CHL1_SCHPO
ID CHL1_SCHPO Reviewed; 844 AA.
AC O14147;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP-dependent DNA helicase chl1 {ECO:0000250|UniProtKB:P22516};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P22516};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000250|UniProtKB:P22516};
GN Name=chl1; ORFNames=SPAC3G6.11;
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 -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II (By similarity).
CC {ECO:0000250|UniProtKB:P22516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P22516};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16287.1; -; Genomic_DNA.
DR PIR; T38730; T38730.
DR RefSeq; NP_594977.1; NM_001020408.2.
DR AlphaFoldDB; O14147; -.
DR SMR; O14147; -.
DR BioGRID; 279550; 27.
DR STRING; 4896.SPAC3G6.11.1; -.
DR PaxDb; O14147; -.
DR EnsemblFungi; SPAC3G6.11.1; SPAC3G6.11.1:pep; SPAC3G6.11.
DR GeneID; 2543118; -.
DR KEGG; spo:SPAC3G6.11; -.
DR PomBase; SPAC3G6.11; chl1.
DR VEuPathDB; FungiDB:SPAC3G6.11; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; O14147; -.
DR OMA; QTHQFRD; -.
DR PhylomeDB; O14147; -.
DR PRO; PR:O14147; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; ISS:PomBase.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IGI:PomBase.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR028331; CHL1/DDX11.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF41; PTHR11472:SF41; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cytoplasm; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..844
FT /note="ATP-dependent DNA helicase chl1"
FT /id="PRO_0000351016"
FT DOMAIN 9..418
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 118..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..365
FT /note="DEAH box"
FT COMPBIAS 146..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 844 AA; 96204 MW; 19232A24457F12A8 CRC64;
MCHSKEVKFK TNFHHPYTPY DIQLEFMRSL YSSISDGKIG IFESPTGTGK SLSLICASLT
WLDEHGGVLL EDNEKSNDNK SNTSSKIPDW VLEQDLKIQK DLVKETHARL EQRLEEIRKR
NQSRKNQMSN NSTTYHRETK RRNINAEAST SDNCNNSNTS VDPMDEYLVT AEYTMPSTSE
QSEDLFNNGY SSKVSELLRK LSPDNEKPPI VQKIYFTSRT HSQLQQLVQE IKKLNNQTFS
TPIRVVSLAS RKNLCINNEV RKLRPTSALN EKCIELQGSA HKCPFLQDNT QLWDFRDEAL
AEIMDIEELV ELGQRLKVCP YYGTREAVDS AQIVTLPYPL LLQESARNAL NLTLKDNICI
IDEAHNLIDA ICSMHSSSIS FRQVCIAETQ LQQYFLRFEK RLNGNNRMHI KQLIKVVYNL
KSFFLNCLET NTNSKVINVD SLLVSNGADQ INLHHLSEYL NVSKLARKVD GYTKYMHSLG
TQELESLNDL RSERFSNGNG YEEDPYTPVL MQLESFLLNI ANPAPEGKLF YEKQTGDNPY
LKYLLLDPSK HVEILTEQCR SVNLAGGTMS PIDDFITLLF SDEQSRILPF SCDHIVPPEN
ITTILVSQGP AGVPFEFTHK RKDDENLLKD LGRTFQNFIS IIPDGVVVFF PSFAFLQQAV
KVWEMNGITN RLNAKKPLFI ESKDFGDNPL DTFEHYKQSV DAGLSGMLFS VIGGRLSEGI
NFSDKLGRAV MVVGMPFPNS QDVEWQAKVS YVEEKAKEKG INAKQASQEF YENTCMRAVN
QSIGRAIRHR DDYASIILLD SRYNRSSIQR KLPNWLSKNI HSSPNFGPAI RQLATFFRAK
KMCD
