ID A0EB91_PARTE Unreviewed; 918 AA.
AC A0EB91;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Chromosome undetermined scaffold_87, whole genome shotgun sequence {ECO:0000313|EMBL:CAK92558.1};
GN ORFNames=GSPATT00025292001 {ECO:0000313|EMBL:CAK92558.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK92558.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK92558.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK92558.1,
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; CT868668; CAK92558.1; -; Genomic_DNA.
DR RefSeq; XP_001459955.1; XM_001459918.1.
DR AlphaFoldDB; A0EB91; -.
DR STRING; 5888.A0EB91; -.
DR EnsemblProtists; CAK92558; CAK92558; GSPATT00025292001.
DR GeneID; 5045740; -.
DR KEGG; ptm:GSPATT00025292001; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_310467_0_0_1; -.
DR InParanoid; A0EB91; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF132; PHD FINGER PROTEIN RHINOCEROS; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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:PRU00146}.
FT DOMAIN 249..299
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 363..482
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 704..756
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 865..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..177
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 790..823
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 865..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 108353 MW; C05E7BD54F0B93A6 CRC64;
MQNIDPATKR RKQTRVRRQL VNKSLHEESE EHQQVEVQQK VTKKYQNYLH AIQKMGEFDW
TDVENTNNPK VIYPIQFLQA STLQFMIGAM YFNCDHDYLQ HNLQDVQKLL KKTEQPNGTL
QQDDCKKQKN KKGYDVNDDI FILEMRQLKI QDLDDIIANQ ELKLEKIQKE NEEAIQHFLT
AEIPDLKPSI KTDQSNSLLR DIFGLTEFEK QYIEKIELKI QTDGQSDITQ ETGKKTQGGR
IHLQPILDDA LCQVCNDGDY TDDNLIVFCS KCNISVHQKC YLIEVIPNED WICDVCQTFG
PNGQYLRCAL CPKLGGAMKA TQIDASCFEN LNQTYFESQG ETMMKNDLVS KLFQQIDDDE
ELYYDFSKLP NRDIRDLENN KDVKEPQPQK VWIHLSCFYW SPECFLDEKQ DILRGVDNIN
QKRFTLSCSL CNIKKAGMCI QCARSSCQTG FHVECARRSG IFLTQIIVNT KSDYQIFCQK
HVPLKVKRIL ESKQRLYERE IIDFFRAYEK CKSVHKKSQQ RVKKAKSSKE SQQQLELQDH
QENEFDLIDF AIKLKEFIDQ LLDQKFIVNL KLEQGKYVFE SLTEPQFKQQ KQYYLTKLPE
VYQSKVDQNG QIITQFYKST ITATDELWKF FKYRDFEKDI IYKMYEKLRR RASKFMQELN
PQKKQAKLID MLMLKKFKKS KKSDLKKEII IEQVGDEYYQ RDDNLYCVCR GKFKDGDPMI
CCESCEEWFH FDCLEIIIPN EEISKMTYYC FLCLDELPRE RQIEIYNSYT NVFKDTSFKL
QRELADKCAL DESRKARMNE QKEAKLIEEN NTIEQDNQQQ EQIQVEQQNN NFGGLEMSNL
YVNNQLQKEL NSGEDNDIQI EMQNDGIEKN KKGDEHVKTP SKTQSVEDPD NKLDVPETQE
KLNGKLKQKS IHNYIPKQ
//