ID D7LM34_ARALL Unreviewed; 645 AA.
AC D7LM34;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN Name=ATHMG {ECO:0000313|EMBL:EFH51728.1};
GN ORFNames=ARALYDRAFT_905150 {ECO:0000313|EMBL:EFH51728.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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. {ECO:0000256|RuleBase:RU364013}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC and SSRP1. {ECO:0000256|ARBA:ARBA00011111}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364013}.
CC Chromosome {ECO:0000256|RuleBase:RU364013}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060, ECO:0000256|RuleBase:RU364013}.
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DR EMBL; GL348717; EFH51728.1; -; Genomic_DNA.
DR RefSeq; XP_002875469.1; XM_002875423.1.
DR AlphaFoldDB; D7LM34; -.
DR STRING; 81972.D7LM34; -.
DR EnsemblPlants; scaffold_500854.1; scaffold_500854.1; scaffold_500854.1.
DR GeneID; 9311537; -.
DR Gramene; scaffold_500854.1; scaffold_500854.1; scaffold_500854.1.
DR KEGG; aly:9311537; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_2_2_1; -.
DR OrthoDB; 5488575at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblPlants.
DR GO; GO:0035101; C:FACT complex; IEA:EnsemblPlants.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0010197; P:polar nucleus fusion; IEA:EnsemblPlants.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR CDD; cd22013; HMG-box_AtSSRP1; 1.
DR CDD; cd13230; PH1_SSRP1-like; 1.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR048993; SSRP1-like_PH1.
DR InterPro; IPR000969; SSRP1/POB3.
DR InterPro; IPR035417; SSRP1/POB3_N.
DR InterPro; IPR024954; SSRP1_DD.
DR InterPro; IPR038167; SSRP1_sf.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF21103; PH1_SSRP1-like; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU364013};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364013};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364013};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU364013};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364013};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364013}.
FT DOMAIN 561..629
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 561..629
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 469..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 71642 MW; A7CCAA085E974EA8 CRC64;
MTDSHSFNSI SLSGRGGTNP GLLKINSGGI QWKKQGGGKA VEVDRSDIVS VSWTKVTKSN
RLGVKTKDGL YYKFVGFRDQ DVPSLSSFFQ SSYGKTPEEK QLSISGRNWG EVDLHGNTLT
FLVGSKQAFE VSLADVSQTQ IQGKDDVTLE FHVDDTAGAN EKDSLMEICF HIPSSNTQFV
GDENRPPSHV FNDTIVAMAD VSSGVEDAVV TFDSIAILTP RGRYSVELHL SFLRLQGQAN
DFKIQYSSVV RLFLLPKSNQ PHTFVVISLD PPIRKGQTMY PHIVMQFETD TVVESELSIS
DDLMNTKFKD KLERSYKGLI HEVFTTVLRW LSGAKITKPG KFRSSQDGFA VKSSLKAEDG
VLYPLEKGFF FLPKPPTLIL HDEIDYVEFE RHAAGGANMH YFDLLIRLKT DHEHLFRNIQ
RNEYHNLYTF ISSKGLKIMN LGGAGTTDGV AAVLGDDDDD DAVDPHLERI KNQAADESDE
EDEDFVMGED DDGGSPTDDS GEDDSDASEG GGGEKEKSIK KEPKKEASSS KGLPHKRKVS
AADEGSSKRK KPKKKKDPNA PKRAMSGFMY FSQMERDNIK KEHPGIAFGE VGKVLGDKWR
QMSAEEKEPY EAKAQVDKQR YKDEISDYKN PQPVNVDSGN ESDSN
//
