ID I7MAY7_TETTS Unreviewed; 1461 AA.
AC I7MAY7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=DNA repair helicase (Rad3) {ECO:0000313|EMBL:EAS06738.2};
GN ORFNames=TTHERM_00688780 {ECO:0000313|EMBL:EAS06738.2};
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:EAS06738.2, 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; GG662260; EAS06738.2; -; Genomic_DNA.
DR RefSeq; XP_001026980.2; XM_001026980.2.
DR STRING; 312017.I7MAY7; -.
DR GeneID; 7836965; -.
DR KEGG; tet:TTHERM_00688780; -.
DR eggNOG; KOG1132; Eukaryota.
DR InParanoid; I7MAY7; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EAS06738.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 49..338
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 1408..1447
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1263..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 168230 MW; 46BE5DA89065CCA5 CRC64;
MSSSDILDVE QRQKAKLEPI IKVEKHHISK REIELDQAKM LIHHQLNFHG VDILFPFKPY
QIQEDYMRSI VEALNSKSNA LLQSPTGTGK TLSLLCACLG WLRQKRASQQ IQSDGIVNRI
YFCSRTHSQL KQVMKELKAT AYKPKVCIMG SREQYCLKKE YSNLKDLELN GSCKDAIKKK
TCQFYNYSGD GGKQQPKILD EVLDIEELQE RGRCKKFCPY YYSREIKDDA DLIILPYSFL
LKQSRFQEFQ VILKDSIIIF DEAHNVPSAA EEGTSYKVDQ NLIEESNKEL DYLEKNLTPN
MRTDTYHIKE ARQLINAIGN LIKYFEKEGK IEKFRDGTNG FVCSVSTLFE KIEQIGGQLL
NYSNNKKKIS YEKYKKTSLS GTQFFDYKDM LTNIKKQRDD RSKPQSSQQQ PTLFNFNFKK
NAMQSNELVC DKTTSDDLKD TDQEDNQVND NQFLSSFGYK SNKQSAELSM KRIVQISKKL
SMIIQDMQTM KCQNIDFFAG FIVGICDMYE QEQLFLKGKT IKKLSDYYKF YFHKSSTKYE
QSSINLWCLD PSVAFQNILN EGPYSIMLTS GTLHPMNSWE SELNIKFDVK LATSHIINIQ
KSVVGGVVKN GPNKMEMNFS FNNRQNGIKI YEELGQFLIQ LCNIVPNGIL VCFSSGSLMQ
LARDSWLESQ LNIIQRLNAI KDVFFEPRSN VELSSTMKSY CNAAERDDRG AIMFCVCRGK
ISEGIDFTDK LARSVVVVGV PFPPAADTWV VTKMDYLDKK QSKENTDIEL KTLNGKEWYF
LCTVRALNQA IGRVIRHKDD YGSVYLCDNR FTQNQFQDQI SGWVRPALKN YSTFEYLLND
CQNFFNSKNQ SVTTFDEILK LGNNKKSNVQ SVREIAQKEL AEGKLSCLTQ EKSITQNADS
KRKVYGSFKQ ILMEKEKKNQ QSPLNNVASP NNFNNFSISP NKFQQQQQQS GDNQFTNIFL
ENQKKLMSQS NSSNQGKIQQ SIPQNISTKN IFQLIQECES SNSNPFLYEQ PSKNDSFYKT
TQDHEKMRSD LQTFQQAFSN NQQKNSTLKD IETSQMEIEN QPIKPNDARI NIKFEDSMTN
QSQYQDQDTS FSINSKKGGM FEQIRQKRRI IINESQEPVV FQKSPMSVEK NIVCNSQSQQ
DLQQPRILRL KSSSIPKEPS FIMNQKDRAL SQQSLITLNK PLIMKGDRDE MINLFRNGSD
DESSNSFEIM RPQNDRGSLN IKSVESKESS LNFLNDIFKK HQALLINENQ NIRESSLDQK
VTLSLQKSKE SSSPQSENLI ESSLRKRKKS LKLTPSTKEE GMSQQKSFIE IINSRNSTGS
IKSISPISKL QQYNQNDNQQ DDKVTTNQIV ISPSEQKLNV KPNQKIMLQN SARGLASFDG
DVIKYQRKQN KDEETPIKSA SKEQDNLCPI CYEVPKNNHK STACQHYACY SCWQTWLAEQ
LTCPMCRVRC RVAYLEPFSL N
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