YE02_SCHPO
ID YE02_SCHPO Reviewed; 1030 AA.
AC O13799;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Uncharacterized helicase C17H9.02;
DE EC=3.6.4.-;
GN ORFNames=SPAC17H9.02;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, 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 -!- INTERACTION:
CC O13799; Q10295: pla1; NbExp=2; IntAct=EBI-8993901, EBI-7997221;
CC O13799; Q9UTR8: red1; NbExp=4; IntAct=EBI-8993901, EBI-1117407;
CC O13799; Q9P7B7: SPAC140.04; NbExp=3; IntAct=EBI-8993901, EBI-9002253;
CC O13799; O42975: SPBC20F10.05; NbExp=3; IntAct=EBI-8993901, EBI-9003631;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11211.1; -; Genomic_DNA.
DR PIR; T37868; T37868.
DR RefSeq; NP_593572.1; NM_001019004.2.
DR AlphaFoldDB; O13799; -.
DR SMR; O13799; -.
DR BioGRID; 278648; 273.
DR IntAct; O13799; 13.
DR STRING; 4896.SPAC17H9.02.1; -.
DR iPTMnet; O13799; -.
DR MaxQB; O13799; -.
DR PaxDb; O13799; -.
DR PRIDE; O13799; -.
DR EnsemblFungi; SPAC17H9.02.1; SPAC17H9.02.1:pep; SPAC17H9.02.
DR GeneID; 2542173; -.
DR KEGG; spo:SPAC17H9.02; -.
DR PomBase; SPAC17H9.02; -.
DR VEuPathDB; FungiDB:SPAC17H9.02; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR InParanoid; O13799; -.
DR OMA; GADGIYM; -.
DR PhylomeDB; O13799; -.
DR PRO; PR:O13799; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:1990477; C:MTREC complex; IDA:PomBase.
DR GO; GO:0016604; C:nuclear body; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0043630; P:ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process; ISO:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:1902802; P:regulation of siRNA-dependent facultative heterochromatin assembly; IMP:PomBase.
DR GO; GO:1902801; P:regulation of siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0043144; P:sno(s)RNA processing; IMP:PomBase.
DR GO; GO:0016078; P:tRNA catabolic process; ISO: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; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1030
FT /note="Uncharacterized helicase C17H9.02"
FT /id="PRO_0000102099"
FT DOMAIN 134..290
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 357..561
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 238..241
FT /note="DEVH box"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1030 AA; 118461 MW; 1E088BCE01118789 CRC64;
MSENSTDSKN FQFSEGSRES SNDELKVLLR DTETKEDEKS SFSNSEEESI IENLSDSSVN
KEYAKNSLKL SDAVSESKYL NPLLKDKRHD RSFALHKVVV PDDYDYIPLN KHIPSDPPAK
TYPFELDPFQ STAIKCVERM ESVLVSAHTS AGKTVIAEYA IAQALKNRQR VIYTSPIKSL
SNQKYRELLS EFGDVGLMTG DVSINPSASC LIMTTEILRA MLYKNSEIMH EIAWVIFDEV
HYMRDKDRGV VWEETLILLP DAIRFIFLSA TLPNALQFAR WISEIHKQPC HVVYTDYRPT
PLQHFIYPQG ADGIYMLVDE KNKFKTENFK KVLEVLDHST RQENYSKSSK KVKKSSSLER
IINMVLSNRY DPIIVFCFSK KECEINAHQF GKLDLNDTEN KELVTEIFDS AINQLSEEDR
GLRQFEEMRS LLLRGIGIHH SGLLPILKEL VEILFQEGLV RILFATETFS IGLNMPARTV
LFTKAQKFSG NNFRWLTSGE YMQMSGRAGR RGIDTKGLSI VILDQSIDEQ AARCLMNGQA
DVLNSAFHLS YGMILNLMRI EEISPEDILK KSFYQFQNME SLPLIKEELM QLKNEETSIN
IPNETAVKEF HDLKLQLEKY GEEIQKVMTH PDNCLPYLQS GRLIQIKLGG IIFPWGVLVN
VIKREFDPNT REQVAPHETY VLDVLLPISS NSMSNHKVNP SILVPPRPNE TPLYEIVSVL
LTAVCNISSI RIYMPRELNS NESKLRAYRR VNEVIEEFKE IPYLDPLEHM HIESSTLSLS
LRKLEILEPK LFDSPYYKDS KHRAEYHEFR KKLNLRAQIK DISTKITNTE AIIQLRELKI
RQRVLRRLGF CTLENVIDIK GRVACEITSG DELLLVELIF QGFFNQMPPE EIAAALSCFV
YEDKSEVSTL NLKEPFKKMY LTIIEAAKRI ATVSLESKLQ FNESDYLHQF KPDIMEPVSL
WINGASFQEI CIVSKLYEGS IVRTFRRLDE LLKQLEHAAI VLGNNELKEK SVLTEQKLHR
DIIFSASLYL
