ID A0A1E3QSI6_9ASCO Unreviewed; 1757 AA.
AC A0A1E3QSI6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BABINDRAFT_160907 {ECO:0000313|EMBL:ODQ80665.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ80665.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; KV454429; ODQ80665.1; -; Genomic_DNA.
DR RefSeq; XP_018985993.1; XM_019128530.1.
DR STRING; 984486.A0A1E3QSI6; -.
DR GeneID; 30146383; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000094336; 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; cd19672; UBR-box_UBR1_like; 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:SF26; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 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 SUPFAM; SSF57850; RING/U-box; 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:UP000094336};
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 96..169
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 96..169
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODQ80665.1"
SQ SEQUENCE 1757 AA; 197390 MW; 7C5DD0D05CC36D4D CRC64;
MPEDLALQLR HFLAALPSSL HFKADHNVRL NVFRALYFAL GTETLHRLFP ANAALFPDSW
DTVFTTTDLT KVGRSNLRRS RFFESTLKAN YAHPNRPCGR KFMKGEPVYR CLDCLFDETC
VLCFHCFNKA DHEEHQISVE IAKGLKNGIC DCGDPEAFVT ELLCLCTSDM ELEKFPPNVE
GALKIVIDVA LEFIIDVTDS AINTIPEVHS YMLPLSASSS MKISEKSALL KAKYGDDFNS
QEYLLVLWND EYHNWDDAKG RIIAATGCTL EKAEEMSASI DSIGRQILKR SADPVALLGA
QTLVESTGLV STIMSSRDYV RGEIVSLVVD WLLAMLTVHD VSFQTAVRRA LCQSLIGSFA
FESSPANAVV DDIITPMLGV TIGNKIPALG SILAQSRVQF LMYYDIRHWK SLRDRIHDVI
TPVLASDLTY KPLFCTQYIE IYHQLTHLMG TADREWELNL SCDASTQLFT CPTNASAIVG
TGKFPVVVGA LYALFQLGSI QNADGSFTFT NDKDTSAYKS LEETLTRGMN DVIHIVDTCT
NKKALLEEAN LSPLLLFVGL FQGSWKIVKK YGDHVPLEDS AFIKHFEYCA YMYTIIKHIA
EGVTGDLAVD RAIQTIALYL SPGPLHEVNG QSICHFDIST EPVSFMNPLN SLLSFFLEKG
TLPDVDLLPI SDVSLRSIVL CSQVKIGAWI RNGRYVSRQA ALYSGTFMNE CGYARDVYLN
QLAALHVPHK RFLYNMLDRW QLLEWFTGCQ SYKQTVYEDR IPYILEEFLK YVYTLVSSRL
EFLHADAATK TRAKIKRVVA YCLAQGPRTF SDLCDDVPST AAEDSSFEDI LEEIASYSAP
SGFSDTGMYR LKNEMYRTLD PMSYAVDTND YPEVLVALTA QMAIQTKTKE DEVVLVPVLE
PLPAEFAGLG DFTRSPDFAK LVYKLLQVAI DTQEEAFVPE LLHLVHAILI DNEAAGLPVD
YLDKPICNLL LSVVGSSMAR SIVLKANFLL DYFLERNKDI LESLTSSFGE DYMLDYKKTK
TGLFESTEEK RRRLAKERQE RIMEKFAKRQ EQFLANNQDM VDEDPMEDEE EPFSEEDLRT
CILCQNPETN DEIFGLPAWV AESAIFWQLP ANSVEYTERA YGAEHTAQTD KVGRGFPIES
KDTATKAIFG PNFKLKYTAT TCGHGMHYKC FKEGVKTSWS FTLGFGCPLC RSINNAFIPS
FIGNTESVRL NQSKPPTSSK YNQILQECDG GNCTELGPVL FNAEMTEMLV SLSLNKSKLL
RELTSVLKEN LVLCDMLAIK TNFFATSQGL SLLLGNTIAM HEITSRIDHA EPLAGLRAMK
LKDKSLVKSL MQTRVILSIL EKDLVAGFKK ESEYATFWEN NNLTDGIFSE FCMLYFQTNE
SFSTLSRMVL TKAFTTTLYS VLLRSLREEA QLIALYSAPM TEVQPDFNSL VAVVIEGIKK
MYPDLDSTAF EDEKLLSHTF AAVERCLRPL YCNLIFFREV LEATPEAETC PTEGLFRLLQ
AQTGLPDLCV LVGCIMNGGT FESSIFDNVL NGKIAKFWEV GILNVEYPGV IELMGLPEKL
STFMDISNID SEKNSKDRVV KRLDYSICLI CGTKVFAPES RKAFMTQSHL VNHLSSHCTN
RTAVYFNPAP ADNHIDVLVR SNNGVFPISI GSPYLNKHGE NSRRGLRKGQ TAWLNEKRYQ
ELTKMWLSGE LYAYLSRLLF NNMRARNVVN LDGVDVNLAD DESESEDELD AFSEGDDQVY
MLNDEDIEED LDAADID
//
