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Database: UniProt
Entry: A0A0D9RUN1_CHLSB
LinkDB: A0A0D9RUN1_CHLSB
Original site: A0A0D9RUN1_CHLSB 
ID   A0A0D9RUN1_CHLSB        Unreviewed;      1720 AA.
AC   A0A0D9RUN1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   Name=POLR1A {ECO:0000313|Ensembl:ENSCSAP00000012320.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000012320.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000012320.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000012320.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|RuleBase:RU004279}.
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         ECO:0000256|RuleBase:RU004279};
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; AQIB01042089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007968183.1; XM_007969992.1.
DR   STRING; 60711.ENSCSAP00000012320; -.
DR   Ensembl; ENSCSAT00000014344.1; ENSCSAP00000012320.1; ENSCSAG00000016251.1.
DR   GeneID; 103219930; -.
DR   KEGG; csab:103219930; -.
DR   CTD; 25885; -.
DR   eggNOG; KOG0262; Eukaryota.
DR   GeneTree; ENSGT00920000149138; -.
DR   OMA; NREDYQQ; -.
DR   OrthoDB; 169836at2759; -.
DR   BioGRID-ORCS; 103219930; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 14.
DR   Bgee; ENSCSAG00000016251; Expressed in fibroblast and 7 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR   GO; GO:0005736; C:RNA polymerase I complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0071667; F:DNA/RNA hybrid binding; IEA:Ensembl.
DR   GO; GO:0001054; F:RNA polymerase I activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IEA:Ensembl.
DR   CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.357.120; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 1.
DR   Gene3D; 6.10.250.2940; -; 1.
DR   Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 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   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          295..642
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1365..1498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1371..1394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1409
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1425..1445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1720 AA;  194630 MW;  295F9167C9C06C40 CRC64;
     MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS
     KEVCSTCVQD FNNCSGHLGH IELPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAVIHLL
     LCQLRVLEVG ALQAVYELER ILNRFLEENA DPSASEIQEE LEQYTAEIVQ NNLLGSQGAH
     VKNVCESKSK LTAVFWKAHM NAKRCPHCKT GRSVVRKEHN SKLTITFPAM VHRTAGQKDS
     EPLGIEEAQM GKRGYLTPTS AREHLFALWK NEGFFLNYLF SGMDDDGMES RFNPSVFFLD
     FLVVPPSRYR PVSRLGDQMF TNGQTVNLQA VMKDVVLIRK LLALMAQEQK LPEEVAAPPP
     DEEKDSLIAI DRSFLSTLPG QSFIDKLYNI WIRLQSHVNI VFDSEMDKLM MDKYPGIRQI
     LEKKEGLFRK HMMGKRVDYA ARSVICPDMY INTNEIGIPM VFATKLTYPQ PVTPWNVQEL
     RQAVINGPNV HPGASMVINE DGSRTALSAV DMTQREAVAK QLLTPATGAP KPQGTKIVCR
     HVKNGDILLL NRQPTLHRPS IQAHHARILP EEKVLRLHYA NCKAYNADFD GDEMNAHFPQ
     SELGRAEAYV LACTDQQYLV PKDGQPLAGL IQDHMVSGAS MTTRGCFFTR GQYMELVYRG
     LTDKVGRVKL FPPSILKPFP LWTGKQVLST LLINIIPEDH IPLNLSGKAK ITGKAWVKET
     PRSVPGFNPD SMCESQVVIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GETSGKVLTC
     LARLFTAYLQ LYRGFTLGVE DILVKPKADV KRQRIIEEST HCGPRAVRAA LNLPEATSCD
     EVRGKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQFP ENSLQMMVQS
     GAKGSTVNTM QISCLLGQIE LEGRRPPLMA SGKSLPCFEP YEFTPRAGGF VTGRFLTGIK
     PPEFFFHCMA GREGLVDTAV KTSRSGYLQR CIIKHLEGLV VQYDLTVRDS DGSVVQFLYG
     EDGLDIPKTQ FLQPKQFPFL ASNYEVIMKS QHLHEVLSRA DPKKALRHFR AIKKWQSKHP
     NTLLRRGAFL SYSQKIQAAV KALNLESENR NGRSPGTQEM LRMWYELDEE SRRKYQKKAA
     TCPDPSLSVW RPDIYFASVS ETFETKVDDY SQEWAAQTEK SYEKSELSLD RLRTLLQLKW
     QRSLCEPGEA VGLLAAQSIG EPSTQMTLNT FHFAGRGEMN VTLGIPRLRE ILMVASANIK
     TPMMSVPVLN TKKALRRVKS LKKQLTRVCL GEVLQKIDVQ ESFCMEEKQN KFRVYQLRFQ
     FLPHAYYQQE KCLRPEDILR FMETRFFKLL MESIKKKNNK ASAFRNVNTR RATQRDLDNA
     GESGRSRGEQ EGDEEEEGHI VDAEAEEGDA DASDAKRKEK QEEEVDYESE EEEEREGEEN
     DDEDTQEEQN PHREGARETQ ERDEEVGSGA EEDPALPTLL TQPRKPTHSQ EPQGPEAMER
     RVQAVREIHS FIDDYQYDTE ESLWCQVTVK LPLMKINFDM GSLVVSLAHG AVIYATKGIT
     RCLLNETTNN KNEKELVLNT EGINLPELFK YAEVLDLRRL YSNDIHAMAN TYGIEAALRV
     IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIRSNSSPLQ QMTFETSFQF
     LKQATMLGSH DELRSPSACL VVGKVVKGGT GLFELKQPLR
//
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