ID A0A183I2S9_9BILA Unreviewed; 397 AA.
AC A0A183I2S9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Nuclear transcription factor Y subunit beta {ECO:0000256|ARBA:ARBA00015277};
DE AltName: Full=CAAT box DNA-binding protein subunit B {ECO:0000256|ARBA:ARBA00029965};
DE AltName: Full=Nuclear transcription factor Y subunit B {ECO:0000256|ARBA:ARBA00031126};
GN ORFNames=OFLC_LOCUS14041 {ECO:0000313|EMBL:VDP15346.1};
OS Onchocerca flexuosa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0001404901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:OFLC_0001404901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP15346.1, ECO:0000313|Proteomes:UP000267606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC box motif found in the promoters of its target genes. NF-Y can function
CC as both an activator and a repressor, depending on its interacting
CC cofactors. {ECO:0000256|ARBA:ARBA00025263}.
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; UZAJ01040555; VDP15346.1; -; Genomic_DNA.
DR STRING; 387005.A0A183I2S9; -.
DR WBParaSite; OFLC_0001404901-mRNA-1; OFLC_0001404901-mRNA-1; OFLC_0001404901.
DR Proteomes; UP000050787; Unplaced.
DR Proteomes; UP000267606; 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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 60..125
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43550 MW; 46E2D9774987DE9A CRC64;
MINEDDGNNY LDKYSQESDT CQAEGSTTED NNAERILTVA NIASEENSMA RKPILEQDRF
LPIANISRLM KNMIPRSGKV AKDAKECVQE CVSEFISFIT SEACDRCLNA SEKRKTITGE
DIIGAFSTLG FDNYVGPLSA YVRKFREAFR TERSNETLLV EPSGSHPSFL EKINVRDSNE
SASSSDVFAI QTEPMASSST CTPQIIFAGE DDPDGAIRVM STGNVQHLQL LMDPATGQHY
INVQNPNGTQ QLLPVQVTTV ADSSATPLTL PCADVQNLTD GKAIDKEMFN FSKIEFRNSL
PKSDNIASTS YKELSCSIKC SFLNLGFPLN IFSNGSTYGL KHSSVGLSTA NQHKQQVPYA
GNMGQFGHHS NSGDTSGGIR EQPRKRSHDS IDYISFD
//