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Database: UniProt
Entry: A0BJS2_PARTE
LinkDB: A0BJS2_PARTE
Original site: A0BJS2_PARTE 
ID   A0BJS2_PARTE            Unreviewed;       548 AA.
AC   A0BJS2;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Chromosome undetermined scaffold_110, whole genome shotgun sequence {ECO:0000313|EMBL:CAK58789.1};
GN   ORFNames=GSPATT00029418001 {ECO:0000313|EMBL:CAK58789.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK58789.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK58789.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK58789.1,
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; CT867998; CAK58789.1; -; Genomic_DNA.
DR   RefSeq; XP_001426187.1; XM_001426150.1.
DR   AlphaFoldDB; A0BJS2; -.
DR   STRING; 5888.A0BJS2; -.
DR   EnsemblProtists; CAK58789; CAK58789; GSPATT00029418001.
DR   GeneID; 5011971; -.
DR   KEGG; ptm:GSPATT00029418001; -.
DR   HOGENOM; CLU_030542_0_0_1; -.
DR   InParanoid; A0BJS2; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
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   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          7..47
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          100..141
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          205..232
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   548 AA;  63628 MW;  55FACEF51AA24723 CRC64;
     MHQELNCPRC EISFDIYDRT PQMLPKCGHS MCMQCLREQT KIICPEDGIV QPQDLNLYPV
     NQAILKIINK SSLKNSQIDS TELGETVRLS KCENFFEVME STSLCKEHNK KIELVCLEDH
     NTICVSCALF GVHKHHNVRN IDEVVSEIQH SLEETVDLMQ QIQSKIKSLK QPIINKKIRD
     QIRLCIKQQQ ALAEEQFKEM ITQLMMKQRK VVEEIEYKYK QVEDQLIKRE QQYVNQVVEK
     ADLWMLASQE RINQFASLTE KGEIAFFLLQ KDTSNSQAKQ IIEELEDFMK KFQTRLQEVT
     QGQITPQVHL SKDLMGNFEY NYPQVQQSFF DDPNILRDVS MIDQSFLKDI DDKPPHNEFL
     THNLLNPQPL YQSQSALQSQ PSSNNISQNA ISPNYEKKSS DILVSPKLRR QSSMSPKRPT
     KKKFNTKVES ILLNCNGDTL DLSQQDLGDD GMILLEESIK NKKLKILKLV RNKISDTGAT
     KLLELHCQIL HLQSNVITER FLDTIQQLIQ KQTQIHIKTI YLGQNLMNLF RVKKKIEDLK
     KLGITIQI
//
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