CSB_ORYSJ
ID CSB_ORYSJ Reviewed; 1187 AA.
AC Q7F2E4; A0A0N7KC63; Q655K6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DNA excision repair protein CSB {ECO:0000305};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=Cockayne syndrome protein CSB {ECO:0000305};
DE Short=OsCSB {ECO:0000303|PubMed:15150342};
GN Name=CSB {ECO:0000305};
GN OrderedLocusNames=Os01g0102800 {ECO:0000312|EMBL:BAF03666.1},
GN LOC_Os01g01312 {ECO:0000305};
GN ORFNames=P0402A09.26 {ECO:0000312|EMBL:BAB62641.1},
GN P0455C04.20 {ECO:0000312|EMBL:BAB92143.1},
GN P0672D08.47 {ECO:0000312|EMBL:BAD45511.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15150342; DOI=10.1093/nar/gkh591;
RA Kimura S., Tahira Y., Ishibashi T., Mori Y., Mori T., Hashimoto J.,
RA Sakaguchi K.;
RT "DNA repair in higher plants; photoreactivation is the major DNA repair
RT pathway in non-proliferating cells while excision repair (nucleotide
RT excision repair and base excision repair) is active in proliferating
RT cells.";
RL Nucleic Acids Res. 32:2760-2767(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP INDUCTION BY GAMMA IRRADIATION.
RX PubMed=25124817; DOI=10.1093/jhered/esu025;
RA Hayashi G., Shibato J., Imanaka T., Cho K., Kubo A., Kikuchi S., Satoh K.,
RA Kimura S., Ozawa S., Fukutani S., Endo S., Ichikawa K., Agrawal G.K.,
RA Shioda S., Fukumoto M., Rakwal R.;
RT "Unraveling low-level gamma radiation--responsive changes in expression of
RT early and late genes in leaves of rice seedlings at Iitate Village,
RT Fukushima.";
RL J. Hered. 105:723-738(2014).
CC -!- FUNCTION: Essential factor involved in transcription-coupled nucleotide
CC excision repair (TCR) which allows RNA polymerase II-blocking lesions
CC to be rapidly removed from the transcribed strand of active genes. Upon
CC DNA-binding, it locally modifies DNA conformation by wrapping the DNA
CC around itself, thereby modifying the interface between stalled RNA
CC polymerase II and DNA. It is required for transcription-coupled repair
CC complex formation. {ECO:0000250|UniProtKB:Q03468}.
CC -!- SUBUNIT: Homodimer. Binds DNA. {ECO:0000250|UniProtKB:Q03468}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468}.
CC -!- TISSUE SPECIFICITY: Expressed in proliferating tissues. Highly
CC expressed in shoot apical meristem (SAM). Expressed in roots, young
CC leaves, flag leaves, and panicles. Expressed at very low levels in
CC mature leaves. {ECO:0000269|PubMed:15150342}.
CC -!- INDUCTION: Induced by gamma irradiation. {ECO:0000269|PubMed:25124817}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD45511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS69937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB111944; BAD04853.1; -; mRNA.
DR EMBL; AP002969; BAB92143.1; -; Genomic_DNA.
DR EMBL; AP003610; BAB62641.1; -; Genomic_DNA.
DR EMBL; AP003727; BAD45511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF03666.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS69937.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015621784.1; XM_015766298.1.
DR AlphaFoldDB; Q7F2E4; -.
DR SMR; Q7F2E4; -.
DR STRING; 4530.OS01T0102800-01; -.
DR PRIDE; Q7F2E4; -.
DR GeneID; 4326441; -.
DR KEGG; osa:4326441; -.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_7_0_1; -.
DR InParanoid; Q7F2E4; -.
DR OrthoDB; 372069at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1187
FT /note="DNA excision repair protein CSB"
FT /id="PRO_0000438216"
FT DOMAIN 384..580
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 716..876
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..534
FT /note="DEGH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..350
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 397..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1187 AA; 132132 MW; BB9F72D188B97117 CRC64;
MEDDDDDQRL LHSLGVTSAD IHDIERRIIS QATTDPADSS GPTINGGHQP DDALAKLHHK
LRSVQIEIDA VASTIKGAKL KQPSGNKPHE HKGKDQPDHH GAGHLQQALA ADRLTSLRKA
KAQIQKEILQ SHPSPSASNR KDKMLAMLVQ DEPRHKKPPV GPKNIVKRPM KTVTYDDDNN
FDAVLDGASA GFMETEREEL IRKGLLTPFH KLKGFEKRVE LPEPSHRQDD SAGQTEEAME
ASRIARVAQS LKQIAQNRPA TKLLDSESLP KLDAPAAPFQ RLGKPLKRPV SPSSDEQEKK
RPRNKTKRPL PGKKWRKANS IKESSLDDND VGEAAVSVSD DDEDQVTEGS DELTDVTLEG
GLRIPGTLYT QLFDYQKVGV QWLWELHCQR AGGIIGDEMG LGKTVQVLSF LGSLHNSGLY
KPSIVVCPVT LLQQWRREAS RWYPKFKVEI LHDSANSSSK KSKRSSDSDS EASWDSDQEE
AVTCSKPAKK WDDLISRVVS SGSGLLLTTY EQLRILGEKL LDIEWGYAVL DEGHRIRNPN
AEITLVCKQL QTVHRIIMTG APIQNKLSEL WSLFDFVFPG KLGVLPVFEA EFSVPITVGG
YANATPLQVS TAYRCAVVLR DLVMPYLLRR MKADVNAQLP KKTEHVLFCS LTTEQRATYR
AFLASSEVEQ IFDGNRNSLY GIDVLRKICN HPDLLEREHA AQNPDYGNPE RSGKMKVVEQ
VLKVWKEQGH RVLLFTQTQQ MLDIMENFLT ACEYQYRRMD GLTPAKQRMA LIDEFNNTDE
IFIFILTTKV GGLGTNLTGA NRIIIYDPDW NPSTDMQARE RAWRIGQTRD VTVYRLITRG
TIEEKVYHRQ IYKHFLTNKV LKDPQQRRFF KARDMKDLFT LQDDDNNGST ETSNIFSQLS
EDVNIGVPSD KQQDQLYAAS ATPTTSGTEP SSSRHGQGKE DHCPDQADEE CNILKSLFDA
QGIHSAINHD AIMNANDDQK LRLEAEATQV AQRAAEALRQ SRMLRSHESF SVPTWTGRAG
AAGAPSSVRR KFGSTLNTQL VNSSQPSETS NGRGQSLQVG ALNGKALSSA ELLARIRGTR
EGAASDALEH QLNLGSASNH TSSSSGNGRA SSSSTRSMIV QPEVLIRQLC TFIQQHGGSA
SSTSITEHFK NRILSKDMLL FKNLLKEIAT LQRGANGATW VLKPDYQ
