ID A0A8J6ALY0_GALPY Unreviewed; 827 AA.
AC A0A8J6ALY0;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN ORFNames=J0S82_004538 {ECO:0000313|EMBL:KAG8524054.1};
OS Galemys pyrenaicus (Iberian desman) (Pyrenean desman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; Galemys.
OX NCBI_TaxID=202257 {ECO:0000313|EMBL:KAG8524054.1, ECO:0000313|Proteomes:UP000700334};
RN [1] {ECO:0000313|EMBL:KAG8524054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBE-C5619 {ECO:0000313|EMBL:KAG8524054.1};
RX PubMed=34295371;
RA Escoda L., Castresana J.;
RT "The genome of the Pyrenean desman and the effects of bottlenecks and
RT inbreeding on the genomic landscape of an endangered species.";
RL Evol. Appl. 14:1898-1913(2021).
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}.
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:KAG8524054.1}.
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DR EMBL; JAGFMF010011395; KAG8524054.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000700334; 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; cd20362; BRcat_RBR_RNF19A; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 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 FunFam; 3.30.40.10:FF:000052; 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; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
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:UP000700334};
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 350..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..340
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 121..169
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..47
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..631
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..672
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG8524054.1"
SQ SEQUENCE 827 AA; 89887 MW; 18BD84A8EEE29D19 CRC64;
NICDNRYLQI ELFQEFLKER NMSLHRQMGS DRDLQSSASS VSLPSVKKAP KKRRISIGSL
FQRKKNNKRK SRELNGGVDG IASIESIHSE MCTDKNSIFS TNTSDNGLTS ISKQIGDFIE
CPLCLLRHSK DRFPEIMTCH HRSCVDCLRQ YLRIEISESR VNISCPECTE RFNPHDIRLI
LSDDVLMEKY EEFMLRRWLV ADPDCRWCPA PDCGYAVIAF GCASCPKLTC GREGCGTEFC
YHCKQIWHPN QTCDAARQER AQSLRLRTIR SSSISYSQES GAAADDIKPC PRCAAYIIKM
NDGSCNHMTC AVCGCEFCWL CMKEISDLHY LSPSGCTFWG KKPWSRKKKI LWQLGTLVGA
PVGIALIAGI AIPAMIIGIP VYVGRKIHNR YEGKDVSKHK RNLAIAGGVT LSVIVSPVVA
AVTVGIGVPI MLAYVYGVVP ISLCRSGGCG VSAGNGKGVR IEFDDENDIN VGGTNTAVDT
TSVAEARHNP SIGEGSVGGL TGSLSASGSH MDRIGAIRDN LSETASTMAL AGASITGSLS
GSTMVNCFNR LEVQADVQKE RYSLSGESGT VSLGTVSDNA STKAMAGSIL NSYIPLDKDG
NSMEVQVDIE SKPSKFRHNS GSSSVEDGSA SRNHPVGSSS GLPEGKSSAT KWSKEATAGK
KSKTGKLRKK SNMKINETRE DMDAQLLEQQ STNSSEFEAP SLSDSMPSVA DSHSSHFSEF
SCSDLESMKT SCSHGSSDYH ARFATVNILP EVENDRLENS PHQCSISVLT KTASCSEVPQ
SNHIAEEHGN NGIKPNVDSY FGDALKETNN NHSHQTVELK VAIQTEI
//
