ID A0CD08_PARTE Unreviewed; 254 AA.
AC A0CD08;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Chromosome undetermined scaffold_169, whole genome shotgun sequence {ECO:0000313|EMBL:CAK68675.1};
GN ORFNames=GSPATT00037460001 {ECO:0000313|EMBL:CAK68675.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK68675.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK68675.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK68675.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR EMBL; CT868062; CAK68675.1; -; Genomic_DNA.
DR RefSeq; XP_001436072.1; XM_001436035.1.
DR AlphaFoldDB; A0CD08; -.
DR EnsemblProtists; CAK68675; CAK68675; GSPATT00037460001.
DR GeneID; 5021857; -.
DR KEGG; ptm:GSPATT00037460001; -.
DR HOGENOM; CLU_1096051_0_0_1; -.
DR InParanoid; A0CD08; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044286; SINL_plant.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632:SF16; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 10; 1.
DR PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 109..167
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
SQ SEQUENCE 254 AA; 29057 MW; 5B8DABDBA2838352 CRC64;
MNFPLPENRI ANYAKVSTFL PHLVCQCCKS LSLQQLICLK CHENFCFKCI PYADDQIPEP
IEITVQTILI NKNTKYVQDI NYRGFCPNCE VVTVLTSQLP KMFHKLYTSV KFSCQNRING
CSEELCYPDL RIHEQKCGYN TITCPKQECS QQTYKKDFIT HVSICNPTTE CVCGSTNQHD
QQKCLRLQCE TLKSQLNTQT KELQLLKDVQ TTFSYSSPQK QLNRIVVNQS PYVATSPFSL
QGLLQQSAQI LNDG
//
