ID H9FSL1_MACMU Unreviewed; 1720 AA.
AC H9FSL1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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|EMBL:AFE77620.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE77620.1};
RN [1] {ECO:0000313|EMBL:AFE77620.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE77620.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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; JU333865; AFE77620.1; -; mRNA.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
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 2: Evidence at transcript level;
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 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..1497
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..1444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1720 AA; 194697 MW; 8B6C3DC8224B6BAC CRC64;
MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS
KEVCSTCVQD FNNCSGHLGH IELPLTVYNP LLFDKLYLLL RGSCLNCHLL 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 EQYMELVYRG
LTDKVGRVKL FPPSILKPFP LWTGKQVLST LLINIIPEDH IPLNLSGKAK ITGKAWVKET
PRSVPGFNPD SMCESQVVIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GETSGKVLTC
LARLFTAYLQ LYRGFTLGVE DILVKPKADV KRQRIIEEST HCGPRAVRAA LNLPEATSYD
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 TKKALKRVKS LKKQLTRVCL GEVLQKIDVQ ESFCMEEKQN KFRVYQLRFQ
FLPHAYYQQE KCLRPEDILR FMETRFFKLL MESIKKKNNK ASAFRNVNTR RATQRDLDNA
GESGRSRGEQ EGDEEDEGHI VDAEAEEGDA DASDAKRKEK QEEEVDYESE EEEEREGEEN
NDEDTQEERN PHREGARETQ ERDEEVGSGT EEDPALPALL TQPRKPTHSQ EPQGPEAVER
RVQAVREIHS FIDDYQYDTE ESLWCQVTVK LPLMKINFDM GSLVVSLAHG AVIYATKGIT
RCLLNETTNN KNEKELVLNT EGINLPELFK YAEVLDLRRL YSNDIHAMAN TYGIEAALRV
IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIRSNSSPLQ QMTFETSFQF
LKQATMLGSH DELRSPSACL VVGKVVKGGT GLFELKQPLR
//
