ID A0A0N4Y7J6_NIPBR Unreviewed; 934 AA.
AC A0A0N4Y7J6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=NBR_LOCUS12134 {ECO:0000313|EMBL:VDL75723.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001213301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001213301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL75723.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; UYSL01020680; VDL75723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4Y7J6; -.
DR STRING; 27835.A0A0N4Y7J6; -.
DR WBParaSite; NBR_0001213301-mRNA-1; NBR_0001213301-mRNA-1; NBR_0001213301.
DR OMA; CDVNYQL; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR003649; Bbox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR047153; TRIM45/56/19.
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 InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF229; NHL (RING FINGER B-BOX COILED COIL) DOMAIN CONTAINING; 1.
DR Pfam; PF01436; NHL; 1.
DR Pfam; PF00643; zf-B_box; 2.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00024}.
FT DOMAIN 134..181
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 193..233
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 292..323
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 496..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 102147 MW; E6B20A1AA6F65287 CRC64;
MYENICYLQL KCYRSSTSSP LLNTEPLPLD DQSHCPYCHK DFRKPRVLDC LHSMCEDCII
AQLDGRRDAQ KATESNRNPT DCELETPKLK ERPTPPGVIR CPICAQESHV GNDVRYVHTM
LLDYVRLAEN EEAVGERRCR ACKSEQPAIA VCKQCQSDLC SNCLSAHGVM RMFEGHEVMT
YAEMEQRGQR GDVRPVQCPT HSLPYKMLCA TCETLCCKVC LEMEHLNHKV VDVNARVVFT
IQSEIEKLAD NVEKKWRDSM AEWSAIPDRS ASLHEQYEAA KVHVEMAFDD LLKALEEAKT
NKLAQLEETR QKQEVAIEDL YRKMNLNEAR VSDALRFARN LLSKSNGMEL LASRRKVVQQ
LNNLAHTMPA LGIQVELEYQ PLSKKQLDSH MNAICGNVIG RMVSATVKEN ITVQQSASQQ
VQQTQGDYQP NRNGTAALPN TSDWNRTLTN GHGSCSDLGA IGVERKKSSI ASAWSNSVAP
SRISGPGGDA FGWPPSSHPP DLPSPSPPIP LKDVTPPSFT ASGPGIIGQP SATNPTVSAP
GGNPLLTGTS NTASMIYNNY QWPPSSNPAQ AADLRLFPSM THPNSVVGAS QLKLAQAQAA
QLQAALLLQN NGLANPNLLM QARLRSLAPG VDPLLALGSL SLAGGPGDGG ALLGGGAQRT
SPQEVLSSTR VPELKIHSVF GTSQQGSSMR ELHCPSGFCL SESDDILIAD TNNHRIVVCG
PPHPWKIGRP GTDDGQLCFP RKVIALKGDV TRYAVLDKGV DGKTRAQLFD QRGEFIKRIN
MVLLVPRGGI EVSAASCTSA GHLLLVDTSG VVYCIDVDAP RVVFWFDASS HLGEASDVAI
YEKNVYITDF KHHCVQVFNT DDVSKNGDVL VADTHGNHLH VVVFTADGTL QQSFTHNEFR
LSRCVGLRVA GSGHVVTLCK HNHTLFVFKP LYIR
//
