ID A0A1I8CAK1_9BILA Unreviewed; 1983 AA.
AC A0A1I8CAK1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000221800.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000221800.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000221800.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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|ARBA:ARBA00004906, 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 WBParaSite; RSKR_0000221800.1; RSKR_0000221800.1; RSKR_0000221800.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095286; Unplaced.
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 Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
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; PF02617; ClpS; 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 PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
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 1..70
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 1..70
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1338..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1983 AA; 224562 MW; B487CD0895AACC92 CRC64;
MHDLELSQDK GRIRKDCETD RTCVMCKLCF ENSVHKNHNH KVTVSQGGGY CDCGDPEAWK
NDYACDIHET CGTDSSESIG ETILPPPIET RIREVTSSIL QYSISVLAWC ANDKLPCFLF
PPAGSKNNSN FQAVLLNDET HTYESVIRAL MGSIGCTEPK AAKIATIVDK EGRASVKFGN
KSECEKVKAS IQRKTSKETN SRTQRTGPLA VEIMNCNLVA HQDFACFLLK WITNQMEIFP
PLALIVAGIV ESRKFNAIGA LFQPTFPSTP KSATYVDDDG IEHVGFDAFA DSGKNFSDSS
DVGLDQLRVD SGSNLSDVPV AGINLFITKT RMREQRAAEE AAKRKKTRIS LEEDTLLIAM
MKHNRDWWKT ARKLTQNLII AASFRSAEYK VSFAKIYMQH YEELVNAYVN DDHDHVMSIT
SLSVQLFTVA SVAKALAQED DVLATIFGTL VRYMAKYVKK ARHNSVIDVY DFQEHPMGSY
PTVMKRLFQV IMIDLQYLLQ VVPTQEEWTK EMRTSFLSGM DLFIKYIQYC QDMDQVKKQI
GEHQVYEMEW ETAFNMQLQV QSILPNLMAW LKSDEEVHRE FFRKMCNALK TQIYKHPEFK
AEKECVTING TSASCIKFDI SADPLSIHQG LWRTFASLFA THLDTFLEEV KASSDEKRLA
WDTTKYYEPH PNVQTDCTYP LYVYIEAPAL IEFSLRCQVL IAHVNAGLWR KNGFGVVNQC
HNYSAANCRY EMFDKDILML QVGAATSNPD QFLVRVLHKY GLHNWAEADF TWEIYKKKLA
EAAIKEKAAA ICGESAPRFT VGPVLDELMD DESPTPHQTP LHLEETSKPL TSIAESMFDL
VIHLVCERYV EGVGKVTLED ILERELIHKL ALGPKPFSKL EIMLSYMSVE YEEQTFLKCL
DNVSVFTQPK ASQPGQFTLK AERKAEWGPF FSHYVKSESA KALEQQKEKN DTYFCKPPKM
PEFCNFYKTV PNLLKCPTFV KLQKIILERV MKKSRYASAG LLHRALYTIA LGLNEQLNEK
NPKQFDYVEQ AEKENIYETL RIFSNTSESA YHKQLLEYVM DLYKTVHNKY QGVKMAEEIK
KDPAIEEMST AEKAAIRAEK IRKVRLMAEE KMKKKAVNFE ASITSTTDSP TTSKGDETTR
KKLISVVDDD EDVGTLKNDQ SFPVCIGHKK SELLPMAPAV ARCILCQSEE ELKFGKNGFI
SCSLSFKSML FNQKKGPNNL NNEFDVMVDA SLPEALTIRT CGHTMHYECY KNFHDSAATK
ERQRRINGFN SKIIDMDGGE YLCPLCKRIA NGALPILPGM EFSGMTKLSS ANKENQEESF
SSWLVKYRTG IERPIVPYNV DEDGKPKKGH SRKRSHSERS LLDLAKHDDT EGILNSTGTT
TKCVSEISLA VNNLSGERND FLPSANSQDT SLFSVVSSKM TNPFSRIFQN EKKAMVIPEV
LKDDKMIADF TKRLNEARVK KENIPKFLQA CNIWQTTVFV LRSVAGVLEV ENKPLFGALN
IRQKETIKCM SRLSVASTCF LSTVELRSLA SLLLQPLLYP LQSETKSKTS FANMIPILNN
ITRGSSVSSD DDRIREVRSP EHTSRLKQGI QSPILFFGQF NPDSLQSRVS NKTKRQDHIL
NIDCLTLTFQ LLMVIGHSSV NGEVTFSDKK REDANYIYID GSQEELHVIQ LGLYAHLFQI
ISTFAEAASE ETDTDFEMIE EPDASLIIQL AETIHFEDPN TIQMLRKNSR HLKARVIDGV
LGFLRPLALL YKFVSTVPPP ESLKDPSFEQ LSPLLRYMGL PNTLEGLLNC GGVDSLFTMW
GKQLPKGVNI STHYIAQPVK INQLIDLPNE FTELVEKAAN FACPSSSRIE NNISNIPALC
LLCGTIVCAH GVCCQVKMKN GDDLGAANLH MQHCSGQNGA FLRMRDCIIN LITPKNRGAF
FDGPYVDKYG EQDGGHRRGN RMFFNSELYA KFKKAWLHQE IIETIIHENE VNQRNTVYDW
RVF
//
