ID A0A1A6A0K7_9TREE Unreviewed; 1959 AA.
AC A0A1A6A0K7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=I303_05884 {ECO:0000313|EMBL:OBR83604.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR83604.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR83604.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR83604.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) 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; KI894033; OBR83604.1; -; Genomic_DNA.
DR RefSeq; XP_018261446.1; XM_018409174.1.
DR STRING; 1296121.A0A1A6A0K7; -.
DR GeneID; 28969583; -.
DR VEuPathDB; FungiDB:I303_05884; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000078595; Unassembled WGS sequence.
DR GO; GO:0008023; C:transcription elongation factor complex; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
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 CDD; cd19673; UBR-box_UBR3; 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; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
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; PF10390; ELL; 1.
DR Pfam; PF18995; PRT6_C; 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 Ligase {ECO:0000313|EMBL:OBR83604.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000078595};
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 174..257
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 174..257
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1959 AA; 222501 MW; 8F4C37F1C356E545 CRC64;
MPMPGERFLP SSLNPFSRST ASSSSQSTPN NSANPHTSHF TQAASSSASI GSQRFLSSSQ
HANAVPMTDP HRLLSEILAT SHTQRDGRFS NSMKAALIRN LFQCIWQKQE WIKYFLPPSE
DSELPSFNYS NDWLVSDQDT SMTKPWSLKE AQDRAEAASL AKGKGSIRKV RNGTICGKVL
NRFERTFTCK TCAINPSVVL CADCFHASDH EGHEVLFQQC YSFSASCDCG DPSAWRSSAS
ENGASPGQAV GCSHHPPLAA NEKPKQTLKY EIPDNLLLSI HRTIVIILEF MIQTLQHSLL
PSDYSRLPKT ETELRDSDTP TGESKERRSR GPWSVVMWQD EKHVLNEMTR QLRDALGIKW
EVAEQWIREV DEVGRKVVLV APNPVVAFHA ANMMQQIDAP VSLRLALDTY REELVGILIT
WLNDMVHCTV DGDDTVVKRM LAKALYEPRL RNSGVGAGTP LSTDLKDLEW GKIMGGHDAR
RIDWLLQLDS RLWKKAKWEM RQIYCSVLLF DQDVRKDLAS RFAINYPRLV EHYLFQEREL
DSNIIYSSAY LVFTNGAVCV HATTKGQLYN NVINVAHAWY TGQVIKTDGC DRLVIPPNQF
DQNDHSAKGR MDVDVPAFRS KKGLALLGHL RSMMRHPEMR KLIVRQPQLF NRALSFINMF
VGLQPQRRET AEHVEYEVDW YRSFIILPDM AKLCREVGEI FQSGVPDNVL GSMVVVVNRI
LTDMMLMSNT LDKEKYKRPI EHDVQDVLYT GSRFSLIKQS ISKITAFSFH HYLNFLLAEM
VKSSKDMFDP TNGTLKGLRF KEVIEQFVLR ANNPSDSERM KLLIIEWSLQ THVVLSQIRT
DMWKKNGAAM RMQHHHYREM TLREATIDQD FFLLQLGLTI IDPVKFMVTV IERYGLAQWF
RGNPKNPDIW LHHSTEPKQR INLLEDFLLL VIHLVSYPAI IDGWSRDKIT RKNIIHQLAV
QPLTYYEIFK KLPERSQEKS IIPILKSVAD FREPTESAPG QYSLKDELYD EVDPYWHYYT
KNDQRSAMDR ITARAKKQNP SLADDPLILP QPLALPPAGR PFSTVGDFLH TTVVSDIVYW
ALSHCLHIGN SDQWAVIVHA ATPAEVKSAP VIPTWDFVLD YTLHLIMIAL SVAPKSFAEN
CLQIKGTEGD HSTFQNLWLM QTHSAYKPYK TRIDYILDTI VKNLPRDYTA DYRAHQEAEN
LLQLNSPTKK PDPKAAAAAR QKQIMAAFAK QQQDFAAMMD DDLEEEDDSM LIEDDSANEE
TTYGQCIVCQ EDITPKHPGG MMALLQPSRT LREAVHDRDW LEESLLAPTS LDKATRYHRF
SHQPIDGSHP PVYEPTSTQG YPSTNLKFGV NISACSHYMH ESCMANYFDA TKTRHTQQVQ
RHHPENAVRL EYMCPLCKSL GNVLIPVESS ATIKKSPIVI KKDGETPPSL SRMIRRVSSE
GLLRVADSQR IWDHHFETGE VIPWFSDCVF SVHSLDHDHR RGHMRSTSRM ADRMRGLIRP
LSEQSQRIRG KKTHMYLPDD LVGYTVSMAE ITQRGLSGPS SINGNPILSV AEQIPELQLK
LIKKLIGLLQ LELDLYFGPN FDRTALRVGI FARFLPDWYR SSTLPSPLLL RRPLGMVIEC
AAIAPDLLQP VIVMAYYAEL TRTILGLSLF IKRAYATSSK APSPRSTPPK DETYADGLDL
FQGFKAIMSS VLKNAGPFTD ADGVLNLISD EDLSKLVYSH TLPFLRRAAI IYHAVSGSYP
LSNPETLALI ENTPQMSEYR KLLVLLGIPP PRETLKDPTA TETPIVGRWL SQWTHQGRIL
PTLEYPGTYE LIRLPTKWED LILEYQNVKC TKCRTKPTYP ALCLFCGEMV CLGGDCCSVG
EEGECNLHMR ECGAVVGMFV DIRRWVILYL YAGSGSFGHM PYLDEHGELD ISMRRGHRQY
VHLGRLDELR KATWLMHNIP HLTARRLELT TDGGGWGCL
//
