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Database: UniProt
Entry: A0A0V1MJS3_9BILA
LinkDB: A0A0V1MJS3_9BILA
Original site: A0A0V1MJS3_9BILA 
ID   A0A0V1MJS3_9BILA        Unreviewed;      2002 AA.
AC   A0A0V1MJS3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   Name=Ubr3 {ECO:0000313|EMBL:KRZ71875.1};
GN   ORFNames=T10_12513 {ECO:0000313|EMBL:KRZ71875.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ71875.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ71875.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ71875.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRZ71875.1}.
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DR   EMBL; JYDO01000088; KRZ71875.1; -; Genomic_DNA.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054843; 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; 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:UP000054843};
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          106..177
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         106..177
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          975..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1134
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1179..1198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2002 AA;  230600 MW;  D554CC3BA0927393 CRC64;
     MDTSSNVDAM WLEKPLLDWM NDRKEASAMI FQEFCMQMKR LSRRPEAEEQ YMIMRAQMDE
     FCLNLLSFFE RTSTRLPNHN WCVQLIAGGM SKEDFLAEVR KYDYSALCGY IWLSGHVAYR
     CRTCQINPSM SICASCFHNG DHKNHDFNMF RSQTGGACDC GDKTVMRSEG FCSHHGDGIL
     ASATKPPEIL ICSAEQIIPY IIWRLLICYR DYSYVLSGMP GMEHNDFSGI IMLLQTYSEA
     GEPLKRIIAE CLLDEKLYKK FCTDLTTSTH NYLVQMTGHY DKAVDYMKPI YSFHEVEHYD
     CQDLYGLLVH RNMMQELVFW LVKHHFPQSL TNFLLSLLPN ADFKIAFAET YAKHYPHLAK
     ILSQELNPDV VANRVVHISV QILSNNELAY FLVDKCSFLR LVMFSLNSMV RYCLVASSIQ
     SSASEVHLVV DCRAPIMEKH SYWAIALDLH SLLGHKDLAL MMLRDPVVLD LWITMALFFQ
     GMNPNHRMLD KHVDYEMKTY SAAFTAEVDM FSSTLWSFLQ HLTSEDSFDC ILMVLQAASG
     ALQDWLRNMY YGSYPWQLPP LELCFHYPLH RIYVAFLQRG LRLGMELVIP SESFLRMLML
     HPLRIQVGRC EIASGMWVRN GASIRYQSYL YSQSHFCSSF IDLDLYLMQL CMQKCNPEWF
     VLTVFDCFHT ASWFSFSPSA RNPYLRPDWI AAQVDSALQL IATLYVWIVN LVSSEEDILK
     LEVMTLLSGG EYTYSQITDH LPERGSMCEF TALFDKTLNE LADYKQPTFD RSGQMTQGTY
     VMKDWVWEEL YDPLYVMSRT SSLKDFRNSF NLFNQYATRT RNLSASESNA LWIPLRFPKK
     TLPPNDSIWR VLHSRSLHSI IYTILHRAVF RTACISDFTL SLCIFFLELA IRNPPEESTI
     QKSSVGTSVL DLQYCSWFPS NSIELNLSHR IFHVICSDDF VQILQRQDDR RENVISFYDL
     IHLWEIDSQT ASEDSANSTL SDTAPDSTDG QQLSSSIPFI DSSVHGNVYT DAEEFRSRMI
     AMLHPTVRTR LFSQLTGNER AVQNDAEMNG TNDNDGRISV SNGEQPTQGM QFCRAIELLS
     YGCSSGERTE DEEEEEGDEE EEGEGEEEEE EEEEEGEGAE GDEEGEGETE GDEQDIEELL
     RRIQQVQRIR LLQRRQQQQQ QQQQQQQQQQ QQQQQQHEQE QEGVDEVDGQ RSSKEKKSSH
     GMITALSFDG HSILSLLVVL HFRMLKEKLK NGKVTRPLYY QYPTERPSDE DEEPPIGDGI
     YFMERVLNRA YFINQSCRDE IHRICEQISK PASEILQASA PPEDRKQLEA KRKQEILAKF
     QEKQGNIMKD WMIKHAELMK DDVEEQKDKE ETPYTCVVCN QHCGPSMENP ISLLLHMQST
     NVVSKQRLDV KSRADMGIIS ADRGELTLKF HKMLSDKFGP VATFNAFGSG LERGVFIQSC
     GHCIHATCHA DYLKALKSDQ HIVSSFSLHL NNNELLCPLC RRVCNAIAPI LEFSPPESCR
     RDETSFDQSL ADIAAMLNIP PTNVPETLAL CGTFVGQLWT KCNQPQKYLA NSSELSVLQN
     FVVSTARITT ELNATIRRSP NAIFPHCNEI IMRVLAIVSS NMAVGDLQEY AIQWWQLSGG
     HLMDSCYRLL KVPMVPILLQ DAYILLIRYV LFILPKAEAV KSRFHAICRV VWNVLITQIL
     LSELLVASDE EYQSFPEVKS GVRTKKFSFM HNNIDGLLSC LASRIGELRN LPMSNSIYKN
     VDNCVRLDDM NAVVKLVQAK MLPYLRYAAF LKCVVCKLPL PDDDQFEDFY FLKRFCLDLS
     ETDQEMVIFW QSNYVAETLY RQLAQLIQYF KNNPNDGELM VMSVPRVWLQ PKLIDLPDSY
     QTLFEKYHFA VCDLCETHSE DSLLCLLCNE FLCFRSSCCR NAEGLSEAEW HSCKCNAGTG
     VFLSIEESSV IITRDKRYAE WGFLYLDSHG EEDRGLKRGK PLKLCRDRLA FLVEQWLTHG
     FDYFIKRWSW ITRNPNVYSA TT
//
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