ID A0A091HNH0_CALAN Unreviewed; 1228 AA.
AC A0A091HNH0;
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=N300_13191 {ECO:0000313|EMBL:KFO97818.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO97818.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO97818.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO97818.1};
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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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DR EMBL; KL217677; KFO97818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HNH0; -.
DR STRING; 9244.A0A091HNH0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054308; 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; 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; 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:UP000054308};
KW Transferase {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 818..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO97818.1"
FT NON_TER 1228
FT /evidence="ECO:0000313|EMBL:KFO97818.1"
SQ SEQUENCE 1228 AA; 141538 MW; DE25FB5594368944 CRC64;
WCDERFNFQA TFLQCLAKNV PNIYSAEMDP LLEKQEEMVQ AAILYPLECY LFGEDPDMFL
EKLQQSGTSQ LCGKVFKGGE TTYSCRDCAV DPTCVLCMDC FQNSIHKNHR YKMHSSAGGG
FCDCGDTEAW KAGPLCTKHE PGASGSAKEN SEYQLNEEIM EHSRRVFPAV MKYIVDMLIW
EEEKELPPEL TVSREKADSY YCVLFNDEHH SYDHVIYSLQ RALGCELGEA QLHTTAIDKE
GRRAVKAGHY ASCQEAKEEI KRHSENVSQR PLHVEVLHAD VMAHQKFALR LGSWLNKLMG
YSSDFRQIFC QICLKEDAGS EKPCFISKLM LWDAKLHKGA RKVLHELIFS SFFMEMEYKK
LFAVEFVKYY KALQKEYISD DHDRVLSVTA LSVQMFTVPT LARHLIEEQN VITTITETLL
EALPEYLDKN DKFNFQGYSQ DKLNRVYAVI FDLRYILVSK PTLWTDRLRE RFLEGFVSFL
RILTCMQGME EIKRQIGQHI EVDPDWEAAI AIQMQLKNIL LMFQEWCACD EELLLRAYRE
CHKAVMRCST NGRSREKTVF HLCGHTLESR PYRVSADPVS IHLPLSRTLA GLHVRLSKTG
TISRLHEFVP PEEFQVELLV EYPLRCLVLV AQVAAEMWRR NGLSLISQVF YYQDVKCREE
MYDKDIIMLQ IGASLMDPNQ FLLLILQRYE LADAFKKIKP TKDQDLIKQC NVLIEEMLQI
LIYVVGERYV PGVSNVTKED VIMREIIHLL CIEPMAHSAI TKSLPENENH ETGLENVIDK
VATFRKPGVS GHGVYELKDE CLKEFNMFFY HYTKTQHSKA EHTQKKRRKQ ENRDEALPPP
PPPDFSPAFS NVVRILNCDV MMHILRTILQ RAVELETHLW TEAMIQMVLH LLSLGLLEEK
QQLQKAPEEE VTFDFYHKAT RMGSSALNAV NVLMLLEKLK RVPQLEAQKD TVSWILQMFD
TVKRLREKSS LTSVAATSGS ETTRCDEFWA PQFKKDREVL ERVQRRATKM IKGVEHLPYE
ERLRELGLFS LEKRRLRGDL INVFKYVRAI DYSRIALGPK RGPSVAEKEV LTCILCQEEQ
EVKLESAAMV LSACVQKSTA LTQNRSRILD VSGDTSDPLF MHPDLPCGTH TGSCGHVMHA
ACWQKYFEAM QLNFRQRLHV EQIFDLENGE YLCPLCKSLC NTVIPIVPLQ TQKINSEDAE
AVAQILSLAR WLEIVIVRIS GYSVKNTK
//
