MED5_CANGA
ID MED5_CANGA Reviewed; 1099 AA.
AC Q6FV36;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 5;
DE AltName: Full=Mediator complex subunit 5;
GN Name=NUT1; Synonyms=MED5; OrderedLocusNames=CAGL0E05060g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380951; CAG58827.1; -; Genomic_DNA.
DR RefSeq; XP_445908.1; XM_445908.1.
DR AlphaFoldDB; Q6FV36; -.
DR STRING; 5478.XP_445908.1; -.
DR PRIDE; Q6FV36; -.
DR EnsemblFungi; CAG58827; CAG58827; CAGL0E05060g.
DR GeneID; 2887379; -.
DR KEGG; cgr:CAGL0E05060g; -.
DR CGD; CAL0129110; NUT1.
DR VEuPathDB; FungiDB:CAGL0E05060g; -.
DR eggNOG; ENOG502R1HB; Eukaryota.
DR HOGENOM; CLU_281615_0_0_1; -.
DR InParanoid; Q6FV36; -.
DR OMA; FTCFAQF; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0070847; C:core mediator complex; IEA:EnsemblFungi.
DR GO; GO:0016592; C:mediator complex; IEA:EnsemblFungi.
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: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..1099
FT /note="Mediator of RNA polymerase II transcription subunit
FT 5"
FT /id="PRO_0000302771"
FT REGION 41..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 125498 MW; 92A4F440AB4ED6BC CRC64;
MESKSLNTLA LRCAARKIPA SEFLNLYKEF YNETFPANSI DNDDAKTQEG SGSQDKTDVE
ESISKPVGSK NDPVAILCAE FMKLLENGKY VILADYVVEV LFVNYHSELV REFLPKLKDL
MNKGILIHFF SKSCAFFVNL TDNLVISQLI KDLRATIVPC ILETNFCDIS NELVVAIAKF
LQAVLRFTPQ PIQINSETYR DNTFNLTKRL SLINKILSKK FAGIIDKKLQ FKEVLGPFTK
DSTLDFDNSP SITSPQFIPS PLPSMKERSV TSSQSAIKYK DLKLLRYYKN IWLNSKLMNW
QPFDSEFISN YSAIKSSLYP DQVQNIQNVD LLFTDLIETA FTCFAQFVSN KLYHQSNSTY
NLLERKWILF LSKILPLLVY KNSSRTAHVI GNALDGIDDK VIKAISAYYQ ENDDGRSRND
DLFDDYPSTS LDIRHDFIKS LTMLGVVPPV FITNYLRGDQ TVDSKALATT DDLTFTNQQG
IIEIVNDIPN FIRSSLEGME MENVSEPTLV SSNGLLQVLS NFDTVSPTKQ FELANAIVDM
LSESSTTFEL NTFVKLTAVL TFNYSHSLTS ILMYVTPEVL TKLYLEFVDK HWNSQVIGKQ
ETDGESQFEN VNISMSFSWA ILMLTILYKQ YHIDFVSMRA DYTTDNIKNS FAITFVENLP
DISDLFFIDE KNSDDPEVQV KSHKLVRDWL NDLFVNGSLS DSLLQNIEPK QLAILVPYIF
KQVTLAMEIG AVGDLQNLIG GFEYFLQPFM LVGLIKVMYW LEQYLSCLKS DETDEKLIQK
VLSLLNTIIC PSTLNEDSKA FHFAVLRLNA IPLLGILYQF RSNKHAESNY GIYSSDNEGN
PTLELMISRL ISSLSISPVY DIDSTILVTD NNFVQKPPKF QSFFVTNEIS MNKMLTNQMN
SFWSLHSSTY YNLDFLKTLI DTLTPKQFLL DVLRTLEYKV ETLGVKDVRN KSSSNESDQV
IDYLFYFLVL YDIENSEDAK AMAQFMEDTV DISINGDSGI VKQETQPKSE YNPDDDIDML
FGENDTSMQA NEEDTLDNKE LKSDRNCALG KNRHTFGFII HEIKLSYGTL ESDSMSYEDY
KKICEYHSRY LKMLKTCIF