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Database: UniProt
Entry: A0A0V0WVE2_9BILA
LinkDB: A0A0V0WVE2_9BILA
Original site: A0A0V0WVE2_9BILA 
ID   A0A0V0WVE2_9BILA        Unreviewed;      1762 AA.
AC   A0A0V0WVE2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 30 {ECO:0000256|ARBA:ARBA00019664};
DE   AltName: Full=Mediator complex subunit 30 {ECO:0000256|ARBA:ARBA00031981};
GN   Name=Vps11 {ECO:0000313|EMBL:KRX79698.1};
GN   ORFNames=T06_9800 {ECO:0000313|EMBL:KRX79698.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79698.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX79698.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX79698.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025687}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004492}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004492}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004492}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 30 family.
CC       {ECO:0000256|ARBA:ARBA00010606}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX79698.1}.
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DR   EMBL; JYDK01000049; KRX79698.1; -; Genomic_DNA.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR018790; DUF2358.
DR   InterPro; IPR021019; Mediator_Med30_met.
DR   InterPro; IPR022127; STIMATE/YPL162C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF10184; DUF2358; 1.
DR   Pfam; PF11315; Med30; 1.
DR   Pfam; PF12400; STIMATE; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        559..581
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        675..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        720..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1609..1647
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          162..199
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1762 AA;  201962 MW;  078A35450678405D CRC64;
     MSQQNQNSFI QTFPLPPRPL NSNGNNLDAN YGYPQGIGPS SVSSPIQSLV NSFGSRREVP
     SPSPASVSES TNVAPGKTTQ ADESQQEHHA EREAWSAQGS KAFNVNPFFA FSMSQILQSN
     DNNGPLALCI IGRDFTREVI NRTCDICGAL KSLQLPTAPE AVKQHQDKLQ RINESLKQVN
     IILERLEAID RKIDNFRKEL LPADAEDHLK DLVTYDGKNE WLRKLTEERK SREVFTQTKQ
     QYDEVKKELE THAPSCSARS FNFCSLKLAQ FDPREFGLRL KPYIANSDDI HIPFRRPFFS
     CTNSLIYPDY NSYFIPIIRN LSSKKSKNDS VSESLVKRRV SFNFSAVYSQ VVNQCSSTEK
     SPTHYFERGK PNWDQLQHVI YRLSETVPTF FLRRLDYTFY SDDVLFLNRI CGSEVKGLRN
     YWLHLATLSV LSRIPCPYIE MKILNCMPIV EEGSVHLRWR VLYLTVPEFL YVVVRERSAD
     IETLRRNARW FDGFSYFYVG SDGLVYKHVA DRVMRDPEEI AANSKRVGLL NRLLGSSARS
     PIWKQFNLDK EKKNLVDSYG LSIQLILATL AFASLIVKRL LEPKQTRRPW TIWFFDTSKQ
     AVGSSVIHAM NIFLAGVFRG DPCTWYFVSF LLDSTLGLLI IYTGVKLVTA AASCRKDWST
     LRFGEYGDPP QCRPWLHQCL AFVILSVIEK FFVTLLLLMR FWKSVREIAL SPIRNPKVEV
     TLVILVFPFL INTIMFWVVD NFTMKRRAVS KKFNSNNSNS LIIANNGSSS SGIRRVHDES
     AVKLLDEYDN NSQQNDALAL FPADNILQHR NSSTLAGIFV FFIHFNSDCE SSTIIMASSL
     FQSWRRLVFF DRQLIADVEN ADESFTEFKD LNIACVAWKS NRVFIGEVDG GVHMYDKDFS
     DTYFKAYKVN LSLLYCPRSS DSLVSIGEDD NGVNPYLKVW LLDKLDKQGK PFAVRCSKTS
     PGNRPVKVTS VAVDSSGQLM VVGFEDSSIL LYRGDVCKEK QPKSQLIRDG STCASEGSIV
     GMELCDHSSQ AVILYVVTTR FTFSFTISFK EKDITKTVLE IEGLHMRRCW ALAGEELKNQ
     FVVARNMGFY FYQPEEKAYE ASFPDISEVF IAWNFIFILC MESGKLFRLK EMSIESQLDI
     LFRKNLFDLA ISIGEKQCQQ EGTVEYLSIL RGLFLQVRLD TDCFQCFEVE LLKNRKRDYS
     NALKQYMRTI GTLDTSYVIR KLLDAHRIEN LAEYLEAVFH AKLGTVDHSN VLLSCYIKMN
     AIDKINSFIQ NKETVAPLDV EAAVKLFRKF GLYRQAAFLT KRHGYPKRCL DLLVSDLKDF
     KQAINYISSL ESDVIAEFFT RYSKLLLENV PEETMTLLGE ILKRDGCSEK NWVQSVVLRL
     IAHPDRLEAF LEQSLMANKV DVKLYNLLLY AYLRRYSSTM ENDVAKEQIS RKIDQLLKNI
     SSDNQSLLEA LRFCYQWAYH PGILYLLERQ KMYSHLLKHQ MFLKDYDSVI SACLKYGDRR
     SGDKTLWSFA LQYFSEDPTI SEEYVKKLLT SSELTGDVHP MLAVQTLAKS KTLTFACVKD
     FLSHWVDKES KSIEMDEQDS LRLCNEIKRT EAIIDDIQKN PQIFQMSKCT ACDIILETPT
     VHFLCKHSYH QHCFENYAES EAECPVCLLD KKRFQNQCKT DSSTSSEALN HSFKEELMNT
     NNVIGTLTSY FGKTLFPDKD VDAENCEIHQ QDTSKSVQSL NPFEGELRIS NDSSGVILSA
     KYSSFDLHKF TLLNFCFVMP NA
//
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