SPT16_NEUCR
ID SPT16_NEUCR Reviewed; 1032 AA.
AC Q8X0X6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=FACT complex subunit ctc-2;
DE AltName: Full=Chromatin transcription complex 2;
DE AltName: Full=Facilitates chromatin transcription complex subunit ctc-2;
GN Name=ctc-2; Synonyms=spt16; ORFNames=123A4.150, NCU01164;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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: Forms a stable heterodimer with ctc-1/pob3. The dimer of ctc-1
CC and ctc-2 weakly associates with multiple molecules of nhp-1/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; AL670009; CAD21367.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32294.3; -; Genomic_DNA.
DR RefSeq; XP_961530.3; XM_956437.3.
DR AlphaFoldDB; Q8X0X6; -.
DR SMR; Q8X0X6; -.
DR STRING; 5141.EFNCRP00000004253; -.
DR PRIDE; Q8X0X6; -.
DR EnsemblFungi; EAA32294; EAA32294; NCU01164.
DR GeneID; 3877710; -.
DR KEGG; ncr:NCU01164; -.
DR VEuPathDB; FungiDB:NCU01164; -.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; Q8X0X6; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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..1032
FT /note="FACT complex subunit ctc-2"
FT /id="PRO_0000245187"
FT REGION 446..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 485..506
FT /evidence="ECO:0000255"
FT COILED 624..658
FT /evidence="ECO:0000255"
FT COILED 785..805
FT /evidence="ECO:0000255"
FT COILED 949..1010
FT /evidence="ECO:0000255"
FT COMPBIAS 446..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..1002
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 118058 MW; 9DC0D3185C116DC7 CRC64;
MADIKIDSKV FQERVSHFYN AWKADKRSGD ALFGGVSSIV ILMGKVDENP EFHKNNAIHF
WLLGYEFPTT LMLFTLDTIY ILTTQKKAKY LDQVKGGRYP VEVLVRGKDA AENEKLFIKI
TDAIKAAGKK VGVLTKDTSK GPFIDEWKKV YADNCKDVEE VDVAQALSAG AFSVKDETEL
RAMRTSSKAC VALLTPYFLD EMSNILDQDK KIKHSALADK VFNKLEDDKF WKTVELPNRQ
KLPADLDPEQ LDWILGPIVQ SGGKFDLKWQ ADSDNDILHP GIIIAAMGLR YKSYCSQIAR
TFMVDPNKSQ ESNYKFLLAV HNLILKEIRD GAIVKDVYTK AYNFVRSKKP DLEKHFLKNV
GFGIGLENKD PTLILNNKNT RTLKDGMTLV VTTGFSDIQN PNPQDKNSKV YSLILSDTIR
VTSSEPVVFT GEAPVDVDAT SFFFKDEEEA QPTPKKEKRD SRVGAVATKN ITSTRLRSER
NTTVDEDADK RRREHQKELA QKKQKEGLAK YAESTADENG VEIKKFKRFE SYKRDNQFPP
KVKDMGIVID QKNATIVLPV MGRPVPFHIN TIKNASKSDE GEWSFLRINF LSPGQGVGRK
DEQPFEDASA HFVRSLTFKS TDGDRYADIA NQISNLKRDA VKKEQEKKDM EDVVEQDKLV
EIRNRRPAVL DNVFIRPAME GKRVPGKVEI HQNGIRYQSP LSTTQRVDIL FSNVRHLFFQ
PCQHELIVII HIHLKDPIII GNKKKTKDVQ FYREATDIQF DETGNRKRKY RYGDEDEFEA
EQEERRRRAE LDRLFKSFAE KIAEAGRNEG IEVDMPLRDL GFNGVPFRSN VYIQPTTECL
IQITEPPFMV ITLEDIEVAH LERVQFGLKN FDLVFVFKDF TRPPYHINTI PVESLEDVKE
FLDSSDIAFS EGPLNLNWGV IMKTVTANTH QFFLDGGWGF LQNDSDDDEV EEEEEESAFE
IDESELEDAS ESSEEDSEYD SNASEEASDE AEDSEEEEGE DWDELERKAK KRDRESGFDD
EEERAAPKKR RK
