ID A0A319CG73_9EURO Unreviewed; 786 AA.
AC A0A319CG73;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE SubName: Full=YL1-domain-containing protein {ECO:0000313|EMBL:PYH84876.1};
GN ORFNames=BO82DRAFT_381298 {ECO:0000313|EMBL:PYH84876.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH84876.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH84876.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH84876.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family.
CC {ECO:0000256|ARBA:ARBA00006832}.
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DR EMBL; KZ821682; PYH84876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CG73; -.
DR STRING; 1448315.A0A319CG73; -.
DR VEuPathDB; FungiDB:BO82DRAFT_381298; -.
DR OrthoDB; 2056942at2759; -.
DR Proteomes; UP000248340; 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:UP000248340}.
FT DOMAIN 654..683
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 84294 MW; 5044F24107DCB551 CRC64;
MADEHETPSS AEEETQVESL IQGRAKRSTA GLHMSALLDA AADDDLALLF EEVEDDNEFA
VDAEEMGGEE DDMRFDTSSE DEDDQGPSAK DDDFEGEQQL QKEERADKKK KRAKDDLRYK
IAAKRVKIDP TAVSAVPAPR PKKKSERVSW IPTPEEGPTR SSSRRQTMQN KELTHARLKD
SEEKRIRLIA TMEEAAKRKA QFKPKEMTQA ERLAEAERVE RHNSKSLNRW EEMEKRKAEE
RKAKIEALQN RRLEGPVMSY WSGIATWADG RLTRVGKVDI TPKPEKEDTT RKKSKKSDKE
GKNVTEQKPT EDGATVEPAT PQAAPPATNE AEKPKDSVEI AGGEPVKGNP EPSEVPPTDT
RPVQEGDAPS ESKTTIADSE ASPCAPEAAS ASATAPAPAE ASAAAPEQPS TSAPVEASGT
EKSSELPPVD VELKDTEMKD AEPQNPVQDT ASPGGEAETD KAESKVEKPD AEKPEKATEA
AAQAPQSSAQ PSGDETSAAE PAKQPEVEVP ATQPKPSEAE QPTEENLSDG KKEPISEPLA
TTGQGIEAVA ASEELSPTAV PAAADAPSQA DSLKDALVPT QSEKDTPELH ANQPNVVTED
APQVVVPQPP SIIEQTGRNL TILENFDDKT AQSREFSIYF NAKKPPRLTK ISSSLCVITS
LPSRYRDPDT SLPFANAYAY HEIRNAVSQK FSWSPMLGCY VGPAGVAARG VPARFLGGPE
AKEETKELAP STVDDKAPND SPATKANGEP KAPAAAEASK TATPDPGSAA ASTPTPAATG
DPMEVD
//