ID R0FBU1_9BRAS Unreviewed; 1072 AA.
AC R0FBU1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=CARUB_v10000096mg {ECO:0000313|EMBL:EOA19251.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA19251.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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DR EMBL; KB870810; EOA19251.1; -; Genomic_DNA.
DR RefSeq; XP_006286353.1; XM_006286291.1.
DR AlphaFoldDB; R0FBU1; -.
DR STRING; 81985.R0FBU1; -.
DR GeneID; 17882971; -.
DR KEGG; crb:17882971; -.
DR eggNOG; KOG1189; Eukaryota.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF18; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|RuleBase:RU367052};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|RuleBase:RU367052};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 24..191
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 554..707
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 832..922
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 504..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1006
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 120321 MW; 2AC4D467BE81DEF9 CRC64;
MAGNGNVRAP IGGVPPKPGN TYSINVKNFI SRARALYEHW KKHSADMWGS ADALAIATPP
ASDDLRYLKS SALNIWLLGY EFPDTIMVFT PKQIHFLCSR NKASLLEVVK KPAHDELKVD
VVMHVKPKGD DGTGLMDAIF RAIRELSRGD GNDSQVVGHI AREVPEGKLL ETWTDRLKNA
KFQFVDITGG LSDLFAVKDD TEVMSVKKAA YLAYSVMKTV VVPNLEGVID EEKDITHSAL
MDLTEKAILE PTKAGVRLKP ENVDICYPPI FQSGGKFDLK PSAASNDELL TYDPASIIIC
AVGARYNSYC SNVARTYLID ATSLQIKAYE VLLKAHDAAI NALRSGRKIN TVYQAALSVV
EKNAPEFVDK LTKSAGTGIG LEFRESGLNI NAKNDKVLRP NMAFNVSLGL QNLECESESR
SKIKKFSLLL ADTVLVTEQN PEIITKCSKS VKDVAYSFKE DEEEEKPRKK AKISGSENYI
TKTALRSDDH VVSKEELRKQ HQAELARQKN EETARRLAGD SSGAGDSRST SKTSADVVAY
KNVNDMPQPR SLEVQTDSKN EAVLLPIYGS LVPFHVATIR TVSGNQDTNR NCYIRIIFNV
PGTPFNPHDS NSLKNQGAIY LKEVSFRTKD SRHSSEVVQQ IKALRRQVMA RESERAERAT
LVTQEKLQLA GNKFKPLRLS ELWIRPPFSG RKKIPGTLEA HANGFRYSTT RPDERVDVLF
ANIKHAFFQP AEKEMITLLH FHLHNHIMVG TKKTKDVQFY VEVMDVVQSL GGGRRSAYDP
DEIDEEQRER DRKNKINMDF NHFANRVNDM WQLPQFASLD LEFDQPLREL GFHGVPHKTS
AFIIPTSSCL VELIEYPFLV VSLSEIEIVN LERVGFGQKN FDMAIIFKDF KKDVLRVDSV
PTSSLEGIKE WLDTTDIKYY ESKLNLNWRQ ILKTITDDPQ SFIDDGGWEF LNLDGSDSES
GGSEESDKGY EPSDVEVESE SEDEASESES LVESEDEEDE DSEQESEEEK GKTWDELERE
ATNADREHGV ESDSEEERKR RKMKVFGKSR PGGSSGSSMK NMPPSKRKHS HR
//
