ID B6K2E8_SCHJY Unreviewed; 1011 AA.
AC B6K2E8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=spt16 {ECO:0000313|JaponicusDB:SJAG_02416};
GN ORFNames=SJAG_02416 {ECO:0000313|EMBL:EEB07329.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07329.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07329.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(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: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; KE651166; EEB07329.1; -; Genomic_DNA.
DR RefSeq; XP_002173622.1; XM_002173586.2.
DR AlphaFoldDB; B6K2E8; -.
DR STRING; 402676.B6K2E8; -.
DR EnsemblFungi; EEB07329; EEB07329; SJAG_02416.
DR GeneID; 7050061; -.
DR JaponicusDB; SJAG_02416; spt16.
DR VEuPathDB; FungiDB:SJAG_02416; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0140713; F:histone chaperone activity; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0140719; P:constitutive heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
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:SF15; 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|ARBA:ARBA00022454, 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|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
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 6..170
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 535..685
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 808..898
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 445..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 116002 MW; FD14F191CC19E50F CRC64;
MSEYEIDVPL FFKRIQRLLD LWNDPSHSEE YFHGIDSLLV VTGTENIENP YQKSAALHTW
LLGYEFPQTL ILFTKTKVTF LSSSKKITML EQLSQGSSGS SINLEFLKRT KNPEENLKLF
QQVIEAVSAT NKKVGHFPKD SLDGKFVNEW KAALEQAKAE FEYVDVSLPV AVAMSVKDDV
ELPIVKTASR ASTGVMTRYF ADQLSKFIDE GKKISNSRFS DLIEQKIDDE SFFQQKALHL
GNMDMDQLEW CYTPIVQSGG SYDLKPSAIS NDKLLHGGVV LCSLGLRYKS YCSNIGRTYL
FDPNADQLKY YNFLVQLQTK VLELCTHGAV IKEIYAKAVE YVRSKYPELE SHFVRNLGAG
IGIEFRESAY LINAKNPRKL ESGMTVNLSV GFANLENSKA KTAEGKVYSL LLIDTIQITK
DAPLVFTESP KSHADISYYF GEDTTAEKEQ TTRKPTRTTA TISSHKGKTR DVDDSAEKRR
IEHQKQLAAK KQTEGLRRFS DGSAHNTDEQ KTIVKRYESY KRDTQLPHAI ANLQILVDTR
AQSIILPIFG RPVPFHISTL KNVSKNDEGD YVYIRLNFIT PGQVGGKKDE QPFEDQNAEF
IRSFIFRSAE GSRLSHIFKE IQDMKKAATK REAERKQFAD VIEQDKLIEM KSKRPAHLND
VFVRPALDGK RLPGFLEVHQ NGIRYQSPLR SDSHIDLLFS NMKHLFFQPC EGELIVLIHV
HLKAPIMVGK RKTQDLQFYR EVSDMQFDET GNRKRKYMYG DEDELEQEQE ERRRRSQLDR
EFRAFAEKIA EASDNRIELD IPFRELAFSG VPFRANVLLQ PTTDCLVQLT DTPFTVITLS
EIEIAHLERV QFGLKNFDLV FVFKDFHRAP VHINTIPMDQ LDNVKEWLDS CDICFYEGPL
NLNWATIMKT VNDDPVAFFE EGGWDFLSTG DDEEAGESEE EVSEYEASGS DFDESEESED
YSDYEGEDED SESEMEDEEE SGEDWDELER KARQEDAKHD RGDERPMKRR R
//
