ID A0A2V0P8N4_9CHLO Unreviewed; 2540 AA.
AC A0A2V0P8N4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=Rsub_08769 {ECO:0000313|EMBL:GBF96224.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF96224.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF96224.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF96224.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(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|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:GBF96224.1}.
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DR EMBL; BDRX01000076; GBF96224.1; -; Genomic_DNA.
DR STRING; 307507.A0A2V0P8N4; -.
DR InParanoid; A0A2V0P8N4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000247498; 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; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 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:UP000247498};
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 47..118
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 47..118
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1112..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2540 AA; 254293 MW; DB421A7DFF68B1B5 CRC64;
MQPAPDARWM ADLQACLQDS EALLCRMGGH ATYAALLASL QPREGGAQCS NVWTAGTIAY
RCRTCQTNPT SAVCVSCFRA GGHEAHDWVQ YRSGSGGCCD CGDLSSWAAE GCCPQHRPRE
LSDAPVHLGT ALAEAFSTAL CLAWTRLIVG IEASSRDPPL ALRTGDLPAA LKLCAWLQPL
LRIAPVRAAA CALVAAALPG AGEAGASELE AFAHPSAWPA LRALCSKLAP AAAAPQYGPP
PGKKDCLLRR LLFSLSSMPS DLSTEAVTLL LLLLYDTGCK FTAASHLLDF YCLMLSQIAA
SRSGARSLMR ALDRLMVQLV NSDPVVDALM GQQRLLEVLL DGVRLVTAGA IARLAGPPGP
AAAFNTAWAG PLAAHRRAIG DLNTATHHAQ LARAVLERPE LFEGRLLASL CAVQGAVPHR
RVPVGDMLQA TQGPLAAFQI EIYLLIGLTD VISTAAPRDG AAPGALRSAA ATFLRAASAA
AAAAVAWPAP AQEIAPGAAG SSARCHHSPR AAPLWARLLS SELPASLHLP LHRAAAHALV
ATLRLEQPGA AAGADGGGGA DAGAAAAALR SELGARSAAA LADWDWAALC GPLLAARALA
AQVDGQLWVR NGDDVVTDVH YYTSAKDLLA DPDWLLLQAW LAASAAKGQD ATSAALRAWL
DAFGCSPVID AIALVTGHAP PAAPGAPAPP HPPTAAARLL SALGAPSSRL GLEAALHALV
AALRDRTVGG QPPAARARAA LLHWLALGDA GYQYLTERLP TDLSSHHAEA VEGALSELAA
HSEARLGQGG RYRLRPEAWR LFSPFFLHYT RTSRGQASAR AASQAGYSPA WQLDPPPRGL
LPAALAPLEG FAAAPEAFAL ARYLLACALE GEPWGLPANA NAAAAAPEAA PVDAAASEAR
RAPWGLGGGA AGGQQAALAA LAANVRQAAG ARGGFWDGEP LVREEALLCT LHLLCLGLHP
LLAELRALAP GAAPGAAAAD ALGHLAGPPA AARSGEAIVP REGGGAPPGL PGAAASLAAL
LGEAPAGAWG GAAAPAPPAG LMSQEASACC RAALALAREA LTLGRGADGA ALAAGGEGAA
AGSGGAAAAA DRRSAARAAQ AALQQRLQAQ QAAFLSRRGP GVPAGSGRGG ASEGDGDSDD
EGSGGRAAAA AAAAAAAAAR AAADMDVDAP ASDGAEAERA PPLSLVRSRL VQLSGECVLC
HEGAGAGGGG GGGAGGGGGG GPLGLLCHAK MCGRLGTALG PRRAWDAPVP VGDLDQQEQL
ERQQQEQRRR EQLPGGAGSG AMLSAADWQP GLHLHTCGHT MHYTCFNSYW EGIQSAWEMG
EGFPGEGVIK VERREMPCPL CKRITNALLP WVARADDGIE ARLPSEAAEA ARAGGGAAAG
GVPLRRGEQQ QQQQQQGQQQ QQRQWWQQLE GEEGEQGEEA MQREEEEEEA DEWDGDESFE
EASGGAGDDA PPGPGAPFAG AADGADAEWF DARASGSMEG DEDGGDAGGS RGGASSGGSG
SGIGSGIEDE LGEDDEDDEP SDLFGGGHPR TSEAAAARDA RPRVGAHWPV LRRLMRQAGD
ELEWFCLEAA RLVDAVRPAW MGGPPAAGPG GGAAATAWAA AVQAAAGAAP AAGGAALPGV
PIRLPRQMLR AILDQVQQQL GPEARPINIR SVAARIVDGR VMLILPGTPV RAVFLGAAPP
GGGAPFGVQF PPVALGGEEA QEEQQQAEAA AQQQQEQQQQ QQQQQQQAGA QAAEHAQLQQ
QQQQQQQQQQ QQEEEEAAAP PPAAIAQGGA PLAGAQLIDD EIEEDEETEA SEYLDEDDAV
GAAAFAAAAA AAAGGGPPGA AAPAARGGGG GGGPGGGGGA AAEGAAGRLE SCTQMLQRLE
HASLEQLLWS CLAHGVAHAE AMARPMPAAA AAAAVAAAAA AAASPSPDRG AASPVPPPPG
GGGGGTSSAA AAVVQQTRAL ASIAALCTTL AGSAAADGGA QPWLWPSTWP PNAASDGGAP
GSLAQRQRAA ARVLAWLDSG SGGVPGGGGG GGDDWRALLP ALGGDDGAPA GGEGMPLLCL
ADALPGRVLE PLLAAARRSP DGGAAAVAAS AELHSWARLA GVAEDGGGGG AGGDMWLLLL
ELLASTLAAS ALPLPASAAG PPPDGAAPGV VARTRAPQDA LLLLLRVVLP LAAAQAMLWC
ALRARAAGAL PAALRGAWEA VEAAARGGHG GGAALRPAAA ELLREMARTL LQTHAAGGSG
GDAAAAAAAV LAEGVCAQLL PLLMRAHLLH SLLAQQQPDE HAVSLYSRVR APGAPPASQA
QTPAGVLPSE AAGALLDALR QGPLAALLSH AAARGDGGGA AAGPLARPDW LAAAVAGLAQ
QRGAAAAAAG AGPSRGWGAP APPGALPLAV RPALIPLPAL FQDPFLHYSG AQCPACGTSP
REPGLCLATG RWLCSLHGCP SGGPGIDLHA TLAAGGAAPV LLLRTSRVAV WRAARLTVAG
SPYLDAHGEE DAGLKRGRPL RLAAGVYGAL SDLWGGAAFD YDSYMVSRAR AVDDDGGIGG
GGGGGGGGGG GAQWWAGLPA
//
