ID A0A168HZ71_CORDF Unreviewed; 1042 AA.
AC A0A168HZ71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein HIR {ECO:0000256|RuleBase:RU364014};
GN ORFNames=LEL_05327 {ECO:0000313|EMBL:OAA78504.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78504.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78504.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78504.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA78504.1}.
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DR EMBL; AZHF01000003; OAA78504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HZ71; -.
DR STRING; 1081108.A0A168HZ71; -.
DR OrthoDB; 5478541at2759; -.
DR Proteomes; UP000076881; 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; 8.
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:UP000076881};
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..208
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 711..965
FT /note="Protein HIRA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07569"
FT REGION 427..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 112663 MW; 02376B1E71D9570B CRC64;
MLLIKPSWLS HSGEQKDFEV YSCHVSPDGK RLATAGGDGH VRIWSTEAIY NSRDPSYTKP
RQLCHMSHHL GTIHSVRFSP NGKYLASGAD DKLICVYHLD KGPPPATFGS DEPPPVENWK
TYKRLIGHEN DVQDLAWSYD SSILVSVGLD SKVVVWSGYT FEKLKSLPAH QSHVKGICFD
PANKFFATAS DDRTIKIFRF TSPGPSSTQH DMINNFVLET TISSPFKSSP LTTYFRRCSW
SPDGNHIAAA NAVNGPVSSV AIIERTRWDC EINLIGHEAP TEVCLFSPRL FHTSKPGGEA
SESDQPSLVT VIAAAGQDKT LSLWNTNTSR PVVILQDLAG KSISDLAWTP DGETLFAASL
DGSIVVARFE DGELGWVATA EENDRALQKY GASRKGMGIA EDVDGLMLED QSKAGESRDL
QSRMGALMGD APAGEGNASA ATNGTQTGDS TPKPAANGVS SEKPEQDKTA ERVKELKSRV
TVGKDGKKRV APLLVSSSGT GQSSLPQTQL IGSTSTTKTS QNDAPLTVLD LSKPFNGLPE
GGIASLLLGN KRIRTGAETE EGEEPLAKRP AGGPTAIVTG GVAGVEPAVL ANIENGVIPT
PEFLRPAVLN PALSVAAVRL AVPRVRSHII RPLEKGILGA ESATTKTAEI TILEAKNAAN
PNDPSRVIVS KRGAVVWHEF LPRAVILVTG NKNFWAAACE DGSIHVWSPA GRRLLNPMIL
ESQPVILECR DHWLLCITAV GMAYVWDIKT QSSPHPPVSL APILDAAVSS LDQHHTFTGG
PGVTSAHLNT TGHVVVTLSN GDGFYYARDM YTWQRLSESW WAVGSQYWNS NDSSVSALQS
TVVGPKSRTR STRRKSRRKQ EEQEPEEPAV DVSSGIIPFL ERHTTNEFMA KGRAYVMQRI
IKTVIQRKES EDLESVVSIA HLENRLAGAL QLGARDEFRL YLAMYAKRLG AEGAHGKVEE
LLKTLVGGIL QGDDADAEGG KGWFSKADEL CGWDRKELLK GVVLSLGKYR ELQRLTGQYA
RLLDLDLGSG AGADADSMEI EN
//
