ID A0A0V1P6Q1_9BILA Unreviewed; 1003 AA.
AC A0A0V1P6Q1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=Supt16h {ECO:0000313|EMBL:KRZ91864.1};
GN ORFNames=T08_4605 {ECO:0000313|EMBL:KRZ91864.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ91864.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ91864.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ91864.1};
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:KRZ91864.1}.
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DR EMBL; JYDM01000040; KRZ91864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P6Q1; -.
DR Proteomes; UP000054924; 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:UP000054924};
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 511..671
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 800..884
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 908..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..962
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 115468 MW; ADF2B920402DF8F0 CRC64;
MEIDNKIQVE RFPLRLQKFM NYWKKGIHEI ISQVDAMVFC LGSTKDVVYS KTLTFHTWLF
GYELSDLIIV ITKESLTFLG SEKKIEFLQA YLKSCENLSL GTKCLVRQKE DLDKSNFATL
LKILREHRKI GLFQKEKFAG EFAGAWKKCF DDERFFTVDI TIPFALLTSV KDDLEIEYTQ
TACDASCAIY NKFFKQELIS IIDDERKVQH SILAKSLEDA TMNSKYLPDD ADINSMDLCF
PPIIQSGGRY ALKFSVMSDD NNLHYGNIIC SFGVRYRHYC SSLIRTLLVE PNKHLQDAYA
LLLDVELKVM ECLRPGVKLS EVYGYAEDLI RARKPQYLEY LTKSIGFGMG IEFRESALLI
NGKNNVYLHG ICDYYPGMVF NVHVGFCNFP NPEAKEKLDK VTALFIGDTV LITEAESEVE
TDGNKENIDE VLSRTKRTVV LTDQLRVNKE TGEERRKSHQ KELVKILNLT ARERITTTKK
QNVVPEQRKP VISYKARSLF PKNKEVKHLE FFIDRKYDSV VVPIFGVPIA FHITTVKNIS
QSIEGDFTYL RINFSRPVSA MVKNKDSTAA FQGLLYVKEL TFRSSNLKEP GELDPPSANL
REAYFKIKEV QKAFKARETE ARDKQGIVQQ DRLIICTNRV NPRLKDLFIR PNIVTKRISG
TLEVHSNGFR YLSFRGDKVD IMFNNIKHAF FQPCDHEMII LIHLNLKDSI MFGKKKTNDV
QFYTEVGEIT TDLGRYGSRS DRDDLYAEQK IWKEACILDS EAERELRNKL NSAFRSFCDR
VEKVTNGAVE FDTPFRDLGF YGAPYRASVL LQPTSCCLPT FVLTLDEVEL VHFERVHLQL
KHFDCIFIFK DYSRKPAMVS AIPQHMLDHV KEWLDSCDIV YTEGIQSLNW GKVMKSITDD
PEGFFESGGW NFLTADDDTE KEDDSDESEA TDDVYEPDSG DEGESDDDSE EYESEISESS
GTPEEDTDSG MSWSELEEEA RRADRQKDLE MEGRPQAKRA RRH
//
