ID I7MER3_TETTS Unreviewed; 1113 AA.
AC I7MER3;
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=DNA-binding protein smubp-2 {ECO:0000313|EMBL:EAR97413.2};
GN ORFNames=TTHERM_00339940 {ECO:0000313|EMBL:EAR97413.2};
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:EAR97413.2, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; GG662666; EAR97413.2; -; Genomic_DNA.
DR RefSeq; XP_001017658.2; XM_001017658.2.
DR AlphaFoldDB; I7MER3; -.
DR STRING; 312017.I7MER3; -.
DR GeneID; 7824392; -.
DR KEGG; tet:TTHERM_00339940; -.
DR eggNOG; KOG1803; Eukaryota.
DR InParanoid; I7MER3; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18044; DEXXQc_SMUBP2; 1.
DR CDD; cd02325; R3H; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR InterPro; IPR000058; Znf_AN1.
DR NCBIfam; TIGR00376; IGHMBP2 family helicase; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000313|EMBL:EAR97413.2};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00449}.
FT DOMAIN 771..833
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 1006..1060
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 703..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 720..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 127751 MW; CBA96732FDAA0994 CRC64;
MDKNIETNQV QLFNQQGQVG QRMYKDGMEF LQRQKKMLED EHAEEMKEHE FIIKQSTCSD
LEELGLAVNR LKLKSVKTGL YGRTLVTFAH PHYSMDKIKE SPQLAKMVKL PESKFQSGDN
VSIYKQSLTF DGNPLEKGVI FKKNDYKFVV AFDEEVNENQ LSNEVISIVM EVNEVTYNRF
LKCLQNIEEK YSDVNFKGSQ LLRVLLDGSD PTNPNPNIKP VHILSKPIVD FYKKDLNEEQ
KDAINFCLSS QTIGLIHGPP GTGKTMTVCE LIYQAVKMGL RVLACAGSNI AVDNMVERLA
KTDLKVMRIG HPARMLPTIY EQCLDNKLRK TTCFKELKAL KQNINKQLQK LQKDISYGEK
KEIKKLLTEL RKEMREQEQL SIKEVIQDTQ VVCCTNSGAA DYIFKRDFGK VEFDLVVIDE
CAQALELSCW IPILLGKRVV LAGDHKQLPP TIKSKNQGLS VTLFDRVLKE FQPENVSRLL
KVQYRMNQQI MEWSSQYVYG GQLKAHESVA THSIGGESIL LFIDTAGAKM GETINENAND
KNKSKSNLGE ADLVKIIFEE LKLQGLQEKE VGVITPYNAQ VDLIKKLFEN NNINTQQVEV
STVDGFQGRE KECIIISMVR SNPLNQVGFL SDYRRMNVAV TRARKFVCLI GDSETVSSDK
FLDEMVKYFQ EHGEVRSAME YVGMQDVHFN CGFIDDKAKK EIKAEGNKAN QSAQQQKPKS
EGQKKQKNKE QSKKDDDKQK QQNENAKKQP ETSTKKHEHQ EQEPRKKFSE EELKSQYTRE
ISIFLMSSAK ELKYDQINSF QRRVLHELAD SFKLYHESIG TSAIKDFVIR KIANSEGTQK
NKLNDNDSNS DDDQEESKQN KEGEEQKQDT KNKKKNKKKE QKSKLPQGIL IGTSDSSNQK
ANSSTQNINQ SDVKQPENTK VSLGLSSNPV VPEGVQGDQK NQYQEYVLKK QQEQQEKLKQ
QQLLLEQQKQ QQQQKKANKQ KNKDKKEKKD DVVDELDDLA FLEKLAEEKK YCKFQLSSGK
KCGVYVEMLG SDCKYCDSRY CIKHGLPEDH GCGDKVKKDA REAFQKQFMM QHRGEKPLRQ
DQLNNLQSRL QDKIKQNIDS RKIKQPEKNE KKK
//
