YF2C_SCHPO
ID YF2C_SCHPO Reviewed; 897 AA.
AC O13762;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Uncharacterized ATP-dependent helicase C17A2.12;
DE EC=3.6.4.-;
GN ORFNames=SPAC17A2.12;
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}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB16565.1; -; Genomic_DNA.
DR PIR; T37813; T37813.
DR RefSeq; NP_594246.1; NM_001019669.2.
DR AlphaFoldDB; O13762; -.
DR SMR; O13762; -.
DR BioGRID; 278902; 41.
DR STRING; 4896.SPAC17A2.12.1; -.
DR PaxDb; O13762; -.
DR PRIDE; O13762; -.
DR EnsemblFungi; SPAC17A2.12.1; SPAC17A2.12.1:pep; SPAC17A2.12.
DR GeneID; 2542440; -.
DR KEGG; spo:SPAC17A2.12; -.
DR PomBase; SPAC17A2.12; -.
DR VEuPathDB; FungiDB:SPAC17A2.12; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_0_1; -.
DR InParanoid; O13762; -.
DR OMA; YSQFSQY; -.
DR PhylomeDB; O13762; -.
DR PRO; PR:O13762; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA: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; NAS: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:0006338; P:chromatin remodeling; ISS:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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: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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 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; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..897
FT /note="Uncharacterized ATP-dependent helicase C17A2.12"
FT /id="PRO_0000310749"
FT DOMAIN 263..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 727..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 606..655
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 25..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 397..400
FT /note="DEAH box"
FT COMPBIAS 28..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 276..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 897 AA; 101376 MW; 334FC00F7B2C63E8 CRC64;
MDSLSAYPPQ STFQQLQNDE ELARRLQDEW NSSSPSSAPS SSSSQNQVEL DEQFARSLQN
SQSSSYSLPP FDHPPSKNPT SSSLSTRKRW RQKRLWSFKN FPFRPPTRLT STPSNSSSLP
SIPSSSSTPS ISSIPHTTSS VSNDIPSVLG SSDHPIDLDN PEHLTPPSSF ITAKQLSRLP
TPLPPPSSSS LPTGTISTNS FCPYERKVQP EHVTKELHQL LQHNTPSPFD TIDLQLKNEQ
VQSAGLLVSL LPHQVEGHAW MESMEQSSKC GGVMADDMGL GKTIQTIALL LTQKSQDPLR
KTNLIVVSVA LLHQWAEELS TKVHPSKKLS VYIHHGSTKK NLDSYELSQY DVVLTTYSML
AYEMKQNDAF NNNNPATATP PPACSLLETS WYRIVLDEAH TIRNRDTLAA KCCVKLDAKY
RWCLSGTPIQ NHIDEFYSLL KFLRIKPYCV WSLFAKDISR PLKSYRADIV EAALKRLRIL
LASTVFRRTK ETRVNNLPIV NLPPKTIRTV SVNLLPEERA LYNEQMSSAQ SLVDNYFNND
HDLSRYGFLL VSLLRLRQFC CHPWLVKSSS LDNSFRIRDS ENVRNACKSL DPLTIERIAT
LQDFNCSVCL DPCLAPVFII PCGHFTCQEC MSMLVGQKYG SSSTSTIIAK CPMCRGNIVQ
DSLVDATILQ AIHGPLNSLK QLELDMNQSF SEQESIKLRW ENRIDQMFTK KFGKRASEWK
SSSKLNQARQ TILDIIGSKR NEKILVYSQF SQYLCLVSHM LKLENIRHVR YDGTMSANQR
QKSLHSFNND KDVLVMLVSL KAGSVGLNLT IANHVILQEP FYNPSIEDQA IDRVHRLGQQ
KPVTVYRFIT KDTIEERIVS VQRKKRQLVK EALDSNENNP LSRLDKEELL YLFGLNS
