UniProt: X0J017

Database: UniProt
Entry: X0J017_FUSOX

LinkDB:  X0J017_FUSOX 
Original site:  X0J017_FUSOX

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (24)   
   InterPro (14)   
   Pfam (8)   
   PROSITE (1)   
   SMART (1)   
All databases (32)   

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ID   X0J017_FUSOX            Unreviewed;      1741 AA.
AC   X0J017;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=FOPG_00230 {ECO:0000313|EMBL:EXL89585.1};
OS   Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL89585.1};
RN   [1] {ECO:0000313|EMBL:EXL89585.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL89585.1};
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., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW808.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXL89585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL89585.1};
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   "The Genome Annotation of Fusarium oxysporum PHW808.";
RL   Submitted (MAY-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   -!- 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}.
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DR   EMBL; JH658799; EXL89585.1; -; Genomic_DNA.
DR   Proteomes; UP000030676; 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; 2.
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; 3.
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   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          243..549
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          154..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1524..1741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1555..1582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1596..1741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1741 AA;  191407 MW;  835A96A4C947A49E CRC64;
     MANLYFTHSS APLKTVEEIQ FGLMSPEEIK NMSVCHITYP ETMEENKTKP RDGGLNDPLL
     GSIDRQFRCK TCTQAMGECP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADDR
     DPEFVNAINT RDPKVRFNRV WEVCKKKRRC ENDEAKQKDD EFGTKTGPPR GHGGCGNMQP
     NVRQAALQLK AAFDEVTVDE DGQKSKKKET TPITPEMAHS ILRRITEDDL VNMGLNSDYA
     RPEWMVLTVL PVPPPPVRPS ISMDGTGTGM RNEDDLTYKL GDIIRANGNV KQAIREGSPQ
     HIARDFEELL QYHVATYMDN DIAGQPRALQ KSGRPVKAIR ARLKGKEGRL RGNLMGKRVD
     FSARTVITGD ANLSLHEVGV PRSIARTLTY PETVTPYNIG KLHQLVENGP NEHPGAKYVI
     RADGQRIDLR HHRRAGAISL EYGWKVERHL MTGDYIIFNR QPSLHKESMM GHRVRVMPYS
     TFRLNLSVTS PYNADFDGDE MNLHVPQSEE TRAEVKELCL VPLNIVSPQK NGPLMGIVQD
     SLAGAYKLCR RDVFLTKEQI MNCMLWVPNW DGVIPQPAIY KPRPRWTGKQ LISMVIPKEV
     SLFNGTDSGE NAPLKDEGLL IQAGQLMYGL LTKKNIGAAA GGIVHISYNE LGPEGAMAFL
     NGVQQVVTYW LLNNGHSIGI GDTIPDAATI AKVQVHIDEE KAEVARLTAM ATANELEALP
     GMNVRATFEN KVSMALNQAR DKAGTTTQKS LKDSNNAVTM ASSGSKGSSI NISQMTALVG
     QQIVEGKRIP FGFKYRTLPH FTKDDYSPEA RGFVENSYLR GLTPSEFFFH AMAGREGLID
     TAVKTAETGY IQRRLVKALE DLSARYDGTV RNSLGDIVQF LYGEDGLDAM IIEKQKLGIL
     NMSNSAFEKK YRLDLANPPD WFKHDYEFGN ELTGDKESME YLDQEWEKLL ADRRQVRQIN
     KAKGNEEMMQ LPLNITRIIE SAKRVFNVKA NDRSNLRPSE VIPAVQNLLD SMKIVRGTDE
     ISIEADANAS ILFKALLRSR LAFKEVVKEH RLNKLAFDHI LGELQNRWDR AFVNPGEMVG
     VLAAQSIGEP ATQMTLNTFH FAGVSSKNVT LGVPRLKEIL NLAKNIKTPS MAVYLNTPLA
     RQEQAKKLRS MVEYTNLRSV TSVTEIYYDP NITETNIPED VDMVESYYMI PDESVDPTAN
     QSRWLLRITL DRQKLLDKEI KIDDVAQRIK EEYPTDLAVI FSDNNADEQV IRIRTLQTGD
     KDEEGEGGME EDVMLKRLEA HLLDTLTLRG VPGIERAFLT KGTRLTEGPD GALLAIKDDP
     RCTQWYLDTS GTALRDVLAV DGVDATRTYT NDLYQIVEVF GIEAARAALA KELTNVLAFD
     GSYVNHRHIA LLVDVMTYRG SISAVTRHGI NRADTGALMR CSFEETVEIL LEAAATGELD
     DCRGISENVM LGQMAPMGTG NFDVLLDPKM LETVISDNSR MGLMAGMPTK GGDVEGAATP
     YDTGSPMADS GYLSLSSSAA GNFSPIQGAG SETPGGFTTV GGDHGFGGAS PYNRGAASPF
     SSTSPTSPFS YSPSSPNMGY SPTSPLIDGG GMSRYGPTSP SFSPSSPSFS PTSPMLRPTS
     PASPNYSPTS PSYSPTSPSS PRHYSPTSPA QFNSPTSPSY SPASPNYSPT SPNIHGAGPT
     SPSYSPASPS WSPTSPEAYS PTSPSFQRSP GAQQSPTSPS YSPTSPAFSP RTPGPGTSGN
     Q
//

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