ID C3YXS8_BRAFL Unreviewed; 564 AA.
AC C3YXS8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BRAFLDRAFT_90099 {ECO:0000313|EMBL:EEN54887.1};
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:EEN54887.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54887.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN54887.1};
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}.
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DR EMBL; GG666563; EEN54887.1; -; Genomic_DNA.
DR RefSeq; XP_002598875.1; XM_002598829.1.
DR AlphaFoldDB; C3YXS8; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3YXS8; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR Gene3D; 2.60.220.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR PANTHER; PTHR25464:SF2; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 18..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 564 AA; 61913 MW; 2993202276B4298C CRC64;
MAAAPSSLGT DFREELTCSI CLELFTRPKV LPCMHTFCQD CLQGINVARR EMPFKCPLCH
RQVKLPPQGV EGLPDNHLIT TLCERLQQVT LSGRKEETHL LSQINILTEA VGKYRGKAAT
PPLQTQSAVF RHTYDPGSAR VMVFAPTKTA MGGSINLKLQ RQTGSVALEE GFQKTLESIF
CRLDKRDSRL LQRVWSARTA DQQSPDMEGP VDLMKSMVKS GYIITGDIRM LEKDMIAAGI
SLPAIARDIP GVLEVCCSKK TEASVGPIGG EVEVPGFVKL AVPPGALQRD TTVTVSIADI
PGILSSPEGV NWTSGYPWSL KDACKRELLD QVLFSPAVGV SLHGAKLSRP IELETWRPPG
SEGMECVLLK HHTGEGWRDI TASTRHQIHP DKVSIFLQSF CPLVPVWIDP AATGSSPGSG
DRTIAVKDTL VAALESRTLD CYFTAYIKPI AHADQMRFHV VCRERCVKAE EYLPGFKLCG
SNKATRLLFH GDGIDVTVSV NRCPKRSKQV NVCAGHCLEP SGQQIQMNLD RPDGNPATGE
VQVRKIQQLP WPVVCELDFE EVKD
//
