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Database: UniProt
Entry: G7YE45_CLOSI
LinkDB: G7YE45_CLOSI
Original site: G7YE45_CLOSI 
ID   G7YE45_CLOSI            Unreviewed;       958 AA.
AC   G7YE45;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   ORFNames=CLF_105745 {ECO:0000313|EMBL:GAA51229.1};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA51229.1, ECO:0000313|Proteomes:UP000008909};
RN   [1] {ECO:0000313|EMBL:GAA51229.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA51229.1};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-2011) 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; DF143127; GAA51229.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7YE45; -.
DR   Proteomes; UP000008909; 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; 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; IPR036005; Creatinase/aminopeptidase-like.
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; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   Pfam; PF21091; SPT16_C; 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   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:UP000008909};
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          440..600
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          719..809
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          314..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..859
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..911
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..936
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..958
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   958 AA;  108641 MW;  F75B59442B495EF4 CRC64;
     MLFIMSIMKG RVIGHLSKDK FSSELTKAFQ SALSSGSFEL RDVSGSISDL FAVKDENELN
     ILKKASAVTC NIFSKHLKEE IMEIIDYDKK VKHDKLSSGC HSALKKTNLL NGLDPDSLEM
     CYDPIIQSGG NFNLKFSIES DTQNLHFGTI ICALGVRYQS YCSNVIRSLM VNPTEDQAAV
     YAYLHDLFDW AIAAIKPGVK IAEFCQSIQD KVQSERPELA DCLVRSFGFV TGIEFRDSHQ
     LLTSKSTGVF REGMTLNFNI GLQNVKNPKA ENSKDKQYAL WLGDVVGVAT EADGSNTVFT
     LAAKRRPKSV SLYIRDEEED EEDEQGEDNA AAEGSKKSSS KRDSALNGLE KRSIPNGDAE
     LLGRGHRRTI IAQKTRSEQT AEEKRMSRRR ELFDQLVTSS TNRLSGMKTD TGPDTKAKST
     VAYKGAGQMP KEDDIRRLRL FVDKKYETVI LPIFGLPTPF HISTIKNVST SIEADYTYLR
     INFHHPGAIV GAKDVSGFQT PEAIYVKEMT YRASNLRRHG EATIPATNLN NTCRIIKEVL
     KRFRSREAEE RERADLVEQD QLIVDHAKGA FRLKDLYIRP NIATKRITGT LQTHTNGFRF
     TSIRGDQIDI LYNNIKHAFY QPCDGEMIIL LHFHLKNAIM YGKKKQQDIQ FYTEVGELTT
     DLSKAHSRMQ DRDDLEAEQR EREMREQIKT AFRSFVDKAE ALARRYNLEF ETPFRDLGFY
     GCPHRSTVFL MPTSSALISV TELPPFVVTL DEVEFIMLER VTLSIRTFDM VFVFKDYTKK
     PAMINSIPST ALELVKEWLL SCDLYYAEGT KSLNWPKLMK SILDNPEGFI EDGGWSFISP
     EEDDDEDEEN SEEEDENYAP SASELSGEGD EDASGADSSS EDDDDEDWEA EEESDEPESL
     DSDESEGKDW EELEEEAKRE DAKNLLLDED DSSRRKSSKK RHHSPDSHKK SSKKHKHR
//
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