ID A0A443S6G8_9ACAR Unreviewed; 309 AA.
AC A0A443S6G8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN ORFNames=B4U80_00318 {ECO:0000313|EMBL:RWS23136.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS23136.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS23136.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS23136.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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:RWS23136.1}.
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DR EMBL; NCKV01007048; RWS23136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443S6G8; -.
DR STRING; 299467.A0A443S6G8; -.
DR EnsemblMetazoa; LDEU008905-RA; LDEU008905-PA; LDEU008905.
DR VEuPathDB; VectorBase:LDEU008905; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000288716; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR015036; NRDP1.
DR InterPro; IPR037255; NRDP1_C.
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; PTHR10131:SF157; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR Pfam; PF08941; USP8_interact; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716};
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 COILED 135..162
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 309 AA; 34982 MW; A0690380D45823F9 CRC64;
MGFDLGRFRG DVDDELICAI CSGVLQEPLQ APGCEHSFCS FCIKQWLLRQ MNCPVDRQPL
TTTQLKAVPR ILRNLLSRLN IECDNAVFGC TAVVKLDCLT SHCLECSYNP KKPVTCELGC
GLIIPKDELK DHNCVRDLRS LVEKQQEQIS KLQQQFSDLK LEVNMLKDCA RAMRSSNEGN
VPAIVEHFEQ DEVVRWAHTL PTARVTRWGG MISTPDANLQ EGVRKALIDS GCPPHIVTEL
MENSHERRWP LGLSTLEIRQ MNRRVYDNYV CRKISSRQAV VVMSCDNTHM SEDMILDPGL
VMIFAHGIE
//
