RPB7_BOVIN
ID RPB7_BOVIN Reviewed; 172 AA.
AC Q5E9B8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB7;
DE Short=RNA polymerase II subunit B7;
DE AltName: Full=DNA-directed RNA polymerase II subunit G;
GN Name=POLR2G;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. RPB7 is part of a
CC subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and
CC RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems
CC to lock the clamp via RPB7 in the closed conformation thus preventing
CC double-stranded DNA to enter the active site cleft. The RPB4-RPB7
CC subcomplex binds single-stranded DNA and RNA. Binds RNA (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the
CC 10-subunit Pol II core complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; BT021002; AAX09019.1; -; mRNA.
DR RefSeq; NP_001015633.1; NM_001015633.1.
DR PDB; 5FLM; EM; 3.40 A; G=1-172.
DR PDB; 5OIK; EM; 3.70 A; G=1-172.
DR PDBsum; 5FLM; -.
DR PDBsum; 5OIK; -.
DR AlphaFoldDB; Q5E9B8; -.
DR SMR; Q5E9B8; -.
DR DIP; DIP-61192N; -.
DR IntAct; Q5E9B8; 2.
DR STRING; 9913.ENSBTAP00000012481; -.
DR PaxDb; Q5E9B8; -.
DR Ensembl; ENSBTAT00000012481; ENSBTAP00000012481; ENSBTAG00000009483.
DR GeneID; 526320; -.
DR KEGG; bta:526320; -.
DR CTD; 5436; -.
DR VEuPathDB; HostDB:ENSBTAG00000009483; -.
DR VGNC; VGNC:33141; POLR2G.
DR eggNOG; KOG3298; Eukaryota.
DR GeneTree; ENSGT00390000008975; -.
DR HOGENOM; CLU_085878_2_0_1; -.
DR InParanoid; Q5E9B8; -.
DR OMA; MRQPGLG; -.
DR OrthoDB; 1140388at2759; -.
DR TreeFam; TF103042; -.
DR Reactome; R-BTA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-BTA-674695; RNA Polymerase II Pre-transcription Events.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000009483; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; IBA:GO_Central.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW RNA-binding; Transcription.
FT CHAIN 1..172
FT /note="DNA-directed RNA polymerase II subunit RPB7"
FT /id="PRO_0000073985"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5FLM"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5FLM"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5FLM"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5FLM"
SQ SEQUENCE 172 AA; 19294 MW; AF3CE655F658CD5C CRC64;
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ
PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE IGPMSCFISR HSIPSEMEFD
PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT RVDKNDIFAI GSLMDDYLGL VS
