ID C3YGR0_BRAFL Unreviewed; 1246 AA.
AC C3YGR0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
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_79421 {ECO:0000313|EMBL:EEN60570.1};
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:EEN60570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60570.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN60570.1};
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; GG666512; EEN60570.1; -; Genomic_DNA.
DR RefSeq; XP_002604559.1; XM_002604513.1.
DR AlphaFoldDB; C3YGR0; -.
DR eggNOG; KOG1598; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3YGR0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19756; Bbox2; 1.
DR CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1.
DR CDD; cd05819; NHL; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 1.20.5.650; Single helix bin; 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; IPR011665; BRF1_TBP-bd_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR013150; TFIIB_cyclin.
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; PF07741; BRF1; 2.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF00382; TFIIB; 2.
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; SSF47954; Cyclin-like; 3.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 483..523
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 564..605
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 817..857
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 1008..1051
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 268..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..267
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 678..712
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 292..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 138527 MW; 0F603CAD270C1776 CRC64;
MPAVPENSGC VSAGDPCLYI HRFAHKLEFG ERTHEVSMTA LRLVSRMKRD WMHGGRRPSG
LCGAGVNDGT APGVTDEAGL DARRQAALRT VCLFACVNDG TVPGVTDEAG LDARRQAALR
ALRSRYVFVC LFVCLLEVSM TALRLVSRMK RDWMHGGRRP SGLCGAGMCL FVCLFEVSMT
ALRLVSRMKR DWMHGGRQPS GLCGAALLVS ARLHDFHRTQ KEIIKVLEEQ LDKEIEGELT
SLEVEIEKEL EREREKRMKK MKNLLAAKGI TESDIRGTPA GSPMPPLEGQ EDGTSSPGTP
CSRVDSPSVV PGTSSSGNPP EQKHSEQQHS EQQLPQEQQL SEEEVMGKIL SPFAGIAPAL
GPEPTPESLG IKDSLDECLK VASEKEEGTE DEDGEKEEGG ELDLTGINDE ELDWFLLNDE
EVRIKTEIWT LANADYIQKM KEKEEKEALE KEQGIHKPEQ KKVNKMAAAP SSLGAQFREE
LSCSICLELF TRPKVLPCQH TFCQDCLQDL AGKNKHLKCP NCRKHVWLSR KGVAGFRDNH
LVTSLCERLQ NQATVSGETR EQPQFGNRCS FHPSEVLKVY CKQCQIPVCD HCLEVTHDGH
GTTTIKKAAQ ERSLTVQPLI NEGRNILEGY CSFIRGQMEE EKTLKEQKQQ RDNSIIQAYN
QMVQKVTESK DLLLSESQQI HRENLEKMQN ERDRVLADVK ELSAACDQAE QELQQGWVEF
LSQQTALTLM TEVVGKYRGK AAPTPVQTQS AVFQPTDTPV PLLGHMRVQA LPSAPIPAAP
APIPGAAVSS NDAAGGMGHH HGNQRQEATQ SHDQVTFGEE GSGTGQFDCP CGVTVSDEGE
IFVADRWNQR IQVFTLQGTF VRQFSTVVSG EEKMWPCDVA MDGEGNLWVV GETGDDISDE
FAVQYNKQGR LLRKFDLQTT GLCRGVAVDT RRNHILITQS KIVNTRYIYN QHGEVLVFRP
DGTLVRTVGQ QQGMVYPWFI TGNEVGNIFV LDCHNHHVYG YNEDGQFLFQ FGGEGSGEGQ
LKNPLGICTD RAGNIIVADT WNNRVEMFDK AGKFLKHITT GKTMPHAIAM APQGQLRRKP
KKKQPIQAST AGEAIEKMLQ EKKISSKINY DVLRDLNKET ETKKPLEITP SRLTPSRLQQ
PLMSPAVPAR TALRLPTGGS SKRPHLKVEE TEEKPVVKKP KLEGSEVVVE TGPVEYAKVE
PGTVDHEEEA EDYYEEDEPI SAAQLMGRTE VDHEDYDDGY DMDEYD
//
