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Database: UniProt
Entry: A0A0B2QX20_GLYSO
LinkDB: A0A0B2QX20_GLYSO
Original site: A0A0B2QX20_GLYSO 
ID   A0A0B2QX20_GLYSO        Unreviewed;      1068 AA.
AC   A0A0B2QX20;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   ORFNames=glysoja_034835 {ECO:0000313|EMBL:KHN24177.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN24177.1};
RN   [1] {ECO:0000313|EMBL:KHN24177.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN24177.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) 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; KN655680; KHN24177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2QX20; -.
DR   GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:SF18; 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   Aminopeptidase {ECO:0000313|EMBL:KHN24177.1};
KW   Chromosome {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|RuleBase:RU367052};
KW   Hydrolase {ECO:0000313|EMBL:KHN24177.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW   Protease {ECO:0000313|EMBL:KHN24177.1};
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          25..192
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          555..709
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          834..924
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          459..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..793
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..1014
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1045
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1068
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  120306 MW;  AF847CED4E78C3C2 CRC64;
     MADHRNGSTQ PPNGKASAAG SAYSIDLNAF QSRLKYFYKH WDDHKTDLWG SSDAIAIACP
     PPSEDLRYLK STALNLWLLG FEFPETIMVF MKKQIHILCS QKKASILESV KKSAKEAVGA
     DLVLHVKPKN DDGTALMDAI FRAIRALPKS DGHDSSTVGY ISREAPEGKL LETWTEKLKN
     TKFQLTDVAN GLSYLFAAKS SEELTSIKRA AYLTTSVMKN FVVTKLENVI DEEKKISHST
     LMEETEKVIL EPSKVNCKLK ADNVDICYPP IFQSGGEFDL KPSAVSNDEL LHYDSASVII
     CAVGARYKSY CSNIARTFLI DADPLQSRAY EVLLKAHEAV IGSMKPGNKL SVAYQAAVSV
     VERDAPDLIS YLTKSAGTGI GIEFRESGLN LNAKNEQIIR EGMVFNVSLG FQNLQCENSK
     SKNKQFSLLL ADTVIITKDK TEIVTATSSK ALKDVAYSFN EDEEEERPST KPDAKKAEPF
     MSKTTLRSDN HEVSKEELRR QHQAELARQK NEETARRLAG GGSETGESRS SARTSAELMA
     YKNINDLPPP REMMIQIDQK NEAVLLPING SMVPFHVAFI RTVSSQQDTN RNCYVRIIFN
     VPGTPFSPHD ANSMKFPGSI YLKEASFRSK DSRHISEVVQ SIKTLRRQVV ARESERAERA
     TLVTQEKLQL ANNRFKPIRL SDLWIRPAFG GRGRKIPGTL EAHVNGFRYS TTRQDERVDI
     MFPNIKHAFF QPAENEMITL LHFHLHNHIM VGNKKTKDVQ FYVEVMDMVQ NVGGGKRSTY
     DPDELEEEQR ERQRKNKINV EFQTFVNRVN DLWGQPQLNG LDLEFDQPLR ELGFPGVPHK
     SSVFIVPTSA CLVELIETPF LVVTLSEIEI VNLERVGLGQ KNFDMTVVFK DFKRDVLRID
     SIPSTSLDGI KEWLDTTDIK YYESRLNLNW RQILKTITDD PQSFIEGGGW EFLNLEATDS
     ESENSEESDK GYEPSDVEPE SDSEDEASDS ESLVESEDDD DDEDSEEDSE EEKGKTWEEL
     EREASNADRE KGNESDSEED RKRRKAKSFG KSRGASLSSS MPKRSKLR
//
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