ID A0A3S3Q7J7_9ACAR Unreviewed; 2006 AA.
AC A0A3S3Q7J7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=B4U79_01515 {ECO:0000313|EMBL:RWS04809.1}, B4U79_05920
GN {ECO:0000313|EMBL:RWS05949.1}, B4U79_11720
GN {ECO:0000313|EMBL:RWS04950.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS04809.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS04809.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS04809.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS04809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS04809.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS04809.1}.
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DR EMBL; NCKU01005259; RWS04809.1; -; Genomic_DNA.
DR EMBL; NCKU01005154; RWS04950.1; -; Genomic_DNA.
DR EMBL; NCKU01004430; RWS05949.1; -; Genomic_DNA.
DR STRING; 1965070.A0A3S3Q7J7; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000285301; 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; cd16483; RING-H2_UBR3; 1.
DR CDD; cd19673; UBR-box_UBR3; 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:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 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 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:UP000285301};
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 86..157
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 86..157
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 975..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1022
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2006 AA; 227214 MW; 178DFE3A1891A85A CRC64;
MSSSIVDFEG LLKKGKKVAS CLIHSQCVKL NNGEECALFN QFCDYLLDPK KNISEPEIVD
WLRWIISAGM TPDEFANEVK KYDTATTCGL VWTANFVAYR CRTCGISPCM SLCAECFQNG
NHEGHDFNMF RSQAGGACDC GDSSVMKESG FCVRHGPKPN KEKPKPPKEL LSVAKLLMPK
MFFRLLVQLR RDNPECLKEV DGFITNVLNH LTEMGAAMRH LICEVLIDPK IYASLANACD
SKELDVKDLL VERHQSYLLA KRKMHNFKPP SSLLQSCSVC HKDKCGIKAF DKDFIHSSFV
EELLFWTIVY EFPQKLVCFL LNMLPDAFYK EAFAEAFVYH YSRISMMLAR FRNGEDSNNH
SSKPSPHDLL SNCVVHVSVQ LFSNETLVAK LCEQQHLLHI IIASLRATIE GTEDSIDDNL
GILTKSGMQD ASKNKHMVVK CDHYIMKKHS YWPLVSDLNN ILTHAPVANL FMSKCELLDL
WLKFITAFQA MNLNEREMNQ HVEYENDSYY AAFSAELEIC ATPMWTLISH LKDSSSAHLT
KQVVLHTQRC LDDWFSLIGF TSDDIPHPYQ STFHIPLHRY YAIFMHHGVQ HQGLRLQNML
PSDEAKLKLY LAHPLQVQIS FYEILCGLWV RNGLQMKGQA MTYIQCHFCN SLVDPDLFLI
QQCASKLNPD WFIRTTLERF LVDLKKKKHF VHFFLARFHV WDWFSFSHNT ETGFRCEFLE
ADQVMPMLEA ALTFLATIFS LRTNLGMTEE EIVRQEMVTL LAMSDRTHSQ LTDLLPEKCG
TSQNKEFESI LKDIADYRGP SLESGGNLSQ GMFSPKPKVW EEEYDPLHVL LRAVHRRDYQ
SSVDRYSQFV KQNNKLKDRS SQPWPPFRIP KDPDTSKFFD PRMLLYSKVL HGALFTILYK
ALNVCEVSDQ VLSLTIFLLE MALTYPSPKE TSLAPKMSGL TRTQSVVKDQ KYNEWFFSDW
ILDNINTLIE NVTVDKDRSS SRKQESTIEE MEIDRNSNDD DDDDDNYPEY MSAEEDIDSS
QESPEGDREI EGAPPTPQLP SSNVRLALTG PPTTATAMVP AHNSMTLSSP VANSSVNLSP
TRFNQSRPAL PGPSTSPQQT NSTAMVPFLP SALFRRNQAN RRRILLRRRQ ICDQSPKQVE
MSMSDMGHNR QMLDKMLVTE LIRALPASGN TLVTVPVNES LLSLLLKLHS KLSATQDSYR
PDNEVSDSCI GDGSFFVKKV IDLYCKLNVS SGVKDVEDWR ARLWPPKTKA SSPSESSVQV
GSVGSVGSAG SDTESSKSGD DRDERRRKAK ERQQKLMAEF ASKQKAFMKA MNESLALEKD
EKPAENDGSV GSTSSISGSF LKAKTYECVI CGQTTPSTVD RLVGTVVLLQ STSVLGHAQP
DYSLPFANPL TNERESGRNL PCSEDETAKC QERTTLASYM EKRIEQLSQH FDPSWLNAVN
IGWVGGVHVQ SCGHYIHLDC HKSYLQSLRD ASQQSHNRHG AEQGEFSCPL CRQMANTVLP
VNPEMGHHGA VVRCRPNDLE AVAVELMNLL ATPITPDPVL LKLLFNFNQD LTKATGHQYK
NFHTRPTNQS LFLFMCSIAR TNLEAELLVK LSKATPTGAK KSCFVSLFHC LALDVKGVIS
PSYAPLWSQL TGLSPPEEFS LTLAQVEVPL ILRDTCALLI QIFFALPLNV DKAYYTCVVQ
MLFNLNTIQA FAQLTCLVTE EERIKLKSNY LGKNESKLQS VNDYMGYIVS QLESSGLYSG
IDEDDQKMPN RVWTCKELIE GVKNICIPFL RIAALLQTHL YKDHFPNTIA DDTENEYSIL
CNYLCIQGSK KSNLGSDLIF PCWIKNELSP IKTWCSEFSS FVTKATISAR KLLRDKPLRW
RRPALLRLPK TYDQLFLYYN CRSCKNCNKV PKEPCICLVC GTLVCMRESC CRTHNSLEAC
VHAEACGAGT AIYLAVNSST IIVIRGKRAC VWGSVYLDAY GEEDRDLKRG KPLYLCSKRY
SVLEQQWLTH SFDHTNKRWV WHKDTL
//
