SSN2_PHANO
ID SSN2_PHANO Reviewed; 1375 AA.
AC Q0U6W8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Mediator complex subunit 13;
GN Name=SSN2; Synonyms=MED13; ORFNames=SNOG_12496;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445346; EAT80309.2; -; Genomic_DNA.
DR RefSeq; XP_001802717.1; XM_001802665.1.
DR AlphaFoldDB; Q0U6W8; -.
DR STRING; 13684.SNOT_12496; -.
DR EnsemblFungi; SNOT_12496; SNOT_12496; SNOG_12496.
DR GeneID; 5979626; -.
DR KEGG; pno:SNOG_12496; -.
DR eggNOG; KOG3600; Eukaryota.
DR HOGENOM; CLU_002210_0_0_1; -.
DR InParanoid; Q0U6W8; -.
DR OrthoDB; 117651at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR InterPro; IPR041285; MID_MedPIWI.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
DR Pfam; PF18296; MID_MedPIWI; 1.
PE 3: Inferred from homology;
KW Activator; Coiled coil; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1375
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000314250"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..216
FT /evidence="ECO:0000255"
FT COILED 297..324
FT /evidence="ECO:0000255"
FT COMPBIAS 20..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1375 AA; 150059 MW; 6C7325767E66A1E5 CRC64;
MKASEMARPP MRPGNPHAFA SPATTPSRTA SPNNAQGANV RTTQGGNQAG ASEQQQPLDC
FVVYELFASA VTALVSFFLV KDCGAVALNY RTFVSKVEPQ QEEGKIVTDL DRLYWLTSVH
VHWFSSGTLL VSTSTERTLA LQCLGDLSED EQQKLVDRCI RVAPNAMLAS ISSFDDPRQL
SADDSNRRTS KKKAKMDSLE QNIEKWRMSV QRWLSRRGYS LPNLDKNSAW VTIRVGQLAQ
FPAMSPHLPT SARDVLWPRS LCFMQSLVPD DLKWFEVPGS AGFRDPIDAA QDWFTGQLER
DKILDMQRKA KKAEEDAMRR KDEAPGLYPS SPFTARTGVY GDLQPVSGVY PTPPDGIVPG
TGISSTDTPS VSGTASNVVL VPGGNTPAIN LSAPQDYTTT DNQQHASTSP TFPAPLEPFQ
TSGEDDDLFE DMEGDGFGGP DVEEADFDFF DGPDGDDVNM ADAPALPETT NKPHKQLNND
VAMAHEEEHS VKEEMSDPLA ALESALAAPY RPINDGMPEE KVSEKEAKAV VPVEALATSP
AQIKQNPPAK KEATPPLSPS AIAKTLQPSP PKKQSSFPAS LQRTNSAFHS LDFSRRLSLV
DAKYQDGRFA ARIEKTEDDE SAVNPGRLKS LKDLPLLNKL RYAVASASTA KSTEALSLAR
AVSDDSASDS ESETSDMSEG SPEDPVDTHP LPYLGRLIIP AKRKLPTEGH GTPLSVTSFA
ESLAGDWQDS NSLLLDESSL TFFEPNTWDW SIPDLSMEPP EEKPLNGKES IAVTQILTDQ
IVSATLDLLD ENALVESTSS IEPSSETRWQ ICIKELFPKA AECTLSALIA IHDVFPDLSA
QAKGQQRPPP RKPNESNAIP SNHMYPMNPP FIRVRRAETH WDLLPPSIAF WEPLGLAPAS
PPKNVVAFCI YPHSASLRPI LDRFMLNLQL AYDTCKLGSH ARVETVIEYE GGLVPVKANS
QTSAKEAFRA LKDTCIQLGK LLAIQYAQLG EQQDTKIDAF VVYMVDPFGN PAALWELCSA
FWSLFQAYGQ GPPGRSDPTP KPDLVLQIIP IKYLASFDVP VILDAATYVS LAREVYDRCP
PSVASTDKTP LSIYKAPAFQ LEESLPRNVQ FKLLSEPPQD LLRENSYMHI AYAISLDGNW
LTAAWSDSCG KSQAVVSYHL GTRVFGDIAK EIWQTTIEIL QARRVQWRVC IAKSGPLDRE
ELETWVLLIT CPTQVNLFLT ILTVIEDPPY KFTPTTPAPS NSSAQANTNT PGSTPQTGVS
PDPTIGLTPA ATPSADPAPD PAADPEARLI DVTDETWGII LAHRLHNSNS TNQFSPALIS
GLLVKRGITH ATSNSIHHPI PDPLPGPITV AVNILWIGAV GSTWKRAAES RGTQY
