SPT16_GIBZE
ID SPT16_GIBZE Reviewed; 1034 AA.
AC Q4HYB8; A0A0E0RVU9; V6RXH7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN Name=SPT16; ORFNames=FGRRES_10040, FGSG_10040;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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 POB3. The SPT16-POB3 dimer
CC weakly associates with multiple molecules of NHP6 to form the FACT
CC 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; DS231669; ESU16705.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF75374.1; -; Genomic_DNA.
DR RefSeq; XP_011318967.1; XM_011320665.1.
DR AlphaFoldDB; Q4HYB8; -.
DR SMR; Q4HYB8; -.
DR STRING; 5518.FGSG_10040P0; -.
DR EnsemblFungi; ESU16705; ESU16705; FGSG_10040.
DR GeneID; 23556963; -.
DR KEGG; fgr:FGSG_10040; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G07139; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; Q4HYB8; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0035101; C:FACT complex; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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..1034
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245186"
FT REGION 444..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..507
FT /evidence="ECO:0000255"
FT COILED 625..659
FT /evidence="ECO:0000255"
FT COMPBIAS 948..976
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1003
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 117686 MW; 76A33F37835A1C3C CRC64;
MAEIKIDSKI FQERISHFAT AWKNDLRSKD GLFNGAQSLV VMMGKVEEVP EFHKNNAIHF
WLLGYEFPTT LMLFTLDTLY ILTTAKKAKH LEQLKGGRFP IEVLVRGKDA AENEKLFVKL
TDKIKEAGNK VGTIAKDTSR GPFVDEWKKV LAEHCKEVSQ VDISAALSTY AFAVKDESEL
RAMRTASKAC VALMTPYFLD EMSNILDAEK KVKHSTLADK VDKKLDDTSF WKTVQLPSKG
KLPSDLDPAQ LDWILGPAIQ SGGKYDLRFA GESNDDNLHA GIIIAAMGLR YKSYCSTIAR
TYLVDPNKAQ ESSYKLLTLI HNTIIKEIRD GMTAKEVYGR AVGIIKSKKP EMEKHFLKNV
GWGVGLENKD PTLVLNAKNQ RVLKDGMTLI INTGFQDIEN PHPQDKNSKV YALVLTDTIR
VTSSEPVVFT AEAPTSADAN SFFFKDDEET EPAPKKEKKD SRVGAVATKN ITTTRLRSER
TTQVANDDIE KKRREHQKEL AAKKQREGLA RFSESTNDQN GGEVKKFKRF ESYKRDNQFP
VKIKNLEVVV DSKNSTVVLP IMGRPVPFHI NTIKNASKSD EGEWSFLRIN FLSPGQGVGR
KDDQPFEDAS AHFVRSLTFR SSDGERYNEI ATQISNMKRD VVKKEQEKKD MEDVVEQDKL
VEIRNRRPAV LDNVYIRPAM EGKRVPGKVE IHQNGIRYIS PLNAQHRVDV LFSNVKHLFF
QPCQHELIVI IHIHLKDPII VGNKKKTKDV QFYREATDIQ FDETGNRKRK YRYGDEDEFE
AEQEERRRRA ELDRLFQGFA QKIAEAGRNE GIEVDMPIRE LGFHGVPFRS NVFVQPTTDC
LIQVVEPPFM VITIEEVEIA HLERVQFGLK NFDMVFVFKD FTRAPYHVNT IPVEFLDQVK
DYLDSSDIAY TEGPLNLNWP TIMKTVTADT HQFFADGGWS FLQADSDDDG GDPSDEESAF
EMDEDEFDEE SESSDEGSDF GSNASDDEGS DAELDSEDEG EDWDELERKA KKRDRESAME
EEDRGANKKK QRKR
