ID C3Y5W8_BRAFL Unreviewed; 635 AA.
AC C3Y5W8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN ORFNames=BRAFLDRAFT_91314 {ECO:0000313|EMBL:EEN64365.1};
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:EEN64365.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN64365.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN64365.1};
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 ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR EMBL; GG666487; EEN64365.1; -; Genomic_DNA.
DR RefSeq; XP_002608355.1; XM_002608309.1.
DR AlphaFoldDB; C3Y5W8; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3Y5W8; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd09633; Deltex_C; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF36; E3 UBIQUITIN-PROTEIN LIGASE DTX3-RELATED; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF00643; zf-B_box; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 16..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 93..140
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 154..197
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 456..494
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 369..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 212..246
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 635 AA; 70724 MW; 8BCAD0F2CAD0A8CE CRC64;
MAHALIKEIS DDFLTCQICL DTFRKPKLLD CVHSFCEECL KEYVNPGDTT VKCPTCQRDT
ALKQNGVSGL KDNFFILNLV ETIGARKKVQ RSVDKIPCDS CAGKETVVSR CLTCNDFLCE
SCVAIHRTLR AFKGHLVVTL DELRTGKYDG EADKTEPTCD IHAGEKMRFY CKTDGVPVCR
DCTVLDHPKP EHDVVNLTDV AEELRSSCQK IVTELQRALD IAENDVKAAD RAIEDIRAKS
KTAEQLVDEQ VSHLVTFIKK LGEQCKERVQ VTCRQEEKQQ HAEKERLELN KVRLSSTRDF
TETILSRGTD IEVASAFSQI TQSRDELCTS QKSTVERVMY TESEEVGSRD VLQSSAEWEK
LLTISGSIKE RQEEATRPNE QMKPVSRKPV PRKPAVTQGS RRKSKTSPIY LSASSDVATM
VYAQPVATIV TRKSHTRPGD TGKCLTSDGD DTTGDCSICM SGITDPKSLP CKHTFCRACI
DTALSYKSQC PMCNTIVGEL KGNQPPGRME WEMCHGTRLP GYENCGAIMV RYFFPDGTQG
PDHPNPGSWF RGTARRAYLP NNEEGRQLVQ LLKRAFDNRL VFTIGTSVTT GAVDTVVWND
IQHKTNVSGG ASGYGYPDPG YLTRLREELA AKGIK
//
