ID A0A401RZA9_CHIPU Unreviewed; 1754 AA.
AC A0A401RZA9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=chiPu_0001887 {ECO:0000313|EMBL:GCC23491.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC23491.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC23491.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
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:GCC23491.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BEZZ01000031; GCC23491.1; -; Genomic_DNA.
DR STRING; 137246.A0A401RZA9; -.
DR OMA; GEASYMC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000287033; 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; cd19679; UBR-box_UBR2; 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; IPR047508; UBR-box_UBR2.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF28; E3 UBIQUITIN-PROTEIN LIGASE UBR2; 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:UP000287033};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1754 AA; 199707 MW; DFEE30F10D49EFB0 CRC64;
MAATESEEVP AIPKFLMDCS AKDIALNWLQ TTDLTRDVYQ HLADCVPKIY CRGSNPNPLN
EEMLAQHILL GPMEWYLCGE DPAVGITKLE KANKSSQLCG RVFKIGEPTY SCRDCAVDPT
CVLCMECFLA SVHRAHRYRM TTSGGGGFCD CGDTEAWKQG PYCLKHKPAV SGSMEEDPLA
HLSEDMVGRA YNIFAIAFKY AVDMLTWVEE DRLPSGLEPL EKEDTYYCML FNDEVHTYEQ
VIYTLQKAVN CTQKEAVSFA TTVDRDGRRS VRYGDFQFCE QAKTIIVRNT SRQTKPLKVQ
VMHSSVVAHQ NFAIKVLIWL SQVIGYSGGL RRILCEVGLQ QRPDEDNSSL IDKLMLCDSK
LWKGARNIYH QLFMSSLLMD LKSKKLFAVR FAKNYPQLQR DFMEDDHERV VSVTALSVQL
FTVPTLARML ITEENLMTTI IQTFMEHLMR QRGSHGRFQF ERYTAVQAFK FRRVQSLIGD
LKYVLVSKPI EWTDKLREKF LEGFGVFLQL LKRMQGMDPV TRQVGQHIEM EPEWEAAFTL
QMKLTHIISM IQEWCASDEK VLIEAYRKCL IVLLQCHNGL CDGEQPIILS MCGHTLESVQ
YRVSQHQVSI HLPVSRLFSG LHVLLSKTEV AYKFPELLPL SELSPPLLIE HPLHCMVLCA
QVHAGMWRRN GFSLVNQIYY YHNVKCRVEM YDKDLIMLQA GASMMDPNHF LMIMLCRFEL
YHIFNSPDYG KRFNSEHTNK DVLQQNNTLI EEMLHLIIMV VGERYTAGVG QVSAEDELKR
EIVHQLCIRP MAHSELVKAL PEDENKETGM EKVIESVASF KKPGLTGRGL YELKPECAKE
FNVFFYHYSR ADQSKAEEAQ RKLRKQNGED MALPPPVLPH FCPLFASLVN ILQSDVFLYI
LRTVLQWVVE PNGHAWTESM LQRVLHLIGM ALNEEKQQIE SASADSDVTF TFTSKFSCPG
EAPENAPSIL AMLETLQNSP HLEVYKDMIK WILKLFGTVK KMRERSNSAP ILETEGHGME
ECSRDKDKAD RKRKAEIARL RREKILAQMS EMQRHFIDEN RELFQQTIEE LEASSSTAPD
NRPIVPDAAL IALGPRQTRV FEEKQVVTCI LCQEEQEIRM NNKAMVLASF VQRSTVLSKN
RARTIQDPEN HDPLFMSPDL ACGTHIGSCG HIMHAHCWQS YFDAVQAKEQ RRQQRLRVHT
SYDVENGEFL CPLCECLSNT VIPLLPSPRN PLNSDNSKNN AGVPVLSSWL KHTLQQLKVL
KKIQERQTEN LSNTHFEGIE IPEVFQPDVK PKNPFSESIK GMLTTLATAT FKVGLKVHPN
EQDPRVPMMC RGSCAYTIQA VERFLADEEK PLFGHLPCRQ DDCLKALTRF AASQWTVSSL
PVVQNQYTRL LSVLIPDDDK THISPSILDV DMFHLLVSLV LSYPAVHCQD FTGVSLAVGH
LHLFHLVTAA HIVQILLTSS TEENTMDQES ADGDEEAAAL TLYDKLRQYS GSALNSMTSG
WHLWQYIKIG IIPYLRCSAL FFHYLNNVPA PVELQENGPH HFELLCCYLS LPTNLMSLFK
TENDTIEPLI QRWCGVVEVQ SFLKGERTAI SYPREPNKLI ELPDDYSCLI NRASCFTCPK
SGGDESRAPT LCLVCGGMLC SQSYCCQTEL EGEDVGACTA HTYTCGCGVG IFLRVRESQI
LFLAGKTKGC FYPPPYLDDY GETDQGLRRG NPLHLCKERY RKLQKLWQQH SITEEIGHAQ
EANQTLVGID WQHL
//
