ID R0JRH8_ANAPL Unreviewed; 1732 AA.
AC R0JRH8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
DE Flags: Fragment;
GN ORFNames=Anapl_01130 {ECO:0000313|EMBL:EOA99761.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA99761.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; KB743275; EOA99761.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000296049; 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; cd16685; RING-H2_UBR1; 1.
DR CDD; cd19678; UBR-box_UBR1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR047507; UBR-box_UBR1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000296049};
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|RuleBase:RU366018}.
FT DOMAIN 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 70..141
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 820..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA99761.1"
FT NON_TER 1732
FT /evidence="ECO:0000313|EMBL:EOA99761.1"
SQ SEQUENCE 1732 AA; 198095 MW; A0831F89E8AC1052 CRC64;
WCDERFDFQA TFLQCLAKHV PNIYSAEMDP LLEKQEEMVQ AAILYPLERY LFGEDPETFL
EKLQQSGTSQ LCGKVFKGGE TTYSCRDCAV DPTCVLCMDC FQNSIHKNHR YKMHSSTGGG
FCDCGDTEAW KAGPVCTKHE PGASGSPKEN SECQLNEEVM EHSRRVFPSV IKYIVDMLIW
EEEKELPPEL TISREKVDSY YCVLFNDEHH SYDHVIYSLQ RALGCELSEA QLHTTAIDKE
GRRAVKAGRY ASCQEAKEEI KRHSENVSQR PLHVEVLHAD VMAHQKFALR LGSWLNKLMS
YSSDFRQIFC QICLKEETGS GKPCSISKLM LWDAKLHKGA RKVLHELIFS SFFMEMEYKK
HFAVEFVKYY KALQKEYISD DHDRVLSVTA LSVQMFTVPT LARHLIEEQS VITTITETLL
EVVPEYLDKN DKFNFQGYSQ DKMNRVYAVI YDLRYVLISK PTVWTDRLRE RFLEGFVSFL
RILTCMQGME EIKRQIGQHI EVDPDWEAAI SIQMQLKNIL LMFQEWCACD EELLLRAYKE
CHKAVMRCST NSSRLREKTA FHLCGHTLES RPYRVSLDPV SIHLPLSRTL AGLHVRLSKT
GSISRLHEFV SPEEFQVDLL VEYPLRCLVL VAQVAAEMWR RNGLSLISQV FYYQDVKCRE
EMYDKDIIML QIGASLMDPN HFLLLILQRY ELADAFRRIK PTKDQELIKQ CNVLIEEMLQ
ILIYVVGERY VPGVSNVTKE DVTMREIIHL LCIEPMAHSA ITKSLPENEN NETGLENVID
KVATFKKPGV SGHGVYELKD ECLKDFNMFF YHYTKTQHSK AEHTQKKRRK QENRDEALPP
PPPPDFCPAF SNVVRLLNCD VMMHILRTIL QRAVELETHL WTEAMIQMVL HLLSLGLLEE
KQQLQKSPEE EVTFDFYHKA SRMGSSALNA VNILMLLEKL KRIPQLEAQK DMINWILQMF
DTVKRMREKS SLTTVAATSV SEATKGDETQ SSQDKEKAER KRKAEAARLH RQKIMAQMSA
LQRNFIETHK LLYENTSEAQ GKEDAIMEEE SMSSAIDYSR IALGPKRGPS VVEKEVLTCI
LCQEEQEVKL ESAAMVLSAC VQKSTALTQN RSRIVELSGD TLDPLFMHPD LPCGTHTGSC
GHVMHATCWQ KYFEAMQLNF RQRLHVEQIF DLENGEYLCP LCKSLCNTVI PIVPLQAQKI
NSEDAEAVAQ ILSLARWLEI ILVRISGYSV KNAKGEKQNA LAFVNKGLGN SALEFNSILS
FGVQSSAKYS SSIKEMLILF ATTIYRVGLK VAPNEADHRI PMMTWSTCAF TIQCIENLLE
TEGKPLFGSL QNRQHSGLKA LVQFAAAQRT TSPQVLIQKH LIRLLGVLLP NFKMEDTPSL
LEVDMFHVLV GVVLSFPSLY WEDAVDLQPS SISSAYNHLY LFHLTTLAHI TQIVISSAKE
SPTARSHDNS EEACSAQSFC REVCQYTSGC FSQDIPGWLV WDCVKKGIMP YLRCAALFFH
YLLGVSPPEE LQQVSEEGQF KALCSYLSLP TNLFLLFQEY WDTVNPLLQR WCADPVVLSC
LKGKSIAIRY PRKRNSLIEL PEDYSCLLNQ ASQFRCPRSS DDEQKHPVLC LFCGAMLCSQ
NTCCQELVNG EELGACTSHA LQCGAGVCMF LKIRECKVVL IEGKTRGCLY PAPYLDEYGE
TDPGLKRGNP LHLCRERYRK LHLLWQQHCI IEEIARSQET NQIFFGFNWQ LL
//
