ID SPT16_CANAL Reviewed; 1060 AA. AC Q5A1D5; A0A1D8PML2; Q9HF08; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 24-JAN-2024, entry version 101. DE RecName: Full=FACT complex subunit SPT16; DE AltName: Full=CaCDC68; DE AltName: Full=Cell division control protein 68; DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16; GN Name=CDC68; Synonyms=SPT16; OrderedLocusNames=CAALFM_C406500WA; GN ORFNames=CaO19.10402, CaO19.2884; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1006; RX PubMed=12420162; DOI=10.1007/s00203-002-0470-y; RA Buurman E.T., Jiang W., McCoy M., Averett D.R., Thompson C.M., Wobbe C.R.; RT "Validation of Cdc68p as a novel antifungal target."; RL Arch. Microbiol. 178:428-436(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [3] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF253047; AAG48574.1; -; Genomic_DNA. DR EMBL; CP017626; AOW29374.1; -; Genomic_DNA. DR RefSeq; XP_715540.2; XM_710447.2. DR AlphaFoldDB; Q5A1D5; -. DR SMR; Q5A1D5; -. DR STRING; 237561.Q5A1D5; -. DR EnsemblFungi; C4_06500W_A-T; C4_06500W_A-T-p1; C4_06500W_A. DR GeneID; 3642787; -. DR KEGG; cal:CAALFM_C406500WA; -. DR CGD; CAL0000198046; CDC68. DR VEuPathDB; FungiDB:C4_06500W_A; -. DR eggNOG; KOG1189; Eukaryota. DR HOGENOM; CLU_004627_1_0_1; -. DR InParanoid; Q5A1D5; -. DR OrthoDB; 169847at2759; -. DR PRO; PR:Q5A1D5; -. DR Proteomes; UP000000559; Chromosome 4. DR GO; GO:0035101; C:FACT complex; IBA:GO_Central. DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi. DR GO; GO:0008023; C:transcription elongation factor complex; IGI:CGD. 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-KW. 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:0032784; P:regulation of DNA-templated transcription elongation; IGI:CGD. DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IGI:CGD. 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; 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 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; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..1060 FT /note="FACT complex subunit SPT16" FT /id="PRO_0000245181" FT REGION 458..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 977..1060 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 508..532 FT /evidence="ECO:0000255" FT COMPBIAS 978..1041 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1042..1060 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 146..149 FT /note="Missing (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="N -> S (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" FT CONFLICT 412..414 FT /note="Missing (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="A -> G (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" FT CONFLICT 734 FT /note="S -> SQS (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" FT CONFLICT 1030..1032 FT /note="Missing (in Ref. 1; AAG48574)" FT /evidence="ECO:0000305" SQ SEQUENCE 1060 AA; 121334 MW; 9362119DC7CB3C0F CRC64; MSEVNIDAGL FYKRLSIFQK QLTANNIPQA LIIVGARSDD NTYKKSTVLQ NWLLGYEFIH TAIYITDKKC IFITSEGKSK HLKHLTNQKP DLVELWIRTK DVEHNKQLFI KLLETMTKLD SKYGKILKDK YDGKFIDEWN QILNDDNNNN NNNTTNDHAL SAVDLAVTVS QALAVKDSEE FNNTKIASNA SVVMMDTFVN DMMIIVDDEK KITNSQLTDQ IEDKIENNKW YLKTKLGKNL LQSIKDFDPE YLEYCYSPII QSGGDYDLKP SAVSTDKPLI GEGVILSSIG LRYKSYCSNI ARTFLIDPTS EMETNYDFLL QLQKYIVDNL LKDGVPANKV YQDTIDYIKK ERPDLVNHFT KNCGWLLGME FRDSTFILNA KTTDRKLTTG QIISLTIGFN NLSNDKNDKN DKNDNKTNHQ KNKQTYALLL TDTIKITDDS SILLTNYSKD RAAISFSFND DNETQKENNN NNNKRPGLSQ TSNTTALKLE STENTAILKS KLRHENTNAD DANSEKLRQE IQIKLHEKRL QEGLARFSKA DATDADDFKP IFKKYESYVR ESQIPNSVND LKIHIDYKNQ TIILPISGRP VPFHINSYKS GSQNEEGDFT YLRLNFNSPG AGGNVTKKQE LPYEDSPDNS FLRSITIRSR DRQRMVDVYK AIQDLKKDSV KREQEKKQMA DVITQANLIE LKGSRVKKLN NVFIRPTPDT KKIGGVLQIH ENGLRYQSQP QSQSNFKNDQ RVDVLFSNIK HLFFQPCKDE LIVLIHCHLK NPIMIGKRKT FDVQFYREAS DMAFDETGGR KRKYRYGDED ELQQEQEERR RKALLDKEFK GFAELIADSS HGMVDLDIPF RELGFQGVPF RSSVLCVPTR DCLVQLIDPP YLVVTLEEIE IAHLERVQFG LKNFDLVFVF KDFNKPVVHI NTIPVELLED VKSWLTDVDI PISEGQMNLN WVQIMKTVLA DPYQFFIDGG WAFLTGQGES DEEEESDEES DFRVSDEDPQ DEDEESDDYA SEEESDDYSG SDDDGSGGGG DDDDDDSESG EDWDALERKA AKADRNSGFD //