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Database: UniProt
Entry: A0A1V4K6K2_PATFA
LinkDB: A0A1V4K6K2_PATFA
Original site: A0A1V4K6K2_PATFA 
ID   A0A1V4K6K2_PATFA        Unreviewed;      1728 AA.
AC   A0A1V4K6K2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   03-MAY-2023, entry version 17.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   Name=UBR3 {ECO:0000313|EMBL:OPJ80034.1};
GN   ORFNames=AV530_002441 {ECO:0000313|EMBL:OPJ80034.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ80034.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ80034.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ80034.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ80034.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation.
CC       {ECO:0000256|RuleBase:RU366018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU366018};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU366018}.
CC   -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC       ECO:0000256|RuleBase:RU366018}.
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:OPJ80034.1}.
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DR   EMBL; LSYS01004331; OPJ80034.1; -; Genomic_DNA.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd16483; RING-H2_UBR3; 1.
DR   CDD; cd19673; UBR-box_UBR3; 1.
DR   Gene3D; 2.10.110.30; -; 1.
DR   InterPro; IPR044046; E3_ligase_UBR-like_C.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR   PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR   Pfam; PF18995; PRT6_C; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1..48
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   DOMAIN          1168..1223
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   ZN_FING         1..48
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          194..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1023..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1030..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1728 AA;  195650 MW;  F46EC5086147D36C CRC64;
     MSLCAECFHQ GEHAGHDYNM FRSQAGGACD CGDSNVMREA GFCKRHRIKS NSNVPCVPKD
     LLMMSELVLP QFIFSLIQHL REGYNEPALD LPSEKDLHKI LQVLEPHVSF LEDLTKMGGA
     MRSVLTQVLT SQQFYKDLSS GVGENACAKK SHEKYLIALK GSGLAFPEDK IACGVQEEGA
     GTSTLAVQGL AGATATSGQG DSSDEEDQDG SQGVGKRKRV KLSSTTKDQS IMDVLKHKCF
     LEELLFWTIK YEFPQKMVTF LLNMLPDQDY KIAFTKTFVQ HYAFIMKTLK KSHESDTMSN
     RIVHISVQLF SNEELARQVT EECQLLDIMV TVLLYMMESC LIKSELQDEE NSLHVVVNCG
     EALLKNNTYW PLVSDFINIL SHQSVAKKFL EDHGLLVTWM NFVSFFQGMN LNKRELNEHV
     EFESQTYYAA FAAELEACAQ PMWGLLSHCK VRETQEYTRN VVRYCLEALQ DWFDAINFVD
     EPAPNQVTFH LPLHRYFAMF LSKAVKCQEL DLDTILPDQE MLMKLMIHPL QIQASLSEIH
     SNMWVRNGLQ IKGQAMTYVQ SHFCNSMIDP DIYLLQVCAS RLDPDYFISS VFERFKVVDL
     LTMASQHQNT VLDSEHERSM LEGALTFLVL LLSLRLHLGM TDDEILRAEM VAQLCMNDRT
     HSSLLDLIPE NPNPKSGIIP GSLSFESVLS AVADFKAPVF EPGGSMQQGM YTPKAEVWDK
     EFDPVMVILR TVYRRDVQSA MDRYTAFLKQ SGKFPGNPWP PYKKRTPLHP SYKGLIKLLH
     CKTLHIVLFT LLYKILMDHQ NLSEHVLCMV LYLIELGLEN SPEQESDEEE SAGGQERCHD
     SWFPGSNLVS NMRHFINYVR VRVPETAPEV KREPPASTSS DGLAASQNSG TAQVFSLVAE
     RRKKFQEIIN RNTSEANQVV RPKTSMKWSA PGATPQLTTA ILEVKESILS LLIKLHHKLS
     GKQNSYYPPW LDDVDVLIHP ESSRYCHGDG MTAVERILLK AALQSRLNKR IIEEICRKVT
     PPVPPKKISS AEKKALDKEE RRQKARERQQ KLLAEFASRQ KSFMETAMDV ESPDADIAME
     VATSEQHVSE AIYDCVICGQ SGPSTEDRPT GLVVLLQASS VLGQCRSSTE PKKLPTTEEE
     QIYSWDTCAT LHDARLSTLQ RYFKDSSCLQ AVSIGWEGGV YVQTCGHTLH IDCHKSYMES
     LRNDQVLQGF SVDKGEFTCP LCRQFANSVL PCYPGNNTER SLWQSHSNKC MQDLVQEVED
     LQEQLGTFPS ETNLSKEMES VMKDIKSTTQ KKYTDYSKSP GSPDNDFLFM YSVARTNLEL
     ELVHRGGNLC SGGASTAGKR SCLNQLFHVL AMHMRLYSID SAYNPWRKLT QLMQDKNSEL
     VSEELPEVPV LYRDVSSLLL IQILTMPQPL HKEHFTCIIK VLFTLLYTQA LAAFSVKCSA
     EERMAWKESG ALKKNTSSGE KSWEVLLGHV ISELSKGKIY EEQETEELTV VNPDSVECDL
     QQFCLPFLRI TSLLQHHLFG GDLPSCQEDE EFTVLASCLG LLPSFQSAHQ FTSASCLDWP
     VPAFDMISQW CSELVSFSDT HPDQVKMLLM QEPKWDLPRL LQLPENYNTI FQYYHRKTCT
     VCTKVPKDPA VCLVCGTFVC LKGLCCKQQS YCECVLHSQN CGAGTGIFLL INASVIIIIR
     GHRFCLWGSV YLDAHGEEDR DLRRGKPLYI CKERYKVLEQ QFLLDMRL
//
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