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Database: UniProt
Entry: A0A421J9F9_9ASCO
LinkDB: A0A421J9F9_9ASCO
Original site: A0A421J9F9_9ASCO 
ID   A0A421J9F9_9ASCO        Unreviewed;      1019 AA.
AC   A0A421J9F9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protein HIR {ECO:0000256|RuleBase:RU364014};
GN   ORFNames=JA9_001878 {ECO:0000313|EMBL:RLV85455.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV85455.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV85455.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV85455.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) 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|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:RLV85455.1}.
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DR   EMBL; NSDU01000013; RLV85455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421J9F9; -.
DR   STRING; 2028340.A0A421J9F9; -.
DR   Proteomes; UP000286412; 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   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:SF1; PROTEIN HIR2; 1.
DR   Pfam; PF07569; Hira; 1.
DR   Pfam; PF09453; HIRA_B; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
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:UP000286412};
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          8..40
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          736..963
FT                   /note="Protein HIRA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07569"
FT   REGION          141..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  113273 MW;  AF021A87EAA382AC CRC64;
     MKAIVFPTSL HAGEVHTADI SSDGARVLTG GSDGAVSVYK YADFRAFDMS KPCSLTPVKT
     VELDSTVTVG RFCPTDADII AVGTINGSVY LVGENTLVCI FPLSKWNVVQ PTNTGEVKAY
     NAPPNDKPVL AKAPEELTSS GLEKTPELAT LTDKSEKSPP AKPSHTSIST PNILDVAWSP
     DGRLVAWISA FEVHIHDRSK NTYQTLITSK PNSSPRSIAF DPTSSFFVCL GDDTVIDIYR
     YHYKNDMYQF KHFTTNSRMA NAVPNIVNYR RISWSPDGEY VSVPTASKGQ TSLVSLISRS
     SQWSAKVSLV GHDTCCEVVR FNPTIYAWDG GDSKTGIPPV EKPLEPNAEP TNDDSNDNNA
     EDARPHFVYN IVATAGSDMT LSVWNTIKEK PLLLLKDIAT KPISDLVWHP NGQSLLQSSM
     DGHITLYNFE DHELGNPASK TINNQLLEFS KKIIHPFEYT QPVEGATKKP PPPVIIDQKN
     ATEQNSKPDQ EAESVADAAP STAHETKKEK QVPEDEDIRP VVLEPSTGTD TSQHSFLNEA
     PIIKRPKLTS QEPAKLSKQK VSTKDGKKRI QPMLISSTNG SSNTTPLSSN GHDMWNNSNT
     PSLPMEYEKP SYVVADSVSR KRPKNDDSTK KKRELEPIKF IGSQLQNPNT AFAAIRLAVP
     KVRLSFQIEQ NESAFLDVKN GSGNESTPTR LTYVRNDRQL WTDFIPRYVL LATKGTNFWA
     TATADGEIYT YVLESGKRIF PPIVLGSAIS FLESHEQFLL AITSVGELYV WDLNEKRIVL
     HSPQSVKALL DLSSKYEEDV LSKSENITMC SVTSKGIPLI TMSSGSGYLF NKDLGVWHIV
     TESWWAFGSH YWGSLAYNRT SSDSAKQEES IIALLEQKTN EEILRKSRTG RGKFMNKISK
     NMIMKEGFEN LENSISINHL ENRMLASELL GEKDDFHAFF LTYVRRISEL GLQAQLLGIC
     SELYGPEDMK SNGWKPEICE WDKRALLKEL VLTCAKYRNV QRILVHYAEK IGVVSEMYG
//
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