ID A0A2J6PZD3_9HELO Unreviewed; 567 AA.
AC A0A2J6PZD3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=YL1-domain-containing protein {ECO:0000313|EMBL:PMD19368.1};
GN ORFNames=NA56DRAFT_647097 {ECO:0000313|EMBL:PMD19368.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD19368.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD19368.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD19368.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613489; PMD19368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6PZD3; -.
DR STRING; 1745343.A0A2J6PZD3; -.
DR OrthoDB; 2056942at2759; -.
DR Proteomes; UP000235672; 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; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 78..309
FT /note="Vps72/YL1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05764"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 62394 MW; 68318D12BCF3BCB1 CRC64;
MAEEDALMDM DEPENTSMQM EEQEDTPMRM EQEEQTPART EEDTPARTEE GEGSGSGSGS
GSDSEGEEEQ VEWLATTREK RATAGNRLAS LLQQEEPDDE LELLFEEPED DVGFEDAGAD
SDVQMDSSSD DEDQGPAAGD DLEGEKAIQK QERAERQAKK RKLAQVPGIK RKKVKIDPRV
LMKPAARPKK KSERASWLPT AEEAPTRASA RKTTKLSKEQ LHQQMLAREI KRLRQLQNME
KAAAAKEAAK KPEMTQADRL AEAARIEKAN VRTVSRWEQA EQQREEAQRE KLAALQNRHL
EGPVITYWSG MAERFGGKLR KVGKNLILEE KEKGPRKKKA AEMEDGKDEK AEDAKPAEGG
TEAAASVPSE ESGKPEESKQ PAPTEATSHG DTAMPDAKSF DSAKPPETTK PDEAPKPAIP
EILEEVQPIV TPAPLPGPPR SSFLAPPAGL PLTAPPPPPP KSQNPYVLAP PTLDGSAPLP
GFGYNFVRPP LTPSQPTGFA FNPPPPPNLP PPPPEIEHEG RNYIILQNFD EVQIKDKDVQ
TQILFGRKFS KVRSKCPSLV YDLSNHP
//
