ID A0A0D1YL36_9EURO Unreviewed; 1386 AA.
AC A0A0D1YL36;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|ARBA:ARBA00019618, ECO:0000256|RuleBase:RU364134};
DE AltName: Full=Mediator complex subunit 13 {ECO:0000256|ARBA:ARBA00032008, ECO:0000256|RuleBase:RU364134};
GN ORFNames=PV11_05526 {ECO:0000313|EMBL:KIV83507.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83507.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV83507.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83507.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025661, ECO:0000256|RuleBase:RU364134}.
CC -!- SUBUNIT: Component of the SRB8-11 complex, which itself associates with
CC the Mediator complex. {ECO:0000256|RuleBase:RU364134}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364134}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000256|ARBA:ARBA00009354, ECO:0000256|RuleBase:RU364134}.
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DR EMBL; KN846952; KIV83507.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1YL36; -.
DR HOGENOM; CLU_002210_0_0_1; -.
DR OrthoDB; 9289at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR InterPro; IPR041285; MID_MedPIWI.
DR PANTHER; PTHR48249; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR PANTHER; PTHR48249:SF3; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
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 {ECO:0000256|RuleBase:RU364134};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364134};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|RuleBase:RU364134};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364134};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364134}.
FT DOMAIN 9..340
FT /note="Mediator complex subunit Med13 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11597"
FT DOMAIN 886..1045
FT /note="MID"
FT /evidence="ECO:0000259|Pfam:PF18296"
FT DOMAIN 1056..1375
FT /note="Mediator complex subunit Med13 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06333"
FT REGION 491..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 152273 MW; 15FDDDD1DB8D863F CRC64;
MVDGMATSLD FPHNCSTNVY TLNDFGEIAY IVCTVATPPT HDPSAFVSTP ENTLARLRKT
ERQFREASIL AALDVEARQL FTFYKKVDIA NAKDQKTLLT KFGFVLRSNT CTIAYKTAAR
LPDLMKPEQA KLHRLFSTAL ISSIKLLPNG DSALQAFGPN LYMVERFPAN SEDEGFASPK
RWALHRIDLQ IIPSGHIILT IAKERRQTFR QALDIEHDVQ LAEHAKSSGA AVYLAPVGRV
ARFVGLPQGH DFNSGQSDHQ NLDARLKLWR ELLPAWMRNS LNNNAQVQDN CWIEAQIAVQ
ETDRASTDDD SKSVSSVNSG NNASISWRTI FWPANLCFLL ESKEPPALQA FGDNHDPLKF
IQDWVAGVAQ ERLGDGEHQH ELMNMAEEDD EPLFADNGTF DDPEPFQPSG PPAFPGNQSI
YPTPPDVVMT HPTPGISSVD VMGMTPANLP GQSDTAQQLD EEMHDIEEAH TSSEMRAYYD
EDLFEEMPED QFGQEDTADE PNWDFFDQSG METKPNPTTG SNPPNHLSRQ EDAATPNVTH
QAHQALREDG TQNTPAPSQR PATVLHDSPL PVESSGLRDT SHPMAPPQAE ESMSEAPVKL
EQQHDTFAHS TQSAGETDQK VRANGTNTHR HFSIYNGVHP PAEINRDNRY TANGEFWFDP
DKTTLQSSRN PYKLTAKVNR PQSDSDDSDS SMESTSRSEE HNPNQNEQPT TLRPWTEYHP
QSPSVTTHRG EVERTSVKQE IQELLDLLKP RSMQPPPLIR SETQNRVASV GQLTGQKFSQ
VANIMVDQYS QTSLISHKQI DADNEGSSAA RIEIVADLSG INSSTNASTL AQLVSLKADH
TKTRGRITNL KPDQICIRRG DQRLLASVSI LPFWNTLNLQ PENGSKDVTV FCLHPAGEDV
ADGCSNLLQR MSDTYNSCLL GSHAIGLLKG VTSTGLIAWD PKSTTSIAHT CQKVGTAIGA
ADNLSGTALV YMVSQDDSPA SYLEVCQAFH GLFESFAAAA NKQHISDIAL QVVPRGFVAS
SESLVVPNQI AYIKLAIEVY NRLPPPQPKG SPAACDTAIV LSKVENTVHL QLASAYGSPL
SAHGIILHLA YAITADKRWI TAAWTDELGQ VALSMSYCAR RLGSSKKRPR REIFREMWHV
SHDLASKHRG RWRLAIVKHG YLDTMEPVEW YDVFGSSTPA QQRCLPLILT MQLDPVYRLF
PQPHQGKVGQ TGLQNVYGTP VSTPQGGITS PDQLMPATPT PGGTSMMNAS TPPEPGIDPN
VDGDLSLVDP AEESWGVVLP YGVNQSKNMS VLLPAGVTGL LVKRRGPKVE DGHLSIEVNL
LDCTVHVGPD TSKEPSPDEL LEDVIRQYRG LLTLGVTRGC IDPLSECVPW HIATVIRGNG
ALGSVM
//
