ID   MED5_ASHGO              Reviewed;        1098 AA.
AC   Q74Z26;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 5;
DE   AltName: Full=Mediator complex subunit 5;
GN   Name=NUT1; Synonyms=MED5; OrderedLocusNames=AGR380C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       the regulated transcription of nearly all RNA polymerase II-dependent
CC       genes. Mediator functions as a bridge to convey information from gene-
CC       specific regulatory proteins to the basal RNA polymerase II
CC       transcription machinery. Mediator is recruited to promoters by direct
CC       interactions with regulatory proteins and serves as a scaffold for the
CC       assembly of a functional preinitiation complex with RNA polymerase II
CC       and the general transcription factors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 5 family.
CC       {ECO:0000305}.
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DR   EMBL; AE016820; AAS54870.1; -; Genomic_DNA.
DR   RefSeq; NP_987046.1; NM_212108.1.
DR   AlphaFoldDB; Q74Z26; -.
DR   SMR; Q74Z26; -.
DR   STRING; 33169.AAS54870; -.
DR   PRIDE; Q74Z26; -.
DR   EnsemblFungi; AAS54870; AAS54870; AGOS_AGR380C.
DR   GeneID; 4623350; -.
DR   KEGG; ago:AGOS_AGR380C; -.
DR   eggNOG; ENOG502R1HB; Eukaryota.
DR   HOGENOM; CLU_281615_0_0_1; -.
DR   InParanoid; Q74Z26; -.
DR   OMA; FTCFAQF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0070847; C:core mediator complex; IEA:EnsemblFungi.
DR   GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0043966; P:histone H3 acetylation; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IEA:EnsemblFungi.
DR   InterPro; IPR014801; Mediator_Med5_fun.
DR   PANTHER; PTHR35784; PTHR35784; 1.
DR   Pfam; PF08689; Med5; 1.
PE   3: Inferred from homology;
KW   Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1098
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   5"
FT                   /id="PRO_0000302766"
FT   REGION          1019..1041
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1041
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1098 AA;  123999 MW;  353E50595775AD38 CRC64;
     MVRAQETVYD LITKCSVRRV PPKQFVNFYN EFFNERYDSV LENGNPAGES RPTAPVYEEV
     AQDLVRILND SRVNLVADYV LEIVLINLNV DLLRLFLPKL HHVRNVMLLV HLFSRATAFI
     SGLDNKLLAE QISDTVYTDV TPAVLSFNMQ AIDDQLVIVL AKFLHAVLRL PEGQQKMGSV
     PTKQKAATLL QRLSTIDRLL YKRFIADLDG KLRLSGAPAD MSFPLPPSNM PSPSVTSPKY
     ETSSVGVMKR STSMSNEAKY QDIKLARYYK NLWLNNKIHY CTVSDPLFLE KYDSILELAT
     GGGLSADRPV KAKIADLVET AFTCFAQFVS NKLYHQSNSN FSLLERKWTV FVTKQLPLII
     KSSIPDKTDI VLRTLENIDD KVIKAIKSYN TEKEEVKNRT EDLFDDYPVN SLDIRHEFLK
     NLIMMGLQPP TVLNEYLRED QMVDLKSLVT SEHLIIDNSQ GVRETILNVR NFITKSIESL
     EFENLFDDGN QLLVTNDHGI IQIAHNLETI SPTKQLEIAN ILYDLLSAAI ESLDHKTISK
     VLTILTLNVG HLLTNIFCLT GYEKFARAVI RFIDVIWESN KSKSNDMVSD DSEFENINSA
     MAYTLSLCFI IHVVDIYGVN VEALVENPSK STVLRFLSKL GEIPEVFVAP EGDLESSKTL
     LQQWLRELFV KNLISDNLMK SADVKVMGFM IPFIFKQTLL NVEYGIISDI SSFVNGFEYF
     LQPFLSVGLI NIVFWLEKYL LALKTTESFP KINGALFDIL GAIIAPKSIG SDAKAIHSVV
     LKLKCVGLLK ELKSFQVPSE SNYGIYSSQT RQDPRLEALI SKLELIAQSS ALYDVDPRII
     SAVNNNYSQK HISYNKVVLT SDIPINKIMT NQINSFWNLH SSTYYNFDYL LELIDLVTPF
     KFVQDVFQTL KYKVTAYGVP GSATKPSSAA LDQVLGYVFY FMVLRDIKCP EEKSLLLEYL
     DSGRFPSSIS ATVLTSDPTT ISGMPPVSMP YDVKSEQDAM EGVDEDFDML FGESFSGLPD
     DVQKSADMKP DTGIKEDDSE KSSYVSAARL TESFGVIFSK MKKDKLEAYQ AGQISEERYQ
     CFMGLYDKYV QTLRHSVI