ID A0A2S7PJ73_9HELO Unreviewed; 663 AA.
AC A0A2S7PJ73;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Yl1 nuclear protein {ECO:0000313|EMBL:PQE14330.1};
GN ORFNames=CJF30_00006930 {ECO:0000313|EMBL:PQE14330.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE14330.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE14330.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE14330.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family.
CC {ECO:0000256|ARBA:ARBA00006832}.
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:PQE14330.1}.
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DR EMBL; NJPT01000052; PQE14330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PJ73; -.
DR STRING; 2070414.A0A2S7PJ73; -.
DR Proteomes; UP000238072; 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:UP000238072}.
FT DOMAIN 580..609
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71802 MW; 7B1E67A11BDD27D2 CRC64;
MADEIDEDTP MRTEENTSDA GSSDSEGGSG EEEVELMVTS RQKRSTAGNR LTSLLQQEEP
DDELELLFAE DEEDAVYEDA GADSDVQMDS SDDDDDQGPT AGADDLDGEK ELQRKEKAER
LAKKRKMNDG IPKIFKKRVK IDPTVSDKPS PRPKKKSERS SWIPTPEDAP TRASARGTTR
QSKEQLHAQM IDREKKRLKQ LANMERAAAA KEAAKKPAMT QADRLAEAAR VEKSNSKSLS
RWEEAEQQRE EEQRLKLAAL HNRQLNGPVI TLWSGLATWV GGKLKQIGSK KIGQDEAKEK
TKKRKAAEME GDDDGGEKEA DAAPKDPSGV DSTKPGESSS DVQGDATANG GNSATSNSDE
VPATKDASPP RPPVTNTATN SLLRPPAVPE NLPQINSGIF KPPQLPTIPP SSSVLQPPNQ
TSGAVPPISG VLQPPQSHNQ PVPINGNLQP PAHLLNASAP PFFLQPPSLD GSKPLPGFQP
PNTQYPRLVP SQTTPFAFTP TQHYSPYTPA PAPASASSSA PTPPPPPPPP APPVVEYSLR
NCLILSNFDD DEIKSKDVQT RILFNQTFPK APRTYKPRHS LCAITHYPAK FRDPKTGLPY
LNAYAYKEIQ KLRKGEYRWS ALLGCYVGQQ SFAARGVPSR FLKEGGGKVE GAGVGVGENA
GGR
//
