ID C3YHG3_BRAFL Unreviewed; 714 AA.
AC C3YHG3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_102380 {ECO:0000313|EMBL:EEN59950.1};
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:EEN59950.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59950.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN59950.1};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666514; EEN59950.1; -; Genomic_DNA.
DR RefSeq; XP_002603939.1; XM_002603893.1.
DR AlphaFoldDB; C3YHG3; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; C3YHG3; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05819; NHL; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR035892; C2_domain_sf.
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; PTHR10680:SF28; DED DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10680; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE; 1.
DR Pfam; PF17170; DUF5128; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 20..61
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 191..227
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 325..367
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 371..414
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 586..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 78964 MW; 3B8BFBB5EF1C74F4 CRC64;
MAAASTRLSL GTQLREELSC SICLELFTRP KVLPCQHTFC LSPCLENLAG RGGALKCAIC
RQQVRLPPQG VAGLPDNHLV TSLCERLQNQ ATLSGETKEQ PQSGNRCSFH PSEVLELYCK
HCHIAICKQC LEDAHDGHLT TTAKKAAQER SLTVQTLINE GRNIQERGHH HGNQRQGRHQ
PKNLVITFGN GSGTGQLDYP YGVTVSDEGE VFVASRWNNE IQVFTLQGTF VRQFQTVTSG
GLKMGPEDVA MDGEGNLWVV GMTDYGQVPL QYNKQGSVLG TFDLKLSRWV RGVALDTRRN
HILITQTTGD KDDKHGEVLV FRPDGTLVRT VGQQQGMKHP WYITVDGEGN ILVSDYDGHC
VYMYNEDGQF LFQFGGEGSG EGQLKGPRGI CTDRSGNIIV SDTGNRRVEM FDKTGKFLKH
INIATDVKVP QAVAMAPQGQ LPQYNTYEPV WEEAFNFLIQ NPLHQELLAE VKHEKTKKSL
GKKVISVKIR CLRYLTLFLQ VKDEKTKKTL GKKVISVKIR CLRYLTLFLQ VKDEKTKKTL
GKKVISVKSL LTLDRMSTKR PFRLDGTSAE LHMELILRIL SSEAEESDDL DEIEPVSPTA
AGPSMPAAPP TEPAQPSPAS STEDRQANNS NGSVVRRRIN ANAASSTTPT RPKSEPAHAV
DGPNPYTCQI QLSLHHSADT DKLLVTVHKA TFELKQDVGS LSRSSSVSSY RSEL
//