ID   SPT16_CAEBR             Reviewed;        1034 AA.
AC   Q61E63; A8XF02;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=FACT complex subunit spt-16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit spt-16;
GN   Name=spt-16; ORFNames=CBG12204;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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: Component of the FACT complex, a stable heterodimer of spt-16
CC       and hmg-3 or hmg-4. {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; HE600958; CAP31224.3; -; Genomic_DNA.
DR   RefSeq; XP_002639851.1; XM_002639805.1.
DR   AlphaFoldDB; Q61E63; -.
DR   SMR; Q61E63; -.
DR   STRING; 6238.CBG12204; -.
DR   EnsemblMetazoa; CBG12204.1; CBG12204.1; WBGene00033188.
DR   GeneID; 8581845; -.
DR   KEGG; cbr:CBG_12204; -.
DR   CTD; 8581845; -.
DR   WormBase; CBG12204; CBP02968; WBGene00033188; Cbr-spt-16.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; Q61E63; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
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; 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 spt-16"
FT                   /id="PRO_0000245172"
FT   REGION          433..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          617..642
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        433..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..948
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..990
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1024
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1034 AA;  117848 MW;  671DBE411069CE22 CRC64;
     MGDKRVVLNK DIFFQRAERL YELWETGQVG LDSVNSIAVA YGDSENPYTK SSALHSWLFG
     HEINDTALLF LKDHIYILGS NRKVEFFGTV TGVQYNGRVP PVSTLLRDKS DKDAGNFEKL
     IDYIKRAEGD LGSFVKEKFN SDFVNAWNDA LKADDINKTD VSLAFMHLFA VKDDKELELV
     RKSAQVTTTS WTAARQRYVE IIDSERRVRH SVLSSEFSAY MKDPKIQQSL AKYNADTCYD
     PIVMSGGNYS FKWNHDNSEA HLHNQFGSII TSFGARLSDY CTNLTRTMLI FPSAELEAAY
     EAILAAEFAV IAALKPGVKL KDVYKIGVDT LTEKNPKLAE TLNKKELGFA TGIEFRESRL
     SINAKCEEVV KEGMVFIVYI GVDSIPNKNK GEKGKPAAIA ISDTILVKAE GDNEVLTEKA
     KSRLKSNVIK FKEEQENRET ERDTDQKKLL GRGQRSVVLN DQTRNKTTNE DLRKERQKEL
     GKQLNLNAKA RLSKQDGGTD EKKVKKSNVS YKNEERFPQD TDVQKMLIFV DRKYDSVIVP
     IFGIPVPFHI SMIKNCSQSV EGDFTYLRIN FATPGSQVGK DNAQFPHPLA HFMKELTFRA
     SNIKEHHSDA TPPSSNLSTA FRQIKEMQKR FRTEEAEERE KDGAVKQDKL ILSQNKLNPK
     LKDLLIRPNI IQKRITGSLE AHTNGFRYTS LRGDRIDVLY NNIKHAFFQP CDNEMIILLH
     FHLKNPVMWG KKKYKDVQFY TEVGEITTDL GKYHHMQDRD DMHSEQQERE LRRRLNTTFN
     SFCEKVSRLT NDQFEFDSPF AGLGFFGVPF RSATTLKPTA SCLVNLTEWP PFIVTLSEVE
     LVHFERVSLQ LKNFDMVFIF KDYKMKTQMV AQIPMSSIDK IKEWLHTCDI WYSEGIQSLN
     WAKVMKTITD DPEDFFENGG WTFLDAESEG EDAGDDSDES DAYDPEEADA SDGGSSSASD
     EDESEGEETE SDDDEEGSLD SDESEGKDWS DLEEEAAKAD KRREVEDGGR DRDRDRDRKR
     PSSSKAGPSH KRRK