NFYB_PETMA
ID NFYB_PETMA Reviewed; 209 AA.
AC P25210;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Nuclear transcription factor Y subunit beta;
DE AltName: Full=CAAT box DNA-binding protein subunit B;
DE AltName: Full=Nuclear transcription factor Y subunit B;
DE Short=NF-YB;
GN Name=NFYB;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549471; DOI=10.1093/nar/20.5.1087;
RA Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C.,
RA Mathis D.;
RT "Evolutionary variation of the CCAAT-binding transcription factor NF-Y.";
RL Nucleic Acids Res. 20:1087-1091(1992).
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.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC dimerize for NF-YA association and DNA binding (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Can be divided into 3 domains: the weakly conserved A domain,
CC the highly conserved B domain thought to be involved in subunit
CC interaction and DNA binding, and the Glu-rich C domain.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR EMBL; X59712; CAA42232.1; -; mRNA.
DR PIR; S22818; S22818.
DR AlphaFoldDB; P25210; -.
DR SMR; P25210; -.
DR STRING; 7757.ENSPMAP00000001363; -.
DR Ensembl; ENSPMAT00000001369; ENSPMAP00000001363; ENSPMAG00000001234.
DR GeneTree; ENSGT00940000154917; -.
DR HOGENOM; CLU_066247_9_2_1; -.
DR OMA; PRWDWFL; -.
DR TreeFam; TF314521; -.
DR Proteomes; UP000245300; Unplaced.
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; -; 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; PTHR11064; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..209
FT /note="Nuclear transcription factor Y subunit beta"
FT /id="PRO_0000204613"
FT DNA_BIND 60..66
FT /evidence="ECO:0000250"
FT REGION 1..53
FT /note="A domain"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..143
FT /note="B domain"
FT REGION 87..98
FT /note="Subunit association domain (SAD)"
FT /evidence="ECO:0000250"
FT REGION 144..209
FT /note="C domain"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 22676 MW; E89B0F0289882350 CRC64;
MDADGSTTDA SQLGITGDYI GGGHYVLQSS DGDAEGSLAS GDHDESCGSK DPYREQDIYL
PIANVARIMK TSIPSSGKIA KDAKECVQEC VSEFISFITS EASERCHQEK RKTINGEDIL
FAMSTLGFDS YVEPLKQYLQ KYRESMKGEK GINATVVTTT DAIPEELTEE SFSGPLATSI
ITADGQQQNV MVYTTAYQQI PGVQPIQFT
