ID A0A0C4E0A1_MAGP6 Unreviewed; 1032 AA.
AC A0A0C4E0A1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=MAPG_05769 {ECO:0000313|EMBL:KLU86759.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_05769T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU86759.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU86759.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU86759.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU86759.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_05769T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_05769T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_05769T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_05769T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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; ADBL01001379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876969; KLU86759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4E0A1; -.
DR STRING; 644358.A0A0C4E0A1; -.
DR EnsemblFungi; MAPG_05769T0; MAPG_05769T0; MAPG_05769.
DR VEuPathDB; FungiDB:MAPG_05769; -.
DR eggNOG; KOG1189; Eukaryota.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0140713; F:histone chaperone activity; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0140719; P:constitutive heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IEA:EnsemblFungi.
DR CDD; cd01091; CDC68-like; 1.
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 InterPro; IPR033825; Spt16_M24.
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 Reference proteome {ECO:0000313|Proteomes:UP000011715};
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 6..167
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 546..696
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 821..911
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 940..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 625..655
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 941..1002
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 117750 MW; CF15E768291BF908 CRC64;
MAEIKIDGKL FQERVSHFIN AWKSDKRSGD ALFGGVSSIL IMMGRVEESP EYHKNNAMHF
WLLGYEFPTT LMLFTIDTLY ILTTAKKAKH LDQIKGGRFP VEVLVRGKDA AENTKAFVKI
TDAIKEAGNK IGVLTKDTAK GPFVDEWKKI FAENCKDVEE SDIAQALSAA AFATKDEAEL
RAMRTSSKAC VALMHPFFLD EMSAILDQEK KVKHSALAEK VEKKLDDDKW WKTVTLPNKQ
KLPGDFDPEQ LDWILGPNVQ SGGKYDLRWA TEPNDDNLHP GIIISALGLR YRSYCSSIAR
TFLVDPNKSQ ESNYKLLHAT HQLILKEIRD GAVVKEVYQK ALAYVKSKKP ELEKHFLKNI
GCGIGLEHRD PTMILNAKNS RSLKDGMTLC ITSGFSDIEN PTPQDKNSKV YSLVIIDTVR
VTTGEPVVFT GDAPTDADAS SFFFKDEETQ PAPKKEKKEA RVGAVATKNI TSTRLRSERS
TQVDEDAEKR RREHQKELAM KKQKEGLARF AESTNDQNGT EVKKFKRFES YKRDNQLPPK
IRDLSIVVDQ KNATVIVPVM GRAVPFHIHT IKNASKSDEG EWSFLRINFL SPGQGVGRKD
DQPFEDATAH FVRSLTFRSL DGDRYTEIAN QIANMKKESA KKEQEKKDME DVVEQEKLVE
IRNRRPAVLD NVFIRPAMEG KRVPGKVEIH QNGIRYQSPL AAQQRVDILF SNVRHLFFQP
CQHELIVIIH IHLKDPILIG NKKKTKDVQF YREATDIQFD ETGNRKRKYR YGDEDEFEAE
QEERRRRADL DRLFKAFAEK IAEAGRSENI EVDMPLRELG FNGVPFRSNV YIQPTTECLI
QITEPPFLVV TLEDIEVAHL ERVQFGLKNF DLVFVFKDFT RAPTHVNTIP VESLEDVKEF
LDQSDIAYTE GPLNLNWPTI MKTVTSDTHQ FFVDGGWSFL QADSDDEDNE DEDDQESAFE
ISESELEEAS ESSEEDSEYD SNASDDASEE GSDEDEEEGE SWDELERKAK RKDRESGLDD
EEDRGKKKQR KR
//
