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Database: UniProt
Entry: W9K1Z7_FUSOX
LinkDB: W9K1Z7_FUSOX
Original site: W9K1Z7_FUSOX 
ID   W9K1Z7_FUSOX            Unreviewed;      1658 AA.
AC   W9K1Z7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=FOZG_11394 {ECO:0000313|EMBL:EWZ35478.1};
OS   Fusarium oxysporum Fo47.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660027 {ECO:0000313|EMBL:EWZ35478.1};
RN   [1] {ECO:0000313|EMBL:EWZ35478.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ35478.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EWZ35478.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ35478.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2012) 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; JH717903; EWZ35478.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:FOZG_11394; -.
DR   HOGENOM; CLU_000487_2_4_1; -.
DR   Proteomes; UP000030766; 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; 1.10.357.120; -; 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; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
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   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          363..683
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          268..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1350..1431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..434
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1386..1416
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1658 AA;  182756 MW;  C636E558AC1258FC CRC64;
     MNIAQPVASG VESVEFTFLS PKEIRAISVK RIENPETFDN LLNPVPGGLY DPALGSWGDA
     PCTTCNLNQA TCPGHAGHIQ LPVPVYHPVF MDQAYRLLKA ACVYCKGFRL PQKELHKYVC
     QLKLLQHGLI QEAHVVGAIG DNELAIELGD FSELESEAEE EGGTNSIDNV TRARDKYVDK
     CLSGIKIKRG DTKRGKHEGS SEMRREIIKE FLAEITKRRV CASCGGISPS YRKDRFVKVF
     ERSLSDKDKA KMAQKNFKQA DAMARVHQAA TKQKPDGYSS DEGVADVASP TRETSRVNGD
     VTDQDTEMID ADTASTSSSP QRYISAMEVR ARLNELFTKE QELVSLLYNA KPPTRSSTNV
     TPDMFFLTTI LVPPNRYRPE ARTGESEISE AQQNSLYKNI LRGCGTIARL HRELQEEKAD
     VNRMHQASAE LQESVNALID KNKNPVQGAA AKRNEDGIKQ KLEKKEGLFR KNMMGKRVNY
     AARSVISPDP NIETNEIGVP PVFAKKLTYP EPVTSHNFRD MQQAVINGVD KWPGAFAIEN
     ENGQIVNLRN KSVDDRVSLA NQLLAPTSSN AARTRNKKVY RHLTNGDVVL MNRQPTLHKP
     SIMGHRVRVL PGEKTIRMHY ANCNTYNADF DGDEMNMHFP QNEVARAEAL QIADTDHQYL
     SGTAGKPLRG LIQDHISVSV ALCNRDTFFT KGDYQQLVYN ALRPESGHIV GERIELVAPA
     VIRPVARWTG KQVITTILKN MQPPNCGGLS MKAETQIKAS QWGVNSEEGT VVFQDGEFIA
     GILDKSQIGP SSGGVIHAVH EIYGPAVAGK LLSSLGRLLT RYLNMRAFSC GMDDLRLTPE
     GEQARREALV PADSVGLKVA SSYVSLEQDP GPRDPLLLER LEEVLRDDSK QEGLDLLMKE
     GLSKITDKIQ TATMPVGLEK AFPFNQMQAM TTSGAKGSRV NASLISCNLG QQVLEGRRVP
     IMVSGKSLPC FNPFETHARA GGYIVQRFLT GIRPQEYYFH HMAGREGLID TAVKTSRSGY
     LQRCVIKGME GLTVAYDTTV RDADGSMIQF LYGEDGLDVS KQKYLTDFSF ILENVTSEAS
     QLRYDPSVGD RLGMHRDAIT KYMKKALKHT NIKDPKAQDP ISGLFNPATT AFATSENFYK
     AMTSYIKENK DGLVRDKSDK NKLALSRVSL NKKNAEMLFA MKYLRSLVEP GEAVGIVAGQ
     SVGEPSTQMT LNTFHLAGHS AKNVTLGIPR LREILMTASD KISTPAMSIY PIEEMSVEDA
     EIFAKSISVL PLGFILDSIN VEEKFFDSEE YTKTYAINIS DVVEAVERKL LHRLLALVKK
     DIRKRMTMST MATPDVGAKA GVVETAAPNA EAAGNFDDDE DDEDGDDDAT NAKQRAKRSE
     AVSYGPNDDD DDAVQQEMER DAGDDDADED EDFGGSPQQA EGDGDGDDVD WSAKARTNRV
     LEQYAEVTDF SFDEKTGASC SFTLEYDSTI PKVLMLNLVQ DAVRKTVIQE ISGVGACTLV
     EEKDTKVIHT AGVNLQAMQR YSDFIDPNRI QTNDIAAVLA VYGVEAARQN IVQELAGVFG
     SHGIKVDNRH LNLIGDHMTR NGGFTPFNRM GLKGNVSPFT KMSFETTLAF LKDAVLDGDW
     DDLSTPSGRL VMGRLGKVGT GGFDVLAQLP TYHVDSLA
//
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