ID A0A0D2GHX5_9EURO Unreviewed; 1394 AA.
AC A0A0D2GHX5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=PV04_00132 {ECO:0000313|EMBL:KIW71904.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW71904.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW71904.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW71904.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-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; KN846956; KIW71904.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2GHX5; -.
DR HOGENOM; CLU_001331_1_0_1; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000054266; 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; 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; 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}.
FT DOMAIN 559..632
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 817..877
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 55..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 152615 MW; 7FE7BFAD17FB07EA CRC64;
MPVEHLRSKK SEAQRLVQSR KRKLNELFSI SIPAHDPTYK QKLQAFHDAN DLEKGCRFDE
DTLPPLPHIV LRSRKSTPKQ PHTAASPTSG TLYQPKSISK TTAPPSPSPK PATQPIAAKQ
TLSVPKPLEG NKRDEDATSA TKEDHELDSQ QSAEAISNTQ NGEFIASPGR GDRRSRSPRV
PSIEATAIDR SDGTTLGSSS ARNGNSPSGS AEPGPHLPVN HRSSRSPPAL APIAQPADPQ
SSPASSNGHE SSNTPAPDAG SPGTSPGVDL APAPSLVPQA SKAMDTSQPG TMLSPRPQVA
DYRHSAKKTE NPSVEVEMTG VEDGELANSS LPDQSKLSAE PSKFPGPQRP LMRIDTRTES
DSYFNARPTG GIVESPAQLT GTTPRRNIPA TASAEEPPKR ATRISSGVLQ KKSVSEILGE
TPRTTTPQAE SPRDSFGATT PQGRTAERDR RDKDRSRLST VVFAKREKAV IDEENLEVVP
FDGEAKGKSS GERDYLYTLF ENKAHSMSRQ TSMSYLVQNA HKTLSTSDHL IEYELSAECR
ILKRLYQLQE KQRWALRQYK RAEEAPRPTS HWDFLLDHVK WMRTDFKEER KWKMAAAKGL
AECCADWVAS SAEQRKRLQV RVRQPNLLPK PTSSHDVAME EGPVASLSSQ TTPELVPSNE
DDSMSDDIAD LRDVQISSAP ATLFSLGPLD FNFSVDKTPA LDKLLNELPL YGPYVEPDTS
KTALAGRLDA KWRTDIVPVS RWATEKLPVK DYKPPVKRSR YDYDLEPSPK KKSEPLPPEE
TNVALFMPEN KIIRDRIHPG HSFRPPSEHP MPTQAFFETR SSSQWTAAED DELKRLVKDY
SYNWSLISSC LTPPSLYTSG ADRRTPWECF ERWIGLEGLP ADMSKTAYFK TYSGRIEAAG
RHVAAQIEEA QRRAGANVQI SARRRTTQPV KVERKRTQRH LAMLDAMRKL AKKRETALQK
QQHQADLAAM RKVNDANVPK PSYKTPAEFS QLKQEREQKL AERQEIYRQQ LIAHQRATAQ
QQRTQNGQPN GLPNGMPAAA PGMRAPSIGG MPGMPNGNMQ MPNGHRPHPA MIAAMQGNMQ
LPPGMMAPKL TPQMQAQMQA QMAARGGMTS PQQMRMLQEA TRVQQEQLMR QAQQAQNGPH
SSPNNPHAAL ANGQGLNNAA YRAAMAAAAN GTGSPSGPMN GSSPRPNTAN SGQALSSGHI
PVLTQIANKI REHHPNLSDE EVQRLASQQL QTYQHQATQA AAGHTSQKRP QHNQAALNAA
LGAMNAGNNA SAATAASAAQ LGHPGMMTNE QVQQYNQRIR MQQAQQHAQR NLQAMQMQQQ
MGGGMPNVNG MAGSPVMNMA RPVSQHANPQ GHMSRSATPR DQRSGSQGGI NGNSAGNGQG
QQSSPRQTAQ SMQT
//
