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TLH1_SCHPO
ID   TLH1_SCHPO              Reviewed;        1887 AA.
AC   P0CT33; Q5EAK4; Q9HGP6;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=ATP-dependent DNA helicase tlh1;
DE            EC=3.6.4.12;
DE   AltName: Full=Sub-telomeric helicase RecQ homolog 1;
DE   Flags: Fragment;
GN   Name=tlh1; ORFNames=SPAC212.11;
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 [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   [2]
RP   FUNCTION.
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).
CC   -!- FUNCTION: Exhibits ATP-dependent 3' to 5' DNA helicase activity and has
CC       a role in telomerase-independent telomere maintenance.
CC       {ECO:0000269|PubMed:15591066}.
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   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The annotated sequence does not include a stop codon, because
CC       it is at the end of an incomplete sub-telomeric contig of the genomic
CC       sequence. RACE data from PubMed:15591066 suggests an additional 32
CC       residues at the C-terminus, consistent with the SPBCPT2R1.08c (AC
CC       Q1RKN3) annotation. {ECO:0000305}.
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DR   EMBL; CU329670; CAC05745.1; -; Genomic_DNA.
DR   RefSeq; NP_595040.1; NM_001018168.1.
DR   AlphaFoldDB; P0CT33; -.
DR   SMR; P0CT33; -.
DR   BioGRID; 278420; 2.
DR   STRING; 4896.SPAC212.11.1; -.
DR   EnsemblFungi; SPAC212.11.1; SPAC212.11.1:pep; SPAC212.11.
DR   GeneID; 2541932; -.
DR   KEGG; spo:SPAC212.11; -.
DR   PomBase; SPAC212.11; tlh1.
DR   VEuPathDB; FungiDB:SPAC212.11; -.
DR   HOGENOM; CLU_235408_0_0_1; -.
DR   Proteomes; UP000002485; Chromosome I.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1887
FT                   /note="ATP-dependent DNA helicase tlh1"
FT                   /id="PRO_0000255584"
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"
FT   NON_TER         1887
SQ   SEQUENCE   1887 AA;  215812 MW;  7E0CCA91EE4F59B0 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 LQGDVRD
 
 
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