ID A7RR57_NEMVE Unreviewed; 99 AA.
AC A7RR57;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=NEMVEDRAFT_v1g181003 {ECO:0000313|EMBL:EDO46054.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO46054.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO46054.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC {ECO:0000256|ARBA:ARBA00009273}.
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DR EMBL; DS469530; EDO46054.1; -; Genomic_DNA.
DR RefSeq; XP_001638117.1; XM_001638067.1.
DR AlphaFoldDB; A7RR57; -.
DR STRING; 45351.A7RR57; -.
DR EnsemblMetazoa; EDO46054; EDO46054; NEMVEDRAFT_v1g181003.
DR GeneID; 5518202; -.
DR KEGG; nve:5518202; -.
DR eggNOG; KOG2930; Eukaryota.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; A7RR57; -.
DR OMA; RQNNRCP; -.
DR OrthoDB; 3546417at2759; -.
DR PhylomeDB; A7RR57; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16466; RING-H2_RBX2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR11210; RING BOX; 1.
DR PANTHER; PTHR11210:SF57; RING-BOX PROTEIN 2; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 47..89
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 99 AA; 11663 MW; 8F7E1B727E504E01 CRC64;
MEDLTTPKDK ESQKMFSLKK WNAIAMWSWD VECDTCAICR VQVMDACLRC QSDNKQEECV
VVWGECNHSF HNCCMSLWVV QNNRCPLCQQ EWVVQRIGR
//
