SPT16_DICDI
ID SPT16_DICDI Reviewed; 1072 AA.
AC Q54S43;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN Name=spt16; ORFNames=DDB_G0282677;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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). {ECO:0000250}.
CC -!- SUBUNIT: Forms a stable heterodimer with ssrp1. The spt16-ssrp1 dimer
CC associates with a HMG box DNA-binding domain protein, probably nhp6, to
CC form the FACT complex (By similarity). {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; AAFI02000047; EAL66198.1; -; Genomic_DNA.
DR RefSeq; XP_640196.1; XM_635104.1.
DR AlphaFoldDB; Q54S43; -.
DR SMR; Q54S43; -.
DR STRING; 44689.DDB0231753; -.
DR PaxDb; Q54S43; -.
DR PRIDE; Q54S43; -.
DR EnsemblProtists; EAL66198; EAL66198; DDB_G0282677.
DR GeneID; 8623736; -.
DR KEGG; ddi:DDB_G0282677; -.
DR dictyBase; DDB_G0282677; spt16.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; Q54S43; -.
DR OMA; HQFFLDG; -.
DR PhylomeDB; Q54S43; -.
DR Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DDI-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DDI-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DDI-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q54S43; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0035101; C:FACT complex; ISS:dictyBase.
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:1902275; P:regulation of chromatin organization; ISS:dictyBase.
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; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
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 3: Inferred from homology;
KW Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1072
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000327489"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 486..522
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 120903 MW; B4BD9782FF322406 CRC64;
MSQSTTTTTT TTAAPAVPTG PREATLDAGN FCKRVKILYD SWNSDSNLWK SANSLVLALG
QPNESNPYQK VTSLQTWLFG YELKDTIIVF LEKEIYIVST SKKINLFQKL SETEQVKTEL
SSIKFNFLTI DKSDKNKSNF EKLIGEATKA GSNIGVIIKE TYIGDLALQW EAALNECPLT
KVDITPALSS CLLVKDLQEQ KNIITSAKIT SKVLKSHILP KIETIIDKGE RQTHNQLADY
AADIFESPEK ISSKLTVEHV DYSYVPIIQS GGIYDLRASA SSDDNPLHFG TIIVSCGARY
KNYCSNIART YIIDPTSDQK KNYAILLNVQ SNVIKAIKPD VTFSSLYEKA IQTIKESSKP
ELVDHFPKNV GYGIGIEFQE SLAVLNATNS RTLKAGMTLN IACGFQKISN PEGKDEKSKT
YSLLISDTVL LNDEGKVEVL TDVGKKASDV VYMLGGEDDD DDNDNDPSVK LELPDDVKGI
TGRTIETKEK SKSVEERRRD HQKMLEQKNL QEAENKIKAM TDPNGKKGTP EVDYTAITKL
QPIYSSVGAY PQDIVKNKMY IDPKKETVLF PIFGYMVPFH ISTIKNISKS EEYIRVNFNT
PTSYTQEQID AGFVPPQLMY IREVTYKVND PKVLANNIRL IKELKKKFTT RETEDREKRN
LITQEKLILL RGKFPRLPEV HARPTLSGAR RTIGILEAHE NGIRFNPTST KDRTPIDVLY
KNIKHAIYQQ ADQESMAVIH FHLHDALMIG KKKTKDVQFY IEISEMSQSL DVSSRFNDEE
EEERRERALK EKINNDFKTF IKRVEEIAPE PGLEFDVPYR ELGFYGVPNV STVFIQPSVH
CLLSILEPPF FVLTLDDVEI ACFERAIRSL KNFDLSFVFK DYNRPPIRIS VIPRNYFETV
KEWLDSFNIK FYQSERNYNW KRIMDTIKSD VKKFHDDGGW SFLDLEEEEE EEDSGDDDYH
SNSDESESSD YISSMSSGSD DDDEDSSEGE NWEDLEQKAE RDDKMKTFDE TNKRKRDEKS
VSSSNRPSSS KSGSSSSGGG GGGGGSSRSK SSSSSSKGSS SSSSKSSSSK RK
