ID I4YEH0_WALMC Unreviewed; 1663 AA.
AC I4YEH0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=WALSEDRAFT_60038 {ECO:0000313|EMBL:EIM22362.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM22362.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM22362.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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DR EMBL; JH668228; EIM22362.1; -; Genomic_DNA.
DR RefSeq; XP_006957616.1; XM_006957554.1.
DR STRING; 671144.I4YEH0; -.
DR GeneID; 18473701; -.
DR KEGG; wse:WALSEDRAFT_60038; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_0_0_1; -.
DR InParanoid; I4YEH0; -.
DR OMA; GEASYMC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005242; 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; cd16482; RING-H2_UBR1-like; 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; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PF18995; PRT6_C; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Transferase {ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 90..147
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
FT DOMAIN 1202..1640
FT /note="E3 ubiquitin-protein ligase UBR-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18995"
FT REGION 929..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..945
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1663 AA; 189421 MW; F89A7EE840CC22CC CRC64;
MTAGGCCDCG DPEAWRIDPG RPSHLDEPDT IQVDLPEEAL ERARQYISTI LRFIIDTIAH
SPSEFTPPNN VPKVKSLATS KPNTPTDAGP WSVVLWNDER HSFDEVIEQV SLAIDCYHSV
SRSVAERIDK HGREVLRSST DINALLKIAV IINSIDLAVT IRPSYDTNLE DICHLLLEFL
FDLCHSRPQE LRSIVAEELL KLTTSPFTEH ISKDRRQMTN LQCLLLLESR MWKKARKIFR
DMLVAMLGVN QDVRCQIGLQ FALVYKNLVE SYLLQDHEPE LSSLMFSIQV FTTPSVASLI
CFNSEFHANS LLTTILHLIY AFLTEQRTSP KQIKLIDTIG NNVIDCESTS IRHKRYLTIV
QDLKTLLTNE AVIDELPKRI DLLDDFVKFF IPFTDMNQFQ RAVHEHVEYE SDAWINAFNC
TIQLTKVTNA LGDLSYNFTP QQLFTLIKHI LDGIAETIHR PNFFTKLTSI QFGGYSYNVV
DYSVAYEPVS FHHPLHWWLG NVLKHVKILG HFYPGGVNTR ELPLVFGERA RNNLLPVIAL
FEQPMRVCAF VAQARCGLWV RNGFSVRGQV HHYREITFRD NTYDLDLFNV QVMFTIVDPE
QALVSLMTKF DMLTWFEGYI YHSVYDEKQT PAMAEEFILL LIACLTEPSN IAGWPKEKRI
ERSLIHALCF GPSTYSEFTR IVSDTLVDDP SFDRILEKVA KYKSPDGTAD YGTYELKDEY
YKFVDPFFMN FTRNMRESAA NSLNKYYKRI GKEGATHIPE KLDLPDNGPY NSLIGVYKTE
VFQQIVYASL FNAFNERDEQ GRPATSFTRD ILIEAALHLM MCALVEAKVI FAKLAGSRTY
LMHSTLVELL CKYENDQRLI NVKSRITWIL DQLADVCGDV VGANRVVNEH KKDEKAEDHA
ESQKAAAKAR QAAIMEKFAN QQKSLLDQLG DEDDDMDDED YDSKVEENID GPNADTRDFG
DCIVCQETLN GTSFGSLAFI QPSKMLRNTP SLDPNFVYDP LWMSDSLDRQ QQSNMSEEYK
QQFIQSKSNT RAGNSGITTQ GFPSDQTRLG LHMSTCGHRM HMSCFETYFA SSVSRHQSQI
ARTQPDEPKW KEFVCPLCKG LGNVVMPIFK RPESATNNVK ITEWVRSASI DLLKDPKVSL
LNDFQEQETG SGEFWPWYVR SAPSKSGSLE EDPKSALTDR LMALIKPIST NAEDLRQSSV
PAAQELSSEG MYLPGELVAY TISSIEVALR GIDSQDKLVA DQVNDSQLLM IESMLGCLEN
LATRHPTHST NGPQIIAKGI FQRILPEFGR EDNVRQPLLL RDPFSLLVET AAIAPESLSP
MITLTFYAQL VRTVIALIQA SRTDGVADSP LLRPPTEIEK LPDNAEQIFG NISSVIHYML
QSFTALYNDG ERMLKLLPNE HLSKLMYSYM LPFLRRVSIL NKVVRKAPYV FTKRSNDNDT
KMHLYDDDNQ CEFRRLMTEL DILPPNEALN QSSERQTTIQ RMVEGWCSHF GHHVQELRPR
DYALKLDYPE VYKLTNLPYQ LSALIDDVLT RVCPNCNQVP PDPALCLLCG ASLCHQSFCC
HDQLTKVGEC NTHMKKCGGI VGAFFMPKKS ATFYLYDLRG SFAQPPYLDA HGEVDIGIRR
GKPQYLHKQR LDEIYRIWVN HQIPSWIGRK LDLVSDQGGW RTM
//
