MIT1_SCHPO
ID MIT1_SCHPO Reviewed; 1418 AA.
AC Q9P793;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chromatin remodeling factor mit1;
DE EC=3.6.4.-;
DE AltName: Full=Mi2-like interacting with clr3 protein 1;
DE AltName: Full=Snf2/Hdac-containing repressor complex protein mit1;
DE Short=SHREC protein mit1;
GN Name=mit1; ORFNames=SPBP35G2.10;
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).
RN [3]
RP FUNCTION, INTERACTION WITH CLR3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-587.
RX PubMed=17289569; DOI=10.1016/j.cell.2006.12.035;
RA Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R.,
RA Grewal S.I.S.;
RT "SHREC, an effector complex for heterochromatic transcriptional
RT silencing.";
RL Cell 128:491-504(2007).
CC -!- FUNCTION: Required for proper positioning of nucleosomes at
CC heterochromatic loci and for transcriptional gene silencing (TGS)
CC function of the Snf2/Hdac-containing repressor complex (SHREC).
CC {ECO:0000269|PubMed:17289569}.
CC -!- SUBUNIT: Interacts with clr3. {ECO:0000269|PubMed:17289569}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome,
CC telomere. Note=Associates with major heterochromatin, centromeres, sub-
CC telomeres, rDNA and the mat locus.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB87372.1; -; Genomic_DNA.
DR RefSeq; NP_595385.1; NM_001021292.2.
DR PDB; 5IKF; X-ray; 2.80 A; A=1156-1417.
DR PDB; 6FTO; X-ray; 1.60 A; C=1-81.
DR PDBsum; 5IKF; -.
DR PDBsum; 6FTO; -.
DR AlphaFoldDB; Q9P793; -.
DR SMR; Q9P793; -.
DR BioGRID; 277847; 24.
DR STRING; 4896.SPBP35G2.10.1; -.
DR PaxDb; Q9P793; -.
DR EnsemblFungi; SPBP35G2.10.1; SPBP35G2.10.1:pep; SPBP35G2.10.
DR GeneID; 2541336; -.
DR KEGG; spo:SPBP35G2.10; -.
DR PomBase; SPBP35G2.10; mit1.
DR VEuPathDB; FungiDB:SPBP35G2.10; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_005007_0_0_1; -.
DR InParanoid; Q9P793; -.
DR OMA; HQDMQAI; -.
DR PhylomeDB; Q9P793; -.
DR PRO; PR:Q9P793; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0070824; C:SHREC complex; IDA:PomBase.
DR GO; GO:0110129; C:SHREC2 complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IDA:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
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; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR040934; Znf-CCCH_6.
DR InterPro; IPR041299; Znf-CCCH_7.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF18585; zf-CCCH_6; 1.
DR Pfam; PF18586; zf-CCCH_7; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Centromere; Chromosome; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Telomere;
KW Zinc; Zinc-finger.
FT CHAIN 1..1418
FT /note="Chromatin remodeling factor mit1"
FT /id="PRO_0000339420"
FT DOMAIN 568..738
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 875..1034
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 212..271
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 215..269
FT /note="RING-type; atypical"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 581..588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 587
FT /note="K->A: Weak silencing defect."
FT /evidence="ECO:0000269|PubMed:17289569"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:6FTO"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6FTO"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6FTO"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:6FTO"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6FTO"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6FTO"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6FTO"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6FTO"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6FTO"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:6FTO"
FT HELIX 1223..1230
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1241..1253
FT /evidence="ECO:0007829|PDB:5IKF"
FT STRAND 1286..1289
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1293..1301
FT /evidence="ECO:0007829|PDB:5IKF"
FT STRAND 1306..1308
FT /evidence="ECO:0007829|PDB:5IKF"
FT TURN 1312..1314
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1324..1326
FT /evidence="ECO:0007829|PDB:5IKF"
FT STRAND 1330..1332
FT /evidence="ECO:0007829|PDB:5IKF"
FT TURN 1334..1336
FT /evidence="ECO:0007829|PDB:5IKF"
FT STRAND 1337..1339
FT /evidence="ECO:0007829|PDB:5IKF"
FT STRAND 1342..1345
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1348..1350
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1353..1364
FT /evidence="ECO:0007829|PDB:5IKF"
FT HELIX 1370..1381
FT /evidence="ECO:0007829|PDB:5IKF"
SQ SEQUENCE 1418 AA; 162633 MW; DFEFD1A14D9D4BDB CRC64;
MPKEDDSLCK IVVRREPLDV LLPYYDASET TVQKILHEND STLSVKFLAG VEALIKKDEL
DKYKNGKACL RVWLKHKSRK RYHGYMTSTD KDEEEKNDYL LKSNGSKVLR DSTRTKKFKF
GKEFHCALNP SFVSDETASD SATSSSSDTN KKVNRKEHNE LSLSHLSFND TSDFGSSDLS
SSEIESTEND NKAPYFSLLY SDGFDFIKFL HVCVCVKCHG REHRSSGKNF VYCDHCSNVY
HYDCSPLPSL NKETRNYSQQ NGFICPLCSK NSKDVLCNTG FVSGVSSGQD LVIPPSLADR
ESLSILVNYC KSIRFRCFRC RRVEYFFYLD SNPLSIQRTI THFIKKLVCN ECSMHPCDIE
EIIAWRTLNS LYPSKATLSN NFVSTSDLSF WSREYFVRSK GKSYLHCFWC SASWLAGISL
AKKKNFDGLE NASYDATKPI IPVSYTIIDK VWDVQYRSGK NARTAKYKTK KHQLKAISEV
TFAFVSWRGL TYYMSNWEPP PKETDRNRWK AWLKGYSDLL ECLWIEKAPT ASINIDLPFT
NLEWHSQPSF IKGGTLMPYQ LKGLNWLYLR WYTHHPCILA DEMGLGKTVQ VISFISVLFY
RHKCFPVLVI VPHATVANWE RELKKWAPFL QINVLVGSEK NRSLVRDYRL INQKDPKHVS
THVLVISASN VEREISLLRK FQWKVLIVDE GQRLKNDQSS LFYYLSSVKS DFKLLLTGTP
LQNNVRELFN LLQFLNPMKI NAAELEKRYS IIDTEKVTEL HQILKPFFLR RVKSEVLDNF
PTKVEVIIPL SMTPVQKGLY KSILSKNLSL LRNITGYANT SSSGGQRTTS LNNILMQLRK
TLAHPYIYSP DIEDRNLPYE LAMRSLEEAS CKFLILRLLV PKLITRGHRI LLFSQFIQQL
DILEDWFEYK NIAYARFDGA SSEMERQSAI DSFNAPNSEL SCFLLSTRAG GVGINLASAD
TVIILDPDFN PHQDMQAIAR AHRYGQKKKV LVFVLTTRDS VEEKIIQNAQ KKLVLDHLIV
ESLDQNHNSE KDLESILRHG ARALFEEAGD EPSIKYNEYS VELLISEAEK QEDTSTDESD
IKSNKFGFFR VWDNKHISSN HYEVKENVLV DEEDVWSVIL KQREKDAMLE KTDETTSNRR
LRAHHKIHYG EDLNIYDNSD DTDYTVNDRS SPGSPFPIET ETISSITDTL SDKQKLKYDS
SVNIENLNDE SDSQKSADVH FDSILAKSLL ATTPKEDEFN KTLSTINLEV ANKLTSSEYI
NDSEMQLIDD PVFYPPYEII EKNHQLVGRS LSKAVLDNFF LLSSLSDNVR CRCCGIKHLP
AHCPLSIVPL EICFLCGTPH FSGRDTCPML RNKEAIYRLK DSLSKSREPF HIKKQAMARL
NSFLQKKEEP TVSSSAKTNE LSSKVIIKES IINEAKTL
