ID T0JU21_COLGC Unreviewed; 1703 AA.
AC T0JU21;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CGLO_17274 {ECO:0000313|EMBL:EQB44013.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB44013.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQB44013.1}.
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DR EMBL; AMYD01004125; EQB44013.1; -; Genomic_DNA.
DR STRING; 1237896.T0JU21; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_3_1; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000015530; 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; -; 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:UP000015530};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 369..693
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 256..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1465
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1703 AA; 188056 MW; 9B40887FD8F421A6 CRC64;
MNISQPISSS VETVEFTFLT EEEIRAVSVK RIENDSTFDN LLNPVPGGLY DPALGSWGDS
LCATCNLNQS SCPGHAGHIE LPVPVYHPIF LDQVLRLLRS QCAYCKGFRM RHREINRFSC
KLRLLQHGLL HEAHLVDAIG EELKGLAMPG VPTDYDSEAE EEGTSTVDNV IGAREAFVRQ
SLKAHKLSLG ELRKGKHEGS IEMRRELIKE FMVQITKPRK CDNCGGISPA YRKDRFVKIF
EKALSERDLA HMAQRSLHMK DSMATAATTS KSKTTRGSDH ADEGVADVDL APSEENDVEM
RDASSSDEHR PMDKGEEDAT NVSPGQQRYI SAMEVRARLR ELFEKEQEIM SLIYNSKPMT
KKAAKITADM FFLRTILVPP NKFRPEARTG DSISEAQQNS LYKNILRNCV SIARIHQNVG
GTDQYGRARD ISDLHQIWTE LQESVNSLID KSKNPVQGAA AKRNEDGIKQ KLEKKEGLFR
KNMMGKRVNF AARSVISPDP NIETNEIGVP PVFARKLTYP EPVTSHNFRD MQQAVINGVD
KWPGAAAIEY ENGQIVNLRS KSTDDRVSLA NQLLAPTNNQ MSGVKSKKVY RHLTNGDVVL
MNRQPTLHKP SIMGHRVRVL PGEKTIRMHY ANCNTYNADF DGDEMNMHFP QNEVARAEAL
QIADTDHQYL SGTAGKPLRG LIQDHLSVSV ALCNKDTFFD RDSYQQLIYS ALRPESGHIL
GERIELIPPA IIKPIPRWTG KQVVTTILKN IKPPNGEGLW MTGKSQVKGE QWGKGSEEGT
VLFQDGQFLS GILDKAQLGP SSGGLIHAIH EIYGPAVAGK LLSGIGRLLT RYLNMRAFTC
GMDDLRLTPQ GEVSRKETLK AAKGIGLEVA ARYVSLEDNK PGSDDPELLT RLEEVMRDDS
KQEGLDMLMN QSSAKVSSMV TAACLPVGLV KQFPKNQMQS MTTSGAKGGQ VNANLISCNL
GQQVLEGRRV PLMVSGKSLP CFRPFETDVR AGGYIVQRFL TGIRPQEYYF HHMAGREGLI
DTAVKTSRSG YLQRCIIKGM EGLTVSYDST VRDADGTLVQ FLYGEDGLDP TKQKYLTDFG
FVLRNIGSET AQLNFGSQFK DRFAGNKDDV LKHMKSAIKH AKVDIAAKDP IIALVNPARV
AFATSEKFYE KMSKYIKNNE DGLIRDKSKD LSGLINAPAV NRKSAELVLA AKYMRSLVEA
GEGVGIVAGQ SVGEPSTQMT LNTFHLAGHS AKNVTLGIPR LREILMTASR SISTPSMTLL
LHEELSATEG EIFAKSISVL PLADVLDTAS VNERIGKGQN SALAKLYDVR LNFFPSEEYT
KTYAIDASDV MDTVEKRFLD HLLKIMTKEI KKRRSESSSA TPDIGARAGV VEMATGNGET
RGGGDDNDDN DDDGDGDATN AKNKANREEA VSYGPNDDED DAIQRQMERE ESAEEDEGFG
GSPVPETRQE VSDEEEEAED DESESEGAWR AERVKERYLR VTRFSSDEAG EWCEFTLEFE
ADTPKVLMLN IVQAAVKKSV VQQIPGVGSC TFTADHKTTD PITGKDISVP AIYTSGANLR
AMHKYGDFIN PNKIATNDIA AVLDVYGVEA CRTNIVSELA GVFGGHGISV DNRHLNLIAD
YMTRNGDFTP FNRNGLRGNI SPFTKMSFET TLSFLKDAVL DGDWDDLRTP SSRIVMGRLG
RIGTGAFDVL TALPTHHMSS HAE
//
