ID A0A2T3Z130_9HYPO Unreviewed; 1058 AA.
AC A0A2T3Z130;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Protein HIR {ECO:0000256|RuleBase:RU364014};
GN ORFNames=M441DRAFT_70878 {ECO:0000313|EMBL:PTB38503.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB38503.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB38503.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB38503.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for replication-independent chromatin assembly and
CC for the periodic repression of histone gene transcription during the
CC cell cycle. {ECO:0000256|ARBA:ARBA00002677,
CC ECO:0000256|RuleBase:RU364014}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364014}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family.
CC {ECO:0000256|ARBA:ARBA00007306, ECO:0000256|RuleBase:RU364014}.
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DR EMBL; KZ679265; PTB38503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3Z130; -.
DR STRING; 1042311.A0A2T3Z130; -.
DR OrthoDB; 5478541at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR031120; HIR1-like.
DR InterPro; IPR011494; HIRA-like_C.
DR InterPro; IPR019015; HIRA_B_motif.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13831; MEMBER OF THE HIR1 FAMILY OF WD-REPEAT PROTEINS; 1.
DR PANTHER; PTHR13831:SF0; PROTEIN HIRA; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF09453; HIRA_B; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU364014}; Nucleus {ECO:0000256|RuleBase:RU364014};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364014};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|RuleBase:RU364014};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364014};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364014};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 20..47
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 66..107
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 125..166
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 167..198
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 741..982
FT /note="Protein HIRA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07569"
FT REGION 433..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 115296 MW; E3D0FCD53F5A5C5B CRC64;
MRIIKPSWLS HSGEQKDFEV YSCHVSPDGK RIATAGGDGH VRIWSTEAVY HADDESYKKP
RQLCHMSHHL GTIHSVRFSP NGRYLASGAD DKLICVYHLD KGPPAPTFGT NDPPPVENWK
TYKRLIGHEN DVQDLAWSYD SSLLVSVGLD SKVVVWSGHT FEKLKSIPAH QSHVKGITFD
PANKFFATAS DDRTIKIFRF TPPAPNATQH DMINNFVLDA TISSPFKSSP LTTYFRRCSW
SPDGNHIAAA NAVNGPVSSV AIIERTRWDS EINLIGHEAP TEVCMFSPRL FHTVKPGQNG
AANGHGGQLV TVIASAGQDK TLSIWNTNTS RPVVILQDLA GKSISDLAWT PDGQTLFASS
LDGSVVVAKF DEGELGWVAQ QEENAKALQK YGGSRKGMGI AEDVDGLMLE EHSKAGESRA
VQSRMGALMG DFQPESAKES TPATQGSKAE SSTSVTEKLA TNGNADSDRD KEKEKDKDKD
KDKDKSEKPD EPADKTAERV RELKSRVTVG KDGRKRVAPL LVSSSGTGQS SLPQSQLVGS
TTTKNTQNDA PQTILDLSKP FDGLPKGGIV AMLLGNKRRV NAADIDDDEE PTAKRTAGGP
TAVVTNGVDG VEYAALVPVE HGVVPTPEFL RPAVLNPSIS YAQVRLAVPK IRSHILRPLE
RGILQPDAAS LDDASKLPEN IILEAKNDPN PRDPAHVLVT KRGVLVWQEF MPRAVILVTA
SKHFWAVACE DGSLHIWTPA GRRLLNPIIL ESQPVILECR DYWLMAITAV GLVHVWNLKT
QSSPHPPVSV GPILDIATTS LNQHSATPGP GITSAHLNST GHIIVTLTNG DGYFYARDMF
TWQRLSEAWW AVGSQYWNSN DSSISALQST AVGPNSKEDK DKGSHAATVS SGIIPFLERH
TTNEFLLKGR AYALQRIIKT VMQKSGSEGL ESSVSIAHLE NRIAGALQLG ASDEFRLYLF
MYAKRLGAEG ARGKVEELLN SLLGGVLEDK ESEKTSSRGW YSSDEQLCGW DRKELLKGVV
LILGKFRELQ RVTSQYARLI DLNLDNVSAD ADSMDVEA
//
