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YBMA_SCHPO
ID   YBMA_SCHPO              Reviewed;         830 AA.
AC   Q10332;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Uncharacterized ATP-dependent helicase C582.10c;
DE            EC=3.6.4.-;
GN   ORFNames=SPBC582.10c;
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 264-443, 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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB46673.1; -; Genomic_DNA.
DR   EMBL; AB027965; BAA87269.1; -; Genomic_DNA.
DR   PIR; T37973; T37973.
DR   RefSeq; NP_595178.1; NM_001021086.2.
DR   AlphaFoldDB; Q10332; -.
DR   SMR; Q10332; -.
DR   BioGRID; 277423; 18.
DR   STRING; 4896.SPBC582.10c.1; -.
DR   iPTMnet; Q10332; -.
DR   MaxQB; Q10332; -.
DR   PaxDb; Q10332; -.
DR   EnsemblFungi; SPBC582.10c.1; SPBC582.10c.1:pep; SPBC582.10c.
DR   GeneID; 2540907; -.
DR   KEGG; spo:SPBC582.10c; -.
DR   PomBase; SPBC582.10c; -.
DR   VEuPathDB; FungiDB:SPBC582.10c; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_8_1; -.
DR   InParanoid; Q10332; -.
DR   OMA; YDGGMRN; -.
DR   PhylomeDB; Q10332; -.
DR   PRO; PR:Q10332; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:PomBase.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..830
FT                   /note="Uncharacterized ATP-dependent helicase C582.10c"
FT                   /id="PRO_0000074382"
FT   DOMAIN          249..433
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          662..816
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           384..387
FT                   /note="DEAH box"
FT   COMPBIAS        11..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   830 AA;  93945 MW;  47086968FDD951CB CRC64;
     MEKASKNKES GVKKANNSFL QNFGVNTAGK ENESTSLPRL PKSEDESIPK QSIKSKNKKK
     TQHFLSDAFE SLKRQEIDTN EKEVIVSAPI TSKPAQVFYS KKLERKDEGI RKWEKDPFAP
     ISVKSGAWKK PYTKVPEVSI NKATSKRTDL INDKPIVIPI PRASTSTLYF GKHNKPTSEN
     RKGPIGIPTE EILTSQNTQA MLHKLFENNV LDNVKDDSMQ RQSSFIPGMH IRLLDHQVQG
     LTWLKSRETV SKSSASGGIL ADDMGLGKTI QMIALILSHP LPKKKHSIKS TLVVAPLSLI
     KQWESEVQTK SKLTAIVYHG ASRYKLLKVI HEYDVVITTY QILVSEWVSH NTTGTDGKSP
     TEAKSYEKKK PSLFAFYWWR IILDEAHTIK NKSSKSALAC CALQGINRWC LTGTPLQNNV
     DELYSLVKFL HINPFNDQSV WKDQISLPLC QGEENLVFKR LRMLLSVIML RRTKTLLEAN
     AGKDGTGGAL KLSKRLVYKV ICKFEESERD FYSNLARNME RTMSNFVNSG KLGKNYTNIL
     CLLLRLRQAC NHPQSLNFQF EQDVDAFNAL DGAANTNKLA SDQDVDDLAN LLETVEIGSR
     KKSFCTICMA ELPPDFHEKK CKDCSRNFKE LDKGIQDPND KTLYKSSKIR EILKILSLDE
     QEEDDTVRGL RKTIIFSQFT TFLDIIDLHL RKAGIGFVRY DGRMNNRARE KSLDLLRSDS
     GTQVLLCSLK CGALGLNLTC ASRVILCDVW WNPAIEEQAI DRVHRIGQRR DVLVYKLVVE
     NTIEEKIVEL QNLKRDLAKQ ALGDGKKSVF TSKKLTLNDL LFLFNKRAAA
 
 
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