SPT16_MAIZE
ID SPT16_MAIZE Reviewed; 1055 AA.
AC Q8H6B1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
DE AltName: Full=Global transcription factor group C protein 102;
GN Name=SPT16; Synonyms=GTC102;
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].
RA Bergstrom D., Springer N.M., Schmitt L.T., Guthrie E., Sidorenko L.,
RA Kaeppler S.M., Cone K.C.;
RT "Sequences from the plant chromatin consortium.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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. SSRP1 binds specifically to double-
CC stranded DNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC and SSRP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
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DR EMBL; AF545812; AAN41252.1; -; mRNA.
DR RefSeq; NP_001105557.1; NM_001112087.2.
DR AlphaFoldDB; Q8H6B1; -.
DR SMR; Q8H6B1; -.
DR STRING; 4577.GRMZM5G806358_P02; -.
DR PaxDb; Q8H6B1; -.
DR PRIDE; Q8H6B1; -.
DR EnsemblPlants; Zm00001eb229990_T001; Zm00001eb229990_P001; Zm00001eb229990.
DR GeneID; 542546; -.
DR Gramene; Zm00001eb229990_T001; Zm00001eb229990_P001; Zm00001eb229990.
DR MaizeGDB; 887762; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR OrthoDB; 145488at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; Q8H6B1; baseline and differential.
DR Genevisible; Q8H6B1; ZM.
DR GO; GO:0035101; C:FACT complex; 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 GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
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; IPR033825; Spt16_M24.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1055
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245176"
FT REGION 492..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..333
FT /evidence="ECO:0000255"
FT COILED 480..503
FT /evidence="ECO:0000255"
FT COILED 768..789
FT /evidence="ECO:0000255"
FT COMPBIAS 942..997
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 118504 MW; 7E830FB6AB2A3D5C CRC64;
MADNGDAKGG SGAYAINIEN FSKRLKVFYD HWKEHKSDLW GSSDAIAIAT PPPSDDLRYL
KSSALDIWLL GYEFPETIIV FMHKQIHVLS SQKKGNLIGT LKKAANEAVG VDIVLHVKTK
NSDGADLMDD IVHAARNQSK SDKPVVGHIA KEAPEGKLLE TWIKKLSGSG LRLVDVTNGF
SELFAVKDTT EITCVKKAAY LTSSVLKNFV IPKLEKVIDE EKEVSHSSLM DDAEKAILDP
LKVKVKLKPD NVDICYPPVF QSGGKFDLKP GASSNDEYLY YDSASIIICA IGSKYSSYCS
NVARTYLIDA TPTQNKAYET LRKAHEAAIQ QVKPGNQMSA VYQAAVAVIE RDAPELLPNL
TKSAGTGIGL EFRESGLNLN AKNDRRIKKG MVFNVSLGLH NIQAETTSEK TKQFSLLLAD
TVLVNERGHE ILTAPCSKAF KDVAYSFNED DDAVAAEVKI KSKTIDVMPT KATLRSDNQE
MSKEELRRQH QAELARQKNE ETARRLAGVG TGSGDGRGPA RASNELVAYK NVNDVPFVRD
LVIQVDQKNE AVLLPIYGSM VPFHVSTVKS VTSHQDNRTC TIRIFFNVPG MPFSNDSKFN
SQGAIYLKEI TFRSKDPRHS SEVVQQIKTL RRQVASRESE RAERATLVTQ EKLQIGSNRM
KMMRLSDVWI RPAFGGRGRK LTGNLEAHFN GFRYSTSRSD ERVDIMFGNI KHAFFQPAEK
EMITLLHFHL HNHIMVGNKK TKDVQFYVEV MDVVQTLGGS RRSALDPDEI EEEQRERDRK
NRINMDFQNF VNKVNDHWSQ PQFKGLDLEF DVPLRELGFH GVPYKASAFI IPTSTCLVEL
IETPFLVVSL SEIEIVNLER VGFGTKNFDM AIVFKDFKKD VLRIDSIPSA SLDAIKEWLD
TTDLKYYESR LNLNWRPILK TIIDDPQKFI DDGGWEFLNM EASDSETEDT EESDQGYVPS
DAEPESESED DDSDSESLVE SDDDDEESDE DSEEEKGKTW EELEREASNA DREHGAESDS
EEERRRRKAK TFGKSRAPER SSFKGAPPSK KPKFR
