ID A0CVG3_PARTE Unreviewed; 1014 AA.
AC A0CVG3;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Chromosome undetermined scaffold_29, whole genome shotgun sequence {ECO:0000313|EMBL:CAK74780.1};
GN ORFNames=GSPATT00010948001 {ECO:0000313|EMBL:CAK74780.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK74780.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK74780.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK74780.1,
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; CT868196; CAK74780.1; -; Genomic_DNA.
DR RefSeq; XP_001442177.1; XM_001442140.1.
DR AlphaFoldDB; A0CVG3; -.
DR STRING; 5888.A0CVG3; -.
DR EnsemblProtists; CAK74780; CAK74780; GSPATT00010948001.
DR GeneID; 5027962; -.
DR KEGG; ptm:GSPATT00010948001; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; A0CVG3; -.
DR OMA; HLWENCG; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 144..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 793..845
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 119200 MW; C5407EFCBC4843D7 CRC64;
MSNSSGEENE VIQVEVESDE EQKIQQEEER IKKLEQDKKT FMSSIKQTTK LNANIKFDNI
ESKINTLLEN AEKYAMFLLH RHKRTQESKQ KALTQQRGKH RQVIDDASEE EDLDDAPTVL
DKQPTILRGG QLKQYQMTGV NWMISLFEEG INGILADEMG LGKTIQTIGF IAFLKEYTKI
SGPHLIVAPK STLGNWMREF KKWLPCARVV KLIAVKEERE DIINKFFQPG KFDVCLTSYE
GVNICLKHIR RFSYKYIIID EAHKIKNEDA IISQNLRKIR TNYKLLLTGT PLQNTPHELW
SLLNYLLPDL FDSSEVFDKW FEVNTEAKLK EGNEIIKQEE LDQRNLEMCQ KFQKILRPFM
LRRTKAEVER ILPPKQEIHL FIKMTNLQKQ MYQNILLHNN PHEGDDKGFY MNKLMQLRKI
CLHPYLFPEV EDKSLPPLGE HLVEVAGKMR VLDIFLKKLS DGTHQVLIFS QFTMMLNILE
DYCNYRKYDY CRIDGETEIQ QRDDQIAEFT KPDSKKFIFL LSTRAGGLGI NLATADTVII
YDSDFNPQMD MQAMDRAHRI GQKNRVMVYR MACEHTIEEK IIERQQIKLR WDSLMIQQGR
LSQKQSGKLL SKEDLKELTA HGASQIFKLD GDDIKDEDID ILLKRGEQLT QQMNERIEKK
FESFKDKMQS LDLGLGQINI FEYFNEEKQN KMDEDALEDA LASHLFNENK TRNRDKRAMM
LGANSKKIQG KQIKLQEHHL YENKDRLQSL LQKEEDFLAQ QKTQKKGMDS EENVDCGGLT
QEERQEQKQL LETGFKNWNK QEFSDFITAN EKYGKDAYEK IQEFIKTKTV DEVKTYAQAF
WERIDGLSEK DKIVKQIERG QKLIEQKTNG QKLIEEKCKH FHQPKYELVF TPQLYNKFKS
KYFSLENDKY LIYMTNEVGY GNWTLLKQSI RKEPMFRFDH AFKCKSENEL KNRVISLVKV
LDKEKENNSM GRSPVKNTYV EKPKVQQQDS QKKKMKNEED EIQDGSESVK KVKL
//
