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Database: UniProt
Entry: N1RZ52_FUSC4
LinkDB: N1RZ52_FUSC4
Original site: N1RZ52_FUSC4 
ID   N1RZ52_FUSC4            Unreviewed;       564 AA.
AC   N1RZ52;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=FACT complex subunit POB3 {ECO:0000256|RuleBase:RU364013};
GN   ORFNames=FOC4_g10009144 {ECO:0000313|EMBL:EMT70676.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT70676.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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; KB726312; EMT70676.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1RZ52; -.
DR   STRING; 1229665.N1RZ52; -.
DR   HOGENOM; CLU_017374_3_0_1; -.
DR   Proteomes; UP000016929; 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:UP000016929};
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          374..468
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          482..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..517
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..551
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  63142 MW;  047836883A6B0385 CRC64;
     MTAIESFDNI YLDLSKESGK CRFAETGFGW KPAGGGDTFT LDHNNIASAQ WSRAAKGYEI
     KIVQRAKSGI IQLDGFQQED YDRLAKVFKN WYSTVLESKE HALRGWNWGK AEFSKSELTF
     SVQNRPAFEL AYSEIGNTNL AGRNEVAVEM ALPDTGANAQ LGGARSKGSK AAAGRDQLVE
     MRFYIPGVTT RKEAEGEDAG SDAGNDEQEK NAATLFYETL IDKAEIGETA GDTIATFLDV
     LHLTPRGRFD IDMYEASFRL RGKTYDYKIQ YEAIKKFMVL PKPDEVHYML VMGLDPPLRQ
     GQTRYPFVVM QFKKDEEVTI DLNLNEDELK SKYQDKLEPH YEEPLHQVVA KIFRGLGNRK
     ISSPAKDFIT HRNQYGIKCS IKASEGFLYC LEKAFMFVPK PAVYIAYEQT QSVTFSRVSG
     AVSALSTFDI TVLLKNGAGS SQFSNISRED LKALETFFKL KGLRVKNEID EDANLLAAAL
     DQQMDDSEDE VAAKADRGSA DEDEESVDED FRTDSESDVA EEYDSAHESS GSGSDESNVD
     EDEERDDDDE DAEEERPKKK KKTG
//
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