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Database: UniProt
Entry: A1DG38
LinkDB: A1DG38
Original site: A1DG38 
ID   MED14_NEOFI             Reviewed;        1093 AA.
AC   A1DG38;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-NOV-2024, entry version 82.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 14;
DE   AltName: Full=Mediator complex subunit 14;
GN   Name=rgr1; Synonyms=med14; ORFNames=NFIA_082960;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family.
CC       {ECO:0000305}.
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DR   EMBL; DS027696; EAW18345.1; -; Genomic_DNA.
DR   RefSeq; XP_001260242.1; XM_001260241.1.
DR   AlphaFoldDB; A1DG38; -.
DR   STRING; 331117.A1DG38; -.
DR   EnsemblFungi; EAW18345; EAW18345; NFIA_082960.
DR   GeneID; 4586799; -.
DR   KEGG; nfi:NFIA_082960; -.
DR   VEuPathDB; FungiDB:NFIA_082960; -.
DR   eggNOG; KOG1875; Eukaryota.
DR   HOGENOM; CLU_003573_1_1_1; -.
DR   OMA; ITQGYIP; -.
DR   OrthoDB; 2719576at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0070847; C:core mediator complex; IEA:TreeGrafter.
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; IPR055122; Med14_N.
DR   InterPro; IPR013947; Mediator_Med14.
DR   PANTHER; PTHR12809; MEDIATOR COMPLEX SUBUNIT; 1.
DR   PANTHER; PTHR12809:SF2; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 14; 1.
DR   Pfam; PF08638; Med14; 1.
PE   3: Inferred from homology;
KW   Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1093
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   14"
FT                   /id="PRO_0000304605"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1093 AA;  120836 MW;  EF3E879A3EF3C532 CRC64;
     MPGVIMDNAT VGRLGHAPDT QTPSNGDNLR NGSLHINGAA KGDKDHDPDK ESYTGKPKID
     GHRALPELPH ITQGFFPFST LVNRYVQQCW NELSDLITEL AAIQVSPHSS MPLLPANGKS
     PGNQSPENVQ KKLRILDFAH AKRAEFIKLL VLSQWSRRAH DVSKLIDLQN FIRSRHQAFV
     DALQRVGEMK RDLVQAQVAN PDLQTALEIL SKGRLESLAD LGYKSSKLLT ARGALKRLHR
     INRIISARLA LHDSIPHPFR TYRVHDGRVT FVVRGEFELD LSVGAESELS QFFFVDIRFL
     YSPSSNIPNG RMSNEIDAKI NDKLRDSGLT GCFNFLHGLV LTNKIHILFK QAIELAKGLW
     SETLRVELLH RTLVIQYWAL KPGPKSWVEI GVKSGNGDAD SQGVGVPCLG LRWMRDGQEV
     DSRDIEFDPE DLSMECLLRS VIALHISYLL SSAYGILSEY SLFSTGTLSS QAILNVTEPG
     ECQLSVQLTG SRHLRVSIEP MSGAVTLSAT PGLSERSESD ASLDRSTIDD LVARVSRLRC
     IAAIEELESN VRILGFETVS PKGLRNEIRT VFPANVLRFS LFWHPSWERN WVVAATSSIT
     GDNWWVVQLR RSSEVATDFS VSDTSVPLCS GHSMSDTFLA TSHQTRSSSF PDLGYCLSGM
     VAIYANVSYL SDLQSVEFHP PLCALKVESD LQIPDIFIRY QVSKLPRALQ LVLPAGLKRK
     NLLKDTVRLA FHGIDRHKNS AIFVAYGNLV GPWTDLCTLV SKSDSSLVFK RGGSGFALRL
     LAPAGRPVIV QLFKSLQTLE CTLSILDFLR QRRLTPQSLS LTHIAFAYGP RRDLSAIIGI
     GLSEVPSSAE LDPVRILART DPLLFLTLGI RFKHPNPHRR VQGSLAAILN HASNEAGLDF
     VTEILSFTLP LMRALEQITS NASRQESFRL QVIVRNACTF LLHYTYQGFR FQLTTSQHSG
     QLTWVLRELS SPGAGPGHDQ LKARLRGTLY HSNGNGWKGL GNGVVADVEG VSNVIWALDG
     CFTGAQHNTW LPRETKSDQD YSTQPVPEKQ SQTGAPSQAA MANDTTITAN FVNDKSLQRN
     PVASNAADVI TID
//
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