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Database: UniProt
Entry: A0A3Q3MH39_9TELE
LinkDB: A0A3Q3MH39_9TELE
Original site: A0A3Q3MH39_9TELE 
ID   A0A3Q3MH39_9TELE        Unreviewed;      2106 AA.
AC   A0A3Q3MH39;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|RuleBase:RU364134};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024462.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000024462.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       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. {ECO:0000256|RuleBase:RU364134}.
CC   -!- SUBUNIT: Component of the Mediator complex.
CC       {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   Ensembl; ENSMAMT00000025093.2; ENSMAMP00000024462.2; ENSMAMG00000016385.2.
DR   GeneTree; ENSGT00390000013680; -.
DR   Proteomes; UP000261640; Unplaced.
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; IPR041285; MID_MedPIWI.
DR   PANTHER; PTHR48249; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   PANTHER; PTHR48249:SF4; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   Pfam; PF06333; Med13_C; 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:UP000261640};
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          1336..1661
FT                   /note="MID"
FT                   /evidence="ECO:0000259|Pfam:PF18296"
FT   DOMAIN          1697..2095
FT                   /note="Mediator complex subunit Med13 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06333"
FT   REGION          296..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1950..1983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..540
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..995
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1950..1974
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2106 AA;  232464 MW;  351E4EC2BD5268F0 CRC64;
     MSSCFVPNGA SLEDCHSNLF CLADLTGIKW RRFVWQGPTS SPILFPVTEE DPILCSFSRC
     LAADVLSVWR RHHTPGRREL WLFWWGDDPS FAELIHNELS SEEDGEWESG LSYECRTLLF
     KAIHNLLERC LMNRGFVRIG KWFVKPYQKD EKTINKRCHL SCAFTFFVHG DSNVCTSVEI
     AQHQPLQCLS EEHLSLAQQS SSPLQVILSP YGLNGTLTGQ AFKMSDHPTQ KLIEEWRQFY
     PISPNPKEVQ EDKMEDTDWE DDSLAAVEVL VAGVRMVYPS CLVLLPLSDL PAVAPQGSAN
     TSGSLCGAQQ GQAAHRDPAM SSVTLTPPTS PEEAQTNYQP AQRWLKLSSA SDGYSSDNTL
     HGGKIPRRLA SQMVESVWQE YNINRTGNKR KLTTLTNGTC EEESHKTGLW DFVEPTHRLH
     CNCSRHKNQK QRSSSTSGHP PSSGQPAQPT PKHKLGEKLE KGEKQQKRPQ TPFHHRNSVS
     EESSLEPQTQ RLCLRSQEEG SYPSLHHVDT VPSKAPTLHT HGPPADLVGS PPPPPLSPHP
     CDHVDGDMTP SGMKTSSTPV HQGFYPPSVE PCLLPQKGSS EEPQLENMRM PLPFPPPYSE
     TLEPTVFVGS AINPNEDSTH NPWKYFNLPR KKATNFPTPQ LPVDKMREDS GGGGVTERVS
     QELIKTYAQR RNSHLASTSV DEEHSNEPDP YAFIEGDEEF SFTEKKDKPG AEREGNKKHK
     NLFPLSVLYI GKSNAWSWVS YTVLFCCADG QGPSGSKPST STSLIHENDL AVSYSDLDKI
     FNSDEDELAP GSKRAGVSTE DKYGCKEIKP ATLDPLSCIS SADLHQMFPT PPSLEQQGYS
     PMNSGSKDSL EAAAGVTLLD GSQLNSHFKM EVEEGFCSPK PSEVKDFSFV YKPETCQPFI
     GCSMYAPLKT LPSQCLLPIK LPEDCVYTPS WTLGKMELIN VPSVEPDYSQ TYTPQTHTPF
     MSSSAPPSNS GTGILPSPAT PRFSVPTPRT PRTPRTPRGP SSVQGSLKYD NSDLYSPAST
     PSTCRPLSSV EPATVPSIPE AHSLYVTLIL SESVMNLFKD CNFDSCCVCV CNMNIRGADV
     GVYLKDNGEA QYPCTCGFSA VINRRLGQLA GLFLEDELDM VGRGSDASRD TERCFEELRA
     STTHKAGSLK EKPPDELILL LQDQCTNPFA PMAGVDYPKP SSAPCSFLRV GERDCYNDCY
     MALEHGRQFM DNMSGGKVDE TLVKSTCLHQ WPKFKSADMS KLFSQDILRV LLSLQPVLQD
     TIQKKRSVRS WGVQGPLTWQ QFHKMAGRGS YGTDESPEPL PIPTFLVGYE HDFVVLSPFG
     LPYWEKLLLD PFGSQRDVGY VIICPENEAL LHGAKTFFKD LSVIYEACQL GQHRPICKSH
     PEGILKVRTT EGRSMTEQPL SDWFLKMAAR DGNNEAFNKL KLFAQVCRYD LAPYLSEQSL
     DSSLLSQRSP AMASSSSQTS SSSSTSSGPQ STNTTSSSTS SAQVNSTPPS SGSQTIGGLA
     SSKPSSFSMY GTAGLQGSTS QNGPQSNPQG AGGLAENGPS ANQPQGPTET PESTMERDKV
     GKPTDGESHA VSYPPAIVVY LVDPFSYEDA DKEVHSSTYT LGLLRCYMEM LQFLPAHIRN
     AVSVQIVPCQ YLLQPVHSGE RHLYNQHLKS LAFSVFTQCR RPLPNSTNFK TLTGFGPGLA
     IDMALKNPER PECLRLYTPP FILAPVKDKQ TELGETFGEA SQKYNVLFVG YCLSHDQRWL
     LASCTDQHGE LLETCIISID VPNRARRKKG SARRLGLQKL WEWCLGLVQV TSLPWRVVIG
     RLGRMGHGEL RDWSILLSRR NLQSLSKRLK ETCRMCGISA ADTPSILSAC LVAMEPQGSF
     VIMPDSVSTG SVFGRSTTLN IQTSQLSTPQ DTSCTHILVF PTSAMVQVNT NTSEPIDINF
     NPINPDGSDG MGIFELFDND MVDPDLINIL PNSPTTSPVH SPGSHYQQGG DGSKGQSADR
     MESHEEALNI LQQPMALGYF VSTAKAGPLP DWFWSACPQA QNQCPLFLKA SLHLHVSSVQ
     SDELLHSKHS HPLDSNHTSD VLRFVLEQYN ALSWLTCDPA TQDRRSCLPV HFVVLTQMYN
     FIMNML
//
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