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Database: UniProt
Entry: F7H346_CALJA
LinkDB: F7H346_CALJA
Original site: F7H346_CALJA 
ID   F7H346_CALJA            Unreviewed;      1720 AA.
AC   F7H346;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 62.
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:ENSCJAP00000036331.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036331.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000036331.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000036331.4}
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   RefSeq; XP_002757589.1; XM_002757543.3.
DR   STRING; 9483.ENSCJAP00000036331; -.
DR   Ensembl; ENSCJAT00000038370.5; ENSCJAP00000036331.4; ENSCJAG00000019547.5.
DR   GeneID; 100408689; -.
DR   KEGG; cjc:100408689; -.
DR   CTD; 25885; -.
DR   eggNOG; KOG0262; Eukaryota.
DR   GeneTree; ENSGT00920000149138; -.
DR   HOGENOM; CLU_000487_2_4_1; -.
DR   InParanoid; F7H346; -.
DR   TreeFam; TF103033; -.
DR   Proteomes; UP000008225; Chromosome 14.
DR   Bgee; ENSCJAG00000019547; Expressed in testis and 6 other cell types or tissues.
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; -; 2.
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:UP000008225};
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..1473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1482..1501
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..1448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1720 AA;  194379 MW;  DB5691A8FC519FE1 CRC64;
     MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRFLD SLGNPSANGL YDLALGPADS
     KEVCSTCAQD FNNCSGHLGH IELPLMVYNP LLFDKLYLLL RGSCLNCHML TCPRAVIHLL
     LCQLRVLEVG ALQAVYELER ILNRFLEENA DPSASEIQEE LEQYTTEIVQ NNLLGSQGSH
     VKNVCESRSK IIAFFWKTHM NPKRCPHCKT GRSVVRKEHN SKLTITFPAT VHRTAGQKDS
     EPLGIEEAQM GKRGYLTPTS AREHLFALWK NEGFFLNYLF SGVDNDGMES RFNPSVFFLD
     FLVVPPSRYR PVSRLGDQMF TNGQTVNLQA VMKDVVLIRK LLALMAQEQK LPGDVAVPLT
     DEGKDSLITI DRAFLSTIPG QSFIDKLYNI WIRLQSHVNI VFDSEMDKLM TDKYPGIRQI
     LEKKEGLFRK HMMGKRVDYA ARSVICPDMY INTNEIGIPM VFATKLTYPQ PVTPWNVQEL
     RQAVINGPNV HPGASMVINE DGSRTALSAV DVSQREAVAK QLLTPAMGAP KPQGTKIVCR
     HVKNGDILLL NRQPTLHRPS IQAHHARILP EEKVLRLHYA NCKAYNADFD GDEMNAHFPQ
     SELGRAEAYV LACTDQQYLV PKDGQPLAGL IQDHMVSGAS MTTRGCFFTR EQYMELVYRG
     LTDKLGRVKL FPPSILKPFP LWTGKQVVST LLINIIPEDH IPLNLTGKAK ITGKAWVKET
     PQSVPGFNPD SMCESQVIIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GEISGKVLTC
     LARLFTAYLQ LYRGFTLGVE DILVKLKADV KRQQIIEESI HCGLRAVRAA LNLPEAASYD
     EVREKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQFP ENSLQMMVQS
     GAKGSTVNTM QISCLLGQIE LEGRRPPLMA SGKSLPCFEP YEFTPRAGGF VTGRFLTGIK
     PPEFFFHCMA GREGLVDTAV KTSRSGYLQR CIIKHLEGLV VQYDLTVRDS DGSVVQFLYG
     EDGLDVPKTQ FLQPKQFPFL ASNYKAIMKS NHLHEVLSRA DPKKALRHFR AIKKWQSKHP
     NTLLRRGAFL NYSQKIQTAV KALNLESGNR NGRSLGTQEM LRMWYELDEH SRRKYQKKAA
     SCPDPSLSVW RPDIHFASVS ETFETKVDDY SQEWAAQTER SYEKSELSLD RLRTLLQLKW
     QRSLCEPGEA VGLLAAQSIG EPSTQMTLNT FHFAGRGEMN VTLGIPRLRE ILMVASANIK
     TPMMSVPVLN TKKALKRVKS LKKQLTRVCL GEVLQKIDVQ ESLCIEEKQN KFRVYQLRFQ
     FLPHACYQQE KCLRPEDILH FMETRFFKLL MESIRKKNNK ASAFRNVNTR RATQRDLDNA
     EESGRSRGEQ EGDEEEEGHI VDAEADEGDT DASDAKRKEK QEEEVDYESE EEEEKEGEEN
     DDEDTQEEGN AHGEGAQETQ EQDEEMASGA EEAPSLPALL TQPRKSTHSQ EPQGAEASKH
     RVQAVREIHS FIEDYQYDTE ESLWCQVTVK LPLMKINFDM SSLVVSLAHD AIVYTTKGIT
     RCLLNETTNS KNEKELVLNT EGINLPELFK YAEILDLHRL YSNDIHAMAN TYGIEAALRV
     IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIQSNSSPLQ QMTFETSFQF
     LKQATMLGSH DELRSPSACL VVGKVVKGGT GLFELKQPLR
//
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