ID A0A091HK33_CALAN Unreviewed; 290 AA.
AC A0A091HK33;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog {ECO:0000256|ARBA:ARBA00020000};
DE AltName: Full=Transcription factor-like 1 {ECO:0000256|ARBA:ARBA00032814};
DE Flags: Fragment;
GN ORFNames=N300_10900 {ECO:0000313|EMBL:KFO96663.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO96663.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO96663.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO96663.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deposition-and-exchange histone chaperone specific for H2AZ1,
CC specifically chaperones H2AZ1 and deposits it into nucleosomes. As
CC component of the SRCAP complex, mediates the ATP-dependent exchange of
CC histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC {ECO:0000256|ARBA:ARBA00002050}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family.
CC {ECO:0000256|ARBA:ARBA00006832}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL217598; KFO96663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HK33; -.
DR STRING; 9244.A0A091HK33; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0140849; F:ATP-dependent H2AZ histone chaperone activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR InterPro; IPR046757; YL1_N.
DR PANTHER; PTHR13275:SF4; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 72 HOMOLOG; 1.
DR PANTHER; PTHR13275; YL-1 PROTEIN TRANSCRIPTION FACTOR-LIKE 1; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 241..270
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO96663.1"
FT NON_TER 290
FT /evidence="ECO:0000313|EMBL:KFO96663.1"
SQ SEQUENCE 290 AA; 33145 MW; E0ED456D67C3EA5A CRC64;
QESGDDEYRG DQSDSDDEVD SDFDIDEGEE PPSDPEENEP KRRRVVTKAY RVRVPSPPGV
GATPKHPTIN NQLLPCTPPK KDPAANRKHM RQSTTEHTRQ TFLRLQERQV QSKRKKGPNY
DRPLTQEELL EEAKITEEIN LRSLENYERL EADKKKQVQK KRKCVGPVIR YWSVTMPLVP
EPGKEENVDV EGLDQDPQQT DSLPAPSPAG KCSRTFISFS DDETFERFFP KTKPPRLPVR
ELCPVTHKPA LYRDPITDIP YSNIRAFKII REAYKKYITA HGLPSAAAAT
//
