RPB9_BOVIN
ID RPB9_BOVIN Reviewed; 125 AA.
AC Q32P73;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 I;
GN Name=POLR2I;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 (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; BC108233; AAI08234.1; -; mRNA.
DR RefSeq; NP_001069797.1; NM_001076329.2.
DR PDB; 5FLM; EM; 3.40 A; I=1-125.
DR PDB; 5OIK; EM; 3.70 A; I=1-125.
DR PDBsum; 5FLM; -.
DR PDBsum; 5OIK; -.
DR AlphaFoldDB; Q32P73; -.
DR SMR; Q32P73; -.
DR DIP; DIP-61194N; -.
DR IntAct; Q32P73; 2.
DR STRING; 9913.ENSBTAP00000019969; -.
DR PaxDb; Q32P73; -.
DR GeneID; 614472; -.
DR KEGG; bta:614472; -.
DR CTD; 5438; -.
DR eggNOG; KOG2691; Eukaryota.
DR InParanoid; Q32P73; -.
DR OrthoDB; 1421187at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd10508; Zn-ribbon_RPB9; 1.
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; IPR034012; Zn_ribbon_RPB9_C.
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 SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-directed RNA polymerase; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..125
FT /note="DNA-directed RNA polymerase II subunit RPB9"
FT /id="PRO_0000245341"
FT ZN_FING 17..42
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 82..124
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P36954"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5FLM"
SQ SEQUENCE 125 AA; 14489 MW; 9A206C1608C83B75 CRC64;
MEPDGTYEPG IVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH
EVDELTQIIA DVSQDPTLPR TEDHPCQKCG HKEAVFFQSH SARAEDAMRL YYVCTAPHCG
HRWTE
