RHP16_SCHPO
ID RHP16_SCHPO Reviewed; 861 AA.
AC P79051; O74911; Q9UU12; Q9UU98;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP-dependent helicase rhp16;
DE EC=3.6.4.-;
DE AltName: Full=DNA repair protein rhp16;
DE AltName: Full=RAD16 homolog;
GN Name=rhp16; ORFNames=SPCC330.01c, SPCC613.13c;
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 [GENOMIC DNA].
RX PubMed=8879272; DOI=10.1016/0921-8777(96)00010-9;
RA Bang D.D., Ketting R., de Ruijter M., Brandsma J.A., Verhage R.A.,
RA de Putte P., Brouwer J.;
RT "Cloning of Schizosaccharomyces pombe rph16+, a gene homologous to the
RT Saccharomyces cerevisiae RAD16 gene.";
RL Mutat. Res. 364:57-71(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 538-722, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION.
RX PubMed=10446227; DOI=10.1093/nar/27.17.3410;
RA Lombaerts M., Peltola P.H., Visse R., den Dulk H., Brandsma J.A.,
RA Brouwer J.;
RT "Characterization of the rhp7(+) and rhp16(+) genes in Schizosaccharomyces
RT pombe.";
RL Nucleic Acids Res. 27:3410-3416(1999).
RN [5]
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: Involved in global genome repair (GGR) via nucleotide
CC excision repair (NER), in conjunction with rhp7, after UV irradiation.
CC {ECO:0000269|PubMed:10446227}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA21065.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S83324; AAB49515.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21065.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB027876; BAA87180.1; -; Genomic_DNA.
DR PIR; T41479; T41479.
DR PIR; T52472; T52472.
DR RefSeq; NP_587701.1; NM_001022696.2.
DR AlphaFoldDB; P79051; -.
DR SMR; P79051; -.
DR STRING; 4896.SPCC330.01c.1; -.
DR MaxQB; P79051; -.
DR PaxDb; P79051; -.
DR GeneID; 2538860; -.
DR KEGG; spo:SPCC330.01c; -.
DR PomBase; SPCC330.01c; rhp16.
DR eggNOG; KOG1002; Eukaryota.
DR InParanoid; P79051; -.
DR PhylomeDB; P79051; -.
DR PRO; PR:P79051; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000109; C:nucleotide-excision repair complex; IPI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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:0003677; F:DNA binding; IC: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; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IGI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP: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; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..861
FT /note="ATP-dependent helicase rhp16"
FT /id="PRO_0000056131"
FT DOMAIN 268..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 695..848
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 609..652
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 393..396
FT /note="DEAH box"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 100..105
FT /note="ANPNTG -> VKSQYR (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..123
FT /note="KRSLRSSNLKKKF -> NVIKVLEFEKV (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 425..426
FT /note="LQ -> FE (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 506..514
FT /note="HSLLKHIML -> DSLSMV (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..527
FT /note="ADDLGL -> RIPWI (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 536..537
FT /note="KD -> R (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
FT CONFLICT 808..809
FT /note="RP -> GR (in Ref. 1; AAB49515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 861 AA; 98003 MW; 092EF1E4E0D16052 CRC64;
MGTSCNKINS NSNKGKENMH FVLDDNGDSK GNASNQQVER DDKLDMETTR WNGKEFEEPL
STNKKLIIQS NNTSSQHSTP PLSISDTSTH TGSSTDNVEA NPNTGFSSAR KRSLRSSNLK
KKFVPLSSPE ESNESEFIDD DESDEVASII DIKEDETFDS KVEIPEAAPS SSTESDEESI
PLSYQSKRRR VSARASSSAS SSSRTQAKSI PSHERTHYRL IRQHPELEHV WEKLEEEAPR
EVKQIEQPKE LVLNLLPFQR EGVYWLKRQE DSSFGGGILA DEMGMGKTIQ TIALLLSEPR
GKPTLVVAPV VAIMQWKEEI DTHTNKALST YLYYGQARDI SGEELSSYDV VLTSYNVIES
VYRKERSGFR RKNGVVKEKS LLHQMEFYRI ILDEAHGIKS RTCNTARAVC GLRTTRKICL
SGTPLQNRIG ELFSLLRFLR ADPFAYYYCL QCECKSLHWR FSDRSNCDEC GHKPMSHTCY
FNAEMLKPIQ KFGYEGPGKL AFKKVHSLLK HIMLRRTKLE RADDLGLPPR VVEVRKDLFN
EEEEDVYQSL YMDSKRKFNT YLAEGVVLNN YANIFQLITR MRQMADHPDL VLASKRKTVD
IENQENIVCK ICDEVAQDAI ESRCHHTFCR LCVTEYINAA GDGENVNCPS CFIPLSIDLS
APALEDFSEE KFKNASILNR IDMNSWRSST KIEALVEELY LLRKKDRTLK SIVFSQFTSM
LDLIHWRLRK AGFNCVKLDG GMTPKARAAT IEAFSNDINI TIFLVSLKAG GVALNLTEAS
QVFMMDPWWN GAVQWQAMDR IHRIGQKRPI KVITLCIENS IESKIIELQE KKAQMIHATI
DQDEKALNQL SVEDMQFLFS N
