ID V9EUF5_PHYPR Unreviewed; 1078 AA.
AC V9EUF5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=F443_12077 {ECO:0000313|EMBL:ETI42874.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI42874.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI42874.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI42874.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-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}.
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:ETI42874.1}.
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DR EMBL; ANIZ01002056; ETI42874.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EUF5; -.
DR EnsemblProtists; ETI42874; ETI42874; F443_12077.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000018721; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000018721};
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 31..193
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 573..728
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 849..939
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 463..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 657..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 463..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1040
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 123405 MW; 02ECCBF549AB65C5 CRC64;
MAEDKVTVKQ EVKTEVKTEQ GAAPASNVPR LNAAMFFRRL QRLYSSWKEN KNEPAWGGVD
SFCVLAGRAQ QEESGYRKSA VLQIYLLGFL EFPETLMVFT PQKLYVLTGG KKYTMLEAVA
QENATSDVKL ELLKRNKADG NVANFKVLTD AIKASGAKTG VLTKENPLGE LVASFKKALE
ATDVEQVEVG KGIETVLTVK ESEELENIRW AGALSSKVFK LKFMEDMEQI IDDEKSISHE
KISMAIEDVF DNPSKIKVTI DPVDIEPCYP PIVQSGGKYD LKPSAQSNKD PMKYDVIICS
LGARYKGYCS NVGRTFFIDP TSSMEKSYEL LREAHEMCVK ELQPGKIVGK VVEKVRKFIQ
SRNATLFGKL TKNLGFGIGL EFRESCNLLT TKNQTLIKEG MAFNVAFGFN DIPIPESQRK
KKKLDSYAVF LADTVVVLEN ETKYYTKVPK AWGKVRYDID DDNGEEEEKS KKKSSKGKDS
SIHGSVDTSL SGTRNQVLQS RLRDQQRQLE GKETDQERRD RHQAELMRRK REEAMRRLEE
QNNDKSDDPK KEKSIKAYQG PQDYPSELRE RQVMVDMRAE AVILPINGVP VPFHISTIKN
VSKSEEDKAT YLRINFYVPG TSLGRDVLPA MANAITKFPN KMFIKELGFR STDAHNLNNQ
FRLIKELQKR VKQREQREQE ESDLVVQEDL ILTRDRRVPR LIDLSARPHL TGRKTHGTLE
AHSNGVRFTT NKNQKLDILY ANIKHAIFQP CDKELVVLIH FHLKNHIMIG KKKQKDVQFY
TEVIEGSQTL DNRRRSMYDP DELDEENRER ALREKLNTTF KEFCHKMESV SERHGKPVVF
DIPYRELGFM GTPFKEMVLL QPSVHCLVSL TDMPFFIISL DEVEHVHFER VMFSSKNFDV
VFVFKNFDIM PTRISAVSMS ELERIKEWLD DIDICFTTGT ANLNWKSIMS TIKSDHRFYL
DTDDDGVPKP AGWEFLKMEG SDDEDDEEEE AGDSNYSGGS DEEDDDSDSS DSDGSDWESI
VDEESSSEEP SEDEDAPSWD ELEKEAQASD RMRNEKRDHD DDDEDYRRSS KKKKARRH
//
