ID A0A7K7AXT3_9AVES Unreviewed; 623 AA.
AC A0A7K7AXT3;
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 {ECO:0000313|EMBL:NWY00966.1};
GN ORFNames=NOTORN_R06276 {ECO:0000313|EMBL:NWY00966.1};
OS Nothoprocta ornata.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Nothoprocta.
OX NCBI_TaxID=83376 {ECO:0000313|EMBL:NWY00966.1, ECO:0000313|Proteomes:UP000531938};
RN [1] {ECO:0000313|EMBL:NWY00966.1, ECO:0000313|Proteomes:UP000531938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-MSB-03 {ECO:0000313|EMBL:NWY00966.1};
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:NWY00966.1}.
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DR EMBL; VZSH01000078; NWY00966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K7AXT3; -.
DR Proteomes; UP000531938; 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:000424; 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:NWY00966.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000531938};
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 231..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..221
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2..50
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 483..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..598
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWY00966.1"
FT NON_TER 623
FT /evidence="ECO:0000313|EMBL:NWY00966.1"
SQ SEQUENCE 623 AA; 67409 MW; 81F0CFAF089C65EE CRC64;
ECPLCLVRQP AENAPRLLSC PHRSCGACLR QYLRIEITES RVNICCPECS ERLNPADIRR
LLRDSPQLVA KYEEFMLRRC LAADPDCRWC PAPDCGYAVI AYGCASCPKL TCERDGCQTE
FCYHCKQIWH PNQTCDMARQ QRAQALRVRT KHTSGLSYGQ ESGPADDIKP CPRCSAYIIK
MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK ILWQLGTLIG
APVGISLIAG IAIPAMVIGI PVYVGRKIHS RYEGKKTSKH KRNLAITGGV TLSVIASPVI
AAVSVGIGVP IMLAYVYGVV PISLCRGGGC GVSTANGKGV KIEFDEDDGP ITVADAWRAL
KNPSIGESSI EGLTSVLSTS GSPTDGLSVA PGNYSETASF AALSGGTLSG GVLSGGKGKY
SRLEVQADVQ KEIFPKDSVS LGAISDNAST RAMAGSIISS YNPQDRECNN MEIQVDIEAK
PSHYQLASSS STEDSLHVHT QMAENEEEDE EEEEEEEEDG EREQTCKHQS CEPKDCLASQ
TWDITLAQPE SIRSDLESSD SQSDDVPDIP SDECGSPGPP PAPGRPARAS AAESPSAPLN
HCAHTEGYRL EEMVKLECIE ARV
//
