YG65_SCHPO
ID YG65_SCHPO Reviewed; 1428 AA.
AC O60114;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Uncharacterized helicase C15C4.05;
DE EC=3.6.4.-;
GN ORFNames=SPBC15C4.05;
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18896.1; -; Genomic_DNA.
DR PIR; T39475; T39475.
DR RefSeq; NP_595925.1; NM_001021833.2.
DR AlphaFoldDB; O60114; -.
DR SMR; O60114; -.
DR BioGRID; 276380; 10.
DR STRING; 4896.SPBC15C4.05.1; -.
DR iPTMnet; O60114; -.
DR MaxQB; O60114; -.
DR PaxDb; O60114; -.
DR PRIDE; O60114; -.
DR EnsemblFungi; SPBC15C4.05.1; SPBC15C4.05.1:pep; SPBC15C4.05.
DR GeneID; 2539831; -.
DR KEGG; spo:SPBC15C4.05; -.
DR PomBase; SPBC15C4.05; -.
DR VEuPathDB; FungiDB:SPBC15C4.05; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_3_1; -.
DR InParanoid; O60114; -.
DR OMA; REMRYNS; -.
DR PhylomeDB; O60114; -.
DR PRO; PR:O60114; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
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; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1428
FT /note="Uncharacterized helicase C15C4.05"
FT /id="PRO_0000310783"
FT DOMAIN 641..811
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 886..1064
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 REGION 249..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 758..761
FT /note="DEAH box"
FT COMPBIAS 10..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 654..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1428 AA; 161460 MW; 2D7E3942B2A7B310 CRC64;
MAKKKSKASN SARGYATTSI PSRSASSPAN KNQVKGEKNN KTQKVEPKNA FKVENQSNDI
GVDTVDAFDH LLLDKTLPTI DAETEVIKNT SLSNSKSFLH SWQTDIRLRK NDNVLGLTED
EIQQILKTFR DSWKSSLKES YAFSNRSSFS LRKRYLWTTF LSLKGMGFEE SEIFGAFSSI
PIVSIDEYIT WMITENLINS EPSNSSFSYE VQPSNYTTFC RMLDEPLPAN NPVQSNSRLV
PLMKDFSNDI KHTPNKETQP SNQVDDSLKS KDSKPLTMSE VLTQLPEDDI PFDDPFDLTS
QYVKVKLKML RLQIANKKNS EEFSTLNLQL ESITSQYLFS SKEAEIVFRK SRIEFMNKLK
ALQQKLENER IVEEIKKNGI QEDSQSTDDS SKDDDNNSES NDMSPHNDAE TRADDDAYLM
GDLFNQEEED IQDTENDLLN ANYTLLPLTT DKSGTRPSTT LQYELHKIGS NIKAEFKTMP
IGKIGYQSTC FVRCSTGQKT FSDLKTVLPT ATLAADYISM IVLFRLMANF TKISLQTFPK
SFKEVYGKFS AEKQNTDLAE DAKISEKLDS IIKSKELETP TSATTSKLMA PMDNIGKFSG
FERPPETLLN KWRQQLESES AEKFKVFRNQ LPATMFRETI IDAVNNSQLL IISGDTGCGK
STQIPAFLLE NSTKNGKAVK IYVTEPRRIS AISLANRVSQ ELGGNPPSAR SHELVGYSVR
LDSKCTPLTP LTYVTTGTFL RLLEVGNEIE SVTHLIIDEV HERSIDSDLL LIHVLHLLKQ
HPHLKIIIMS ATLNAEKFQL YFEGSNLITI PGKTYPVHRF YLEDILSQFG NDKSFGNAAG
QDVIEEDDYE TDQQDASISN KSAEDAIVEM NLIPAWYNEK AINYGLIVYL LKYIFTEGDP
KFSKCVLVFL PGISEILRVK SLIEDMPMFR NHRKFCIYML HSTLSSAQQQ SVFNIPPKGC
RKIVLSTNIA ETGVTIPDVT CVIDTGVHRE MRYNSRRHLS RLTDTFVSKA NAKQRSGRAG
RVQEGICYHL FSKFKHDTQF LSYQTPEILR LNLQEVVLRV KMCQMGDVQD VLGKALDPPS
STNIIRALEK LHQVGALSEN EKLTKLGKFL SQLPVDANLG KILVLGCFYK CVDAASSIVA
MLTIGSPFRK SVDNEFSANK ARLSFAKENT RSDLVLMYYA YCAWREICLS PLGPDEDSFA
KEKYLNLEAL SMTESLKIQL LSELKDMKLL GASDVDTCKS LKRSICRRFA VIPKEHDINS
GNAEILCGVI AASLYPNILR YDYEKRQWST LSTNKRVRIL DVSVNNRSEL PNMPSKFVAY
TNMMSSTRAS EYVNETTMVT LRQLLMMCGL KVENRVSVGQ AKLDNFTVYF ENVYVSASLS
ILRRFIETSL NEFFAEPDKR LLNSHLEVIV NIVSRLNYGT KFQKRLKD
