTNSA IGGRGHHHGN QRQEEPQSEK
     VTFGGEGSET GQFRDPLGVT VSDEGEIFVA DSGNNRIQVF TLQGAFVRQF PTVVAGGRKM
     YPGNVAVDGE RNLWVVGMTG PESADFAVQY NKQGRVLRKF DLQKIGEHRG VAVDTRRNHI
     LITQTTWDGN HHGEVLVFRP DGTLVRTVGQ QQGMKYPWYI TVDREGTILV SDISNHCVYV
     YNEDGQFPFQ FGGEGSGEGQ LGCPLGICTD RAGNIIVADY KNWYVEMFDK TGKFLKHITT
     DMKPYAVAMA PQGQLVVTDT GNKTVSIFPT Y
//
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