ID U6M3P0_EIMMA Unreviewed; 564 AA.
AC U6M3P0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=EMWEY_00010900 {ECO:0000313|EMBL:CDJ57688.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ57688.1};
RN [1] {ECO:0000313|EMBL:CDJ57688.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ57688.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ57688.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ57688.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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|RuleBase:RU367052}.
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DR EMBL; HG719359; CDJ57688.1; -; Genomic_DNA.
DR RefSeq; XP_013334336.1; XM_013478882.1.
DR AlphaFoldDB; U6M3P0; -.
DR EnsemblProtists; CDJ57688; CDJ57688; EMWEY_00010900.
DR GeneID; 25335076; -.
DR VEuPathDB; ToxoDB:EMWEY_00010900; -.
DR OMA; TRANELW; -.
DR OrthoDB; 169847at2759; -.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor 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 Gene3D; 2.30.29.150; -; 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; IPR013953; FACT_Spt16.
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; 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.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW DNA damage {ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052};
KW Elongation factor {ECO:0000313|EMBL:CDJ57688.1};
KW Nucleus {ECO:0000256|RuleBase:RU367052};
KW Protein biosynthesis {ECO:0000313|EMBL:CDJ57688.1};
KW Transcription {ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 22..210
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 330..420
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 444..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63985 MW; E08A9A58BD0B37A3 CRC64;
MEDIKAFTSP EDFPKDLRPS KLYVDMKSEC LFLPFPSRHL PVHLSTVKNV TCSETETSAS
AAAAAAAAAA AGGGGGGAAG GGGKGNRYAI LRINFQVPGS QTLTQKGEEN PLPDIAGKQQ
LFIKELMFKS EDSRHLQNIY RTIKEQLKRV KQKAAEDSQY PGELPAQEKL ILNRSGRRIL
LKDLMIRPNI STGMRKLIGA LEAHTNGLRF TVNTRGQMDV VDVTYSNIKH AILQPCEREL
IVLVHFHLKT PILVGKKRTL DVQFYTEAGT QTDDLDNRRT RSYHDPDETL DEMREREMKK
KLNGEFKRFV QQVEEVSKVE FDLPYRELKF SGVPLKSNVE ILPTANCLVH LVEWPPFVLP
LEDIEIVSFE RVSHGLRNFD MIFVFQDYNK PVKRIDLIPI EYLDNLKRWL NELEIVWYEG
KQNLNWAAIL KEIRDDPRGF VEDGGFDMFL GDNGSDEEGD DSEDDDDEEY AEQSSSDDDK
EYNEDGSEDA SSDQGSDSDS DYSSDDSSLA DESDGYEEAA GTDSDEEEGL SWDELEERAK
KEDRKRQADD DSEEEERRTK KKRK
//
