ID S9X065_SCHCR Unreviewed; 1412 AA.
AC S9X065;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ATP-dependent DNA helicase {ECO:0000313|EMBL:EPY50317.1};
GN ORFNames=SPOG_01077 {ECO:0000313|EMBL:EPY50317.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50317.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50317.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE546993; EPY50317.1; -; Genomic_DNA.
DR RefSeq; XP_013024802.1; XM_013169348.1.
DR STRING; 653667.S9X065; -.
DR EnsemblFungi; EPY50317; EPY50317; SPOG_01077.
DR GeneID; 25035408; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_2_0_1; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProt.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd16568; RING-HC_ScPSH1-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EPY50317.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 284..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1100..1138
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 163201 MW; 3D281D9FADE5FD3E CRC64;
MKGKNEWQER PAKRRKSIKE ETESKLEQSF LQSSFEDAYP AIIEKLSLNM DGWLGSKELM
EQLKVQPLAT VMSLEPEKLL KIYKFTTKKL KSNNKMEPIY CLDANPLSSL VSSRLGLWSR
LWEEYGKVKF LIYFQCFLTL KNGKLEFNIG IFILDSIKAP EEAIMASGTS SIYTSLIDQI
FPSPFIESRK DTQINTNLFY DNARQLAKSL PTVDVRRDKR LLSDLLPFQR RSLEWMIHRE
KDSSKDSCSL PPLWNEYQLP HNDRKVFVNR TYGYITLSKE NVFQLAPAAL KGGVLADEMG
MGKTLEVLSL VLFHQPPIDK LLSTQFDSVL QKNVIFSKAT LIITPSTILD QWISEVELHV
PSLKISHYKG IRKSSGSFSL DQFLDADIVI TSYSDLRFEL LYAESFSRNL RHEKRHVPPK
SPLIDICWWR ICVDEAQMVE TSQSNVAQMI YRIPRVNCWA VSGTPVRGNV DDLFGLLFLF
RYSPIYQHRK QTWIQIMELN RVHEFCDIFS PLVCRNCKQD IAHELRLPPQ HRRYMPTRLT
VVEETNYQDL LTEAAKSLKY LDDQLLDLSQ LDTMKRWLIR LRQACCHPQV GSGNKSAFGG
GPMKSINDVL MFMLEQTNSS LSSTKRQFFS DVVTTGWVFD HLQDYGKALA IWNEILPTVE
TVVVDLEGAI SRTEIDPDES KSHLNLSYAG LNYPGNIRAW QVLLHKVYFF IASTNFALKN
EELEKKYYSL AQDLRRKMMS DIIKKTSKHI DEFGKQFSRK NFVVLPKLPK ASSKGTILSY
LVVEDYEQLR EQLNLQAESL VKFRDRLIYL MKLPLLDQES DPTGDEYEES LNAQSEISYC
IDVYRQMISD RVAAIDGTIN TFVSHETELE KYKLLENIEN AQEIGEKETE ERNKKYMLFF
EEREEARPKT NEYGTFENIL ARLADALGRS NTSSEYTIAQ RLFEQLNEVT KDQSKTCRKL
EKELSLIQLT YNMRIDYYKH LQEISDSLIP PTAPKVSQSQ ASYIKMEQKD LFESALRHAE
EKYNKKLEEE EQSSKSKPAS ESLDEMISRI DIPAHLLLLK ELSTEKQNNL RKIGHFESRL
RYLSNLYEHA VFKAGSKQQC IICRDIIKKG FITTCGHFYC KDCLVAWLKH HPSCPMCKSK
LTKNSAYYIG EGFDIRLRQE FVLGFPNKEK DLEVMDEETL KQIVSIPLKV SFGSKIDAIV
RHLTYLKRIE LYPKVVVFSQ WLDVLEVLHK SFEANGVSYL RFDGKTKISC LKNFKADRDI
EVLTLHSRSQ SAGLTLTNAT HVIMCKFRES RKNYQKLLKK TVWEYITNGV GEPLLNSGIE
LQAISRVHRI GQTRPTYVYY YIVEDTVEDH IMSMSIQKHK QLGRLGLDVP LIGSIQRSTD
SSFGGEVVDE SEIRECLKTA LKRLDLEGEE GL
//
