ID A0A7K7IHL5_LOXCU Unreviewed; 644 AA.
AC A0A7K7IHL5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
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 Name=Rnf19b_1 {ECO:0000313|EMBL:NWY93575.1};
GN ORFNames=LOXCUR_R00587 {ECO:0000313|EMBL:NWY93575.1};
OS Loxia curvirostra (Red crossbill).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Fringillidae; Carduelinae; Loxia.
OX NCBI_TaxID=64802 {ECO:0000313|EMBL:NWY93575.1, ECO:0000313|Proteomes:UP000564784};
RN [1] {ECO:0000313|EMBL:NWY93575.1, ECO:0000313|Proteomes:UP000564784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0011 {ECO:0000313|EMBL:NWY93575.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWY93575.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-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}.
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:NWY93575.1}.
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DR EMBL; VZSM01001791; NWY93575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K7IHL5; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000564784; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; 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; cd20355; Rcat_RBR_RNF19; 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; 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 Ligase {ECO:0000313|EMBL:NWY93575.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000564784};
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 252..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..242
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 23..71
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 505..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..594
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWY93575.1"
FT NON_TER 644
FT /evidence="ECO:0000313|EMBL:NWY93575.1"
SQ SEQUENCE 644 AA; 69836 MW; D161B7752215815B CRC64;
PPPPPPPPEE APVVPEGEEE LECPLCLVRQ PAENAPRLLS CPHRSCGACL RQYLRIEITE
SRVNICCPEC SERLNPADIR RLLRDSPHLV AKYEEFMLRR CLAADPDCRW CPAPDCGYAV
IAYGCASCPK LTCEREGCQT EFCYHCKQIW HPNQTCDMAR QQRAQTLRVR TKHTSGLSYG
QESGPADDIK PCPRCSAYII KMNDGSCNHM TCAVCGCEFC WLCMKEISDL HYLSPSGCTF
WGKKPWSRKK KILWQLGTLI GAPVGISLIA GIAIPAMVIG IPVYVGRKIH SRYEGKKTSK
HKRNLAITGG VTLSVIASPV IAAVSVGIGV PIMLAYVYGV VPISLCRGGG CGVSTANGKG
VKIEFDEDDG PITVADAWRA LKNPSIGESS IEGLTSVLST SGSPTDGLSV IQGNYSETAS
FAALSGGTLS GGVLSGSKGK YSRLEVQADV QKEIFPKDSV SLGAISDNAS TRAMAGSIIS
SYNPQDRECN NMEIQVDIEA KPSHYQLTSG SSTEDSLHVH TQSAENEEEE EEEEEEEDDK
QEQTCKHQSC EQKDCIGSQT WDITLAQPES IRSDLESSDS QSDDVPDITS DECESPQCQT
AAGCPHTPRA RGAQSPSAHL SHCAQAEGCR LDEMVQLECI EARV
//
