ID   YIV5_SCHPO              Reviewed;        1375 AA.
AC   Q9UTL9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Uncharacterized ATP-dependent helicase C144.05;
DE            EC=3.6.4.-;
GN   ORFNames=SPAC144.05;
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: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB59685.1; -; Genomic_DNA.
DR   PIR; T37672; T37672.
DR   RefSeq; NP_594666.1; NM_001020095.2.
DR   AlphaFoldDB; Q9UTL9; -.
DR   BioGRID; 279346; 44.
DR   STRING; 4896.SPAC144.05.1; -.
DR   iPTMnet; Q9UTL9; -.
DR   MaxQB; Q9UTL9; -.
DR   PaxDb; Q9UTL9; -.
DR   PRIDE; Q9UTL9; -.
DR   EnsemblFungi; SPAC144.05.1; SPAC144.05.1:pep; SPAC144.05.
DR   PomBase; SPAC144.05; -.
DR   VEuPathDB; FungiDB:SPAC144.05; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   HOGENOM; CLU_001592_2_0_1; -.
DR   InParanoid; Q9UTL9; -.
DR   OMA; WRTCKSK; -.
DR   PhylomeDB; Q9UTL9; -.
DR   Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   PRO; PR:Q9UTL9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; ISS:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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   InterPro; IPR017907; Znf_RING_CS.
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; 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..1375
FT                   /note="Uncharacterized ATP-dependent helicase C144.05"
FT                   /id="PRO_0000310750"
FT   DOMAIN          277..476
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1190..1336
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         1092..1130
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   BINDING         290..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1375 AA;  159952 MW;  890E78F43EE91615 CRC64;
     MDRTKRRKIE KEASLLNERN NLLESDFANC YRAFQHQLKL DQQIWRGPED ELNRLKSTIY
     PVVFWVDGSE KLHAYSFTQR KISLAKNLIP LFSVDLNKDT YSALKAPLKI WSKLWEDNRR
     LKKIIKYTSY VTVKGSELIL SFGISILDSF LAPQDAILSS GSSSSYTALL DYTFLPSEDE
     EYSCLDINTA LFYDCARKLA KSLRFANVSR DPRLSSELLP FQMRVLEWMK RREEEKFLTS
     NDLPPLWYHC KSLFDDRMVY VNHVYGYMTF SKEKTYLLAS GDIRGGILAD EMGMGKTLEV
     LGLVLHHQLP ISLTDTCTFD QVVGKNVKYS KATLIITPST ILDQWLSEID LHVPSLKVFH
     YQGIRKSNGL KSAKIFLDCD IVVTSYSDLR FELLYTESHS RTLRHEKRHV SPKSPLIDVC
     WWRICVDEAQ MVETSQSNVA QMIYRIPRVN CWTVSGTPVR SEVDDLFGLL FLLRYSPMYL
     YKKQAWMQII EKKRVREFCD LFGSLVCRHS KQDVEEELKL PPQHRICMTT RLSVVEETNY
     QDLLSEAAKS LHFFKDRNLD LCDEESMRRW LVRLRQACCH PQVGFGNKSA FGGGPMKSIN
     DVLVFMLEQT NSTFSSLNRK LYSDKIIVGQ IYDHIKDYNK ALAIWSEVRI PVELAVKELE
     NVIYNSKYED HGKNLPINYF GLDHFIHLRV WYVLLHKIYF FIASAYFSLK NEKFENEFYL
     LAQDLRRKIM SDVIIKTSKH LEEFSEKFIP KKLVKIPRLQ KSYAKGLITG HGIIEDYNRL
     YKELNDQKEV LIKFRDRLIH LMKLPLLDQE SDPTGDEYEE SLNAQSEISY CIDVYRQMLS
     DRVAAVSGTI NTFVSHETEL EKYKLIESIK KSEKSLDKQA EERDKKYLLY FEEREEARPK
     ADQYGSLINI VSRLLDASNR STSSFETSKN MEEYERIDAM AKEQSRICQK LEKELSIIQL
     TYNSRIEYYK QLQEISDSLM PPPVSNISLN NYVKDDEKKQ KFLNSVIIKA SVILEKEISE
     KQDEASQTTN VAELVNQKIS EMNIPGHIHL LRELEEEKSN TQRKIAHFES RRRYLTNLYE
     HIVLKAESHQ ICIICRDIIK QGFITTCGHL YCSFCLEAWL KHSSSCPMCK TKLNKNNAYY
     IGESRDIYSR QEFVTGFNKR DERLEILDDE AYRQISNMEL KESFGSKIDT ISKHLLYLKH
     NELYPKVVVF SQWLDVLDVL HKSFEANGIV FIRFDGKSKN TCLKRFKEER SLQVLTLHAR
     SQSSGLTLTN ATHVFMCEPL LNSGIEMQAI SRVHRIGQTR PTFVYYYIVE DTVEGHILNL
     SLTKHEQLDK LGLDVPLVGN INRTTEASSG GEQVDAAEIK DCLKMALKRL TTEDS