ID G0RJY2_HYPJQ Unreviewed; 574 AA.
AC G0RJY2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=FACT complex subunit POB3 {ECO:0000256|RuleBase:RU364013};
GN ORFNames=TRIREDRAFT_4004 {ECO:0000313|EMBL:EGR48673.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR48673.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR48673.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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|ARBA:ARBA00025370,
CC ECO:0000256|RuleBase:RU364013}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364013}.
CC Chromosome {ECO:0000256|RuleBase:RU364013}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060, ECO:0000256|RuleBase:RU364013}.
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DR EMBL; GL985064; EGR48673.1; -; Genomic_DNA.
DR RefSeq; XP_006965222.1; XM_006965160.1.
DR AlphaFoldDB; G0RJY2; -.
DR STRING; 431241.G0RJY2; -.
DR EnsemblFungi; EGR48673; EGR48673; TRIREDRAFT_4004.
DR GeneID; 18484772; -.
DR KEGG; tre:TRIREDRAFT_4004; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_4004; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_3_0_1; -.
DR OrthoDB; 5488575at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; 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-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0034728; P:nucleosome organization; IEA:EnsemblFungi.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR CDD; cd13230; PH1_SSRP1-like; 1.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR CDD; cd13229; PH_TFIIH; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR048993; SSRP1-like_PH1.
DR InterPro; IPR000969; SSRP1/POB3.
DR InterPro; IPR035417; SSRP1/POB3_N.
DR InterPro; IPR024954; SSRP1_DD.
DR InterPro; IPR038167; SSRP1_sf.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR Pfam; PF21103; PH1_SSRP1-like; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU364013};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364013};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364013};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU364013};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364013};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364013};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364013}.
FT DOMAIN 375..469
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 485..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 64353 MW; E7FD4841150FC4BA CRC64;
MTAIESFDNI YLDLSKESGK CRFAETGFGW KPAGGGDTFT LDHTNISSAQ WSRAARGYEI
RILQRNSGII QLDGFQHEDY ERLSKIFKNW YSTALENKEH ALRGWNWGKA EFSKAEIVFN
VQNRPAFELP YSEIGNTNLA GRNEVAVELA LPVNANDTGT NGQLGGARGK GKKAGAGKDQ
LVEMRFYIPG TTTKKETEGD DAGSDGEEEE QNAATFFYET LIEKAEIGET AGDTIATFLD
VLHLTPRGRF DIDMYEASFR LRGKTYDYKI QYEAVKKFMV LPKPDDMHCL LCIGLDPPLR
QGQTRYPFVV MQFKKDEEVT IDLNIDEEEL QTKYKDKLEA HYEEPLHHVV AKIFRGLGNK
KISSPAKDFL THRNQYGIKC SIKASEGFLY CLEKAFMFVP KPATYIAYEQ TQSVTFSRVS
GAVSALSTFD ITVVMKNGAG SSQFSNINRE DLKALESFFK LKGLRVKNEI DEDANLLAAA
LREEAMDDSD DEVVVPKADR GSADEDEESV DEDFQADSDS DVAEEYDSNH ESSGSGSAES
DVDNDDEDEE MDDVDDDDEE EEERPKKKSK TGKK
//
