UBR1_KLULA
ID UBR1_KLULA Reviewed; 1945 AA.
AC O60014; Q6CJX1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase UBR1;
DE EC=2.3.2.27;
DE AltName: Full=N-end-recognizing protein;
DE AltName: Full=N-recognin-1;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR1;
GN Name=UBR1; OrderedLocusNames=KLLA0F15334g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Waller P.R.H., Varshavsky A.;
RT "Kluyveromyces lactis UBR1, the recognition component of the N-end rule
RT pathway.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; AF061554; AAC15841.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98476.1; -; Genomic_DNA.
DR PIR; T30554; T30554.
DR RefSeq; XP_455768.1; XM_455768.1.
DR AlphaFoldDB; O60014; -.
DR SMR; O60014; -.
DR STRING; 28985.XP_455768.1; -.
DR PRIDE; O60014; -.
DR EnsemblFungi; CAG98476; CAG98476; KLLA0_F15334g.
DR GeneID; 2895834; -.
DR KEGG; kla:KLLA0_F15334g; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_238060_0_0_1; -.
DR InParanoid; O60014; -.
DR OMA; WANTISM; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:EnsemblFungi.
DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IEA:EnsemblFungi.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
DR GO; GO:0090089; P:regulation of dipeptide transport; IEA:EnsemblFungi.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:EnsemblFungi.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 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; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1945
FT /note="E3 ubiquitin-protein ligase UBR1"
FT /id="PRO_0000056133"
FT ZN_FING 109..182
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1193..1300
FT /note="RING-type; atypical"
FT REGION 1901..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1933
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 238..244
FT /note="IQNGKYN -> NPEREIY (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..271
FT /note="QQQTPS -> SNKRHL (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="N -> Y (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="GF -> RI (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="H -> Q (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="V -> G (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="V -> L (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 645..646
FT /note="RK -> KKR (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="R -> Q (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="S -> C (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 938..956
FT /note="LEDNGVFKLKKELYKRIDS -> SKIWCFQTKEGTLQENRF (in Ref.
FT 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1389
FT /note="M -> L (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1435..1452
FT /note="NVLKFYEDIRSSNLPSYP -> MYSNSMKIFVAAIYQVIR (in Ref. 1;
FT AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1578
FT /note="T -> A (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1621
FT /note="E -> D (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1934
FT /note="Missing (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1938..1945
FT /note="FNELNNVE -> LISTS (in Ref. 1; AAC15841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1945 AA; 224077 MW; 61BA660BBC32AB48 CRC64;
MINDTDPESF LRQHVGRTLG CIHSRPEFKD IKGSAERAVM DKELKSFIYG YYYYMISDSG
RLLPHMFTAT NEREFPKNVD QAMEIKLSSK PWYKIDENGG HSKFNHAGRI CGAKFRVGEP
IYRCKECSFD DTCVLCVNCF NPKDHVGHHV YTSICTEFNN GICDCGDKEA WNHELNCKGA
EDNGRLEDEF DDHDGKISKM LESVLIELFD HFIDVFNQNI EPLTTIQKPL IAKLRYFIQN
GKYNEQADML RRLAYRNQYM DEEESQQQTP STSLDPLSTL KDYAILVYND EFHNYSQASA
AIRQGGPDNK HIDLLTAKID SEGRSLLRCS ADIASLMGGF FSVQSNGLSC TITQWYEYLH
QEACKYSIMW INDCLNIPNS TFQSLFRNAI GKVLCSKYEP FYQSIDMTSV VRDYFSDSYL
SDDPYLYADH SVLGEGVKIP LGRHKSLDPG DISAISPILN KVIAEDHHEY TNSRLQYVLF
LENRYWKKLR KIVQDLIIPT LASSAVHKPM FTDQLVEIFP HMTRSVTFMD REPQLTSLRE
SVVQLFTCPT TAYSIFHSGH FNYVIWSVID VFVDFSTMDE GTLVWQRVQR SNPSKSYSIS
FKQGLYAVET LLSKITDPNL LLKPGEFIMI VTLCKLFNGA WKIKRKEGEH VLREDQHFIP
YLEYTTSVYS IIQTFDKVLQ QSKDHIDQRL LIGAINLLDS FLGHRNLSYK LYKDFEIIKF
QISKERVSFM NPVHTLFSFL VQHVPLQVSI QVLSQSKDYL VISDFALRSV VLCSQIDIGF
WVRNGMSVLH QSAYYKNNPE MSSYSRDIQL NQLAFLIEKN DFQRVIYNML DRWELLDWFD
GSVPSTETVY DDKISSIIQQ FVAFLYQILV ERDFYKKFDT LEETQLYNIK NAIIYKLYAE
PLSYTDLLND IPDYLTESVS QFDTVLEEVS TYIEPKGLED NGVFKLKKEL YKRIDSLRLL
NMGNDFEHSA TIVKSHLADS KEKRAKIIVK PQLLELDELD PCARELGSFT RTNLFAKLIF
KLLKLAVSDS SFSFTYELLH LIHAIFRDDE MVNGKDSLPE AYISKPICDL LLSIVDSESG
SFSENVVATA DYLLDNMIMK RPTAVLESLT ECFGTKYIAD YKIRKANQGV NFEETEQERK
RRLAKNRQQQ IMNRFSRQQK KFMDKHEEYS AGNDEDVDMD GEDLAGELNE FHCSLCHDDV
SDDFFVIPIY QNYSPVFLSS NPTPMEIYKP WHGFDNNEHL ATYNTDLFYK KKENGASQLM
HESTQKVLVS CNHAVHYRCF KHYIDKKRYS TDLFICPLCQ TYCNSVIPVD TVKLQSGDRL
LQQKLTGGLD ESLLLTFSEY SSECNDEVGK IILSLKDSNN GLRLNRNDPT WIQDRFLTLS
LQFSNNICML EMLSRLNKDP FGTLLSGEEQ KFKTLQNILK SLAVYTRLTK HTEENVLKFY
EDIRSSNLPS YPFFRVVETV LRSRLSFKDC LQEVLVERLK GLTKDFGSFY RKYESELRAQ
TCLDSSEFSI VLKTTILGAG FGDQVEKHTL DLFYTFLISE LLPTLRRSII LLKALKQFMT
GGDDLDFNEK DVLSGSLTSE SKEKHFHLLI RFLLQTDFYD LLMNSHSPLS PESSLVNAPH
EYCSIIKLTD LATHLNTYVT NNKNITLREE NDQKIRNTVN RLDYKICLIC GVKIHARTDG
LEMQKHMERC SHGSSGLFLI PNISQVCLYL SRPDCTVNIS APYLNSHGES GRNAIERGDL
TVLNHARYEH LTRLWISNGI PGYISRVMGD EFRVAMANNR TFTRNMFWRP GAAFNAGGES
SDEDLMNDDE FGNDDRPDLR FRQPDVELRI NGGPFGGDIP IRLPTERGDI HDFFEFVQNM
RGGMQGDGAD IPTTEDIIEQ LQGNAMNGFF GRADRNREHF ELNDQSDGNE DGEDEEHENN
ASEDQDTEYS SAEEGFDFNE LNNVE
