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Database: UniProt
Entry: L8WR47_THACA
LinkDB: L8WR47_THACA
Original site: L8WR47_THACA 
ID   L8WR47_THACA            Unreviewed;      1531 AA.
AC   L8WR47;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=AG1IA_06747 {ECO:0000313|EMBL:ELU39223.1};
OS   Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS   (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU39223.1, ECO:0000313|Proteomes:UP000011668};
RN   [1] {ECO:0000313|EMBL:ELU39223.1, ECO:0000313|Proteomes:UP000011668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX   PubMed=23361014; DOI=10.1038/ncomms2427;
RA   Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA   Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA   Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA   Wang L., Liu H., Li P.;
RT   "The evolution and pathogenic mechanisms of the rice sheath blight
RT   pathogen.";
RL   Nat. Commun. 4:1424-1424(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   -!- 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}.
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:ELU39223.1}.
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DR   EMBL; AFRT01001873; ELU39223.1; -; Genomic_DNA.
DR   STRING; 983506.L8WR47; -.
DR   HOGENOM; CLU_000487_1_1_1; -.
DR   OMA; MVQYDRT; -.
DR   Proteomes; UP000011668; 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; 1.
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   Pfam; PF05001; RNA_pol_Rpb1_R; 6.
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; 2.
PE   3: Inferred from homology;
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:UP000011668};
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          121..424
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1478..1522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1531 AA;  170833 MW;  584989528E841A23 CRC64;
     MQNDTQFAEK IRHVRDPKKR MALVWAHCKG KMICEADETK DDEGAAAQPA KVGHGGCGHV
     QPLIRKEGLK LFLVYKKGRD GRTSQPEKRL YPASDVYNTL KKIPDSDLAL LGLSEEFARP
     DWMILTVLPV PPPPVRPSIS ADGGTVRSED DLTYKLGDIL KASINVRRCE EEGSPAHVIS
     EFEQLLQFHV ATYMDNDIAG IPQALQKSGR PVKAIRARLK GKEGRLRGNL MGKRVDFSAR
     TVITGDPNLM LDEVGVPRSM AMNLTYPERV TPYNIEWLQM LVRNGPREYP GARYVVRDSG
     ERIDLRYNKR ADTSLQYGWI VERHLKNGDY VLFNRQPSLH KMSMMSHRVK IMPYSTFRLN
     LSVTPPYNAD FDGDEMNMHI PQSEETRAEL SQIAWVPRQI ISPQANKPVM GIVQDTLCGI
     RKITLRDNFL DWNFVQNILL WVPEWDGQVP VPTILKPKPL WTGKQILSLC IPSGINVFRA
     PDKDKRTNRV PANPANDDGI CIENGEILYG VVEKKTVGAS QAGLIHITFR EKGPEITRDL
     FTSLQKVVNF WLLHNGFSIG IGDTIADKDT MSKITIHIET AKNNVLQLIQ KAQYDGLRAE
     PGMTIRESFE SHVNRELNMA RDKTGKDAQD SLKNDNNVKQ MVVAGSKGSF INISQMSGCV
     GQQSVEGKRI PFGFKHRTLP HFNKDDYCAE SRGFVENSYL RGLTPQEFFF HAMAGREGLI
     DTAVKTAETG YIQRRLVKAM EDIAVCYDGT VRNSLGDIVQ FAYGEDGMDG AFIERQSVEP
     YRLSNRAFER KYRVDVLEAG SGFSPGTLQV GLDASSPELQ YKLDNEYAQL VKDRKMLREF
     IFKTADPNQP HYLPVNLRRV IQNAQQIFHI DRRKPSDLEP AYIMDEVAGL SSRLIVVRGE
     DPISLEAQDN ATMLFNMHLR STFATRPVLE ELRLTKQAFD WIIGEVETKF NASIVNPGEM
     CGTLAAQSIG EPATQMTLNT FHYAGVSSKN VTLGVPRLKE IINVATNIKT PSLTVYLQSE
     YASSKHKAKT IQTELAHTTL RTITATTEIV YDPDPTNTII DEDRDFVETF FAIPDESVER
     TLSQQSPWVL RIQLDRAKVL DKKLDMAYIA DRIEQAFYPD MKVIPSDDNA EKLILRCRPI
     VMQDKDEEAF ENTEEDIFIR QIEHNMLDSV TLRGVKGIRR VFMVEHDKPM IDAAGELQPR
     SAKEWVLETD GVNLKSVLSV DGIDFTRTYS NKCPEVFEVL GIEAARAAIL RELRNVIEFD
     GSYVNYRHLA LLTDLMTNRG TLMAITRHGI NRADTGALMR CSFEETVEIL MEAAAVGEKD
     DCYGVAENVL FGQMAPMGTG SFDVALDVDM LKDVIVDSRL PIQNMMAAQM GGGATPAGGL
     AMTPYDSASP MQAEAWRTEG AAFSPLATNA DEASGGFSFI PFGQSPMGPD SRFGGYSPSS
     PGYSPTSPFM PTSPMVAATS PYGASPFGAT SPYATSPAYS PTSPNMNLTS PQYSPTSPQY
     SPTSPTYSPT SPTYSPTSPR YYSTCEYLAR G
//
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