YK16_SCHPO
ID YK16_SCHPO Reviewed; 1183 AA.
AC Q9HDY4; Q9UTZ3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative ATP-dependent RNA helicase PB1A10.06c;
DE EC=3.6.4.13;
GN ORFNames=SPAPB1A10.06c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 582-780, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAC21479.1; -; Genomic_DNA.
DR EMBL; AB027915; BAA87219.1; -; Genomic_DNA.
DR RefSeq; NP_593520.1; NM_001018954.2.
DR AlphaFoldDB; Q9HDY4; -.
DR SMR; Q9HDY4; -.
DR BioGRID; 279793; 4.
DR STRING; 4896.SPAPB1A10.06c.1; -.
DR iPTMnet; Q9HDY4; -.
DR MaxQB; Q9HDY4; -.
DR PaxDb; Q9HDY4; -.
DR PRIDE; Q9HDY4; -.
DR EnsemblFungi; SPAPB1A10.06c.1; SPAPB1A10.06c.1:pep; SPAPB1A10.06c.
DR GeneID; 2543371; -.
DR KEGG; spo:SPAPB1A10.06c; -.
DR PomBase; SPAPB1A10.06c; -.
DR VEuPathDB; FungiDB:SPAPB1A10.06c; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_3_1; -.
DR InParanoid; Q9HDY4; -.
DR OMA; GHQHGCM; -.
DR PhylomeDB; Q9HDY4; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q9HDY4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032040; C:small-subunit processome; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1183
FT /note="Putative ATP-dependent RNA helicase PB1A10.06c"
FT /id="PRO_0000055192"
FT DOMAIN 408..585
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 611..831
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 522..525
FT /note="DEAH box"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1183 AA; 133996 MW; BA8183F0B4CA8BAF CRC64;
MGRLRKRFNE KGRQSGIQKM LNLKRARLHR SVREQESSSE VHANPEPDNQ DSNAEILIDV
PKEERQKRKQ ELKDQLLKEN EGSISSKKKK RLDKYIENKL KKEEVASLIA KLAEERIDTS
LLSSSKNLGK QATAKEKLKK SLLEEKLGLP LSDADSRLYK VVDVETTTTK SSTAETNAPE
KYSTRSGFGF GFSTGTNESE ITPNIKVLPP KKKKNASWGK MLNEDPEYDS AEEDYLSTDS
EEFSEDSDNS SEENKDTNEP STKDAEKTVP EDVVNLRSEQ KLQPSFGHPE FENEDFDLET
SEDDSSDDAT ERASRFKSWA NKQILGADVG EKSHDVAPDN KIDNPDADMV RAQRMPRKLK
MREEDVEPTA DDIEIKGRKT TYTIINRPPE IQESRLALPI VAEEQRIMEQ IFANDVVIIC
GATGSGKTTQ LPQFLFEAGF SSPESENPGM IAITQPRRVA AVSIAKRVSE ELTGFSSKVS
YQIRFDSTIN PDTAIKFMTD GILLRELSSD FLLTAYSAVI VDEAHERSVN TDILLGLLSR
IVRLRREMSK SDQKVKPLKL IIMSATLRVT DFSENKLLFS VPPPIIKIDA RQYPVSIHFN
RTTKPDYLQD AFDKVCLIHK RLPAGSILVF LTGQQEVEQL CQMLRKRFVR SFRPLKSRAR
IVVSRKTMSV ENEDLQSETE DIDQVPTSSS SSVTYDDESE PMYVLPLYSL LTTEDQMKVF
DSSPEGHRMC IVATNVAETS ITIPNIRYVV DCGKAKERVY NEKTSVQKFE VRWISKANAD
QRAGRAGRTG PGHCYRLYSS AVFDSSFPLH SLPEILRTPV ESIVLQMKNM NIDNIANFPF
PTSPGRSRLE KSLKLLSNLG AIDSEGVLTK LGEQMSLFPL SPRFSKMLII GQQHGCLPYV
IALVSALSIN QLFVSKQSLL YDAHDKNSRS EETDLIDDDE IKQKEEYKNR MRGYFNAISR
FQAIDPDAPA LSLLSAVCAY DYASDKRKFC KENYLREKAL EEVTNLRKQI IGLLKRYMVR
VEKEFFKLQL KPPTSVQIKA LRQFIASAYI DQVALYDKEK RGYVTLFPSG SEVVQFVPDR
TYNIDSEYVV YLSLHESRSG RVYMSPLTEI SPEHLARLAK NTTLLSYSKP LSYPPIRYLD
NATKRECWVI PILSANIGTG SPSWNLPAVQ IIQKRINGRW VNC