ID A0A0V0WLJ0_9BILA Unreviewed; 1030 AA.
AC A0A0V0WLJ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=Supt16h {ECO:0000313|EMBL:KRX76657.1};
GN ORFNames=T06_10913 {ECO:0000313|EMBL:KRX76657.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX76657.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX76657.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX76657.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRX76657.1}.
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DR EMBL; JYDK01000096; KRX76657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WLJ0; -.
DR STRING; 92179.A0A0V0WLJ0; -.
DR Proteomes; UP000054673; 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};
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:UP000054673};
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..164
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 532..692
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 821..911
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 935..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..989
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 118523 MW; 3CF78270B1A69B3C CRC64;
MEIDNKIQVE RFPLRLQKFM NYWKKGIHEI ISQVDAMVFC LGSTKDVVYS KTLTFHTWLF
GYELSDLIIV ITKESLTFLG SEKKIEFLQS YLKSCENLSL GTKCLVRKKE DLDKSNFATL
LKILREHKKI GLFQKEKFAG EFAGAWKKCF DDERFFTVDI TIPFALLTSV KDDLEIEYTQ
TACDASCAIY NKFFKQELIS IIDDERKVQH SILAKSLEDA TMNSKYLPDD ADINSMDLCF
PPIIQSGGRY ALKFSVMSDD NNLHYGNIIC SFGVRYRHYC SSLIRTLLVE PNKHLQDAYT
LLLDVELKVM ECLRPGVKLS EVYGYAEDLI RARKPQYLEY LTKSIGFGMG IEFRESALLI
NGKNNVYLHG ICDYYPGMVF NVHVGFCNFP NPEAKEKLDK VTALFIGDTV LITEDGSVCL
TDAAKKRLKN CSMFIRAESE VETDGNKENI DEVLSRTKRT VVLTDQLRNK ETGEERRKSH
QKELVKILNL TARERIATTK KQNVVPEQRK PVISYKARSL FPKNKEVKHL EFFIDRKYDS
VVVPIFGVPI AFHITTVKNI SQSIEGDFTY LRINFSRPVS AMVKNKDSTA AFQGLLYVKE
LTFRSSNLKE PGELDPPSAN LREAYFKIKE VQKAFKARET EARDKQGIVQ QDRLIICTNR
VNPRLKDLFI RPSIVTKRIS GTLEVHSNGF RYLSFRGDKV DIMFNNIKHA FFQPCDNEMI
ILIHLNLKDS IMFGKKKTND VQFYTEVGEI TTDLGRYGSR SDRDDLYAEQ KIWKEACILD
SEAERELRNK LNSAFRSFCD RVEKVTNGAV EFDTPFRDLG FYGAPYRTSV LLQPTSCCLV
NLTDWPTFVL TLDEVELVHF ERVHFQLKHF DCIFIFKDYS RKPAMVSAIP QHMLDHVKEW
LDSCDIVYTE GIQSLNWGKV MKSITDDPEG FFESGGWNFL TADDDTEKED DSDESEATDD
VYEPDSGDEG ESDDDSEEFE SEISESSGTP EEDTDSGMSW SELEEEARRA DRQKDLEMEG
RPQAKRARRH
//
