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Database: UniProt
Entry: A0A5J5EUQ3_9PEZI
LinkDB: A0A5J5EUQ3_9PEZI
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ID   A0A5J5EUQ3_9PEZI        Unreviewed;       159 AA.
AC   A0A5J5EUQ3;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   02-APR-2025, entry version 20.
DE   RecName: Full=Transcription and mRNA export factor SUS1 {ECO:0000256|HAMAP-Rule:MF_03046};
GN   Name=SUS1 {ECO:0000256|HAMAP-Rule:MF_03046};
GN   ORFNames=FN846DRAFT_953881 {ECO:0000313|EMBL:KAA8903591.1};
OS   Sphaerosporella brunnea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Sphaerosporella.
OX   NCBI_TaxID=1250544 {ECO:0000313|EMBL:KAA8903591.1, ECO:0000313|Proteomes:UP000326924};
RN   [1] {ECO:0000313|EMBL:KAA8903591.1, ECO:0000313|Proteomes:UP000326924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb_GMNB300 {ECO:0000313|EMBL:KAA8903591.1,
RC   ECO:0000313|Proteomes:UP000326924};
RG   DOE Joint Genome Institute;
RA   Benucci G.M., Marozzi G., Antonielli L., Sanchez S., Marco P., Wang X.,
RA   Falini L.B., Barry K., Haridas S., Lipzen A., Labutti K., Grigoriev I.V.,
RA   Murat C., Martin F., Albertini E., Donnini D., Bonito G.;
RT   "Draft genome of the ectomycorrhizal ascomycete Sphaerosporella brunnea.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC       association with both the TREX-2 and the SAGA complexes. At the
CC       promoters, SAGA is required for recruitment of the basal transcription
CC       machinery. It influences RNA polymerase II transcriptional activity
CC       through different activities such as TBP interaction and promoter
CC       selectivity, interaction with transcription activators, and chromatin
CC       modification through histone acetylation and deubiquitination. Within
CC       the SAGA complex, participates to a subcomplex required for
CC       deubiquitination of H2B and for the maintenance of steady-state H3
CC       methylation levels. The TREX-2 complex functions in docking export-
CC       competent ribonucleoprotein particles (mRNPs) to the nuclear entrance
CC       of the nuclear pore complex (nuclear basket). TREX-2 participates in
CC       mRNA export and accurate chromatin positioning in the nucleus by
CC       tethering genes to the nuclear periphery. May also be involved in
CC       cytoplasmic mRNA decay by interaction with components of P-bodies.
CC       {ECO:0000256|HAMAP-Rule:MF_03046}.
CC   -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC       complex (transcription and export complex 2), composed of at least
CC       SUS1, SAC3, THP1, SEM1, and CDC31. TREX-2 contains 2 SUS1 chains. The
CC       TREX-2 complex interacts with the nucleoporin NUP1. Component of the
CC       1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5
CC       distinct domains with specialized functions. Within the SAGA complex,
CC       SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA
CC       called the DUB module (deubiquitination module). Interacts directly
CC       with THP1, SAC3, SGF11, and with the RNA polymerase II.
CC       {ECO:0000256|HAMAP-Rule:MF_03046}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000256|HAMAP-
CC       Rule:MF_03046}. Cytoplasm, P-body {ECO:0000256|HAMAP-Rule:MF_03046}.
CC   -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03046}.
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:KAA8903591.1}.
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DR   EMBL; VXIS01000116; KAA8903591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J5EUQ3; -.
DR   InParanoid; A0A5J5EUQ3; -.
DR   OrthoDB; 6221744at2759; -.
DR   Proteomes; UP000326924; Unassembled WGS sequence.
DR   GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0070390; C:transcription export complex 2; IEA:UniProtKB-UniRule.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.246.140; -; 1.
DR   HAMAP; MF_03046; ENY2_Sus1; 1.
DR   InterPro; IPR018783; TF_ENY2.
DR   InterPro; IPR038212; TF_EnY2_sf.
DR   PANTHER; PTHR12514; ENHANCER OF YELLOW 2 TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF10163; EnY2; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03046};
KW   mRNA transport {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326924};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_03046};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_03046}.
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..12
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..23
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..56
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   159 AA;  17978 MW;  229DB504888CAE85 CRC64;
     MGDIQPLSQT HTKSTHRVQR RVVPKLPTKP RSTPYTRTST STSTTTTITS TRMSPPKSSD
     KHASGAHAET VAEINRRILE SGELAKLESH LLQLLQEAGW TEQLRKLCQE RLRDPKAGVS
     NYADLRRAVE KEARESVPEN VRLEMVRRVL QVLRGMVEE
//
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