ID A0A0D9QJQ0_PLAFR Unreviewed; 1056 AA.
AC A0A0D9QJQ0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=AK88_03215 {ECO:0000313|EMBL:KJP87168.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP87168.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP87168.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ001679; KJP87168.1; -; Genomic_DNA.
DR RefSeq; XP_012336259.1; XM_012480836.1.
DR AlphaFoldDB; A0A0D9QJQ0; -.
DR EnsemblProtists; KJP87168; KJP87168; AK88_03215.
DR GeneID; 24268529; -.
DR VEuPathDB; PlasmoDB:AK88_03215; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000054561; 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, ECO:0000256|SAM:Coils};
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 437..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 957..1022
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 122194 MW; 8842A464809B8828 CRC64;
MNESLDIENA KAKLKLVFSF WESCENKSFS QSKAFCVLSG KSSKEENATT QEQFQMWLLG
YQLTETFFLF LNKEKLIILT SDKKKKFLQP LLDSVENVQV MERTNDNTEN FNKIKKMINE
VGTEEIAVLK DKDAMGNFFE SCYNFIKALE IPQLDVNTDL KFLLNFRSES DIKIQKSGSD
IACIILKNIL ITTIENALDS EEYQSHDKIK DKALKFHENK KCVLKLKEKL KVDIDDIDVI
YSNVQSGNEF TLNYKNSNNK SYLSQNEGTI LVGVGVKYKE LCSNVNRTLL LNAKTQHKEL
YSFTLAIEKY VIKECLQVQS TYADVYKKAL SFVKTSKKDY STLSEINVED YFVKCLGHVI
GIEFMEKDFL ITENNTSGMI QKNTSYNLSV GFENVPENDK NNFAIWISDT VCINDAGEVN
VLTDSISKEI NTISYELEDS KSEEENDTKV KSEKKEQNGD YKKEKTGISA SILNNAASVI
VSDRLRRRNK NSLAHNNEQE MEELNKRQSE LKEKKMNEIK IRFSKGTSDY KDPNKKNVKK
LEDVKAYNDV DMLPRDLRPN IICVDNKHEC ILLPINGAHI PFHVSTIKNL SSNYEDNNDI
FVLRINFQVP GGQGVLKGDF NTFPTLQEKE MYIKELIFKS NDERHFQNIV KQVKDLIKHV
KQKEVEADVN DPQHAQEKLI LNKSGRRIML RDLMTRPNIF TGRKILGTLE LHTNGVRYSA
NSRGTTEYID ILFDDIKYAF YQPCDGQLII LIHFHLKRYI MVGKKKTLDV QFYCEAGTQI
DDLDRAKARN VYDPDEMHDE MKEREQKNRL NLIFKNFVQQ MQDISKIEFE IPYPELTFSG
VPNKSNVEIF VTANTINHLV EWPPFILSVE DIEIASLERI HHGLRNFDMI FVFKDYTKPV
KRIDVIPTEY IDTIKKWLTT IDIVYYEGKN NLQWGNILKT ILADIDSFVE SKGFDGFLGD
DDEEDEQSAE DEDDDDEYEL DESEMSAEDD SDYDDSEDES LATESDGEGE VEEDSDDEGL
SWDELEERAK KDDKKRFAYK SDDDEGYNKR KKKKKN
//
