ID C5K4N6_PERM5 Unreviewed; 1098 AA.
AC C5K4N6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=Pmar_PMAR010042 {ECO:0000313|EMBL:EER20308.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER20308.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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; GG670562; EER20308.1; -; Genomic_DNA.
DR RefSeq; XP_002788512.1; XM_002788466.1.
DR AlphaFoldDB; C5K4N6; -.
DR EnsemblProtists; EER20308; EER20308; Pmar_PMAR010042.
DR GeneID; 9053861; -.
DR InParanoid; C5K4N6; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000007800; 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 Reference proteome {ECO:0000313|Proteomes:UP000007800};
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 1..149
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 591..749
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 872..962
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 444..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1021
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 125119 MW; 31B69A790D9BDAAB CRC64;
MFENWPEKQQ AVPLVTTFQA LVAGEVSDDA LEQKTLAMHQ WLLGGELPET IMVIFGGDKD
KRSLWILSDK KKAEILEKLL TGVPLGDKFT IHYEVLDGAS DVAVYDKVFG MAKAIAGEKK
CQVGLLKKEK HVGKMAKGFT NYCSSNDTLA HDSIGNATAT VSSWMMIKDA EEVENMRRSA
IFSTLLMKQV MVRDVESVIE KDAKKSHEAI CDTVESAAEN KEMLTRWAKK FPYLAEDKAV
DVVYTLIQSG KEFTLRPDVQ PNREALDFSC IVVSVGAKYR EYSTNITRTL IVDPTKHQRA
YYNLCLSTMD TIIKSINGKE SVTCQEVYNA AVEHIKQKAS TVEYLHDALS QFQTDCGYSI
GLEFRDGHML LNAKNHKHIT PGMCLNLGVG FAGDKMVNEK KKPYAVWVCD SAYISTGRDG
KMKVELLTSG MSSGKDEVMY YLDTDQPGEN EDVVKSERKD STKKEKKSKK EKRQHDKTPD
KSKREKKRRE EAKSSSGRHK HKKDDLVIES RLRTRRNRAT AEDEEERKRL MEQQYELRAR
KVEECRARLL RSGEDAGDSG DDATNKNKCL DTCKSYATPD DIPRDIRTTK LTVDAKHDTL
LVPINGNLVA FHIRTIKNVS KPNDEGGKYT SIRINFHAPG TSFVQQDMFP EANRSKETLV
YLKELNYRAE DGRNLQAVFR GLKELQKRQR TRELEANTMK DIKEQPSLKL IKDRSRPVLR
DLNVKPQLGS TGRNRAVGTL EAHQNGFRFT SSRAEHVDII YRNIAHAIFQ PCENDQTVLL
HFNLKDPILV SGKKKTYDIQ FYTETRSAGD DLGTRRRAGY DPDEIMDEQR EREMITKLNK
LFREFVRQVE EQVWSQYAPN LEFDMPYREL GFTGTPNKAH VDIYPCRDCI VALSEWPAYV
LSLRNIDIVY FERVSFNLRN FDMTFIFKDY TQTPARISII PTESLDQIKQ WLGELGIVWY
QGPTNMNWTN IMKEINKKKQ AFIDNGAWEG WFGESVDEGS DDGMDEGDEE YTESEDSDVE
SEAGGSEYKG GGSDSDSGSS FLVDEESDSD SEVSLASDES EGLSWDELEK KAANEDRKRR
RSPESSEKKR PVSKKKRR
//
