ID A0A1U7R6H0_MESAU Unreviewed; 1642 AA.
AC A0A1U7R6H0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1 {ECO:0000256|ARBA:ARBA00016625};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
DE AltName: Full=DNA-directed RNA polymerase III largest subunit {ECO:0000256|ARBA:ARBA00033154};
GN Name=LOC101840076 {ECO:0000313|RefSeq:XP_005088494.2};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005088494.2};
RN [1] {ECO:0000313|RefSeq:XP_005088494.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26319212;
RA Ying B., Toth K., Spencer J.F., Aurora R., Wold W.S.;
RT "Transcriptome sequencing and development of an expression microarray
RT platform for liver infection in adenovirus type 5-infected Syrian golden
RT hamsters.";
RL Virology 485:305-312(2015).
RN [2] {ECO:0000313|RefSeq:XP_005088494.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460}.
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DR RefSeq; XP_005088494.2; XM_005088437.3.
DR eggNOG; KOG0260; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 36.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 21.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000313|RefSeq:XP_005088494.2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..221
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1218..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1642 AA; 180670 MW; 1F787C34A0ADABC0 CRC64;
MQKSGRPLKS LKQRLKGKEG RVRGNLMGKR VDFSARTVIT PDPNLSIDQV GVPRSIAANM
TFAEIVTPFN IDRLQELVRR GNSQYPGAKY IIRDNGDRID LRFHPKPSDL HLQTGYKVER
HMCDGDIVIF NRQPTLHKMS MMGHRVRILP WSTFRLNLSV TTPYNADFDG DEMNLHLPQS
LETRAEIQEL AMVPRMIVTP QSNRPVMGIV QDTLTAVRKF TKRDVFLERG EVMNLLMFLS
TWDGKVPQPA ILKPRPLWTG KQIFSLIIPG HINCIRTHST HPDDEDSGPY KHISPGDTKV
VVENGELIMG ILCKKSLGTS AGSLVHISYL EMGHDITRLF YSNIQTVINN WLLIEGHTIG
IGDSIADSKT YQDIQNTIKK AKQDVIEVIE KAHNNELEPT PGNTLRQTFE NQVNRILNDA
RDKTGSSAQK SLSEYNNFKS MVVSGAKGSK INISQVIAVV GQQNVEGKRI PFGFKHRTLP
HFIKDDYGPE SRGFVENSYL AGLTPTEFFF HAMGGREGLI DTAVKTAETG YIQRRLIKSM
ESVMVKYDAT VRNSINQVVQ LRYGEDGLAG ESVEFQNLAT LKPSNKAFEK KFRFDYTNER
ALRRTLQEDL VKDVLSNAHI QNELEREFER MREDREVLRV IFPTGDSKVV LPCNLLRMIW
NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LLFNIHLRST
LCSRRMAEEF RLSGEAFDWL LGEIESKFNQ AIAHPGEMVG ALAAQSLGEP ATQMTLNTFH
YAGVSAKNVT LGVPRLKELI NISKKPKTPS LTVFLLGQSA RDAERAKDIL CRLEHTTLRK
VTANTAIYYD PNPQSTVVAE DQEWVNVYYE MPDFDVARIS PWLLRVELDR KHMTDRKLTM
EQIAEKINAG FGDDLNCIFN DDNAEKLVLR IRIMNSDENK MQEEEEVVDK MDDDVFLRCI
ESNMLTDMTL QGIEQISKVY MHLPQTDNKK KIIITEDGEF KALQEWILET DGVSLMRVLS
EKDVDPVRTT SNDIVEIFTV LGIEAVRKAL ERELYHVISF DGSYVNYRHL ALLCDTMTCR
GHLMAITRHG VNRQDTGPLM KCSFEETVDV LMEAAAHGES DPMKGVSENI MLGQLAPAGT
GCFDLLLDAE KCKYGMEIPT NIPGLGAAGP TGMFFGSAPS PMGGISPAMT PWNQGATPAY
GAWSPSVGSG MTPGAAGFSP SAASDASGFS PGYSPAWSPT PGSPGSPGPS SPYIPSPGGA
MSPSYSPTSP AYEPRSPGGY TPQSPSYSPT SPSYSPTSPS YSPTSPNYSP TSPSYSPTSP
SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPNY SPTSPNYTPT SPSYSPTSPS
YSPTSPNYTP TSPNYSPTSP SYSPTSPSYS PTSPSYSPSS PRYTPQSPTY TPSSPSYSPS
SPSYSPTSPK YTPTSPSYSP SSPEYTPTSP KYSPTSPKYS PTSPKYSPTS PTYSPTTPKY
SPTSPTYSPT SPVYTPTSPK YSPTSPTYSP TSPKYSPTSP TYSPTSPKGS TYSPTSPGYS
PTSPTYSLTS PAISPDDSDE EN
//