ID A0A1X7RN88_ZYMTR Unreviewed; 698 AA.
AC A0A1X7RN88;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Vps72/YL1 C-terminal domain-containing protein {ECO:0000259|SMART:SM00993};
GN ORFNames=ZT3D7_G4023 {ECO:0000313|EMBL:SMQ48873.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ48873.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ48873.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT853694; SMQ48873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RN88; -.
DR STRING; 1276538.A0A1X7RN88; -.
DR Proteomes; UP000215127; Chromosome 3.
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:UP000215127}.
FT DOMAIN 608..637
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 76464 MW; AC5EE5AAF41C6B27 CRC64;
MSDNDERSCS SSESDGEDVT TTGLIATRAK RSTAGNLYAT LRQNLDDEEL QKELLAEEEE
DVGDYEGTDK DDDDDAAMDS SSDDEEDAGP PKEGEVEDLE GEKQLKKAER EAARKKRKMD
EAKMRLPAWQ KKKKVKLADD AKTDDGSAPK PKKKSERSNW LPTAADLPSR QSTRTSAVEF
RTHVHENLKL SNVRSENQKK VMANHIQKSK ANKRADLTQE ERFAKAARIE KETAREFGRW
EREEAERQRI REEQLAAKRR RTIEGPVIRF WSGSVIWEGD KIKVKRVHQN GKVEEVKEEE
EAKLAKAATE MNGKDEEKGN RKDEDGDIAM VNPELDKHGN AGETDNTAVK APVAIADSKP
PMPEGDAAES KPELASTTTT DAATADVRSP LPAEQPQQAS AALQPPDANQ PQASWLDGIH
AYAAQSESTT PSSQLQVTAP SQPDSVNVYL PSAPSVTTGL SSAQHTPFTP QNALESNQTG
QMTSQNHQGW PSVPLQPTFQ QFQLSQQPTA PPPPPEPLLR EHAQRSLLIL SQFPSLAPPT
TSRGKSGPKV KETPLDSTPL SETLIPGSHP PFNPEEARYL LTKLRKKATV VDTRTGELSQ
LPPAPPKAVC ALTSWPAKFK DPRTGLPYAD LPTYKMIKRM LAGGCAWSGT LGAWVGPRYG
EMGRPAKGVP HGFGEARPRV VTMAEGGTDD GLKMEVDG
//