UniProt: A0A091VXE8

Database: UniProt
Entry: A0A091VXE8_NIPNI

LinkDB:  A0A091VXE8_NIPNI 
Original site:  A0A091VXE8_NIPNI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (19)   

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ID   A0A091VXE8_NIPNI        Unreviewed;      1740 AA.
AC   A0A091VXE8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=Y956_16596 {ECO:0000313|EMBL:KFR07213.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR07213.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFR07213.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR07213.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|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; KL411414; KFR07213.1; -; Genomic_DNA.
DR   STRING; 128390.A0A091VXE8; -.
DR   eggNOG; KOG1140; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053283; 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:UP000053283};
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          819..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..836
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFR07213.1"
FT   NON_TER         1740
FT                   /evidence="ECO:0000313|EMBL:KFR07213.1"
SQ   SEQUENCE   1740 AA;  198623 MW;  A3DB3F5619A2BF15 CRC64;
     WCDERFNFQA TFLQCLAKHV PNIYSAEMDP LLEKQEEMVQ AAILYPLECY LFGEDPDTFL
     EKLQQSGTSQ LCGKVFKGGE TTYSCRDCAV DPTCVLCMDC FQNSIHKNHR YKMHSSTGGG
     FCDCGDTEAW KAGPLCTKHE PGASGSAKEN SECQLNEEIM EHSRRVFPSV IKYIVDMLIW
     EEEKELPPEL TISREKVDSY YCVLFNDEHH SYDHVIYSLQ RALGCELGEA QLHTTAIDKE
     GRRAVKAGHY ASCQEAKEEI KRHSENVSQR PLHVEVLHAD VMAHQKFALR LGSWLNKLMS
     YSSDFRQIFC QICLKEEAGS EKPCFISKLM LWDAKLHKGA RKVLHELIFT SFFMEMEYKK
     LFAVEFVKYY KALQKEYISD DHDRVLSVTA LSVQMFTVPT LARHLIEEQN VITTITETLL
     EVLPEYLDKN DKFNFQGYSQ DKLNRVYAVI YDLRYVLVSK PTVWTDHLRE RFLEGFVSFL
     RILTCMQGME EIKRQIGQHI EVDPDWEAAI AIQMQLKNIL LMFQEWCACD EELLLRAYSE
     CHKAVMRCST NGRSREKTVF HLCGHTLESR PYRVSADPVS IHLPLSRTLA GRWGEMRKSG
     EKEKFHVLMR SSEELQVELL VEYPLRCLVL VAQVAAEMWR RNGLSLISQV FYYQDVKCRE
     EMYDKDIIML QIGASLMDPN QFLLLILQRY ELADAFKKIK PTKDQDLIKQ CNVLIEEMLQ
     ILIYIVGERY VPGVSNVTKE DVIMREIIHL LCIEPMAHSA ITKSLPENEN NETGLENVID
     KVATFKKPGV SGHGVYELKD ECLKEFNMFF YHYTKTQHSK AEHTQKKRRK QENRDEALPP
     PPPPDFSPAF SNVVRILNCD VMMHILRTIL QRAVELETHL WTEAMIQMVL HLLSLGLLEE
     RQQLQQSPEE EVTFDFYHKA TRMGSSALNA VNVLMLLEKL KTVPQLESQK DTVNWILQMF
     DTVKRLREKS SLTTVAATSG SEATKGDETQ STQDKEKAER KRKAEAARLH RQKIMAQMSA
     LQRNFIEAHK LLYENTLEAQ AKEDAIMEEE SMSSAVDCSK IALGPKRGPS VAEKEVLTCI
     LCQEEQEVKL ESAAMVLSAC VQKSTALTQN RSRILELSGD TLDPLFMHPD LPCGTHTGSC
     GHVMHAACWQ KYFEAMQLNF RQRLHVEQIF DLENGEYLCP LCKSLCNTVI PIVPLQAQKI
     NSEDAEAVAQ ILSLARWLEI ITVRISGYSV KNAKGEKPNL PAFANKGMGN SALEFHSILS
     FGVQSSAKYS SSIKEMLILF ATTIYRVGLK VAPNEADYRI PMMTWSTCAF TIQCIENLLE
     TEGKPLFGSL QNRQHSGLKA LVQFAAAQRT TSPQVLIQKH LIRLLGVLLP NFKVEDTPSL
     LEVDMFHILV GVVLSFPSLY WQDAVDLQPS SISSAYNHLY LFHLTTLAHI TQIVVSSATV
     GFIFVCAESP TTRSSDNSEE ALSAQSFCRE VCRYTSGCFS QDIPGWLVWD CVKKGIMPYL
     RSAALFFHYL LGVSPPEELL QVSEEGQFKA LCSYLSLPTN LFLLFQEYWD TVNPLLQRWC
     ADPVVLSCLK GKSIAIRYPR KRNSLIELPE DYSCLLNQAS QFRCPRSSDD EQKHPVLCLF
     CGAMLCSQNT CCQELVNGEE LGACTSHALQ CGAGVCMFLK IRECKVVLIE GKTRGCLYPA
     PYLDEYGETD PGLKRGNPLH LCRERYRKLH LLWQQHCIIE EIARSQETNQ IFFGFNWQLL
//

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