SNF21_SCHPO
ID SNF21_SCHPO Reviewed; 1199 AA.
AC Q9UTN6; O14024;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Chromatin structure-remodeling complex subunit snf21;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase snf21;
DE AltName: Full=RSC complex subunit snf21;
GN Name=snf21; ORFNames=SPAC1250.01, SPAC29A4.21;
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 RSC COMPLEX, FUNCTION OF THE RSC 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 chromatin structure remodeling
CC complex (RSC), which is involved in transcription regulation and
CC nucleosome positioning. Controls particularly membrane and organelle
CC development genes. {ECO:0000269|PubMed:14988732,
CC ECO:0000269|PubMed:18622392}.
CC -!- SUBUNIT: Component of the RSC complex composed of at least arp9, arp42,
CC rsc1, rsc4, rsc7, rsc9, rsc58, sfh1, snf21, ssr1, ssr2, ssr3 and ssr4.
CC The complex interacts with histone and histone variant components of
CC centromeric chromatin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:16823372}. Note=Localizes to centromeric and
CC flanking chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AB162438; BAD11105.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB54824.1; -; Genomic_DNA.
DR PIR; T37561; T37561.
DR RefSeq; NP_594861.1; NM_001020290.2.
DR AlphaFoldDB; Q9UTN6; -.
DR SMR; Q9UTN6; -.
DR BioGRID; 279092; 23.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48388N; -.
DR IntAct; Q9UTN6; 12.
DR STRING; 4896.SPAC1250.01.1; -.
DR iPTMnet; Q9UTN6; -.
DR MaxQB; Q9UTN6; -.
DR PaxDb; Q9UTN6; -.
DR PRIDE; Q9UTN6; -.
DR EnsemblFungi; SPAC1250.01.1; SPAC1250.01.1:pep; SPAC1250.01.
DR GeneID; 2542638; -.
DR KEGG; spo:SPAC1250.01; -.
DR PomBase; SPAC1250.01; snf21.
DR VEuPathDB; FungiDB:SPAC1250.01; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; Q9UTN6; -.
DR OMA; YGPGHRY; -.
DR PhylomeDB; Q9UTN6; -.
DR PRO; PR:Q9UTN6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140463; F:chromatin-protein adaptor; EXP:PomBase.
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; IC:ComplexPortal.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0061780; P:mitotic cohesin loading; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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; 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; PF07529; HSA; 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; SM00573; HSA; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Bromodomain; Chromatin regulator; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1199
FT /note="Chromatin structure-remodeling complex subunit
FT snf21"
FT /id="PRO_0000074359"
FT DOMAIN 256..328
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 429..594
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 740..903
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1084..1154
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1017..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 544..547
FT /note="DEGH box"
FT COMPBIAS 1017..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 442..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1199 AA; 140089 MW; 1AD1C7299C4D0028 CRC64;
MRAEKQYTRN EVEETIVRWK KLKESGATEH DNTEYAQLCD VLRSAQSEIE ARRDLKGHIK
RCFSSVDKNT EKLILKQQVL AYKKLSQNLP APDDCILSVL LRLSKDEQLL QSIVKQPLQN
SKVDGKVRRD FGSCQITPSA KQQRKYLQYQ ISEDDAIKNR MFRRMSDLES YPAVMRDVAE
LKDDNERLNL DTIKRNALVE LKKLRLIKQQ ESLRHQVMHC QPHLRTIVNA VERMSCRRPK
LVPQATRLTE VLERQQRSDR ERRLKQKQCD YLQTVCAHGR EINVRTKNAQ ARAQKANRAV
LAYHSHIEKE EQRRAERNAK QRLQALKEND EEAYLKLIDQ AKDTRITHLL RQTDHYLDSL
AAAVKVQQSQ FGESAYDEDM DRRMNPEDDR KIDYYNVAHN IREVVTEQPS ILVGGKLKEY
QLRGLQWMIS LYNNHLNGIL ADEMGLGKTI QTISLITHLI EKKRQNGPFL VIVPLSTLTN
WTMEFERWAP SIVKIVYKGP PQVRKALHPQ VRHSNFQVLL TTYEYIIKDR PLLSRIKWIY
MIIDEGHRMK NTQSKLTNTL TTYYSSRYRL ILTGTPLQNN LPELWALLNF VLPRIFNSIK
SFDEWFNTPF ANTGGQDKME LTEEESLLVI RRLHKVLRPF LLRRLKKDVE AELPDKVEKV
IRCQMSGLQQ KLYYQMKKHG MLYVEDAKRG KTGIKGLQNT VMQLKKICNH PFVFEDVERS
IDPTGFNYDM LWRVSGKFEL LDRILPKLFR SGHRILMFFQ MTQIMNIMED YLHYRQWRYL
RLDGSTKADD RSKLLGVFND PTAEVNLFLL STRAGGLGLN LQTADTVIIF DSDWNPHQDL
QAQDRAHRIG QTKEVRIYRL ITEKSVEENI LARAQYKLDI DGKVIQAGKF DNKSTPEERE
AFLRSLLENE NGEEENDEKG ELDDDELNEI LARGDDELRL FKQMTEDLER ESPYGKNKEK
ERLIQVSELP EFYQREEPEK TTDLLQEEPL GRGARRRTPV VYDEAVRDAQ WMAEMDMESE
ARPTRGRPKR NIASVDETPA LTLNGKPKKK RGPAPDTLTS EHRSLLRRVC LEIYKAVNEL
EDDNGRPLNK LFLELPSKKL YPDYYMIIKS PIALDAIRKH INGTFYKTLE AMKSDLMTMF
NNARTYNEEG SFVYEDANKM QTAMETKIEE LEEDGTLATL RGMEAEATSQ LEDRIENEA
