ID K2S026_MACPH Unreviewed; 1346 AA.
AC K2S026;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Structure-specific recognition protein {ECO:0000313|EMBL:EKG18337.1};
GN ORFNames=MPH_04419 {ECO:0000313|EMBL:EKG18337.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG18337.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18337.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18337.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG18337.1}.
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DR EMBL; AHHD01000209; EKG18337.1; -; Genomic_DNA.
DR STRING; 1126212.K2S026; -.
DR VEuPathDB; FungiDB:MPH_04419; -.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_258007_0_0_1; -.
DR InParanoid; K2S026; -.
DR OrthoDB; 2285587at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; cd00067; GAL4; 1.
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 Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR021858; Fun_TF.
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 InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR Pfam; PF11951; Fungal_trans_2; 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 Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 597..623
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 149904 MW; 9734C582EB74956C CRC64;
MSAWNVNTPP PIANKDAPRD RSEPLRESFD GIYLDLSKQP GRCRFAEGGL GWKPSAGGET
FTLDSSNITQ AQWSRASRGY ELRVFTKNTG IIQLDGFQQE DFERLAKVFK MWYSINLENK
EHALRGYNWG KAEFGKSELS FNVQSRPAFE LPYSEIANTN LAGKNEVAIE FSLPANGEDT
GTNGHLGGAR ARGKKSGGAR DQLVEMRFYI PGTVTKKEKK EEGEGEGEDV SDEGEEEEHN
AASLFYNTLI EKAEIGEIAG DTFITFEDIL HLTPRGRFGL DMYETSFRLR GKTYDYKIQY
DQIKKFFVLP KPDDIHQLIT IGVDPPLRQG QTRYPFIVMQ FKKDEELDEP VPLNIEPDVL
EEKYKGKLEA QYEGPIYRVV AQLLRGLSGR KTIAPSRDFI SHHQQSGIKC SIKANEGHLY
CMDKSFLFVP KPATYISFDQ ISVITMSRVG GNLSSSRTFD ITIRMKNGSD HQFSNINREE
QTPLEEFFKI KNLKTKNEMV DDSGALLAAA LNDDLDESED EQVAVNRGSA DEDSEELDED
FEAESESEVA EEFDSEHESS GSEDEEMADA DGDADGDEDT SMVERPKKKA KTDNQTCRLR
KLKCDERKPV CGPCTKANRE CVFNSGLIFR HQQNASMNGD GDGGEQGLKG FYAYKNTFGH
DAVWLDIPKQ VRFWNTTDPY NEPMSPESET SPGSAPEQPA SAHHDAASMQ WPLTDSFTQP
DAQSPAHALH ALSAVATGDH FAYMHPHVGR HDSTPVPDAP MRSSASLSGM HPPTPLARQA
VDSPISPPVS MTSSTNHNID FILNHPAAAS PPLDPSLQSP YAHSAREVLH ARSGSSRMSM
GSSQFDTNVE VDHEITYLLR YYSEGPGQWM DLFDLGSYFG SYVPVKAQTN PVLKYAAVAY
AAKALGRVKG KRPIMGGNAI RHARTELYPN AHAVDWYHKA TEYYDNAVSL LRQALQDDSR
GISHESGTGD AQWRAADGSD VSFGHAKRNS LSGFPVSRCN SDELLAATAI LCVYEFLDAS
GPEWSRHLSG AKSLIDIAKD SMMPLQLPSP GLALQAQSGK LSKARKATFW NVARQDMLSA
FINATQTRLD TEDLPMWKDA GLQIDDNGFI VPVEPSPSGY PESGDVMKED MIANSLVWLM
SKLVNFMAAG DELPPQPGSP WAQGVPQRTL LDYWTYLKRQ FQIWYDSLPL TFKPCARIPP
TRIPGSLVDD DLDAVLPEVW YSLPMCGSTM QSYHMAQVQL LMNKPHETTQ GRSSIFARFS
SYENAVQESQ AHSREIVSIA LSRPDASVRI NSVQPLYTAG QCLADPRERR LIIKLLREIE
ADTGWATDYR VNQLLEQWEW SEGDIP
//
