ID L2FR02_COLFN Unreviewed; 1704 AA.
AC L2FR02;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=RPA190 {ECO:0000313|EMBL:KAF4482141.1};
GN ORFNames=CGGC5_11146 {ECO:0000313|EMBL:ELA28158.1}, CGGC5_v008956
GN {ECO:0000313|EMBL:KAF4482141.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA28158.1};
RN [1] {ECO:0000313|EMBL:ELA28158.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA28158.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF4482141.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4482141.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4482141.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4482141.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P., Shirasu K.;
RT "Genome sequencing and assembly of multiple isolates from the
RT Colletotrichum gloeosporioides species complex.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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; KB020943; ELA28158.1; -; Genomic_DNA.
DR EMBL; ANPB02000005; KAF4482141.1; -; Genomic_DNA.
DR RefSeq; XP_007282763.1; XM_007282701.1.
DR STRING; 1213859.L2FR02; -.
DR EnsemblFungi; ELA28158; ELA28158; CGGC5_11146.
DR HOGENOM; CLU_000487_2_4_1; -.
DR InParanoid; L2FR02; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000011096; 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:UP000011096};
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 255..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Polar residues"
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..1466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1704 AA; 188100 MW; 55F1869B3901C05D CRC64;
MNISQPISSS VETVEFTFLT EEEIRAVSVK RIENDSTFDN LLNPVPGGLY DPALGSWGDA
LCATCNLNQS SCPGHAGHIE LPVPVYHPIF LDQVLRLLRS QCAYCKGFRM RHRESNRFSC
KLRLLQHGLL HEAHLVDAIG EELKSLAMPG VPTDYDSEAE EEGTSTVDNV IGAREAFVRQ
SLKAHKLSLG EVSKGKHEGS IEMRRELIKE FMVQITKPRK CDNCGGISPA YRKDRFVKIF
EKALSERDLA HMAQRNLHMK DSMATTAMTS KSKTTRGSDH ADEGVADVDL ASSEENDVEM
RDASSSDEHR PMDKGDEDAT NVSPGQQRYI SAMEVRARLR ELFEKEQEIM SLIYNSKPVT
KKVAKITADM 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 CLYGEDGLDP TKQKYLTDFG
FVLRNIGSET AQLNFGSEFK DRFAGNKDDV LKHMKSAIKH AKVDIAAKDP IISLVNPARV
AFATSEQFYE KMSQYIKNNE DGLIRDKSKD VSGLINAPAV NRKSAELVLA AKYMRSLVEA
GEGVGIVAGQ SVGEPSTQMT LNTFHLAGHS AKNVTLGIPR LREILMTASR SISTPSMTLL
LHEELSATEG EIFAKSISVL PLADVLDTAS VNERIGKGQN SALAKLYDVR LNFFPSEEYT
KTYAIDASDV MDTVEKRFLD HLLKTMTKEI KKRRSESNSA TPDIGAKAGV VEMATGNGET
RGGGDDNDDD DDDGDGDATN AKNKANREEA VSYGPNDDED DAIQRQMERE ESVEEDEGFG
GSPVPETRQE ASDEEEEEAE DDESESEGAW RAERVKERYL RVTRFSSDEA GEWCEFTLEF
EADTPKVLML NIVQAAVKKS VIQQIPGVGS CTFTADHKTT DPITGKDISV PAIYTSGANL
RAMQKYGDFI NPNKIATNDI AAVLDVYGVE ACRTNIVSEL AGVFGGHGIS VDNRHLNLIA
DYMTRNGDFT PFNRNGLRGN ISPFTKMSFE TTLSFLKDAV LDGDWDDLRT PSSRIVMGRL
GRIGTGAFDV LTALPTHHMS SHAE
//
