ID G8JMZ4_ERECY Unreviewed; 1042 AA.
AC G8JMZ4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN OrderedLocusNames=Ecym_1211 {ECO:0000313|EMBL:AET37458.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET37458.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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; CP002497; AET37458.1; -; Genomic_DNA.
DR RefSeq; XP_003644275.1; XM_003644227.1.
DR AlphaFoldDB; G8JMZ4; -.
DR STRING; 931890.G8JMZ4; -.
DR GeneID; 11469626; -.
DR KEGG; erc:Ecym_1211; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; G8JMZ4; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000006790; Chromosome 1.
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:UP000006790};
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..179
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 561..714
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 841..931
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 94..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1022
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 119099 MW; 37B20D6E6A0538F1 CRC64;
MSELDIDFKA FEKRLFLLRD KFPTFEESCS SLLFVLGSSD EENPYQKTTI LHNWLLGYEF
PATLISIFKK KCVIITSAAK AKHLLDGIEK INKEQQQGSK GDGDEGGFTI DLWQRNNKDP
EHNTKLFEDL IGLLKEAGQT VGIPLKDSYQ GKFMTEWNPV WESAISEHGF KTVDVSLGLS
TIWAVKDEQE QAMLHVSSKA SDKFMNLLSD ELVRAVDEEL HITNAKLSEK IEHKIDESRF
LKKLSADMLA VYPKGEKFDV NFLDWAYSPI VQSGSKFDLR VSARSSNEQL DGNGCILASC
GIRYKNYCSN ISRTFLIDPS EEMTENYDIL LLLQEEIIKH FLTIGSTPKQ VYDRAVEFIN
KKKPELVSSF TKNVGSLIGL EFRDSQFILN AKNDYRKVEA GDCFNISLGF NNLKDSKSGS
TYAIQIADTV QLSASGEQKV LTSYTKSRSQ ISFYFNNDEG TGTKVKNEKA KSPALSVKPD
AKSKILRSKL RGETRADDEE KEQIRKENQR KLHERLQKDG LLRFSDVDAT DGDQKPQVYF
KKYESYVRET QIPTNVRDLR IHVDWKNQTI ILPIYGRPVP FHINSYKNGS KNEEGEYTYI
RLNFHSPGTG GVNKKNEELP YEDNPEHQFV RSITLRSKDG DRIADIFKQI SELKKESTKR
EQELKVLADV VEQAKLIENR SGRTKRLDQI FVRPSPDAKR VPGTVFIHEN GIRYQSPLRT
DSRIDILFSN IKNLFFQPCK GELIVAIHVH FKNPILMGKK KIQDVQFYRE ASDMAVDETG
NGRRSQMKFR RYGDEDELEQ EQEERRKRAA LDKEFRYFAE AIAEASDGLV DVDTPFRDLG
FHGVPSRSAV FCIPTRDCLI QLVEPPFLVV NLNEVEICIL ERVQFGLKNF DLVFVYKDFA
KAVTHINTIP IEQLEFIKSW LTDVDIPYTV STINLNWATI MKSLQDDPHQ FFLDGGWSFL
ATGSDDEMSG GSEEEVSEYE VSDEDPSDEE VYSEEEYSEA DNEEFSDEGS EDFSDGGGED
GEDWDELEKK AAKADRISRF TD
//
