SPT16_CANAL
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 03-AUG-2022, entry version 95.
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}.
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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 PRIDE; Q5A1D5; -.
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; 145488at2759; -.
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:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
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..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
