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Database: UniProt
Entry: A0A0N5B0K0_9BILA
LinkDB: A0A0N5B0K0_9BILA
Original site: A0A0N5B0K0_9BILA 
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
//
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