ID A0A0N5B0K0_9BILA Unreviewed; 480 AA.
AC A0A0N5B0K0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein AF-9 homolog {ECO:0000256|ARBA:ARBA00022408};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0001080201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0001080201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC Component of the NuA4 histone acetyltransferase complex which is
CC involved in transcriptional activation of selected genes principally by
CC acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Yaf9 may also be required for viability in
CC conditions in which the structural integrity of the spindle is
CC compromised. {ECO:0000256|ARBA:ARBA00025636}.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex and of the
CC NuA4 histone acetyltransferase complex.
CC {ECO:0000256|ARBA:ARBA00038745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
CC -!- SIMILARITY: Belongs to the YAF9 family.
CC {ECO:0000256|ARBA:ARBA00038419}.
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DR AlphaFoldDB; A0A0N5B0K0; -.
DR STRING; 451379.A0A0N5B0K0; -.
DR WBParaSite; SMUV_0001080201-mRNA-1; SMUV_0001080201-mRNA-1; SMUV_0001080201.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16906; YEATS_AF-9_like; 1.
DR Gene3D; 1.20.1270.290; -; 1.
DR Gene3D; 2.60.40.1970; YEATS domain; 1.
DR InterPro; IPR040930; AF-9_AHD.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; YEATS DOMAIN; 1.
DR PANTHER; PTHR23195:SF15; YEATS DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF17793; AHD; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00376}.
FT DOMAIN 414..479
FT /note="AF-9 ANC1 homology"
FT /evidence="ECO:0000259|Pfam:PF17793"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 53588 MW; 68C63743ABAC7966 CRC64;
MAETRLLLPL QIGHESEMLD TLTPSGQSQF RWTVFVRSAE SLQFTDRSFI SKFFRFLCTC
SNRVEKELCA EEKLEANIFM LGLSFLMLVV FELHPDFGNP KRTVKEPPFE VTETGYAGFT
IPIQISFMGV SKTYKLIYDM NLVLEKQSKH CVEQLLLIKQ PSNEFYELAL KYGARIKKEK
KKKEKHSERN YDYESDQSQR YETAAAAEAI EKETSKKKKN LQTDCKSGTL AGSSASSENK
VFSTPTTSTA AAASKNFLPK KVQKASEENE KGEKTRTSRV LSPADRSHGV ATGRGSSPAV
NNSRSKKPPP NTVRDSGGPA KERGKVNNDA NNTAVASSSV PVPPNDKNDK LARKSNPTVG
RFKSGQREKS VERQKCAVPV NGEKLKSSPS ESMKSYADDQ SPPSKKRKQE LSVDTLLAVQ
KNLMDIENSE RMFAVVDAIF SSSEWPVPSL EYSEDTKILS FDLFALDPAL ILKLEELCQR
//