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Database: UniProt
Entry: C3Z056_BRAFL
LinkDB: C3Z056_BRAFL
Original site: C3Z056_BRAFL 
ID   C3Z056_BRAFL            Unreviewed;       711 AA.
AC   C3Z056;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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_85679 {ECO:0000313|EMBL:EEN54115.1};
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:EEN54115.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54115.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN54115.1};
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; GG666567; EEN54115.1; -; Genomic_DNA.
DR   RefSeq; XP_002598103.1; XM_002598057.1.
DR   AlphaFoldDB; C3Z056; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; C3Z056; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19756; Bbox2; 1.
DR   CDD; cd05819; NHL; 1.
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   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; 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; 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   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          17..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          102..143
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          445..485
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          583..625
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          629..672
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ   SEQUENCE   711 AA;  76396 MW;  C96D8CCED1E88B40 CRC64;
     MAAAQLSYEA LLEELSCSIC LEPYTRPKVL PCQHTFCQDC LQEFTGRGGA FQCPNCRQQV
     TLPSKGVAGL PDSHDHINII ANMFERLQQQ TSLSEETREQ PQPGNRCSFH PSEVLKVYCK
     QCEVPVCDQC LEQTHDDHRT TTIKKAAQDK SSTVQAYINE GRNIIESHLS FRGSMMEEEK
     TLNEKKQQLV NSIMQAYNQM VQKLTERKDH LLSEAGELYK KNLDRIQNEM DKVLTLAEVN
     ELSAACDRAE QELQQGWVEI LSQQTTLTEV VGKYRVKAAP TPVQTQPAVF QPTDTSVPVL
     GHVMVQSLPS APAPAASAPI LAGAAPATAA PAPIPGAPAP VKAAPAPIPT APAPIPAAPA
     PVKAAPAPIP AAPAPIKAAP APIPAAPAPI LAAPAPVKAA PAPIPAAPAP IKAAPAPVKA
     APAPITAASN DAAIQGEHQP EKVTFGGWGS GTGQFHGPVG VTVSDHGEIF VADRWNQRIQ
     VFTLQGTFAR QFPTVTSGGK KMYPHDVAMD RAGKLWMVGG TKSAGFAVQY SKQGRVLRKF
     DLQKIKWVRG VAMDTRRNHI LITQTTGDGD NRHGEVLVFR PDGTLVRTVG QQQGMKYPWY
     ITVGGEGNIV VSDISNQCIY VYNKDGQFLF QFGVEGSGGG QLNEPRGICT DRAGNIIVAD
     RGNSRVEMFD KKGKFLKHVT TDMFDPLAVA MASQGQLVAI GIRGGTIFHG Y
//
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