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Database: UniProt
Entry: A0A267ENM7_9PLAT
LinkDB: A0A267ENM7_9PLAT
Original site: A0A267ENM7_9PLAT 
ID   A0A267ENM7_9PLAT        Unreviewed;      1784 AA.
AC   A0A267ENM7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
DE   Flags: Fragment;
GN   ORFNames=BOX15_Mlig005236g1 {ECO:0000313|EMBL:PAA63098.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA63098.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA63098.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA63098.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA63098.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) 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|ARBA:ARBA00004906, 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:PAA63098.1}.
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DR   EMBL; NIVC01001873; PAA63098.1; -; Genomic_DNA.
DR   STRING; 282301.A0A267ENM7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000215902; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000215902};
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          75..147
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         75..147
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          1033..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PAA63098.1"
SQ   SEQUENCE   1784 AA;  197109 MW;  A2FA2E40799033BD CRC64;
     RNLQSYYQAG QLGEGLKQLF FNSGPKVFAP KVRPDLLFLD VLARNQILSP LEQFITASAT
     PDVEFEKLTQ DKNPGICGYI LKNNEPVFTC HDCTADPTSV MCNNCFVHSE HKNHNYKMHL
     SSGNGGYCDC GDPEAFKRYH RCSLHERQAG SQSGAPVSPV EKLPAGMADR FRAICNQVLQ
     LALHLTLLEY RIRLPSNVDR LDEVDLNLLR RWLPHGERTD TSESDAEAGG QYASVLYNDE
     VHSYPQVINT LTQCLGVDEH DANHFATVVD NDGRSVVSLS DWASAKKLCS EIRGTIRESS
     GFELGCYPVR SVSFAYQSMC LYLLSWLGQL IKQSDGLHEL FCQSLLAPVD NFPGTEWAPG
     QPLVYYLLVH TDHLWKAARK SFIEMLIKSL LMKANYKRQI AALYAVNQEQ IFERFCVDMH
     HQEDSIAQLS VQLFTSPSLA MYLITEQKAL KILVDILIKS VLQRSVQQHQ ESGRQLLKFS
     EDDRMPFSRW NRSLHLVRDI EYLLHNDFEQ LEPNFFAAIN EALPSFLQVY SLFQDTCCAR
     RYIVGHIGFD FEWEMPFIFF LSSMYQNHLL AEFLSRDENV FSTILDKVLD AIEQKPPLSA
     NFLADSGQRV RLAGHVLSGR ALAPLMSGRV FISHFQPLVR FLDSLLACTM ANHEASPQCR
     RQLELLANRP GFEIAWLTSA RQLAWSAQIA AGLWKRNGLA LMNVNLQYSS HQSAAVGMSL
     RDLHLVQLAA ATVPPDQFIL RLLDAFELQR WTLGAASSSE SAAERYDNEA ERSIVEEMLR
     CLINVVCERR VPGVGQSVAF MEMVEEDLLQ HLVAEPQSHS KLLRLANDLV RKLPAADRQL
     ECFAKLDGVI DKLAEFRGVQ GQNKGEFHLR EQHYSRFNPF YPRLAKSATS KALHSMTKRR
     AATPAADLPI VRPPQLPAFA AAYQPIVELL HCDVMLGLMR AVVQATKDAG ASSKRHWSEV
     QLERVLYLML VGLDEDQRRG DRRFLDCVLS GIGEASLMSA MESVPKSRLA MDSVRQLHGY
     TLARLRRLCT GQGEGGESGG NEAGEVGGGG SGGLDAARDA AEAEVRRRQQ QKLAQDRRDR
     LMAKMMRMQK NFLAEYGDLV EQADDKSGGA TASENSTEST SAGRRSDGPL IGPNRTVAHE
     PQPGLTCLLC QEANRPDSRD PMLLAGLVQR STVLSQDRGR SRDTDWSGCF VEAELLEGSH
     FSSCGHAMHR SCYSDFMDSP SNVHVNRGGE LGRSRYLCPL CQQLCNCALP VAPSLPCSAE
     QQQQHQFDAN ADSGRFDSWL SSIRDGVAAG LPKWPPQAAA ESRVVAFRKN HDDNSWPGAE
     AAQALNNLAK VCEVRGLGAD LPPELMPTGW KLPEKADPLL LTVAFSLQAA ETAGRATERP
     LFSALPERCA VGLAALVRAV AQRPVASDSD FDRLHQLAIN NLSLLLHLQR PNLPLPCLLE
     ADMSTCLVQL TYCLYRMAGQ PPDCSDADLC RLIRLVAGAH VFQICLTLPS DPDASTNADS
     DADASGDDSD CRKLDRLVRQ CRSAVGLPPA ALSGPGLADQ VAAACLPLLR CAAIFYRALT
     DAPAPSEPEP ASSAEAEFAW LAGLLQLPRR PCDLPTEQLV SLWCQDSARL QARAASPAVR
     YPRQAARLVS LPTDYTDLLL ECSDFQCPSG AGPGPAGRSL QPAKCLACGK LVCSNSNCCQ
     MPVFNGDRAI GGANLHAVMC TGGTGVFLRV LDCTLLLVSA PNRLGCISSA PYVDRYGETD
     EYLRRGQPLQ LSSAMYSRLQ EDWLRHSLAA RAGRDPHSGN FFEV
//
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