ID I7M280_TETTS Unreviewed; 1218 AA.
AC I7M280;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=SNF2 family amine-terminal protein {ECO:0000313|EMBL:EAR99498.2};
GN ORFNames=TTHERM_00137610 {ECO:0000313|EMBL:EAR99498.2};
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:EAR99498.2, 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).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GG662639; EAR99498.2; -; Genomic_DNA.
DR RefSeq; XP_001019743.2; XM_001019743.2.
DR AlphaFoldDB; I7M280; -.
DR STRING; 312017.I7M280; -.
DR GeneID; 7843770; -.
DR KEGG; tet:TTHERM_00137610; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; I7M280; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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:UP000009168}.
FT DOMAIN 145..310
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 448..599
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 799..851
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 142375 MW; 7AD562B09255C1D3 CRC64;
MADETNEKSR GFEDVMDEED DVHEVEKIQG RKSQQQKYLK QISNDDENPQ QEEISDVEKK
MKTLLLKAEQ YASFLVSRHQ QKKNKKQVVQ KRRGQYQEEK EEEEQLIKEE EEEDDNLPTI
LTSQPKILKG GKLKDYQMIG LNWMISLYET GLNGILADDM GLGKTIQSIS LIGFLKEFKK
INGPHLIIAP KSTLGNWFNE FQKWLPCCRT IKLIATKDER EEILQNYIAN SKFDVCLTSF
EGAKLCQKYL KKINFQYIII DEAHKIKNEE SQTALILRMF KTNYKILLTG TPLQNNLHEL
WSLLNFLLPD LFSSSEIFDE WFSANNLSGK NNNEENDTKN IEMISQLHRI LKPFMMRRTK
SEVMQTLPPK KEIHLYVGLT ESQLNIYRNL LSPKKSITGS EDDKKFYLNI LMQLRKVCNH
PYLFEGIEEE GLPPLGEHII TNCGKMMVLD KLLQKLKNGK HQVLIFSQMT MVLDILEDYC
NYRQFKYCRI DGNTDMTDRD NQISDFVKED STKYIFLLST RAGGLGINLA TADTVVLYDS
DWNPQMDLQA MDRAHRIGQK NIVNVYRLIS ENTIEEKIIE RQTIKLKWDQ LIIQQGRLAQ
KNRVLSRDEI KDMIQFGASA IFKSKGGTYT DEDIDILLQR GEQKTKDHNK TIDEKFKKSN
EQVGELSLSS INIYDFLQKN HDNDKTKEDK EALDEQLARE LASELRSRRE KKTMNYNINA
QFSHMMATAP MPKAAKIIKL PEHQLFVERE KLQELLQKEE DFKCMSNRAK KAEKEEENSI
EENGLTPKEN KLKDQYWATG FPTWLKQEYL SFIQGCERFG KTAYKEIAEH IKTKTEEEVS
QYSKAFWERI DTISEKDKII KNIERGEQIL KQKLVMSDLL KERCKIYQNV KEEFEFNSAI
YNKSKSKFYT TENDKFLIYA SYQMGYCNWP VIIKEIKTNP MFQFDHFFKS RSEYELNKRL
QSLLKVVEKE KDFIVQIEAK KLKLKQEQEE KQREQELKKE QQKQQQQLLE QQKAEKEKAN
QQQQQQQQQQ QLNTEIIVTD SQPKPQQNSN NNKDSKNINS AKNSQESQAK QQSTIQKSSN
QQSNQVQQTQ KIKDPQNSSS SKNNNTNSKT NGLKQNSLLN YGVKVDKKVQ QAPILIDLES
EDEEDDKIKI KRLPNVIVPE PLSQESKQET QQKQSQQSSQ SSNKQSTSNA SNNINSKKSH
NVKDDKIEQN PQKKLKRD
//
