ID G2XEQ1_VERDV Unreviewed; 1029 AA.
AC G2XEQ1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=VDAG_08636 {ECO:0000313|EMBL:EGY18302.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY18302.1};
RN [1] {ECO:0000313|EMBL:EGY18302.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18302.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; DS572715; EGY18302.1; -; Genomic_DNA.
DR RefSeq; XP_009651240.1; XM_009652945.1.
DR AlphaFoldDB; G2XEQ1; -.
DR STRING; 498257.G2XEQ1; -.
DR EnsemblFungi; EGY18302; EGY18302; VDAG_08636.
DR GeneID; 20710099; -.
DR KEGG; vda:VDAG_08636; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; G2XEQ1; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0140719; P:constitutive heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
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; IPR048969; SPT16_C.
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 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, ECO:0000256|SAM:Coils};
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 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..697
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 822..912
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 446..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 449..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..1001
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 116799 MW; 997BBC34910EF832 CRC64;
MADIKIDTKV FQERITHLAT AWKNDQRGSN GIFNGATSML VMMGKVEEVP ELHKNNAMHF
WLLGYEFPTT LMLLTVDTIY IVTTAKKAKH LEPLKGGRFP LEILVRGKDA AENQKIFVKI
ADTIKAAGNK VGIIAKDTSK GPFVDEWKKV FAENCKDVEE TDISPALSQI AFSVKDESEL
RAMRTASKAC VGLMTPYFLD EITDIVDGDK KVKHSALTDR VDKKLDDAKF WQNLELPNST
KLPSDMDTSQ LDWVMGPTVQ SGGKFDLRMG VESNDDPLHP GIIIANMGLR YKSYCSAIAR
TYLMDPNKAQ ESTYKLVLNI HNMIIKEIRD GVVAKEVYNK ALAMIKSKKP ELEKHFLKNV
GYGIGLENRD PTLLLSAKNS RVLKDGMTLV VTTGFSDIEN PQPQDKNSKT YSMVITDTIR
VTSSEAVVFT GESPTTADAC SFFFEGEEET APTPKKEKKD GRVGAVATKN ITSTRLRSER
NAQPDDDADQ KRREHQKELA SKKQKEGLAR FSESTAGQNG TEIKKFKRFE SYKRDNQLPP
KVRDLSIVVD AKMGTIILPV MGRPVPFHIN TIKNASKSDE GDWSFLRVNF LSPGQGVGRK
DDQPFEDATA HFVRSLTFRS TDGDRYQEIA TQISNMKRDS NKKEQEKKEL EDVVEQDKLV
EIRNRRPAVL DNVFLRPAME GKRVPGKVEI HQNGIRYTSP LHGSQRVDVL FSNVRHLFFQ
PCQHELIVII HIHLKDPIVY SNKKKTKDIQ FYREATDIQF DETGNRKRKY RYGDEDEFEQ
EQEERRRRAE LDRLFQGFAQ KIAEAGKNEG IEVDMPLRDL GFHGVPFRSN VFIQPTTDCL
IQVVEPPFMV LTLDDIEICH LERVQFGLKN FDMVFVFKDF SRAPYHVNTI PVDFLDAVKE
FLDSSDIAYS EGPLNLNWPT IMKTVTADTH QFFIDGGWSF LQAESDDEDG GEESEESNFE
IDDDELDEAS ESSEEDSDFG SNASDEDDAD MSDEDEGEDW DELEAKAKKR DRESALEEDE
GRNKKKRKH
//
