ID A0A3N4KHV4_9PEZI Unreviewed; 201 AA.
AC A0A3N4KHV4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Histone-fold-containing protein {ECO:0000313|EMBL:RPB10144.1};
GN ORFNames=P167DRAFT_276676 {ECO:0000313|EMBL:RPB10144.1};
OS Morchella conica CCBAS932.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Morchellaceae; Morchella.
OX NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB10144.1, ECO:0000313|Proteomes:UP000277580};
RN [1] {ECO:0000313|EMBL:RPB10144.1, ECO:0000313|Proteomes:UP000277580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB10144.1,
RC ECO:0000313|Proteomes:UP000277580};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC {ECO:0000256|ARBA:ARBA00009053}.
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DR EMBL; ML119145; RPB10144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4KHV4; -.
DR STRING; 1392247.A0A3N4KHV4; -.
DR InParanoid; A0A3N4KHV4; -.
DR Proteomes; UP000277580; Unassembled WGS sequence.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR PANTHER; PTHR11064; CCAAT-BINDING TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR11064:SF9; NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000277580};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 47..112
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 22148 MW; 52019AE3F52CEFAA CRC64;
MSASPSKDLE VEVGAQSPDE QEHMDRDQPE TSQPPPVFDF EVKEQDRWLP IANVARIMKT
ALPENAKIAK EAKECMQECV SEFISFITSE ASEKCQQEKR KTVNGEDILF AMTSLGFENY
AEALKIYLAK YRESQSQRNQ SEGGSRGGGG YGTGNAVGTA TSSSSTYRGR SESANQTLTP
PMEGDEHHQY NDVYGNGDGP Y
//
