YG42_SCHPO
ID YG42_SCHPO Reviewed; 1040 AA.
AC O60177;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Uncharacterized ATP-dependent helicase C23E6.02;
DE EC=3.6.4.-;
GN ORFNames=SPBC23E6.02;
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18870.1; -; Genomic_DNA.
DR PIR; T39936; T39936.
DR RefSeq; NP_596602.1; NM_001022523.2.
DR AlphaFoldDB; O60177; -.
DR SMR; O60177; -.
DR BioGRID; 276992; 39.
DR STRING; 4896.SPBC23E6.02.1; -.
DR iPTMnet; O60177; -.
DR MaxQB; O60177; -.
DR PaxDb; O60177; -.
DR PRIDE; O60177; -.
DR EnsemblFungi; SPBC23E6.02.1; SPBC23E6.02.1:pep; SPBC23E6.02.
DR GeneID; 2540464; -.
DR KEGG; spo:SPBC23E6.02; -.
DR PomBase; SPBC23E6.02; -.
DR VEuPathDB; FungiDB:SPBC23E6.02; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_0_1; -.
DR InParanoid; O60177; -.
DR OMA; PMQNGIE; -.
DR PhylomeDB; O60177; -.
DR PRO; PR:O60177; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0061995; F:ATP-dependent protein-DNA complex displacement activity; IDA:PomBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR GO; GO:1990505; P:mitotic DNA replication maintenance of fidelity; IMP:PomBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
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 InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1040
FT /note="Uncharacterized ATP-dependent helicase C23E6.02"
FT /id="PRO_0000310787"
FT DOMAIN 403..588
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 866..1032
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 746..798
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1040 AA; 118365 MW; F5C7210283512470 CRC64;
MRNNTAFEQF TLNPCEQIPL DDKHNIGFNK NNTPDYSSSA SSDQLLKNDI NRHEMERRIA
FLNRKQALFN AFMHDSSSSL NTMESNIEKV NGLFPNDNSV IALKPNEEKL NSSLSVENND
STYTDATLIA PKIGLDRPNI NAITIDVDGH SLQNEISSST DKLSPSQSDA LFEQKQDSLF
WNDNAVIVVS DSESDDNNVR TKSSLNDHDK VNMKEKRNLE LAFMNSKRKK LELPSLPVLS
TAGPSYTNSL ALPPFHHHNN YKMFNTTHTL EDDKFLQGKG TSNNPISLSD EEDNEINFQN
KRYGSDSVIL PGGLLHDSKL PEPGKHLFHL QWYHDRFHNI EGFNLSDSNN QKVQDDQQQQ
LEELFKDLDE QLVNDPTIRE GTPAGLIPTL MEHQKEGLMW LKRLEESSKK GGILADDMGL
GKTVQALALL VTRPPESKSV KTTLIITPVS LLQQWHNEIL TKIAPSHRPT VYIHHGSSKK
HKIAEQLMSY DIVLTTYNVI AYEFKNKMAY DKSIEDNAPI KKFEHLPFFE AEWYRVILDE
AQTIKNRNTL AARGCCLLES TYRWCLSGTP MQNGVEEFYS LIKFLRIKPY SDWSSFSKDF
TIPLSSNINT SAPMKRFRGL LKAVLLRRTK NTKIDGKPIL TLPPKTAVKS ETDLSSSEME
FYNTLQSGAQ IQMRKYLQEG TITTHYGSLL VLLLRLRQAC CHPWLIVARE AAVDDNDSFQ
AKNRAIYNQI YPEAVNRLKL IETLQCSLCM DVVAELLIIV PCGHFLCREC LTHVITSSED
MAKQTSNENI SPKCSVCEEY IDTERLLSYA LFRRYSGMAP IVDADNKLRT ENISELLPKQ
YSNILENRQM GMKIFTDPKH WTTSTKIEKA LNAVKEIIKK QPTDKILIFS QFVSFLELFT
VPFRQEGIKY LMYTGGLSTA ERNQALINFE VDPNVRVLLI SLKAGNVGLN LTCANHVIIL
DPFWNPYIEE QAVDRAHRIG QDKPVNILRI VTNNTIEERV LALQDRKREL IDSALGEKGL
REISRLNTKE LSFLFGMSSR
