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SSP1A_ORYSJ
ID   SSP1A_ORYSJ             Reviewed;         641 AA.
AC   Q9LGR0; Q0JQ27; Q8LKS8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=FACT complex subunit SSRP1-A;
DE   AltName: Full=Early drought-induced protein R1G1A;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SSRP1-A;
DE   AltName: Full=Recombination signal sequence recognition protein 1-A;
GN   Name=SSRP1-A; Synonyms=R1G1A;
GN   OrderedLocusNames=Os01g0184900, LOC_Os01g08970;
GN   ORFNames=OsJ_00664 {ECO:0000312|EMBL:EEE54009.1}, P0510F03.10;
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].
RA   Klueva N., Tyagi A., Zhang J., Zheng H., Nguyen H.;
RT   "Identification of early drought-induced cDNAs in rice.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC       that acts to reorganize nucleosomes. The FACT complex is involved in
CC       multiple processes that require DNA as a template such as mRNA
CC       elongation, DNA replication and DNA repair. During transcription
CC       elongation the FACT complex acts as a histone chaperone that both
CC       destabilizes and restores nucleosomal structure. It facilitates the
CC       passage of RNA polymerase II and transcription by promoting the
CC       dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC       subsequently promotes the reestablishment of the nucleosome following
CC       the passage of RNA polymerase II. Binds specifically to double-stranded
CC       DNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC       and SSRP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC       Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR   EMBL; AF503585; AAM46895.1; -; mRNA.
DR   EMBL; AP002486; BAB03358.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04151.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS70769.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE54009.1; -; Genomic_DNA.
DR   EMBL; AK066832; BAG90145.1; -; mRNA.
DR   RefSeq; XP_015617055.1; XM_015761569.1.
DR   AlphaFoldDB; Q9LGR0; -.
DR   SMR; Q9LGR0; -.
DR   STRING; 4530.OS01T0184900-01; -.
DR   PaxDb; Q9LGR0; -.
DR   PRIDE; Q9LGR0; -.
DR   EnsemblPlants; Os01t0184900-01; Os01t0184900-01; Os01g0184900.
DR   EnsemblPlants; Os01t0184900-02; Os01t0184900-02; Os01g0184900.
DR   GeneID; 4325652; -.
DR   Gramene; Os01t0184900-01; Os01t0184900-01; Os01g0184900.
DR   Gramene; Os01t0184900-02; Os01t0184900-02; Os01g0184900.
DR   KEGG; osa:4325652; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   HOGENOM; CLU_017374_2_2_1; -.
DR   InParanoid; Q9LGR0; -.
DR   OMA; SKQPGKC; -.
DR   OrthoDB; 915055at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q9LGR0; OS.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 2.30.29.220; -; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR035417; POB3_N.
DR   InterPro; IPR000969; SSrcognition.
DR   InterPro; IPR024954; SSRP1_dom.
DR   InterPro; IPR038167; SSRP1_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF17292; POB3_N; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF03531; SSrecog; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..641
FT                   /note="FACT complex subunit SSRP1-A"
FT                   /id="PRO_0000245196"
FT   DNA_BIND        556..624
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          459..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        543
FT                   /note="D -> E (in Ref. 1; AAM46895)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   641 AA;  71334 MW;  746162D9ED3BF7AD CRC64;
     MTDGHLFNNI LLGGRAGSNP GQFKVYSGGL AWKRQGGGKT IEIEKSDLTS VTWMKVPRAY
     QLGVRTKDGL FYKFIGFREQ DVSSLTNFMQ KNMGLSPDEK QLSVSGQNWG GIDINGNMLT
     FMVGSKQAFE VSLADVSQTQ MQGKTDVLLE FHVDDTTGGN EKDSLMDLSF HVPTSNTQFL
     GDENRTAAQV LWETIMGVAD VDSSEEAVVT FEGIAILTPR GRYSVELHLS FLRLQGQAND
     FKIQYSSIVR LFLLPKSNNP HTFVVVTLDP PIRKGQTLYP HIVIQFETEA VVERNLALTK
     EVLAEKYKDR LEESYKGLIH EVFTKVLRGL SGAKVTRPGS FRSCQDGYAV KSSLKAEDGL
     LYPLEKGFFF LPKPPTLILH EEIEFVEFER HGAGGASISS HYFDLLVKLK NDQEHLFRNI
     QRSEYHNLFN FINGKHLKIM NLGDGQGATG GVTAVLRDTD DDAVDPHLER IKNQAGDEES
     DEEDEDFVAD KDDSGSPTDD SGGEDSDASE SGGEKEKLSK KEASSSKPPV KRKPKGRDEE
     GSDKRKPKKK KDPNAPKRAM TPFMYFSMAE RGNMKNNNPD LPTTEIAKKL GEMWQKMTGE
     EKQPYIQQSQ VDKKRYEKES AVYRGAAAMD VDSGSGGNES D
 
 
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