ID K1W653_MARBU Unreviewed; 458 AA.
AC K1W653;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Negative regulator of DNA transposition protein {ECO:0000313|EMBL:EKD12435.1};
GN ORFNames=MBM_09469 {ECO:0000313|EMBL:EKD12435.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12435.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12435.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12435.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome
CC formation and heterochromatin silencing. Required for the deposition of
CC H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role
CC in the transcriptional regulation of the cell-cycle dependent histone
CC genes by creating a repressive structure at the core histone gene
CC promoter. {ECO:0000256|ARBA:ARBA00037550}.
CC -!- SUBUNIT: Interacts with histones H3 and H4.
CC {ECO:0000256|ARBA:ARBA00038654}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the RTT106 family.
CC {ECO:0000256|ARBA:ARBA00006159}.
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DR EMBL; JH921458; EKD12435.1; -; Genomic_DNA.
DR RefSeq; XP_007297358.1; XM_007297296.1.
DR AlphaFoldDB; K1W653; -.
DR STRING; 1072389.K1W653; -.
DR GeneID; 18765404; -.
DR KEGG; mbe:MBM_09469; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_033828_0_0_1; -.
DR InParanoid; K1W653; -.
DR OMA; AMPEAHR; -.
DR OrthoDB; 1359279at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.29.120; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF3; HISTONE CHAPERONE RTT106; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 263..360
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 377..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49465 MW; 88199F514AFCAD83 CRC64;
MGSSSLDEKS LAKAFEGRVD IQGAIRNASA AGPHYIELFN QISQYVCTVI PGNSPEPANK
KRRIEDQGLV ARPASSGANG HAAIDGATKA AADASSDEPV LLEVKEISVA VPQRKKYTLC
FTSKHLYARL PDSTEPVPGM SFAWSNIEYA FCLPVPEKTV KQHNYILFPR NSAITPSRPI
AGASPNIEPL VFTIPDTAPK AGSISGLEAG AAAAVSDDYK TLFDWALSAR FKAAGKSNFK
ITQADPKSFA SELKQSHRPH EKAVFVKGFR GSKDGYLFFL PNGILWAFKK PLLFLPNERI
SAVSYTSVLQ RTFNLAVEVD TSVPGEAENK AEYEFAMLDQ EDFVGIGNFV KRHGLQDKSM
AEQRKAKRLN INAVKDEDGN IIDSEESNEL EKAATEAEQA AMDEEDEDEE DYDPGSEGES
EGSGSSSEED DSDDEGGTAA GEHSEGDGDG DGHDESEL
//