ID Q22KF3_TETTS Unreviewed; 1332 AA.
AC Q22KF3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=SNF2 family amine-terminal domain protein {ECO:0000313|EMBL:EAR85846.2};
GN ORFNames=TTHERM_00313280 {ECO:0000313|EMBL:EAR85846.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR85846.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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DR EMBL; GG662498; EAR85846.2; -; Genomic_DNA.
DR RefSeq; XP_001033509.2; XM_001033509.2.
DR STRING; 312017.Q22KF3; -.
DR EnsemblProtists; EAR85846; EAR85846; TTHERM_00313280.
DR GeneID; 7824668; -.
DR KEGG; tet:TTHERM_00313280; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_262780_0_0_1; -.
DR InParanoid; Q22KF3; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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:UP000009168}.
FT DOMAIN 502..728
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 936..1092
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 352..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 156601 MW; 78232929A19C8C87 CRC64;
MSQDQFQFNE QRPRKRKLRS IADEKSLSNY LGSFKSELIL GNVEMIVNKE QLFAVKESKW
NFINDIKLAS NYINLENSGK LKKEDVKVNL MEELMKNPCN QDVLVSYGNP QEKKYCLLRH
KFSEMWRFPI YCSFLELRIE VCDDEDLVEN RLFQSINSQM QQTRNSMENE NLKDLVKNFQ
KNPKQNVDEI IAVNKFRNLM KQNIANASKV MCNVHIYLKQ HFYTFPLHIH KGVLEKGCTN
FSECSINEQI ELLSKDSLYL LFSMLNLNKL NQLDIPLSKK IPIMSQYYKM KSKKNILDSQ
RMNISLTNST QKKQTAENEK QSEIYMLLDD KFLESIECSG LNVDDDFLQS KDTVRQSESR
DNSREDTDDS ENLDLQEYDD ESEDEHIYEN EEEDADTKEE DRNNIEEGKN FKKTPTPSQM
LKQFELKEYQ QQGLTWMLHR EQKLSKKKLY EQKWQILSTN NQFKDITMAY EQYLVENPYN
EENVQFYYNP LNGHSCLDIE FEEDEEPVQG GILADQMGLG KTIQAIALLL QSKFKDYLNE
SDTKNQNVKQ KKPKNVRKFY LKNEDSDDSY RGTEDELDDE DKYSDDEDSD QEITLIIAPK
SLVNQWRLEI QATLKDIESL QIYQYEKGQK YSKKKKLFKG IDIVITTYGT LSAEYMSIKK
GKIQKGNLLN QKWERVILDE AHLIRNRNTQ ISQACCELNS KFRWCLTGTP LQNKIEDLFG
YFRFLKVPQI GEWRWWSDYI SKSRNKEKTY QFIKAVLKGM MLRRTKTTKD QEGKPIIVLP
QKIINVDNIS FNKFEGELYT IYFSNQQKLF AGLLDQYEQE RSQRGRLHEQ MFVMVNNLRM
MCNNFQMVKL FQDSNLEKLR KIIIELKKEN KKEAANPNKQ KWDEKFLRMD YPGLTDEQIQ
EKLAQMNQSQ SQNFNEGDDE EEQQQIDYKK LAKTDRVVDI IEQVQKKGEK ILLFTQWHDS
IQRLKKRFED LDIGYCELHG KMTIKQRAKQ VHDFYRLPSK TVMVLSLMAG CVGLNLTCAN
NVIIMDPWWN GAIEDQAVDR VYRIGQKKDV NVYRCLIKHD DSIDLRISEL CKKKEALCNK
ILSLSQDERS ISQNLTIEDF KFLFGLSNPN VPSQIDPNFN QDLNNSNGIF ASKTQNLNQM
VQSKNDIQQN FQRSSNRFIS NLTQSVTISG EKNLNTSGNK LMNSIRQSSS NSNTKEFIIK
DSQQNTSSIY PLFQPAQQLQ RSETLFAQPN VFGKQQSGDF KNNINNYTDQ AFKINNVDAS
ITKPLFSREA VAYGNQNEKP QNVFQNQYYG DDEDYFYESS RKQRSRLSRN RISQNTNFNQ
NPQKQFRAED KL
//
