ID A0A091DQA8_FUKDA Unreviewed; 537 AA.
AC A0A091DQA8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=H920_04280 {ECO:0000313|EMBL:KFO34314.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34314.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO34314.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO34314.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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};
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DR EMBL; KN121985; KFO34314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DQA8; -.
DR STRING; 885580.ENSFDAP00000014747; -.
DR eggNOG; KOG1815; Eukaryota.
DR Proteomes; UP000028990; 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:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR11685:SF109; E3 UBIQUITIN-PROTEIN LIGASE RNF19B; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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}.
FT TRANSMEM 150..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..140
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 421..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57218 MW; 89A9DF50091E56FF CRC64;
MERKNERSAE ADHKPIYAVI AYGCASCPKL TCEREGCQTE FCYHCKQIWH PNQTCDMARQ
QRAQTLRVRT KHTSGLSYGQ ESGPDDIKPC PRCSAYIIKM NDGSCNHMTC AVCGCEFCWL
CMKEISDLHY LSPSGCTFWG KKPWSRKKKI LWQLGTLIGA PVGISLIAGI AIPAMVIGIP
VYVGRKIHSR YEGRKTSKHK RNLAITGGVT LSVIASPVIA AVSVGIGVPI MLAYVYGVVP
ISLCRGGGCG VSTANGKGVK IEFDEDDGPI TVADAWRALK NPSIGESSIE GLTSVLSTSG
SPTDGLSVMQ GPYSETASFA ALSGGTLSGG ILSSGKGKYS RLEVQADVQK EIFPKDTASL
GAISDNASTR AMAGSIISSY NPQDRECNNM EIQVDIEAKP SHYQLVSGSS TEDSLHVHAQ
MAENEEEGSG GGDGGNEEDS PCKHQSCEQK DCPPSRTWDI SLAQPESIRS DLESSDTQSD
DVPDITSDEC GSPRSHTAVC PSTPRTQGAP SPSAHKSLSA PAEGQTVLKS EGSEARV
//
