ID A0A653BIR0_CALMS Unreviewed; 739 AA.
AC A0A653BIR0;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=CALMAC_LOCUS1357 {ECO:0000313|EMBL:VEN35448.1};
OS Callosobruchus maculatus (Southern cowpea weevil) (Pulse bruchid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Callosobruchus.
OX NCBI_TaxID=64391 {ECO:0000313|EMBL:VEN35448.1, ECO:0000313|Proteomes:UP000410492};
RN [1] {ECO:0000313|EMBL:VEN35448.1, ECO:0000313|Proteomes:UP000410492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sayadi A.;
RL Submitted (JAN-2019) 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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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DR EMBL; CAACVG010001579; VEN35448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A653BIR0; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000410492; 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:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20338; BRcat_RBR_RNF19; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 3.30.40.10:FF:000137; RanBP-type and C3HC4-type zinc finger-containing protein 1; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 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:UP000410492};
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 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 340..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..330
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 117..164
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 37..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..451
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 78049 MW; 694C9D926A530DAF CRC64;
MHGSESQQPS SRKKRFPGRW SLRHLIYSSP ILNRRRSSQN VQLASSGGVP KHRREGRDVF
DGKVGHSSKD SERHHVEIHQ ATSRTSVFTT STKSGTAGNE AVPPSGGPLG ASETAECPLC
LAEVLSEEMC ELEACAHRAC HTCLQQYLRV EITESRVAIA CPECLEPIHP NEIRAILANP
ALYEKYEDFM VRRVLAVDPD TRWCPAPDCR FAVIASECAS CPKIKCERPG CDSYFCYHCK
AEWHPNQTCD AARAQRSPNI RSSSISYSQD SQHRDDIKPC PRCQVLIVKM DDGSCNHMMC
AVCGAEFCWL CMKEINDLHF LSPSGCTFWG KKPWSRKKKI LWQLGTLVGA PVGIALVAGI
TVPAMIIGIP VWVGRKLYTR YKSVNKHKRN AAIVGGVMAS VLISPILAGL AVGIGVPILL
FYVYGVVPVS LCRSGGCGGG GGTGGGSGGA GNEEAQPQRG GGTSGVAQAD TASIGAHSAA
TATGANPSIG EASLSMASSS HVVLRGCGDP EDRESSGAST GALAGSIRCG AVKTEEGGGA
KTAAPQRLEV QAEVGSQGGG SSSGGGGGGR QQRYSLTSLT ESVLTADDAA ASVRALAGSA
VLNFKTPGSD SCSCVTMEDC TSERVRFDDN VSFITSSQAE KTSIGSSCSF RSRCARSALA
KNDRVCDTLS NDSICIDMEG DNCSTASAPR SASAARKYSS QAAALRSQFF HEGSRPPAAA
NCSLDDDTII EVSNETLDR
//
