ID Q2HDK0_CHAGB Unreviewed; 1756 AA.
AC Q2HDK0;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CHGG_01704 {ECO:0000313|EMBL:EAQ93469.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ93469.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CH408029; EAQ93469.1; -; Genomic_DNA.
DR RefSeq; XP_001220925.1; XM_001220924.1.
DR STRING; 306901.Q2HDK0; -.
DR GeneID; 4387514; -.
DR VEuPathDB; FungiDB:CHGG_01704; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; Q2HDK0; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 4.10.860.120; RNA polymerase II, clamp domain; 2.
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; 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; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
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:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
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; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 242..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 690..717
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1604..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 194660 MW; 7B926D424592F284 CRC64;
MANLIFTHSS APIRTIKEIQ FGLLSPEEIK GMSVCHIVYP ETMDESRTKP RDGGLNDPLL
GSVDRQFKCK TCTENMTECP GHFGHIELSR PVFHPGFIRR VKKLLEMVCH NCSKVLADRE
DEQYAAAMRI RDPKVRFKRV WDICKSKKRC ENEVRKGKDG EFKPDSENQA AEGGHGGCGN
TQPVIRQQAL TLWGSVETKD EDGVKTKEKK VITPEMALNI FRRMSDDEMI DIGLNISQAR
PEWMIITVLP VPPPPVRPSI SMDGTGTGLR NEDDLTYKLG DIIRANGNVR QAIAEGSPQH
IITDFENLLQ YHVATYMDND IAGQPQALQK SGRPVKAIRA RLKGKEGRLR GNLMGKRVDF
SARTVITGDA NISLDEVGVP RSIARTLTYP ETVTPYNIAK LTKYVQNGPT EHPGARFVVR
SDGTRIDLRH SRRATGIQLE YGWKVERHLL DGDYIIFNRQ PSLHKESMMG HRVRVMPYST
FRLNLSVTSP YNADFDGDEM NLHVPQTEET RAEVKELCMV PLNIVSPQRN GPLMGIVQDT
LAGVYKLCRR DVFLTKEEVM NIMLWVPDWD GIIPLPAIFK PRPRWTGKQI ISMVIPNIIN
IHMPSDQPDR DHPFKDDGLL IQQGELMFGL LMKKSVGAAG GGIVHLCYNE LGPYGAMDFL
NGCQRVVNYW LLHNGHSIGI GDTIPDTITI ELIQKHINDE KEEVRRLTQA ATNNQLEALP
GMNIRETFEN KVSTALNKAR DKAGTSTEKS LKDLNNAVTM ARSGSKGSAI NISQMTALVG
QQIVEGKRIP FGFKYRTLPH FTKDDYSPEA RGFVENSYLR GLTPSEFFFH AMAGREGLID
TAVKTAETGY IQRRLVKALE DAEARYDGTV RNSLGDIIQF VYGEDGLDGI AIEKQRVDHM
NMSNHNFDKR FRLDVMDEAT SVAALESLEY GREMISDPAV QELLDQEYEQ LMADRELVRS
INRRKQAEDQ MQLPLNIARI IETAKKLFKV DDSQRSDLTP NDVIPVVKAL LERMIVVRGS
DPISKEADYN STILFKIQLR SRLAYKRLAV EQRINKLAFE HILGELENRW SRSMVAPGEM
VGVLAAQSIG EPATQMTLNT FHFAGVSSKN VTLGVPRLKE ILNVAKDIKT PSMVVYLDSE
NATQEDAKRM RNAVEHTSLR SVTAVTEIYY DPEVTATNIP EDFDMVESYF LIPDSSDQDS
IENQSRWLLR LTLDRQKMLD KGLRVEDVAQ RIKEEYKKDV AVIFSDNNAE EMIIRIRVIR
QDDDKDEDGN KIIEDDVMLK RLEKHLLDNC TLRGVPGIER AFLNKGTRLV VMPDGSQVAN
KDTPECMEWY LDTQGTTLRD VLTIDGVDTK RTSTNDLYQI VDVFGIEAAR SALMQELTQV
LAFDGSYVNH RHLALLVDVM TYRGSIAAVT RHGINRADTG ALMRCSFEET VEILLEAAAV
GELDDCRGIS ENVMLGQMAP MGTGHFDVLL DPKMLETVIS DNSRMGLMPN MTIKGGQLEG
AATPYDTGSP MADNGHLGSY SPTMGNFSPI QGAGSDSPNG FGTEYGGGFG SSTVNPYATS
PRATSPFSTS PTSPFSYGGG YSPTSPAGYS PTSPLLDAGG RYASSPQFSP SSPSFSPTSP
MLRPGSPTSP NYSPTSPSYS PASPAATRHY SPTSPQQFNS PTSPSYSPTS PSYSPASPNL
HATSPSYSPA SPTWSPTSPD AYSPTSPSFH RSPGQQMSPT SPGYSPTSPS FSPRTPGRGP
SGGSGDQYSP TSPTNE
//
