SNF22_SCHPO
ID SNF22_SCHPO Reviewed; 1680 AA.
AC O94421; Q9UU97;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=SWI/SNF chromatin-remodeling complex subunit snf22;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase snf22;
DE AltName: Full=SWI/SNF complex subunit snf22;
GN Name=snf22; ORFNames=SPCC1620.14c, SPCC830.01c;
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], AND FUNCTION.
RX PubMed=14988732; DOI=10.1038/sj.emboj.7600138;
RA Yamada T., Mizuno K., Hirota K., Kon N., Wahls W.P., Hartsuiker E.,
RA Murofushi H., Shibata T., Ohta K.;
RT "Roles of histone acetylation and chromatin remodeling factor in a meiotic
RT recombination hotspot.";
RL EMBO J. 23:1792-1803(2004).
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 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 [4]
RP IDENTIFICATION IN THE SWI/SNF COMPLEX, FUNCTION OF THE SWI/SNF COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18622392; DOI=10.1038/nsmb.1452;
RA Monahan B.J., Villen J., Marguerat S., Baehler J., Gygi S.P., Winston F.;
RT "Fission yeast SWI/SNF and RSC complexes show compositional and functional
RT differences from budding yeast.";
RL Nat. Struct. Mol. Biol. 15:873-880(2008).
CC -!- FUNCTION: Helicase. Component of the SWI/SNF complex, an ATP-dependent
CC chromatin remodeling complex, required for the positive and negative
CC regulation of gene expression of a large number of genes. It changes
CC chromatin structure by altering DNA-histone contacts within a
CC nucleosome, leading eventually to a change in nucleosome position, thus
CC facilitating or repressing binding of gene-specific transcription
CC factors. {ECO:0000269|PubMed:14988732, ECO:0000269|PubMed:18622392}.
CC -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC complex composed of at least arp9, arp42, snf5, snf22, snf30, sbf59,
CC sol1, ssr1, ssr2, ssr3, ssr4 and tfg3. {ECO:0000269|PubMed:18622392}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AB162437; BAD11104.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA22498.1; -; Genomic_DNA.
DR PIR; T41628; T41628.
DR RefSeq; NP_588472.2; NM_001023463.2.
DR AlphaFoldDB; O94421; -.
DR SMR; O94421; -.
DR BioGRID; 275460; 19.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-48377N; -.
DR IntAct; O94421; 11.
DR STRING; 4896.SPCC1620.14c.1; -.
DR iPTMnet; O94421; -.
DR MaxQB; O94421; -.
DR PaxDb; O94421; -.
DR PRIDE; O94421; -.
DR EnsemblFungi; SPCC1620.14c.1; SPCC1620.14c.1:pep; SPCC1620.14c.
DR GeneID; 2538881; -.
DR KEGG; spo:SPCC1620.14c; -.
DR PomBase; SPCC1620.14c; snf22.
DR VEuPathDB; FungiDB:SPCC1620.14c; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; O94421; -.
DR OMA; MIELRCL; -.
DR PhylomeDB; O94421; -.
DR PRO; PR:O94421; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; 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; IEA:InterPro.
DR GO; GO:0140751; F:histone octamer slider activity; NAS:PomBase.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1900400; P:regulation of iron ion import into cell by regulation of transcription from RNA polymerase II promoter; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Bromodomain; Chromatin regulator; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1680
FT /note="SWI/SNF chromatin-remodeling complex subunit snf22"
FT /id="PRO_0000074360"
FT DOMAIN 429..465
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 704..776
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 881..1046
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1191..1354
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1536..1606
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 61..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 996..999
FT /note="DEGH box"
FT COMPBIAS 61..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 894..901
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1680 AA; 189913 MW; 8D0B978979768775 CRC64;
MFAVQGNQKF PKGLTKDNIQ SLYQQWQVMR NQGATEENNP EFAQISSILR MVQRAHYARM
QQMRNQSSEF PDAENTNLRK QQDTLPTTGF NNLPEGKAGM QTLPGRPASN GPTPPNPGNG
NVGLNNPSYM NSQASPNIMN APLQRDTSVP PAPSMVHPHT NTNANSNNLK VYANQLSQQN
TSNPTYHNAY DMASMMKNGS RMNNSFPPTT PYPPANDTTV NSSLPHSFAS PSSTFEQPHT
VQSRAPSVDT TSSSHSFSAR NIPANVSMQQ QMGRRGSIPV NPSTFSASSP PSGSMLASPY
NGYQNDAASF AHSKLPSSAN PNTPFNSTAT VDVGAAGSHF PYPQPSNLDA INAKTYFQSS
SNSPAPYVYR NNLPPSATSF QPSSSRSPSV DPNTVKSAQH IPRMSPSPSA SALKTQSHVP
SAKVPPTSKL NHAQLAMLKS QIVAYNCLNS PNGQVPPAVQ QAIFGRVYGA SNEVSPSMPF
QQNVPQMSSV KKDTPTRDAN MRTSKAPYIQ NIPNQFQRRA YSATIPVKNE SLAKPSVSPM
PLQQSTGKTE VAKRAQFPTN VNYSSCVDPR TYVKTPIPFS KFSSSENLSL IPSLLPPSIS
WDDVFLSSEI AIACSIANRI DFLEKENRPK SVNKKILQQD KSKSMIELRC LRLLEKQRSL
RETINSVIPH SDSLAAGNLR LMFRNVKRQT MQEANLVLAL AEKQKTEHAM RQKEKLLTHL
RSIMLHRKSI VTKVDKQNKA KTQRCKDIIN FHAHLEKEEK KRIERSARQR LQALRADDEA
AYLQLLDKAK DTRITHLLKQ TDQYLENLTR AVRIQQSNIH SGNTSGKGSN SAELEAPISE
EDKNLDYFKV AHRIHEEVEQ PKIFVGGTLK DYQLKGLEWM LSLYNNNLNG ILADEMGLGK
TIQTIAFITY LIEKKNQQGP FLIIVPLSTL TNWIMEFEKW APSVKKIAYK GPPQLRKTLQ
SQIRSSNFNV LLTTFEYIIK DRPLLSRIKW VHMIIDEGHR IKNTQSKLTS TLSTYYHSQY
RLILTGTPLQ NNLPELWALL NFVLPKIFNS IKSFDEWFNT PFANTGGQDK IGLNEEEALL
IIKRLHKVLR PFLFRRLKKD VEKELPDKVE KVIKCPLSGL QLKLYQQMKK HGMLFVDGEK
GKTGIKGLQN TVMQLKKICN HPFIFEDVER AIDPSGTNVD LLWRAAGKFE LLDRILPKLF
LTGHKTLMFF QMTQIMTIME DYLRSKNWKY LRLDGSTKSD DRCSLLAQFN DPKSDVYIFM
LSTRAGGLGL NLQTADTVII FDTDWNPHQD LQAQDRAHRI GQTKEVRILR LITEKSIEEN
ILSRAQYKLD LDGKVIQAGK FDNKSTPEER EAFLRSLLEH DGDDDHDLTY GELQDDELNE
LISRTDEELV LFKKLDKERA ATDIYGKGKP LERLLTVNEL PDFYKVEVDS FAVQSSSELE
DQYLERKRRR RNSISYTELT LDELNTVDDP SSTLMPRKRG RPRKKTNSGS SLSTPLSQES
SLARSGRKNT PSYKQKALRR YCMEIFERLY NLQSEDGRFV NGLFLYPPNR KLYPDYYIII
KRPIALGKIK RNIKNDRYGD VGELIADFML MFNNAYTYNE EHSIVYEDAK LMEKTLKEVI
EDLEKNNSLH AYEEEALNEE QASLVFLENS EAELPLDSGI VSAEDDKVIT YEDSSSSYSE
