ID A0A401PMI4_SCYTO Unreviewed; 1042 AA.
AC A0A401PMI4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Protein HIRA {ECO:0000256|ARBA:ARBA00021597, ECO:0000256|RuleBase:RU364014};
DE Flags: Fragment;
GN ORFNames=scyTo_0003380 {ECO:0000313|EMBL:GCB74291.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB74291.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB74291.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCB74291.1}.
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DR EMBL; BFAA01000910; GCB74291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PMI4; -.
DR STRING; 75743.A0A401PMI4; -.
DR OMA; NWVTHDG; -.
DR Proteomes; UP000288216; 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; 2.
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; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
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:UP000288216};
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 94..126
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 155..187
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 198..229
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 789..987
FT /note="Protein HIRA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07569"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GCB74291.1"
SQ SEQUENCE 1042 AA; 114885 MW; 202CB669BC8B286E CRC64;
GVRGRGHPGT VTPGASEVQL ESQVSGPSMK LLKPAWVHHN GKPIFSVDIH PDGTKFATGG
QGEDSGKVVI WNMPPVVQEE DEKNEAIPKM LCQMDNHLAC VNCVRWSNNG LYLASGGDDK
LIMLWKRAAY IGPSNVFGSS SKLANVEQWR CVSILRSHTG DVMDLAWSPH DAWLSSCSID
NTVVIWNALK FPEIIATLRG HSGLVKGLTW DPVGKYIASQ ADDRSLKVWR TMDWQLETNI
TKPFDECAGT THVLRLSWSP DGHYLVSAHA MNNSGPTAQI IERDGWKTNM DFVGHRKAVT
VVKFNPKIFK KKPRNGSSNK PSCPYCCCAV GSKDRSLSVW LTCLKRPLVV IHELFDKSIM
DISWTLTGLG LLVCSMDGTV AFLDFSQEEL GDPLTEEEKN MIHQKTYGKS LAITTEQQLS
TTIIENPEML KYQQQQKELQ EQKNALGSRE LMAPKVANML NGESLEDIRK NLLKKQIETR
TADGRRRITP FCIAQLDTGD FSTAFFNSVP ITGALPGSVL PSQISQPQPS SDSNAAKSVS
TKLTQDPAPA TAKSAEDTPN KDGSAITSTS TAVPTSTQLL TSPSRIEPMK ALDSRFTERS
KSTPGTAPIS SARQSDLDRS KEQGLSKDLK PREVQESSSD SEEKIPASKI LSLSKRKNDT
EGEVVEKKKK GRPRKEAKHT SVTITSQAAP SIEKEVSRVS APLIVFKLPT PAPKKAFNIQ
VSTEPAMYIE VENEVPTVTG WKLSRLKCMR EGKQWDTLLT SRILTAAGSC DLVSVACEER
TVSVFSASGR RLLPAILLQS PISTLHCASH FVMALLATAT LSVWDAKKQT VLVKDESLIT
ILSGNDTTIT QSLLTHHGVP VVTLSNGKSY CFNTSLCTWN LISDKQDSLV QCADYRSCLT
SQEAMLCSGP LATVQGCGIN AGRQAARLSS MPHFLQRGTT LAYLENQVAA AMTLKSSQEY
RHWLLIYTRY LVNEGFEPRL RELCKDLLGP VHNSSSSQWE STVLGLRKRE LLKEMLPVIG
QNLRFQRLFT EYQDQLDLLR DK
//
