ID A0A2T3Z0V0_9HYPO Unreviewed; 1030 AA.
AC A0A2T3Z0V0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Vps72/YL1 C-terminal domain-containing protein {ECO:0000259|SMART:SM00993};
GN ORFNames=M441DRAFT_71865 {ECO:0000313|EMBL:PTB38425.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB38425.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB38425.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB38425.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family.
CC {ECO:0000256|ARBA:ARBA00006832}.
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; KZ679266; PTB38425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3Z0V0; -.
DR STRING; 1042311.A0A2T3Z0V0; -.
DR OrthoDB; 2056942at2759; -.
DR Proteomes; UP000240493; 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:UP000240493}.
FT DOMAIN 717..746
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..948
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 109843 MW; B82F01B13DBCCAF7 CRC64;
MSTMDSESRQ QSESQLSAPP PLSDLDSSSD SSDSEAGDSS SKPGPGREPE PVEWLATSRS
RRSTAGNRMK SMLANEEPDS DLELLFAEDE DDQGFTDAGD DASDMQMDSS SDDEGENNAG
DELEGEQELE RQARERRAAQ RKRKAQDAIP AKFRKKVRIN PAASESSTPA PAPRPKKKSE
RTSWLPSPAD LPTRASSRKT TRMSKEQLHQ QMIEREERRL KQLEQMQKKA ARMEALKKPP
MTQEDRLREA AIVEKRNSKS LNRWEVAEKQ REEERRAKLA ALNQRTLKGP VITFWTGLGE
ARRVVIEEEK PKRKRVDKKD KDKGKAAEAV KEDAVPVTAD KDGKENVAPQ EGVQQTDASI
KVVASSENTT AVPKPDAVEP QSKEEPAPAP APAPAPATAP TSTPTPTSGA GEIKTSDAAP
PLKQEDDEMI EPLKSAPIAP PPSSQSPSAA VPPPPPTTAP DTAAGTDTGT ATSSSATGPL
AVPRDDSISP TTTSTAKPPG DVQPAQPVIA APLLSPPPLL SPPPLPSGLA APASSSLSAS
PRQTSPLAAP TGIGSPRPVE AGKPSGVLAL PVLAPPPVMN MDYRPGPAPK SNILALPNTS
LPQTALAPPM QIQPPGSTAG VAPVSTEPVL INTVLRPIIP EPEPISKSAS PNLSEPPSQP
APGPAEAPEV PEAPETTTRN VIIFQNFDEN AIQDKSIQTQ ILFGRKMNKL SKPAPAPICV
ITGLPARYKD PKTGLPYHNV AAYRELQRLD RKELSWSAIL NAWVGSEKMA ARGVPARFLD
PNAPTKTPEE REKERLAQIR AVPPQPQPPP VQQHHQAPPA AVVAAAHKAP QVQHHVQHMQ
HAQQQRPAAT PQPLRAPQPF QAPQQPYVQH QQPAARAQQP QPPPPPQQQP SQQLPNRPSQ
NPPPPPPPQK QQPPVSNATP SVPPAQATPS QAAPPPPALP PQSSPLPPPA AQQQQQQQQK
QQPTPTPPPP PPTSQSPVQK TTTGQLPTPA PVPPPAPEPQ FQPQATSGSQ VVPVEKELPL
PTTTAAPESN
//
