ID   RPB9_ENCCU              Reviewed;         108 AA.
AC   Q8SQU1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB9;
DE            Short=RNA polymerase II subunit B9;
DE   AltName: Full=DNA-directed RNA polymerase II subunit 9;
GN   Name=RPB9; OrderedLocusNames=ECU11_1400;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Component of RNA polymerase II which synthesizes mRNA precursors and
CC       many functional non-coding RNAs. Pol II is the central component of the
CC       basal RNA polymerase II transcription machinery. It is composed of
CC       mobile elements that move relative to each other. RPB9 is part of the
CC       upper jaw surrounding the central large cleft and thought to grab the
CC       incoming DNA template. Involved in the regulation of transcription
CC       elongation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC       of 12 subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P32529}.
CC   -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; AL590450; CAD26050.1; -; Genomic_DNA.
DR   RefSeq; NP_586446.1; NM_001042279.1.
DR   AlphaFoldDB; Q8SQU1; -.
DR   SMR; Q8SQU1; -.
DR   STRING; 284813.Q8SQU1; -.
DR   GeneID; 860100; -.
DR   KEGG; ecu:ECU11_1400; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1400; -.
DR   HOGENOM; CLU_093932_0_1_1; -.
DR   InParanoid; Q8SQU1; -.
DR   OMA; ENVFHRE; -.
DR   OrthoDB; 1421187at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   PANTHER; PTHR11239; PTHR11239; 1.
DR   Pfam; PF02150; RNA_POL_M_15KD; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR   SMART; SM00661; RPOL9; 1.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Zinc; Zinc-finger.
FT   CHAIN           1..108
FT                   /note="DNA-directed RNA polymerase II subunit RPB9"
FT                   /id="PRO_0000121472"
FT   ZN_FING         6..29
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         68..108
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ   SEQUENCE   108 AA;  12600 MW;  C42F855581AB1911 CRC64;
     MSDRFCKECN NLLYPKEDDN TLFLACKNCE HIQEAKSHRL YVKNFRPKHA SIELYARDLV
     QDPTLPSVKI NCGNCGFNKG LYFQPRGGEE DVALSIFYLC CRCYHLWT