ID A0A7J7JFT2_BUGNE Unreviewed; 1298 AA.
AC A0A7J7JFT2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=EB796_017470 {ECO:0000313|EMBL:KAF6024218.1};
OS Bugula neritina (Brown bryozoan) (Sertularia neritina).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Bryozoa; Gymnolaemata;
OC Cheilostomatida; Flustrina; Buguloidea; Bugulidae; Bugula.
OX NCBI_TaxID=10212 {ECO:0000313|EMBL:KAF6024218.1, ECO:0000313|Proteomes:UP000593567};
RN [1] {ECO:0000313|EMBL:KAF6024218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kwan_BN1 {ECO:0000313|EMBL:KAF6024218.1};
RA Rayko M.;
RT "Draft genome of Bugula neritina, a colonial animal packing powerful
RT symbionts and potential medicines.";
RL Submitted (JUN-2020) 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 E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, 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:KAF6024218.1}.
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DR EMBL; VXIV02002605; KAF6024218.1; -; Genomic_DNA.
DR OrthoDB; 26387at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000593567; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
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; cd19672; UBR-box_UBR1_like; 1.
DR FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 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; IPR039164; UBR1-like.
DR InterPro; IPR055194; UBR1-like_WH.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF22960; WHD_UBR1; 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:UP000593567};
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|RuleBase:RU366018}.
FT DOMAIN 96..167
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 96..167
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1298 AA; 146636 MW; 4EF344ACCDFF1A55 CRC64;
MDMGNNSMSI KPSVPNDGII SHVYGALLSK DFSNLEQVLH HNWAVLVPQA FNKEIVAEER
QALQSQLIYN IELFLSQSST PKEVFAKLKA GNAPDLFCGR AFRNGEPTYS CRDCAYDPTC
VLCMQCFEKS AHKSHKYRIN TSSGGGYCDC GDVDAWKAFP ACSEHGKAAA TDNQNPESRL
PEGMVQRAEV LFQCILRYSY QVLSSALDAD LPDSLVEKNV LATDSYCTML LNDEIHTYEQ
VISRLIKAVG VTNKEAVDFA TTVDREGRAP VFTGPKATCQ KLSQEIQKKF NLNDSKILEA
AVMHHSFVSH QDFAQLLLKW LEEIIDYSDG LRKIFCRVAM VPDEDVSDIS LLEKILLADT
SFWKAVRLQF HQLFMTGVFK DVESKTQFAI LLTKHYIDLY RDFVRDDHYR TVSATAVTVQ
AKVLIEKHRL IEVILKTLLK ESERWKNDKG ILDFQSRRDS EAYAIFKRAQ FVIHDLKYAL
GCTLNNPQWT PDLQSSFING FTTFLELLTQ IQGMDAAKRF TTHHIEYEME WETAFTLQLK
LTDIITLFIQ HCRTSPEVLV SAYTAILRYM PKYTIYTNEI TIAGHSANCC VFDVGGPEKC
VSIHLPLHRL LAGLNHHLPP DVNYTSPQFA PMNCQLQLFN LLEEPLRIQV MLAQIYSEMW
KRNGYSIQSQ MYYYMYVKCR PEMYDRDIQL IQSVAAVMEP DSFLIHVIHK YTLTSIFQNS
DSQFTTLSVK QTTEIVREML QLLIIILGER YVEGVGKVTP QQIVQREIIH LLAISRSSHS
DLDKNMPEDV NSETQLENYV REVADFTRDS TGKGMYTLMD ECRALFNPCF YHYSKADQSK
AEDSQKMFRK NSGLDGALPI PFTPQWTERY SSVSRLFTCD VMLHVIHTLL SNMVAKRSRI
RSESHLEKVL HLITLALHED KHEFAAGNKS LPFTNAAQRY KGSSLYSSER LGSRELSILD
LLNECQNSEH VTHAPLKDLL GYVLKYFSEV ASMGHECGGS IVTKKRSTEN LDSAAQAAID
KQKALRAKKA AKSRSKIIEK MMKAQQKFMD GAADLFQTCN VESEGAKETT PMDCSDSLAE
ESKTPVALGP NKSAARPHLE NYVCILCQDA STIDDDTTVV YSAFVQRSTV LSRNSSHRNT
QEDTPTDVSV LLVPSELSHG VFTTTCGHAM HASCFKIYHD SVVARERRRA QRALFQYLNP
AFDFDKGEFF CPLCESIANC VLPVLPCAGR KDSSQSPPVC AVNLSNWLKI LTQLAQPDSA
MSSLEDNCPI PDLAKVAADT VYTNLMELYD FLSSSANQ
//
