ID A0A0R3RIQ0_9BILA Unreviewed; 789 AA.
AC A0A0R3RIQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000135801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000135801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0R3RIQ0; -.
DR STRING; 1147741.A0A0R3RIQ0; -.
DR WBParaSite; EEL_0000135801-mRNA-1; EEL_0000135801-mRNA-1; EEL_0000135801.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19813; Bbox1_BRAT-like; 1.
DR CDD; cd14959; NHL_brat_like; 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; 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:SF300; PROTEIN CBR-NCL-1; 1.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 7..49
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 109..156
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 171..214
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 509..552
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 556..601
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 602..643
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 644..686
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 687..730
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 789 AA; 88063 MW; 1973494811355A9A CRC64;
MLQVVKCPLC LEPYREPKVL ACFHSFCKSC LERQMDDSCA EKIVCPQCRV ETQLSIQLGI
ESLLTDYGLE SVMTRQNLSD DKGLIFGSPS STSSSPPLIE PPSYDQNSNK NSSCTGCKSG
ELASAFCQDC THFLCANCTL AHQYMHCFEG HRVDQLSQED AAALAAAFAE KTACKCIQHR
SQPLRYFCLT CNLAICMECT QVDHVQPTHQ YELISDVADK QMAVMETLVQ DARLKHSELL
ETYKMVDAAQ NRLSCSLTRA HQNVDDATQT LIRIIEDNRR QIIKDLDNAY GAKQLQLTVI
DKKVQQMAEK LAQTIEFTSR LVKYAAPTEV MVFKQLLHTR LQVYFSFNPD SNNILQTTCE
LDFPPLNPNV ARQQIISIMG LVRGASEWPQ GTMSSANTGM PPAPIGRPAS RQLTRPVAAT
SGTLPINNFS DSNLIRPKNE YGGSSQSLGT FVTVDNGFSN QYEKWSMGLE PANGLQLAES
PDLDLEKNMG ISNLYPPRAQ IKRQKMIYHC KFGEFGVMEG QFTEPSGVAV NAQNDIIVAD
TNNHRIQVFD KEGRFKFQFG ECGKRDGQLL YPNRVAVNRL TGDFIVTERS PTHQIQIYNQ
YGQFLRKFGA NILQHPRGVC VDSKGRIIVI ECKVMRVIIF DMFGNILQKF SCSRYLEFPN
GVCTNHKQEI LISDNRAHCI KVFNYDGQFV RQIGGEGITN YPIGVGINYA GDIVVADNHN
NFNLTVFNQD GTMISALESK VKHAQCFDVA LVEDGSVVLA SKDYRLYLYR YQSSGTTTAG
AAVTTNSPK
//
