SSRP1_MAIZE
ID SSRP1_MAIZE Reviewed; 639 AA.
AC Q9LEF5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=Recombination signal sequence recognition protein 1;
DE AltName: Full=Zm-SSRP1;
GN Name=SSRP1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DNA-BINDING, AND TISSUE
RP SPECIFICITY.
RX PubMed=10929132; DOI=10.1046/j.1365-313x.2000.00801.x;
RA Roettgers K., Krohn N.M., Lichota J., Stemmer C., Merkle T., Grasser K.D.;
RT "DNA-interactions and nuclear localisation of the chromosomal HMG domain
RT protein SSRP1 from maize.";
RL Plant J. 23:395-405(2000).
RN [2]
RP DNA-BINDING.
RX PubMed=11425313; DOI=10.1021/bi010548y;
RA Lichota J., Grasser K.D.;
RT "Differential chromatin association and nucleosome binding of the maize
RT HMGA, HMGB, and SSRP1 proteins.";
RL Biochemistry 40:7860-7867(2001).
RN [3]
RP PHOSPHORYLATION AT SER-634 AND SER-638.
RX PubMed=12571244; DOI=10.1074/jbc.m300250200;
RA Krohn N.M., Stemmer C., Fojan P., Grimm R., Grasser K.D.;
RT "Protein kinase CK2 phosphorylates the high mobility group domain protein
RT SSRP1, inducing the recognition of UV-damaged DNA.";
RL J. Biol. Chem. 278:12710-12715(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 (By similarity). Binds specifically to
CC double-stranded DNA. {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 ECO:0000269|PubMed:10929132}. Chromosome {ECO:0000269|PubMed:10929132}.
CC -!- TISSUE SPECIFICITY: Present in leaves and kernels, but not in roots.
CC {ECO:0000269|PubMed:10929132}.
CC -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation.
CC {ECO:0000269|PubMed:12571244}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; AJ244017; CAB96421.1; -; mRNA.
DR AlphaFoldDB; Q9LEF5; -.
DR SMR; Q9LEF5; -.
DR STRING; 4577.GRMZM2G032252_P02; -.
DR iPTMnet; Q9LEF5; -.
DR PaxDb; Q9LEF5; -.
DR MaizeGDB; 411236; -.
DR eggNOG; KOG0526; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9LEF5; baseline and differential.
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 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..639
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000245195"
FT DNA_BIND 557..625
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 460..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 634
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000305|PubMed:12571244"
FT MOD_RES 638
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000305|PubMed:12571244"
SQ SEQUENCE 639 AA; 71418 MW; 963AA72507A450EA CRC64;
MTDGHHFNNI LLGGRGGTNP GQFKVHSGGL AWKRQGGGKT IEIDKADVTA VTWMKVPRAY
QLGVRIKAGL FYRFIGFREQ DVSNLTNFIQ KNMGVTPDEK QLSVSGQNWG GIDIDGNMLT
FMVGSKQAFE VSLPDVAQTQ MQGKTDVLLE LHVDDTTGAN EKDSLMDLSF HVPTSNTQFV
GDESRPPAHI LWETILKFAD VGSSEEPVVT FEGIAILTPR GRYSVELHLS FLRLQGQAND
FKIQYSSIVR LFLLPKSNNP HTFVVITLDP PIRKGQTLYP HIVIQFETEA VVERDLALSK
ELLVEKYKDR LEESYKGLIH EVFTKVLRGL SGAKVTRPGS FRSCQDGYAV KSSLKAEDGL
LYPLEKGFFF LPKPPTLILH EEIEFVEFER HGAGGASISS HYFDLLVKLK NDQEHLFRNI
QRNEYHNLFN FINGKNIKIM NLGGDGQGAS GVVTDVLRDT DDDAVDPHLE RIKNQAGDEE
SDEEDEDFVA DKDDSGSPTD DSGDEESDAS DSGGEKEKSS KKEASSSKPV QKRKHKARDD
EGQEKKKPKK KKDPNAPKRA MTPFMYFSMA ERGNMKSSNP DLPTTEIAKK LGEMWQKMSG
EEKQPYIQQA QVDKKRYEKE SAVYRGEATV DVDSGNESD