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Database: UniProt
Entry: A0A0T6AVK8_9SCAR
LinkDB: A0A0T6AVK8_9SCAR
Original site: A0A0T6AVK8_9SCAR 
ID   A0A0T6AVK8_9SCAR        Unreviewed;      1123 AA.
AC   A0A0T6AVK8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   ORFNames=AMK59_6543 {ECO:0000313|EMBL:KRT79094.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT79094.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT79094.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT79094.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT79094.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRT79094.1}.
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DR   EMBL; LJIG01022714; KRT79094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AVK8; -.
DR   OrthoDB; 169847at2759; -.
DR   Proteomes; UP000051574; 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   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};
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:UP000051574};
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          5..166
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          531..691
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          808..898
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          433..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..982
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1032
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1123 AA;  127935 MW;  F92FE5C6C50EDCCB CRC64;
     MAINLDKDTF YRRLKKLHAA WQKSEGENGF SKMDCLLTAV GVDEEIVYSK SGALQTWLMG
     YELTDTIMVL TENTLYFLAS KKKIDFLRQA ENNKEENSVA LKLLTRDRTD KDENNFKTLI
     SAIKGSKKGK TIGTFSKENY PGEFMDSWRA ALKKEELATI DVSSAVAYVI SPKEDTEILT
     IKKACMVTVD VFTKYLKDQI MEIIDSDKKV KHSKLAEGVE VAITDKKYIS GVDTTQIDMC
     YPAIIQSGGN YSLKFSVVSD KNNLHFGAII CSLGARYKSY CSNIVRTLLV NPSDEIQNNY
     NFLLNLEEEV LKKLSSGTKL SEVYEAGVSY VKKEKADLIE NLTKSFGFAM GIEFKENSLT
     IGPKTTAIAR KGMVFNVNMG FSNLQNKEAS DKEGKVYALF IGDTVIVNEN QPASVLTISK
     KKIKNIGIFL KDESDEEEEN DEEKENTPKP EILGRGKRTA VIESKLRSEQ TSEEKRKEHQ
     KELAHQLNEK AKERLAKQSG AKDVEKVRKN TVSYKNVNQM PRVAEVKELK LYVDQKYETV
     ILPIYGIPVP FHISTIKNIS QSVEGDYTYL RINFFHPGST MGKNESGTYQ QPDATFLKEV
     TYRSTNTKEP GEISPPSSNL NTAFRLIKEV QRKFKTREAE EREKEDLVKQ DTLILSQNKG
     NPKLKDLYIR PNIVAKRMTG SLEAHTNGFR YTSVRGDKVD ILYNNIKNAF FQPCDSEMII
     LLHFHLKHAI MFGKKKHVDV QFYTEVGEIT TDLGKHQHMH DRDDLAAEQS ERELRHKLKT
     AFKSFCEKVD SMTKSEIEFD TPFRELGFPG APFRSTVLLQ PTSGCLVNLT EWPPFVITLE
     DVELVHFERV QFHLKNFDMV FVFKDYHRRI AMVNAIPMSM LDHVKEWLNS CDIRYSEGIQ
     SLNWIKIMKT ITDDPEGFFE SGGWTFLDPE SDEEEARPSD DTEDEDEVYE PSDVESESEE
     SEEDSEYSEG DTESDSATEE SLGSDEDSGK DWSDLEREAA EEDRERSRYT EQIEEGGAKK
     RDRYAERHKG KNDKTRDKRK SHDKHKSSSG SSNRHSSSGR HNSSSSRHST SSSSRHHGGG
     GSGRDKHSSK KDSPNKDKHR SSNDKKRSRD ESGDKHRSKR SRK
//
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