SSN2_CANGA
ID SSN2_CANGA Reviewed; 1345 AA.
AC Q6FNM7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Mediator complex subunit 13;
GN Name=SSN2; Synonyms=MED13; OrderedLocusNames=CAGL0J10472g;
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 SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the SRB8-11 complex, which itself associates with
CC the Mediator complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
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DR EMBL; CR380956; CAG61118.1; -; Genomic_DNA.
DR RefSeq; XP_448167.1; XM_448167.1.
DR AlphaFoldDB; Q6FNM7; -.
DR SMR; Q6FNM7; -.
DR STRING; 5478.XP_448167.1; -.
DR PRIDE; Q6FNM7; -.
DR EnsemblFungi; CAG61118; CAG61118; CAGL0J10472g.
DR GeneID; 2889605; -.
DR KEGG; cgr:CAGL0J10472g; -.
DR CGD; CAL0132930; CAGL0J10472g.
DR VEuPathDB; FungiDB:CAGL0J10472g; -.
DR eggNOG; KOG3600; Eukaryota.
DR HOGENOM; CLU_242296_0_0_1; -.
DR InParanoid; Q6FNM7; -.
DR OMA; FSRELWC; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:1990508; C:CKM complex; IEA:EnsemblFungi.
DR GO; GO:0016592; C:mediator complex; IEA:EnsemblFungi.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:EnsemblFungi.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
PE 3: Inferred from homology;
KW Activator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1345
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000314247"
FT REGION 363..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..484
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 151209 MW; E99C8B215112B0AE CRC64;
MKEATDDYDL SKLVSNFYRL EKITKINYAQ YLPKKQNDQW GIQMEIQMRK KDRKLLVALL
SKELWCFSIN DQVLPSPNDI DPELNVSADK TGSFTADYSK PNLPPHYALF LKSLKRMIYL
NLVEQSKNTL VQFGNSCINI TKNNESNNLL QIEPHLFSNS ELAISICVKD LGLLPLKVNS
IDPAFLSSHA LYMAPSGVRV YLVENKNDNS GTNQEHLHKY LVPVPENGEV LLKTLYASHG
IKLNSSTCQW VNIIPNITHL NGRAPNISQY MDLPKELRTI VWPLDLVFAQ PALDIDSSTT
LSQINGLDTF EDTLSLIDNF LQLKQSSSYR TPGSSGGLTG TNIGTNVFSS EGAYTDQFQV
YPKSQTNQQQ TSSNSKVSPS DAASPYPGID KIIEQKQFTP DFMASPSVSG NSNELFNDRK
NGHTDLLISP SKMDVDTDFP GSNLAGQEAP SQPASDVKKS SVSASDSELF GEEDEDEDDA
DLFGESNNDS TGESNANNSK GEITEDIFAS SDDESSLQPK KESTFYDGIK NGSAESGLNM
QDRANLKRTY LDIRIEETPL SSPLYTDPGA PLPVETPRDR RKSVFAPLNF NPIIAKDVDN
KYKNGGKYSF SPLQKEEALN FDVSRTELSS SEGEDSESSD DELEDLANKN DGVVYDKAEN
IGYKTFANLQ DSVPPGLIKQ DFLGNPYLAS LEGSKEGQNT IWKMPQTDIA QTESPLKAID
TSIGPDGTLP NTTSSEQSKS VYVHDYGISP TKMSNDPAFD TAKIEGKYEF MNNFPSSFPF
LLRHMPLSLI PDTFKHLNPT ITVNERNNQI IDLLAEQIVY DYNILGNLTI PDVPYSGIRN
YSNGVVKNTI DNLFSEFTRL DGTTLISRLY PMETPFVSVR KQHDQIKLRS DVQQFTKYAN
LKPVRGIKNF KFLVLTDSFK EDCIQFISSL SQTYINHELG FCEHLQLTNE DSKGLIYLKD
FEDSKLLLLA AQIVSYLSTN RTSGKEVAFM MIIPVQRCDI SELVEKTAKF QIIQNEVKAK
IPSMELYLKI VPMDFIKSPL TSVDDYTNLC ISIYNILPNK MIKFTHIRKQ IPEKLTFKTS
QQASAFKYDA YIHLAYSRSV DKQWMFAALS DSAGKENMMK TWYLGSSKNK FDEACNHIWE
MALSLAGKNY GKVCLILTRL NGILPDDELM NWRRLSGRNI HLAVVCVDDN TKISFFDRNE
SYPSYKRLYQ NANSIETLVD PERIDDYLIR DLDQDIHGVI FENPFPLVNS LHRCAIKSGA
LVKFNVSTTA TEPHSLDKFE VNLLNCPHSD SFKLLETILE EFRNLAALNV WFGITNGENG
HIPWHVLAVK KMMKTLVHTR VKVAQ