HRP3_SCHPO
ID HRP3_SCHPO Reviewed; 1388 AA.
AC O14139;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Chromodomain helicase hrp3;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase hrp3;
GN Name=hrp3; ORFNames=SPAC3G6.01;
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 GENE NAME, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12127990; DOI=10.1016/s0006-291x(02)00797-0;
RA Yoo E.J., Jang Y.K., Lee M.A., Bjerling P., Kim J.B., Ekwall K.,
RA Seong R.H., Park S.D.;
RT "Hrp3, a chromodomain helicase/ATPase DNA binding protein, is required for
RT heterochromatin silencing in fission yeast.";
RL Biochem. Biophys. Res. Commun. 295:970-974(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1250 AND SER-1285, AND
RP 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: Involved in heterochromatin silencing. Required for
CC transcriptional repression at the silence loci of mat3, where it has a
CC direct role as a chromatin remodeling factor.
CC {ECO:0000269|PubMed:12127990}.
CC -!- INTERACTION:
CC O14139; P40381: swi6; NbExp=2; IntAct=EBI-7414157, EBI-926939;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12127990}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16277.1; -; Genomic_DNA.
DR PIR; T38720; T38720.
DR RefSeq; NP_594967.1; NM_001020398.2.
DR AlphaFoldDB; O14139; -.
DR SMR; O14139; -.
DR BioGRID; 279497; 295.
DR IntAct; O14139; 3.
DR MINT; O14139; -.
DR STRING; 4896.SPAC3G6.01.1; -.
DR iPTMnet; O14139; -.
DR SwissPalm; O14139; -.
DR MaxQB; O14139; -.
DR PaxDb; O14139; -.
DR PRIDE; O14139; -.
DR EnsemblFungi; SPAC3G6.01.1; SPAC3G6.01.1:pep; SPAC3G6.01.
DR PomBase; SPAC3G6.01; hrp3.
DR VEuPathDB; FungiDB:SPAC3G6.01; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; O14139; -.
DR OMA; CSWGARE; -.
DR PhylomeDB; O14139; -.
DR PRO; PR:O14139; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
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:0031491; F:nucleosome binding; IDA:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041150; Cdh1_DBD.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR025260; DUF4208.
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; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF13907; DUF4208; 1.
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; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
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; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1388
FT /note="Chromodomain helicase hrp3"
FT /id="PRO_0000080242"
FT DOMAIN 191..260
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 288..349
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 387..557
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 694..852
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 22..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 508..511
FT /note="DEAH box"
FT COMPBIAS 22..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1388 AA; 159379 MW; F7B431084BD29F8D CRC64;
MSTSAIALAL SSSKAIEQLD HVQTETPNLK QEMSESPSNS GVASKRKLQS TEWLDPELYG
LRRSGRTRSN PGRYVDTDDQ EDVFPSKHRK GTRNGSSFSR HRTIRDLDDE AESVTSEESE
SDDSSYGGTP KKRSRQKKSN TYVQDEIRFS SRNSKGVNYN EDAYFESFEE EEEEEMYEYA
TEVSEEPEDT RAIDVVLDHR LIEGHDGSTP SEDYEFLIKW VNFSHLHCTW EPYNNISMIR
GSKKVDNHIK QVILLDREIR EDPTTTREDI EAMDIEKERK RENYEEYKQV DRIVAKHLNS
DGSVEYLVKW KQLLYDFCTW EASSIIEPIA ATEIQAFQER EESALSPSRG TNYGNSRPKY
RKLEQQPSYI TGGELRDFQL TGVNWMAYLW HKNENGILAD EMGLGKTVQT VAFLSYLAHS
LRQHGPFLVV VPLSTVPAWQ ETLALWASDM NCISYLGNTT SRQVIRDYEF YVDGTQKIKF
NLLLTTYEYV LKDRSVLSNI KWQYMAIDEA HRLKNSESSL YEALSQFKNS NRLLITGTPL
QNNIRELAAL VDFLMPGKFE IREEINLEAP DEEQEAYIRS LQEHLQPYIL RRLKKDVEKS
LPSKSERILR VELSDLQMYW YKNILTRNYR VLTQSISSGS QISLLNIVVE LKKASNHPYL
FDGVEESWMQ KINSQGRRDE VLKGLIMNSG KMVLLDKLLS RLRRDGHRVL IFSQMVRMLD
ILGDYLSLRG YPHQRLDGTV PAAVRRTSID HFNAPNSPDF VFLLSTRAGG LGINLMTADT
VIIFDSDWNP QADLQAMARA HRIGQKNHVM VYRLLSKDTI EEDVLERARR KMILEYAIIS
LGVTDKQKNS KNDKFSAEEL SAILKFGASN MFKAENNQKK LEDMNLDEIL EHAEDHDTSN
DVGGASMGGE EFLKQFEVTD YKADVSWDDI IPLTEREKFE EEDRLREEEE ALKQEIELSS
RRGNRPYPSS AVESPSYSGT SERKSKKQML KDEVLLEKEI RLLYRAMIRY GSLEHRYNDI
VKYADLTTQD AHVIKKIAAD LVTASRKAVS AAEKDLSNDQ SNNKSSRKAL LITFKGVKNI
NAETLVQRLN DLDILYDAMP TSGYSNFQIP MHVRSVHGWS CQWGPREDSM LLSGICKHGF
GAWLEIRDDP ELKMKDKIFL EDTKQTDNSV PKDKENKEKK VPSAVHLVRR GEYLLSALRE
HHQNFGIKSS PAISTNGKTQ PKKQTANRRQ SGKPNVKSAQ KIESATRTPS PAISESRKKP
SSKDTKIETP SREQSRSQTA SPVKSEKDDG NVSLNAEQKA RCKELMYPVR KHMKRLRKDS
SGLGRAELVK LLTECLTTIG KHIEKTVNDT PSEEKATVRK NLWMFACYFW PKEEVKYTSL
ISMYEKMK
