ID F0ZE25_DICPU Unreviewed; 1806 AA.
AC F0ZE25;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=DICPUDRAFT_149555 {ECO:0000313|EMBL:EGC37836.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC37836.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC {ECO:0000256|ARBA:ARBA00006471}.
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DR EMBL; GL870990; EGC37836.1; -; Genomic_DNA.
DR RefSeq; XP_003285681.1; XM_003285633.1.
DR STRING; 5786.F0ZE25; -.
DR EnsemblProtists; EGC37836; EGC37836; DICPUDRAFT_149555.
DR GeneID; 10499072; -.
DR KEGG; dpp:DICPUDRAFT_149555; -.
DR eggNOG; KOG1140; Eukaryota.
DR eggNOG; KOG1754; Eukaryota.
DR InParanoid; F0ZE25; -.
DR OMA; DIASEEC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1490.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR000630; Ribosomal_uS8.
DR InterPro; IPR035987; Ribosomal_uS8_sf.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF49; E3 UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF00410; Ribosomal_S8; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF56047; Ribosomal protein S8; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000001064};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Transferase {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 87..157
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 87..157
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 324..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1806 AA; 208515 MW; 9BA44ED927AAFFC3 CRC64;
MDFHQQQLNW KNFEAFQKKL NDDSDEDDEE EEFNNIQYLQ DEDLFVDSLF KYKPSYIYNK
IAQLISNGEL ETFEKLKQTY SDSTSRSICG KVWKGNSHIY KCLDCQIDEN CAICVDCFEE
DKHIGHRYRL IPSANGCCDC GDLSAWKKEG CCSLHVKREK ESDDKNKLLP VKTVDILVNL
VLKKLLKEIT KPQYTKKADS IIEVLNQFID VFGDQFTMLL GNSIIETGDQ HSRQKVLKSF
CEFTSKPESN LEKFIISLFI CSEFRDMLAL SMTEAFDNEK YDSNLSVQLF TVDSTALKIV
STNKFKHIVN NFYKSIYNTR GSVNNNNNIN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NTDNNSLDIL KTSLSNSTEN LEQQQQEKHN QHLFSLLNND SINVNPFEYF QRVNPINPYL
LKTNYFKPMV SISYILRTKS SFLWLLKNPN LLLRCFDALG LTESMNPNTR LTTSHIEFDD
PSWRTCLSLE FSIQRNIIRS IFKQMEDNYQ MVTENEAIVI RDHILNRILQ FYQASGSYDK
SNKWKKGIKE QIIPEYRVSK QPVSIHIPLH RALFKILHFQ SIYFKRSPRE ILKSISSSPY
FESILIEHIL RTLVLSYQYK AGMWVRNGDS IANQIANYQH GSCDLNSTDV YLLQYVVLSM
DTKQFYSQIL DRSELSSWFV LDGYVNDENN SSPLFLSKLN KLFNNDAVGT NNNNNHPLLN
MNHSRHRSES DRSSTSVAER FLESIIWLVV DRAKLSNLSP EKLLRKELIH ILAIRPQTYS
ELYPQVSDEF GESNELDDTL QEISVYQSAT TTEAGKYRLK TEIWKEWNYF NPHYLKNEQQ
KSEENFHAHC RKEKIENIHA KPLVPLEKPL EMFKGIEIIL HSEILHTILF SVIYNNLSGS
IKTSDSLLSS SLYLLYLSLE TYKENKLNRQ QREKEVKPNK NQKYVNLNNI INDIVPNNFN
QQNTVLSPPP PKSSSPPKSS SPPKSSGFFN SSFQMKSSSP PKSSSPPKSM ISSYQNNVST
PISIAKSLGL VSSKPQHDIL DIGLTSDDIL KNLVQPVKQA TTFLGSPNTI TFISMLNQMN
SLSKFETHHP LISKILNHEI LENLNNSSIN SSSEGLSKSP LSTPLNGEAA SNQMKEIAMK
KQMEMMRLMK EQQKKFIKNN EFDDYEDDDQ EDSDQNDDDQ DDSDEEYYSD TNDDSMVDSN
KELFYFEQDE ASSDLGNCVM CRDVLSVNKT TNNIGYIGNL HKYSLLSYIP LLSCDPSVSQ
ENRRIEKIFQ SKAPNKEFDD SLSIDMNDTD APFINYCSHL IHIGCIDSLI EGNHNGQSRV
RDPLKLQSFQ CPVCRGPSNI VVPFSKQRIS TIKLTQYLKQ TKSKQKALGQ PIEEPEQNFI
KQQFNNWLQS VLECKNLDTS SPMNTEQEQQ KYDNFIILIY QNSTISKSNI DQIEHFWNIF
NSSISAYEIS KRKNGFDLNS FKLIRKPFNN LIKKCVEQSS NNLEQRIYDL QQLVNILSNT
FKDSVKFIKL DMFGLFTRFY FSNESLFTLR SNMDNGIKIP NSPISFLISL FFIGTLLQSI
IYHYKFNNLE KILEFFNSND NCLANLDQEI KRICLSFLRR ICYFIICIDT SIDHAENINN
NNNSNQLDTE FETLLKLIKR SSGADLSIDS IIFRNPVVNK LIGEYWLSPT NINLDIPNIH
QLNLPLRSWK EFSIKTELPQ DYLKFFLENT TKKNCSECDN KNGTVKLIID DHRSGKIVIE
LIGRINKCGV ISPRFDVTLD EIEKWASYLL PSRQFGHIVL TTSLGIMDHE ECKKSHTGGK
LLCFFY
//
