ID A0A0D1Z7H9_9PEZI Unreviewed; 558 AA.
AC A0A0D1Z7H9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=FACT complex subunit POB3 {ECO:0000256|RuleBase:RU364013};
GN ORFNames=PV09_00835 {ECO:0000313|EMBL:KIW08917.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08917.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW08917.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08917.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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|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; KN847530; KIW08917.1; -; Genomic_DNA.
DR RefSeq; XP_016218786.1; XM_016353633.1.
DR AlphaFoldDB; A0A0D1Z7H9; -.
DR STRING; 253628.A0A0D1Z7H9; -.
DR GeneID; 27308808; -.
DR VEuPathDB; FungiDB:PV09_00835; -.
DR HOGENOM; CLU_017374_3_0_1; -.
DR InParanoid; A0A0D1Z7H9; -.
DR OrthoDB; 5488575at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:UP000053259};
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..468
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 62603 MW; 3D94865EB6C55230 CRC64;
MSMETFENVY MDFSKAPGRC RFADSGLGWK PAGGGDTFTL TQEQMQHAFW NRAARGFEVK
IYRKDAPVVQ FDGFQEDDFD RIQKIFKNWY HIPLDKQEHS LRGWNWGRAE FGKAELSFNV
QSRSAFDIPY TEVSNTNLAG KGEVAVEFSL PGDGEETGTN GHLGGARGGG KKAGAARDQL
VEMRFYIPGM TAAKTKSEDG EDGEVDEDAE EQQAADVFYQ TLSEKAEIGE VAGDTIATFQ
DVLHLTPRQA PLHCCVVCFR LRGKTYDYKI QYDSVKKFMI LPKPDEMHVL LTIGLDPPLR
QGQTRYPFVV MQMNKEEEVV LELNMKDEDF EQEYKGKLQK TYEAPLHSVV AALFRGLAGK
KLTMPSKDFQ SHHHASGVKC SIKANEGLLF CMDKSFMFVP KPATYVNMDQ VTLITMSRIG
GAMAASRTFD ITMAMRGGGE FQFSNINREE QKPLEDFFRI KGLKIKNEMA EEEKMTAALL
NGVDDESDDE VVADRGSADE DSEEADEDFQ DDEESDVAEE YDSQHESDGD SDEEMGDADA
ASEEEEERPK KKAKTSGK
//
