ID A0A0T6B8M3_9SCAR Unreviewed; 230 AA.
AC A0A0T6B8M3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase NRDP1 {ECO:0000256|ARBA:ARBA00015711};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein 41 {ECO:0000256|ARBA:ARBA00030556};
DE AltName: Full=RING-type E3 ubiquitin transferase NRDP1 {ECO:0000256|ARBA:ARBA00031762};
DE Flags: Fragment;
GN ORFNames=AMK59_4078 {ECO:0000313|EMBL:KRT83657.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT83657.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT83657.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT83657.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT83657.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT83657.1}.
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DR EMBL; LJIG01009149; KRT83657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B8M3; -.
DR OrthoDB; 5490637at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd16634; mRING-HC-C3HC3D_Nrdp1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR015036; NRDP1.
DR InterPro; IPR037255; NRDP1_C.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR10131:SF157; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR Pfam; PF08941; USP8_interact; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF160088; NRDP1 C-terminal domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 18..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 230
FT /evidence="ECO:0000313|EMBL:KRT83657.1"
SQ SEQUENCE 230 AA; 26654 MW; D888EF093A984463 CRC64;
MGFELNRFQG EVDEELVCPI CSGVLEDPLQ APVCEHAFCK TCIHEWISRQ PTCPVDRQHI
TSAQLRQVPR ILRNLLSRLS INCDNAQYGC SRTLKLDVLA SHLEECEHNP KRPLPCEQGC
GLIIPKDELK DHNCVKELRT LISKQQQKFN DFQQELTEQR FIINEQKREL QLLKDFMRAM
RISNPAMRAI ADAMERDEVL RWSNSLTRAR VTRWGGMIST PDEVLQLMIK
//
