ID A0A109FJ31_9BASI Unreviewed; 1025 AA.
AC A0A109FJ31;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=RHOSPDRAFT_33051 {ECO:0000313|EMBL:KWU45429.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU45429.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU45429.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU45429.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. {ECO:0000256|ARBA:ARBA00025178}.
CC -!- SIMILARITY: Belongs to the EAF1 family.
CC {ECO:0000256|ARBA:ARBA00008913}.
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DR EMBL; KQ954472; KWU45429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FJ31; -.
DR STRING; 1305733.A0A109FJ31; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1.
DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT DOMAIN 376..459
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 738..793
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 738..789
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 109936 MW; A26CCABF66D21809 CRC64;
MVRATASTSG HVAGEANRNQ QTDDAGVRTR AVRAREAKLE ELAATREHQI AELFVAVRDK
PKYTDFEAGL SGRKRRKLVD AAKDDQVSLP GLEDFGRDLQ RLDIALPPLS PAPASEADPS
GGRQAETAIA PPLADDLAIK HVVVDDSEED AEGEVDEDLP MAQAPAPAPT PAGHVQTGRN
ESAPERRAQP TPSTSAAPQI ALTAPSAPPA PSPAPGAPGA PSASTSTQSI APALAQPTPS
PVPSSAPAAA DAPYFPPPVY SSQFGIHEVS SDYIEALPPV PSDVLRQRLN AALLLRASNK
KASKSSAAQA VQPDLYKLHV RSQHMSAKSF LGPGKRVHNV LDTKEWEVGI DEMRAIRAFE
RIEELKAERK WSFRQPKKQR TGVVPKAHWD HVLDEMRWMQ TDFRQERRWK VVTAYTIARD
CRAYVRASPS DRSKLVVPTR PPRTLSDSEI EARMNGSPTS GELPPVGAED LEPAVPGHGG
EKDVDEDDQD AEGEPDDDAG VRVVAASASD ATKGAVPVVS APAGAGKAGG SAGDEATVTV
AAPSSRSQAE ANKAHSQAQH IQNLITFRNP IFDASVADTT ISSSDLAFIR DAAAGGGEKA
ESTEDDPFLG YDFAVLFPDL PLYSDFAIAN DPSLARRVED SSAWSGRLAQ VTRLLEIKPI
LISTLQPGRT RTDKGWSPAL IDALEDVKDS MSTGETPVPA AASTLFAGRK PKDVATGELL
VKPQEVPNAE IRATAILWLP EEDALLLALQ KQYGLNWSLI AQVFNSTTHR PESDYRLAWD
VYDRWDKLVG PGSKKLLPDG TEIVRPPPEW LPPVDRTGRP MPVIADGSKK KTRHAMIVEA
MKKVQKKREG YAAKQPAAGF PRRINMAMHE SHSIPPRPNW TPMEWSIYKA EQEAQKLRLR
QQQQAQVQAA AAMRQQQAQQ NAAGLQQSRP PSSLPPQIAA AHAAARASPT GSAAALPGSP
NAGHSSASPR NAPQQLGGHA PNQQLNGDQI AALQARQREL LQAQAQAIAA QRAAQQQQQR
QAAGS
//
