TLH2_SCHPO
ID TLH2_SCHPO Reviewed; 1919 AA.
AC Q1RKN3; A6X989; Q5EAK4; Q9HGP6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP-dependent DNA helicase tlh2;
DE EC=3.6.4.12;
DE AltName: Full=Sub-telomeric helicase RecQ homolog 2;
GN Name=tlh2; ORFNames=SPBCPT2R1.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=H1;
RX PubMed=15591066; DOI=10.1074/jbc.m412756200;
RA Mandell J.G., Goodrich K.J., Bahler J., Cech T.R.;
RT "Expression of a RecQ helicase homolog affects progression through crisis
RT in fission yeast lacking telomerase.";
RL J. Biol. Chem. 280:5249-5257(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=16407326; DOI=10.1093/nar/gkj415;
RA Hansen K.R., Ibarra P.T., Thon G.;
RT "Evolutionary-conserved telomere-linked helicase genes of fission yeast are
RT repressed by silencing factors, RNAi components and the telomere-binding
RT protein Taz1.";
RL Nucleic Acids Res. 34:78-88(2006).
CC -!- FUNCTION: Exhibits ATP-dependent 3' to 5' DNA helicase activity and has
CC a role in telomerase-independent telomere maintenance. Represses ade6
CC at an ectopic site. {ECO:0000269|PubMed:15591066,
CC ECO:0000269|PubMed:16407326}.
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 -!- INDUCTION: Repressed during various growth conditions, including
CC nitrogen starvation, and by heterochromatin. Repression is strongly
CC dependent on cul4, raf2 and raf1. Derepressed by histone deacetylase
CC inhibitor TSA. {ECO:0000269|PubMed:16407326}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA05660.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BK005597; DAA05660.1; ALT_INIT; mRNA.
DR EMBL; BX784043; CAJ90629.1; -; Genomic_DNA.
DR EMBL; CU329671; CAO77679.1; -; Genomic_DNA.
DR RefSeq; XP_001713158.1; XM_001713106.2.
DR AlphaFoldDB; Q1RKN3; -.
DR SMR; Q1RKN3; -.
DR BioGRID; 857983; 1.
DR STRING; 4896.SPBCPT2R1.08c.1; -.
DR PaxDb; Q1RKN3; -.
DR EnsemblFungi; SPBCPT2R1.08c.1; SPBCPT2R1.08c.1:pep; SPBCPT2R1.08c.
DR PomBase; SPBCPT2R1.08c; tlh2.
DR VEuPathDB; FungiDB:SPBCPT2R1.08c; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_235408_0_0_1; -.
DR InParanoid; Q1RKN3; -.
DR OMA; CVYCSRC; -.
DR PRO; PR:Q1RKN3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; TAS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEP:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1919
FT /note="ATP-dependent DNA helicase tlh2"
FT /id="PRO_0000255585"
FT DOMAIN 1200..1375
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1401..1559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1804..1821
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 329..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1322..1325
FT /note="DEAH box"
FT COMPBIAS 329..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1213..1220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1240..1247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1919 AA; 219379 MW; 502B162C0A746A2A CRC64;
MVVASEIAKV ASKTARDIAG CFTCQCGTQF DNVERIVQHF KECRYRDETC KDDDIVVYEP
SSFVQDEKKD KPIIVEAASE ATSEEACNSS KERQLPALSA LSALSTLTTS ANDDLWTARL
IWQSTNDTKL DNSPSSNYTD LNHKLANYGL SILSIHALMC VECECLLNVI HTAQHMQIVH
KLELNEDLLW FQELRTLKLK SPTNVLQTHS SQTHVYPYIR GLPVLLNGYE CVPCTKNGTG
FVHAIMDTFR HHVRRTHGKV IKLENCIRRT ALQTVKNKYA QRCQFFKVDY VPLNGGEEEE
EEEGEEKEDA QNIKERMVDF CFSKFMEKNQ QRREQQDKGE NKKRQDDVDQ ATDNNTNTIL
EDDEKDNDEE EEEEIVNARE KNLLNQQFNW TAIVKKLGEN WDQLVRFEYT NGIVTLDTIV
NQLIRYYYRG FRHLSGMTMG MRRMFTQGGS YSAQERGLCR LEQKDTVVRY AQSAALYLIF
LLRRPSADSG IRRHLEAMCG ATVERKEGGS NSSSNISNVA NFDSAEDDND NDNDNDRDSN
NNNNNNNTNT DDDDKLAYLE LHEALKLAFL QQYDFSKNVQ DLEIMEFLAC MSLHKDGTSK
YAYEISACFA PLIYTCRLVA ACELQRLIDE KQIDLLSIPS FQTAGSIAYA HVFCFITLGQ
RNLYDVLYET QKVVRDIIRT EGYANTLQGL SPSTVLFQPR SNSMYPCIGD AFNNMVRLDL
SELTALYEGM FAKVQDLLKE LCFDMNVEKL LPISLLRSIG DDINNSKLGY SFFKESIEIR
SSHSVLLRTI LKNSELCHRF FPSMSKKDLT KLFGGVSDQQ RNECDNYSNH YNDNSNDNDN
DVFLKLHWSK SAIKKYETKA SIFNELLFCL VYISAGQPAR AQEMVYWTLR NGKYKTRELY
LMFGRLMIYS RYDKTRNMKF AEKPIPRFLS EPLSILALRY YVLVRPLEAL MKYVTTADRS
KVAVYLDFMF VIAGERLQRD LPYRIFPKAT YQCIQKPLGF RNYRHIAHYF KEKNIEEEMT
RESYFDLQAG HTRNTALYIY GRTMDNLHYL PSDYFANFFR ASYKWQELLQ IRDNPTHGLL
VETKHPFIKR VDQLEEALNE KLARLVGEQM VEGDKEKDKT NEEKNKDEVK AEMTQPVVNQ
DSHDLQDQLA TTPTAPTAFH YRPGLLQPSQ TSVQHCCWAL SQYYGLEAKF RSLKQFQSVY
FSLLNRMNLI TVLPTGGGKS LSFLIPALIE KKRQTPGKVM NMVTLVLVPM MSLRQDMMLR
VNEKGLLVCS GNWTAFKDVR LTLETQLPDL FILTYESALT NSGLRFFESL ATLGRLARVV
IDEAHLLLTS GAWRTALSRA SRLSGLYAPL HLLSATFPRQ LEMVARQTFC TNFYVLRETS
TARENIFYFL HPYDNTEFLL DLRTLMKRTK VFEGDGRAII FCRTKKDVEY IHRRLHQSDL
FAHTHVTIYT GDVSDEERQM NFDAFRNANG KTRIMIATKA FGLGINYMGV RLVVHYGLPA
SSMDYVQETG RAGRDGKYAI AALFYEKYDS TWSSYVEDSM KNFLNDNTMC VRSFLASEMD
GECVCCASFA NCVYCSRCSD SLLGEESTVS TMYGVKPTLP ETPKPAIATH SRYNASFSSS
PPPQPGNSSG MSAMNTNTTS TTPVSLSELS EITLFPSSVS PTWKKSFGNA NTNLKYGLED
MSLSHRRGHK RTYDEHLNNV QQGVNHDMNR VHGSVGGMSG IVGIGIGIGD GDGDGDVDSR
TIHFAEYKSR VQAVKKQWVD STDISAQLER FFRVYKDECL SCTLGNPDTE IRAHTGKACP
VRLSTCYKCG KADHNLRECK LRIRFQGLCL FCGLTKFEHA DSDMAYTSDC RSWARKANLI
SLVYYAWNNV QYRRTIADKF LQGDVRDQAF YGFVCCSTTT NSAFVLVIHY LLSDVLQIM
