ID A0A094ASZ8_9PEZI Unreviewed; 1444 AA.
AC A0A094ASZ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
DE Flags: Fragment;
GN ORFNames=V493_01880 {ECO:0000313|EMBL:KFY30473.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY30473.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY30473.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY30473.1}.
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DR EMBL; JPJV01000729; KFY30473.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094ASZ8; -.
DR HOGENOM; CLU_001331_0_0_1; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000029327; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT DOMAIN 747..822
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 1040..1100
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 86..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1444
FT /evidence="ECO:0000313|EMBL:KFY30473.1"
SQ SEQUENCE 1444 AA; 159246 MW; A4A107C4D4372B9F CRC64;
MSDEVVLAGR KQLTSRLEND ISVIERSRKR KLRELYAVAT CDGPIPLPAY LTLDAPISES
TLEERRFLSA NDIKEGRIFK EHTIPSQRKL RSDGARTTAG IDKSTLAARA GAPDYGQRDG
RESLQERPKT DASYNTGPLY AKAPATTVDR PLSRTPPRGL QDGKAVGAGR KSTPREDALK
LDRAVATKGP TALLDAAVDE TVGDAIYNAN NPPAPTKDDS PTREALEKDH VIKKAEPTPD
TPGVDPNVAI PKTAEDAAQL PGLIVNGAND PSHKPSTVHL PPQEVQEVAM KEREEQRHAI
REQRPVDAAA ARLALEVPAQ HDRQTHADVA SSPGSTVGPL SATTSAHHHE TSADTSPDNE
AHHYDTEAAE EKVIPETPPE LAPSQEEVRE KDAHDRILKS QMDVAREHIL GSSPTAADTQ
LLEEQAAAAS TIPGKDGVAR PAKAAVDGRQ PKVREVVGAP ETASELMDDE KDDQDEVVGV
PTPDEKVPEL APETVETLEK ESATQPADNA EPMDVDVPEP AQAKGKEVEQ TAPAPEPMET
TEPTKPAPAK PEEPKEPSSE RTSTSVSTPS IERMTTRVAS GAMRHKSVSE ILGETPRPSL
TTTPDRTPGR ALAEADSNLP SGISTPRSAS SRMRSVTERA REKERSKLST VVFAKQPVTK
DTKTSALVSA TAKPQGTEYP DYFMPLINAQ SYSAIRGYQT LEALLASAHK TITTTNAALP
FQEAQAQKII RRIHSLQNHD KWSLRQPKRS PEPIRPSTHW DELLKEARWM RTDFREERKW
KTALARRAAY ECALWVNGDQ EQRDVLQRKV VVLESVERGD ETMVDVGDVE AAVEVPAEVP
ADAGDGEAPV DVNVDMDAEI SHPTPDLVAS SDNDTPLDEF DDEPRISLLE TVAPTAIFSL
DNDDLVFGLS RSAASDKLLQ ELPMYGAPLK VHQSDLPTSE VDPDASWRKP YLPLSKYIEG
KIRFTDEPPP RKKSRYEYAE ESDDEDEVVF GERTQRKPQE PLQVDVALFN PENKHIRDRI
HAGHQFRPPS EFPMPLQSFF ENRQPSQWTW AEDDELKQLV REYQYNWSLI SSMLTSKGVY
YTAAERRTPW ECFERWIHLE GLPADMQKTH YFRAYNSRLE AAQRSLLLQI QAQAAQPPPA
VGSAPVRQIR RSTTSVRVER RRNQKHLTLV DSMRKVAKKR ETTAQKQQQA QSLANLRKSN
DTPAQPINKH TPAQFSKIKH DREQAILEQK ARLVQQQEAH RRAQVQALRN QQPNMQLPGY
PNAQQQQQQQ RGNPNMNAPP PPNMGNNPQN NRPANLSVPG QNQHHPQQQP MQQLPNGMGA
PMPMPNIHPG MGGPMPLKGV PQQQGQMGMQ GMPMPPAHRL PAPNATPDLS LVMQAQRISQ
QQRAAVQMQQ HQGGGGPQTM HSSPPNSIRG LPNMGGGPNQ QGFMPTNNMS PNPLQHFAGS
PPTG
//
