ID A0A8J2QGQ1_9NEOP Unreviewed; 1297 AA.
AC A0A8J2QGQ1;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=DCHRY22_LOCUS2947 {ECO:0000313|EMBL:CAG9561438.1};
OS Danaus chrysippus (African queen).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Anosia.
OX NCBI_TaxID=151541 {ECO:0000313|EMBL:CAG9561438.1, ECO:0000313|Proteomes:UP000789524};
RN [1] {ECO:0000313|EMBL:CAG9561438.1}
RP NUCLEOTIDE SEQUENCE.
RA Martin H S.;
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
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:CAG9561438.1}.
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DR EMBL; CAKASE010000046; CAG9561438.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000789524; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-ARBA.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR CDD; cd20349; BRcat_RBR_RNF144; 1.
DR CDD; cd16632; mRING-HC-C4C4_RBR_RNF144; 1.
DR CDD; cd01650; RT_nLTR_like; 1.
DR FunFam; 3.30.40.10:FF:000051; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00647; IBR; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000789524};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
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 TRANSMEM 1232..1254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 355..565
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 359..407
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 144546 MW; 5CFC06C01902D517 CRC64;
MLRPESPLAD HRSLLPRRLL PAKAQIAPVD KKKNRRSLEL NPPSNEHAPY DYPKLLISKT
TDSLNTECPR KLINKQDSSD SLKRALLSKE DKKCALKEVD KKVLTKQDSN ESLKKNPLSR
QDSNDSAKRR DSDPKWLRPD EKKSVEIKRG GDKKGLLETD IDDACKRIYE RRTGCARPTL
PPVAEKGVSP KSPNGSPITP GVVAVAEGVV RWGSGLLSPK DEPRLRPARS WYGYGTLPTD
GDKMGAGANG PGGRRALELI LSGGLKSLAR PPKPVRRAAS RDSVLSQPQP LLEGLRKCST
VLALTDREKA PEPIRAHNKL RAPSVCSRCS SLLSLAGAGG SRYSLDHAGG FVPAAPINCK
LCLDDATSDN VTVISGCGCS FCTRCMKAYV EFEVCNGAYE VSCPDDRCSV GAALSLDEIG
LLVEPSVMEK HLKFRLNHEV AMDAMRAFCP RPGCDTVVQV RAASPAHCPT CRHDFCSQCN
QEWHGGISCE AAAASSSMGG AGAPLLPDSE LIKLCPMCRV PIEKDEGCAQ MMCKRCKHVF
CWYCLASLDK GFLPGISGCL EHNTLLSESL KDARKSERQI TVCWIDLENA FGSIQHELML
FALRWYNFPP LVRDMIASYY SKLRFSIITK EGPSKSLSYN VGLFQGCCLS PIAFNIVINI
LVDKLICNEK KWGYRFKFNN KYTESILAFA DDLAILTRNP KHCQVLLDEV DKFCEWTDGL
RTKPSKCHCL CLGRRNTRYT SYDPGLSLGG QCISTVTENA PFKFLGRKID NIGRTPSLEG
IVDSFLNDLD KLDAGVIKML KLWLGLALTA DSSALFRGSN SFGMSLKRPS ELYKHLRVSK
RYILGKSHDD IVTSLPKDED APELESRLQF HKQFMIGAQS NKVGLGSNRK VQDADILKSF
IRQDENDKYK IHAMNLEMQN EWLDMGDFCI PLALKWRTLI YDWSPALLKF YLNAFQMTLP
DQSNLVRWGK STEKTCYICG KAVGTAKHLL VGCKVLLDSG QYSRRHDRVL EVIREAVSLS
VARAQKGITT NERSVGFVRE GSRATKSNVK PYSILKAASD WTIMMDTYEK QYKIPEDICA
SASRPDIFLF SRILKRVVMI ELTVPWETNI PKDHTIKVNK YYELTNELTR NRFVVDLYAV
EVGARGITAK SLYNLLKDLG LSRTHINAFL ERTSKAALVG SFQIWLGRER SLDSGGERIT
RDDFLLRHYD KGPCKNKLGH SRASVLWHRA QVVGIFAGFG LLLLVASPLL LLAAPCIVCC
KCRLCNPNTK NLEEVDEIES ISPGREDDDE RTRYISD
//