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Database: UniProt
Entry: G7XET1_ASPKW
LinkDB: G7XET1_ASPKW
Original site: G7XET1_ASPKW 
ID   G7XET1_ASPKW            Unreviewed;      1020 AA.
AC   G7XET1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   ORFNames=AKAW_03738 {ECO:0000313|EMBL:GAA85624.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85624.1};
RN   [1] {ECO:0000313|EMBL:GAA85624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85624.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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; DF126453; GAA85624.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XET1; -.
DR   STRING; 1033177.G7XET1; -.
DR   VEuPathDB; FungiDB:AKAW_03738; -.
DR   eggNOG; KOG1189; Eukaryota.
DR   InParanoid; G7XET1; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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, 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          7..168
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          541..691
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          814..904
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          441..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          620..647
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        443..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..993
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1020
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  115249 MW;  F3C65804D24926A2 CRC64;
     MAEEIVIDKS TFFNRLSSFY NAWKADKRSS HANFGGVSSI VILMGKTDEA NSFQKNNAMH
     FWLLGYEFPA TLLVFTTEMV YVVTTAKKAK HLEPLKGGKI PVEILVTSKT PDEKMKSFEK
     CIDVIKNAGK KVGVLPKDTT AGPFAEDWKK AYATLSNEVE EVDISPALSA TLSVKDTDEL
     VSIRNASRAC SGLMSEYFVD EMSRLLDEEK QMSHKALSMR IDAKIDDAKF FNKLAKLPAE
     FDPQQIDWAY GPVIQSGGKY DLKLTAISDN NNLQPGIIIA GFGIRYKTYS SMIARTYLVD
     PTKTQEANYA FLLNVREAIL KDVRDGAVAK DLYSKAMNMV RTKKPELESH FLKTVGAGIG
     IELRDANMVL NGKNDKVLKS GMTFAVTVGL TDVEDASIKD KNRTVYSMII TDTVRVGETG
     PLVFTKDAGV DMDSVSFYFG DEEEPQRPVK EKKEAKSSSV ANRNVTRTKL RAERPTQINE
     GAEARRREHQ KELAGKKTKE GLDRFAGTTG DDNGVTQKKF KRFESYKRDN QLPTRVKDLT
     VYVDQKASTV IVPIMGRPVP FHINTIKNAS KSDEGEYAYL RINFLSPGQG VGRKDDQPFE
     DLSAHFLRNL TLRSKDNDRL AQIAQDITEL RKNALRREQE KKEMEDVVEQ DKLVEIRNRR
     PVKLPDVYLR PPLDGKRVPG EVEIHQNGLR YMSPFRNEHV DVLFSNVKHL FFQPCAHELI
     VLIHVHLKTP IMIGKRKTRD VQFYREATEM QFDETGNRRR KHRYGDEEEF EAEQEERRRR
     AALDREFKAF AEKIADAGKD ESVDVDIPFR EIGFTGVPNR SNVLIQPTTD ALVQLTEPPF
     LVITLNEVEI AHLERVQFGL KNFDLVFVFK DFHRAPVHIN TIPVESLEGV KDWLDSVDIA
     FTEGPLNLNW TTIMKTVVSD PYGFFADGGW SFLAAESDSE GGSDEDEESA FELSESELAA
     ADESSEDDSE FDDDASAEAS DDFSADEESG EDWDELETKA KKKDRESGLD DEDRGKKRKR
//
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