ID C5E4S4_ZYGRC Unreviewed; 1030 AA.
AC C5E4S4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN OrderedLocusNames=ZYRO0E08382g {ECO:0000313|EMBL:CAR31035.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR31035.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928181; CAR31035.1; -; Genomic_DNA.
DR RefSeq; XP_002499290.1; XM_002499245.1.
DR AlphaFoldDB; C5E4S4; -.
DR STRING; 559307.C5E4S4; -.
DR GeneID; 8204845; -.
DR KEGG; zro:ZYRO0E08382g; -.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; C5E4S4; -.
DR Proteomes; UP000008536; Chromosome E.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 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:UP000008536};
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..167
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 547..700
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 827..917
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 447..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..1011
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 117842 MW; 98874E09F575FD1A CRC64;
MVELNIDFDV FKKRLLTLHS QYKTYENSPN SLLFVLGSSN TENPYQKTSI LHNWLLSYEF
PSTIIAVLPD KVVIITSAAK AKHLEKAVEL FSNEPVKLEL WQRNSKDPEH NKKLFEDVID
VIQKAGKSVG APEKNVYQGK FMLEWSPLWD EAVKKYELNV VDISAGLSQT WEVKDDNEKA
LLSVASKSSD KFMDYLADEM VRAVDEELRI TNVKLSDKIE NKIDDDSFLK KIAPELSKLC
PKGYPFNLDL LDWTYSPIIQ SGEKFDLRVS ARSTNDQLDG NGSILASCGI RYNNYCSNVT
RTFLIDPSDE MVRNYEFVLE LQKEIVNNKL KVGSTPKEVY DSVVEFVQKV RPDLVGNLTK
NLGSVIGLEF RDSSFVLNAK NETRKVQAGD CFNISFGFNN LKDSKTDKSY ALQLSDTVLL
ASEENSEPQY LTNCARSPSQ VSFYFNNEED ENESKKAKKP AKPEPNSKIL KTKLRGEARG
DSQENQKEQI RKENQKKLHE KLQKNGLLRF SAADANGTGN EQRQYFKKYE SYVRDSQIPS
NVRDLRVHVD WRSQTVILPI YGRPVPFHIN SYKNGSKNEE GEYTYLRLNF HSPGAGGISK
KTEELPYEES PDNQFVRSIT LRSKDGERMS DVFKQITDLK KESTKREQER KVLADVVRQD
KLIENKFGRT KRLDQIFVRP SPDPKRVPST VFIHENGIRY QSPLRSDSRI DILFSNIKNI
IFQSCKGELI VIIHIHLKNP ILMGKKKIQD VQFYREASDM SVDETGTGRR GQSKFRRYGD
EDELEQEQEE RRKRAALDKE FKYFADAIAE ASNGMLTVES AFRDLGFQGV PNRSAVFCMP
TTDCLVQLVE PPFLVINLEE IEICILERVQ FGLKNFDMVF VYKDFSKPVT HINTVPIESL
DFLKQWLTDM DIPYTVSSIN LNWSTIMKSL TEDPHQFFLD GGWSFLAMGS DDEGSGESDE
EISEYEASEE EPSDESAFSD DEDAYSEGEA EFSDDGSEEV SADEESEAGE DWDELEKKAA
KLDRVSNYRE
//
