ID W7A9D5_9APIC Unreviewed; 1057 AA.
AC W7A9D5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=C922_01315 {ECO:0000313|EMBL:EUD68295.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD68295.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD68295.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD68295.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-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|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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DR EMBL; KI965463; EUD68295.1; -; Genomic_DNA.
DR RefSeq; XP_008815143.1; XM_008816921.1.
DR AlphaFoldDB; W7A9D5; -.
DR EnsemblProtists; EUD68295; EUD68295; C922_01315.
DR GeneID; 20036589; -.
DR VEuPathDB; PlasmoDB:C922_01315; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000030640; 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 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..160
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 562..718
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 838..928
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 438..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1023
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 122255 MW; 4EC9BAA6B92B1F80 CRC64;
MNESLDIENA KAKLKLVFSF WANSENKSFS QSNAFCVLSG KSSKEENATT QEQFQMWLMG
YQLTETFFLF LKKERLIILT SDKKKKFLQP LLDNMENVQV MERSNDNREN FIQIKKMIKE
AGTEEIAILK DKDATGSFFE SCYSFVKSLD MAQVEVNKEL KFLLNFRSES DMKIQKSGSD
IACIILKNIL ITTIENALDS EEFQSHDKIK EKALKFHENK KCVLKLKEKL KVDIDDIDVI
YSNVQSGNQF SLSYKNSNNK SYLSQNEGTI LVGVGVKYKE LCSNVNRTLL LNAKTQHKEL
YSFALAIEKY VIKECLQVQN TYADVYKKAI TFVKKNKKDY PTLSGVPVED YFVKCIGHVI
GIEFMENDFL ITESNNTGMI EKNTSYNLSV GFENVPGNDK NNLAIWISDT VYINEEGEIS
ILTDSISKEI NTISYELEDS KSEDEDENKV KSEKKEQNGE FSKKKTGISA SILNNAASVI
VSDRLRRRNK NSLAHTNEQE MEELNKRQSE LKEKKINEIK FRFSKGTSDY KDPNKKNVKK
LEDVKAYNDT DLLPRDLRPN IICVDNKHEC ILLPINGAHI PFHVSTIKNL SSNYEDNNDI
FVLRINFQVP GNQGVLKADF NTFPTLQEKE MYIKELIFKS NDEKHFQNIV KQVKELIKQV
KQKEVEADVN DPKHAQEKLV LNKSGRRIIL RDLMTRPNIF TGRKILGTLE LHTNGLRYSA
NSRGTTEYID ILFDDIKYAF YQPSDGQLII LIHFHLKRYI MVGKKKTLDV QFYCEAGTQI
DDLDRAKARN VYDPDEMHDE MKEREQKNRL NLIFKNFVQQ MQDISKIEFE IPYPELTFSG
VPNKSNVEIF VTANTINHLV EWPPFILSVE DIEIASLERI HHGLRNFDMI FVFKDYTKPV
KRIDVIPTEY IDTIKKWLTT IDIVYYEGKN NLQWGNILKT ILADIDSFVN SKGFDGFLGD
QEDDDDEQSA EDEDEDDEYE VDESDLSAED DSDYDDSEDE SLATESDGEG EVEEDSEDEG
LSWDELEERA KKDDKKRFAY KSDDEEGYNK RKKKKKN
//
