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Database: UniProt
Entry: A0E2J6_PARTE
LinkDB: A0E2J6_PARTE
Original site: A0E2J6_PARTE 
ID   A0E2J6_PARTE            Unreviewed;       365 AA.
AC   A0E2J6;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Chromosome undetermined scaffold_75, whole genome shotgun sequence {ECO:0000313|EMBL:CAK89513.1};
GN   ORFNames=GSPATT00022685001 {ECO:0000313|EMBL:CAK89513.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK89513.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK89513.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK89513.1,
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).
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DR   EMBL; CT868655; CAK89513.1; -; Genomic_DNA.
DR   RefSeq; XP_001456910.1; XM_001456873.1.
DR   AlphaFoldDB; A0E2J6; -.
DR   STRING; 5888.A0E2J6; -.
DR   EnsemblProtists; CAK89513; CAK89513; GSPATT00022685001.
DR   GeneID; 5042695; -.
DR   KEGG; ptm:GSPATT00022685001; -.
DR   eggNOG; ENOG502SQQT; Eukaryota.
DR   HOGENOM; CLU_066774_0_0_1; -.
DR   InParanoid; A0E2J6; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0061659; F:ubiquitin-like protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19756; Bbox2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF557; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          157..200
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|SMART:SM00336"
FT   REGION          86..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          208..245
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        86..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  42073 MW;  E69C685292E8617B CRC64;
     MMNVSKCSKC LNVPDDILML TCSHDLCLLC AAKSFSQQPS KRSKKVKHPL IIEQFFVCDI
     CSSNTELDAN SVYELEKLHL TTALQDRSNR KPASQSKSNI TSEKQLKPRS QNRQENKENA
     KEKPIKYTAQ TMEARVSVHQ SQRNMSKQQS ENSFIQNSRG MCIDHPEEEV SYYCFDCNSK
     CICPECIIHG IHKNHEVKTI KKSYPIVRKQ LEDQLEQNNQ CIIQVENQKQ ELEKKQIQQQ
     AIQDHLRLQI AQEFQALHQL LNSKQSELLE KVDNQPTIME QQDGYINRLN EVEFKLSNFN
     EKINDVIDSK DECGLLNYYG SIYGQPTPQI PPLPNIKEVQ LSNQIFTQIN DVKKLIGGLD
     IDCNQ
//
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