HRP1_SCHPO
ID HRP1_SCHPO Reviewed; 1373 AA.
AC Q9US25; Q92369; Q9UU28;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Chromodomain helicase hrp1;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase hrp1;
GN Name=hrp1; ORFNames=SPAC1783.05;
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 [GENOMIC DNA].
RC STRAIN=JY741;
RX PubMed=9520266; DOI=10.1007/s004380050653;
RA Jin Y.H., Yoo E.J., Jang Y.K., Kim S.H., Kim M.J., Shim Y.S., Lee J.S.,
RA Choi I.S., Seong R.H., Hong S.H., Park S.D.;
RT "Isolation and characterization of hrp1+, a new member of the SNF2/SWI2
RT gene family from the fission yeast Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 257:319-329(1998).
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 852-1021.
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 CHARACTERIZATION.
RX PubMed=10756203; DOI=10.1093/nar/28.9.2004;
RA Yoo E.J., Jin Y.H., Jang Y.K., Bjerling P., Tabish M., Hong S.H.,
RA Ekwall K., Park S.D.;
RT "Fission yeast hrp1, a chromodomain ATPase, is required for proper
RT chromosome segregation and its overexpression interferes with chromatin
RT condensation.";
RL Nucleic Acids Res. 28:2004-2011(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-145; THR-1259;
RP SER-1260 AND THR-1264, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Seems to play a role in mitotic chromosome segregation and
CC maintenance of chromatin structure. Has ATPase activity.
CC -!- INTERACTION:
CC Q9US25; O59797: SPCC364.06; NbExp=2; IntAct=EBI-7414005, EBI-7414085;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; X99021; CAA67494.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB66168.1; -; Genomic_DNA.
DR EMBL; AB027852; BAA87156.1; -; Genomic_DNA.
DR PIR; T43334; T43334.
DR PIR; T50107; T50107.
DR RefSeq; NP_593660.1; NM_001019092.2.
DR AlphaFoldDB; Q9US25; -.
DR SMR; Q9US25; -.
DR BioGRID; 278827; 77.
DR IntAct; Q9US25; 7.
DR MINT; Q9US25; -.
DR STRING; 4896.SPAC1783.05.1; -.
DR iPTMnet; Q9US25; -.
DR MaxQB; Q9US25; -.
DR PaxDb; Q9US25; -.
DR PRIDE; Q9US25; -.
DR EnsemblFungi; SPAC1783.05.1; SPAC1783.05.1:pep; SPAC1783.05.
DR GeneID; 2542363; -.
DR KEGG; spo:SPAC1783.05; -.
DR PomBase; SPAC1783.05; hrp1.
DR VEuPathDB; FungiDB:SPAC1783.05; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; Q9US25; -.
DR OMA; YLWHRNE; -.
DR PhylomeDB; Q9US25; -.
DR PRO; PR:Q9US25; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0140673; P:co-transcriptional chromatin reassembly; TAS:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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 Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1373
FT /note="Chromodomain helicase hrp1"
FT /id="PRO_0000080241"
FT DOMAIN 203..276
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 304..365
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 402..573
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 708..869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 524..527
FT /note="DEAH box"
FT COMPBIAS 10..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 68
FT /note="I -> M (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="S -> R (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> G (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> S (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> M (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..489
FT /note="NIREYEFYLST -> ILESM (in Ref. 1; CAA67494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1373 AA; 158549 MW; 7ABAFA7BD4C2503B CRC64;
MEPEHSNYDL KNHPTSVQES TLNGSAVTDP QFGNTTNSLP SMNGLLNHEN SFASQQSLSS
SAFDDSEIVT STANSTVVSS ALSTPKIDDA QNSDDVRVDG TRRSSRAKRP VYRDFSYTEI
DEHEIPIPKK RKSKPAPKQK KSVASDDEDA YDKRHRFSIN SASGTEIRTS LRSSKGKSVN
YNEQEFYDDF EDEEEEVEEQ VEEEYEPIID FVLNHRKRAD AQDDDPKSSY QYLIKWQEVS
HLHNTWEDYS TLSSVRGYKK VDNYIKQNII YDREIREDPT TTFEDIEALD IERERKNMLF
EEYKIVERIV ASETNEEGKT EYFVKWRQLP YDNCTWEDAD VIYSMAPNEV YQFLQRENSP
YLPYKGVFYN TRPPYRKLEK QPSYIKGGEI RDFQLTGINW MAYLWHRNEN GILADEMGLG
KTVQTVCFLS YLVHSLKQHG PFLIVVPLST VPAWQETLAN WTPDLNSICY TGNTESRANI
REYEFYLSTN SRKLKFNILL TTYEYILKDK QELNNIRWQY LAIDEAHRLK NSESSLYETL
SQFRTANRLL ITGTPLQNNL KELASLVNFL MPGKFYIRDE LNFDQPNAEQ ERDIRDLQER
LQPFILRRLK KDVEKSLPSK SERILRVELS DMQTEWYKNI LTKNYRALTG HTDGRGQLSL
LNIVVELKKV SNHPYLFPGA AEKWMMGRKM TREDTLRGII MNSGKMVLLD KLLQRLKHDG
HRVLIFSQMV RMLNILGEYM SLRGYNYQRL DGTIPASVRR VSIDHFNAPD SPDFVFLLST
RAGGLGINLN TADTVIIFDS DWNPQADLQA MARAHRIGQK NHVNVYRFLS KDTVEEDILE
RARRKMILEY AIISLGVTEK SKNSKNDKYD AQELSAILKF GASNMFKATE NQKKLENMNL
DDILSHAEDR DSSNDVGGAS MGGEEFLKQF EVTDYKAEDL NWDDIIPEEE MERIEEEERM
LAAQRAKEEE RERREEEERE NDEDHPSRTY KRTTKSITKR QQRREEMVRE KEIRLLYRAM
IKFGLVDERF DTIVKEAELQ ATDPKRIYSL SADMVKACDE AVERLGADDT KNKQPRKAIL
IEFKGVKNIN AETVTLRVKD LTHLHRAYKG LDPLKQIIGY PIRSVHSWNC SWGIKEDSML
LAGINKHGFG CWQAIKNDPD LGLHDKIFLD EAKNDKESRY VPSAVHLVRR GEYLLSVVRE
HPDLFVVKTD QPTKRKYNRK APTKSSTRQT TLDGSISNTK KSSRTKKKKE EETNRGDETS
PEGTVGEDEV EEEPRQAEPP KRALRSNSGK AASNKRTTRN SMKTHSAMDT LTAVAALDAE
LDNMSNEKAK EEVDHVKSEN GESVNEPNTE DLSLETEENT TVSDISPLVK NEA
