ID A0A162KKP7_CORDF Unreviewed; 1354 AA.
AC A0A162KKP7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=LEL_06092 {ECO:0000313|EMBL:OAA76408.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76408.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76408.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76408.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA76408.1}.
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; AZHF01000004; OAA76408.1; -; Genomic_DNA.
DR STRING; 1081108.A0A162KKP7; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000076881; 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:UP000076881}.
FT DOMAIN 512..587
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 785..839
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 83..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 146411 MW; 8DC0C6096BE5AE36 CRC64;
MLMSKSAIVT SRKRKLRELF AVATQTQPLP QQAHALPDAP AATTAEWQFL QTNDILQERI
FDEASIPPRP PQSVEALKRS ISAQLAATSS PVNSPVAATP GQPSSANSAR STPGAQSPAN
IQNGPKPTIT PQNSAAALAA RAQNPSQQLT DASRRPNQVS FPPGTKGSPS LTPTPVPNRV
ATDAPLADGS LSIKLSHDAA KITDAMSSPG STAASATTTA AHDISANTSP DNEGPRSPEV
AQQPAQAMPK PETKDSAASP KPPSDEDQLL QESIRSAAAS GSDDEAPPTT GPTSKPQTSN
PEASSAEVPD SQDEADKMDV DVPETIQESI NVKPTPPLLT PQPTRESVPV ERAVTRVSSG
AMRLKSVNEI VGATPRSTID RGTPKDLEDQ LTPSASAPES PASRSKPRKD RNKGQVSTVL
FGKQPKRVED KAVAPSQKEQ FHPFDDYYTP LFIQNFTGAT NWMQPIEKIL FHANKTIGTS
DANLAILDNQ ACKVLRRVYH LQQHDKWSLR QPKRCPEPTR PTSQWDVMLQ EMKWMRTDFR
EERKWKTTVA RNLAYACVDW HESSAEERLA LQVAAHIPPR RSADGDDART GGAEVTGAEN
HPTPDLEPSG DADSPLHDDI SEVFVETVAP SAIFSLQEDD VVFGLRRTQA ADQLLDELPL
YGAPLKIPQT DLTNPEFDPD AHWRRPALPL SKYVEGEMKV TARGPPRKRG RFDYRNEDSD
DEGDYTFAAD QTVNPTRTEA ITSNVALFNP ESKPIRDRLH AGHQFRPPSE HPMPMQSFYE
CRSASQWTVA EDDELRGLVR EYSYNWSLIS SMLSTRSSFV SGPERRTPWE CFERWISLEG
LPADMQKTQY FKAYNGRIEA AQRIIAQQNQ IAAQQASAAG SNVPALRRRP SVPVRVERRR
SQKHLTLIDA MRKLAKKRET AQQKQQHTAS QNAVKKAAEP VSQRPSKTPR DYSLLRHERD
EAVREKMAQF AARSEAQRRA QLQARAQSQA AQMAGAAQGA QANQGAAQAA ANGTSQAGAQ
RPEVPAHLVA AAAAAAAGQR PRMPSLSGVN GAPQATPGLP SQISPAMVAA AAQMKGIPAA
QLQAAMQAQA QQHRMPMPNQ AADANLMLRA QQMANQQRAA VQIQQQQQVH HQQQRPNSAV
QQNGQGSPPM HNGVNGMNGV NQQTFMNNAQ AAMAAYNGNN ANRNGGAANG MHMQNGVPNG
SPGPRVSTQL PPNIALQLNQ LEVQFRTKNP SLTPEQSRQL ATEHLTRAMM AQRQSALNAA
AGVTGQPGLS NSIAATTSPH QYAALLRQQQ QQQAAAAAAA QQRQQQTQQG QAQQQQQPSQ
GQQLSGNSTA GSPVPPANHQ RQSSGSATPS STSK
//
