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Database: UniProt
Entry: A0A1V9YWA3_9STRA
LinkDB: A0A1V9YWA3_9STRA
Original site: A0A1V9YWA3_9STRA 
ID   A0A1V9YWA3_9STRA        Unreviewed;       966 AA.
AC   A0A1V9YWA3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Protein HIRA {ECO:0000256|RuleBase:RU364014};
GN   ORFNames=THRCLA_09472 {ECO:0000313|EMBL:OQR90005.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR90005.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQR90005.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR90005.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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|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:OQR90005.1}.
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DR   EMBL; JNBS01002615; OQR90005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9YWA3; -.
DR   STRING; 74557.A0A1V9YWA3; -.
DR   OrthoDB; 5478541at2759; -.
DR   Proteomes; UP000243217; 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; 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; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 7.
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:UP000243217};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364014};
KW   Repressor {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          14..47
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          61..102
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          121..162
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          168..209
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          680..866
FT                   /note="Protein HIRA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07569"
FT   REGION          436..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  106256 MW;  68BC034F27E7C7D2 CRC64;
     MLLEKPSEVR HSNAAGQDCA IYAIDAHPNQ LKVATGGGDT CVKIWSIVDK DGPCFELLAT
     LAWHEKSVNC VRWSHSGKYL ASGSDDHSVF IYEFKEGAPS AVPFGSKQQP NKEKWERCAI
     LKNHTMDVQD VAWSPDDRML ATCSIDNSIL IWSMDQITPV MTHPIQHLTG HNGWVKGVAW
     DPVGKYLTSA GEDKSVIVWK VDTWEIEERI QTPFELCASS SHFRRLSWSP DGSLICATHA
     HKSKQDVGAL VERKSWVNEV NFVGHRGVVT TARFNPRLLA KKSTNKEFTC CALGGDDCTV
     SIWLADVARP LAVVKDCFDA SVTDLSWSHD GFTLFSSSLD GSICFFQFTA DELGTPITPQ
     QQSRLLQQKY GSLAGLTSGS TLVEDPLQLE LEACEKSTGP TSTMDMLAKR ITPMGEASQV
     LNQAPAPSVF TLTARPKSTT APEKDIATPK TTDNNEPQAP AANTLVPRPK PIAITNTENI
     SPKTAQPPTI AVTEPTAVKA AQKALEPTTN TVKPTAPASE PTANSITTLV ARPKSKAPAT
     TSAPPSSIQK DDDNAPIKRK RNLEVTPAAK ARSSMLVYSI ALVAGLLKFF CRVEADERED
     VLAEISPRDV FNHTITLPRN KTRTLECRVS DDSCNITCTE AGDCLWMDRL PGHVVCMAGN
     QSFCAFGTED GSLYIVSATG RRLFPCMALG HGFASIETSP NATPYLLVVL RNGAVKTWNV
     LQPSLFIDTT LRSMVTFKST LIRSLVTDKG QPIVTMALSS GGRSRLHSFT FDLAMKCWMR
     VADDHFSYSD FTTSVLTDTI VVASEVPVGP LRRLQNASSH ARNAKNMLDN FTNINLQRHV
     TRTHLEQQLT SAIALQSRGE YKYWLVDLKG TFLSDDYCIR LKIYARYLAQ EGDVARLEEL
     CTDLVGPMSA SSTTVNNPRQ TWQPLIMDMV KRDLLRTIVM PQMATNRILQ RLVTKYRVQL
     DTHGST
//
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