ID J3KB81_COCIM Unreviewed; 1690 AA.
AC J3KB81;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CIMG_03378 {ECO:0000313|EMBL:EAS32354.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS32354.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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|RuleBase:RU004279}.
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DR EMBL; GG704916; EAS32354.3; -; Genomic_DNA.
DR RefSeq; XP_001243937.1; XM_001243936.2.
DR STRING; 246410.J3KB81; -.
DR GeneID; 4564172; -.
DR KEGG; cim:CIMG_03378; -.
DR VEuPathDB; FungiDB:CIMG_03378; -.
DR InParanoid; J3KB81; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; 1.10.150.390; -; 1.
DR Gene3D; 1.10.357.120; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 2.
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:UP000001261};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 373..700
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 142..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1690 AA; 188743 MW; 9A7BC60565DEE467 CRC64;
MASFTRPVSS TISGVDFEVL SDNEIKSVSV KRIHNTPTLD SFNNPVPGGL YDPALGAWGD
HVCTTCRLNA WSCAGHSGHI ELPVQVYNVT FFDQLFRLLK AQCIYCHRFR MSKIQINTYV
CKLRLLQYGL VEEASTIGTM ELRKGKHNKE DGESDSSEDE DEEDLIDRRN AYVQKCISGL
ASYKTRQNYM KMAKNPAAAE MRRNLVRDFL KDVASVKKCA SCSGISPPYR RDRYSKIFRK
SLPQKAKAAM VAAGFQIPNP LVLMEEANRL SKKHKTIQKE DSVNGIIDDG NISVITETHG
AEQQVSMGNA VLAAVEDTGS SEIGGQLDDS QQYIPSSEVY ASVRFLFEKE QEILDLVYDS
RPGSGRRSHV NADMFFIKNL LVPPNKYRPA AQQGPGQIME AQQNTSFTRI LKLCDQINQI
SRERQGDNGE SISRIRSYRD LLHAIVQLQD AVNSLIDRDR NPAQGAAGIQ NEDGIKQRLE
KKDGLFRKNM MGKRVNFAAR SVISPDPNIE TNEIGIPLVF AKKLTYPEPV TNHNYWELKQ
AVINGPDIYP GAAAVENELG QVVNLKFKSV DERIAIANML LSPSNWKLKR SRNKKVYRHL
TTGDVVLMNR QPTLHKPSIM GHRARVLTGE RTIRMHYANC NTYNADFDGD EMNLHFPQNE
IARAEAMQLA DTDHQYLVAT SGKPLRGLIQ DHISMGTWFT SRDSLFDEED YHQLLYSCLR
PENSHTVSEK IELMPPTILK PKPRWTGKQI ISTILKNITP ENRAGLNLIG KSSTPGDRWE
IGSEEGKVIV KDGELLCGIL DKAQLGPSAG GLIHSVHEVF GHVVAGKLIG ILGRLLTRFL
QMRAFTCGMD DLRLTKKGDE ERKKQLKRGD NLGHEVALQY VTLDESPVED KETELQRRLE
DVLRDDEKQA GLDSMFNSRT AGLSSDITAA CLPSGLEKPF PWNQMQAMTV SGAKGSVVNA
NLISCNLGQQ VLEGRRVPVM ISGKTLPSFK PFETKLVAGG YVSGRFLTGI KPQEYYFHAM
AGREGLIDTA VKTSRSGYLQ RCLIKGMEGL KAEYDNSVRD TTDGTLVQFL YGEDGLDITK
QKHLQDFSFL AQNYLSILSQ VNGMDEFNKV NSEVAAKWNK SAIKKVKKTG QVDAKDPVLA
HYHPGANFGS TSESFATALK EYEKKNPDKL LKDKGQGIDG ISKKDFEHIM NMKYMRSVVD
PGEAVGIVAG QSIGEPSTQM TLNTFHLAGH SAKNVTLGIP RLREIVMTAS TQILTPTMSA
NFYEQVSTKD RELFAKGISR LTLAEVVDKL SVHERISNRG NVKAKVYDIH INFFPAEEYT
QEYAIKVQDV LETLEKRFVP KLVKLTRAEL KKRTSEKSLS DFSAAQPEIG ASVGVVEEGP
RNTEGREAAN DDDEDEDQDD AKRARSSQNR SNQVSYEAPD EDDQDIIRRQ DSSELDSEDE
DESSENKENR PASGDEDVEM KDASDVEDED KEREESIRDK HAEVTRFKFD PKKGTSCIIQ
LQYDVSTPKL LLLPLVENAT RAAVIQFIPG LGSCTYVPEE RDTPAHVLTD GVNLLAMRDY
QHIINMHTLY SNSIHHMLTL YGVEAARASI VREMDSVFKS HSIAVDNRHL NLIGDVMTQS
GGFRPFNRMG IVKDSTSPFM KMSFETTVRF LRDAVLERDW DNLAAPSSRI VMGRVSTVGT
GSFDVLAPVG
//
