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Database: UniProt
Entry: A0A2H3JHK1_WOLCO
LinkDB: A0A2H3JHK1_WOLCO
Original site: A0A2H3JHK1_WOLCO 
ID   A0A2H3JHK1_WOLCO        Unreviewed;      1408 AA.
AC   A0A2H3JHK1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=WOLCODRAFT_163287 {ECO:0000313|EMBL:PCH41652.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH41652.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH41652.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH41652.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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|RuleBase:RU004279}.
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DR   EMBL; KB468113; PCH41652.1; -; Genomic_DNA.
DR   STRING; 742152.A0A2H3JHK1; -.
DR   OMA; AVCPPYN; -.
DR   OrthoDB; 169836at2759; -.
DR   Proteomes; UP000218811; 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: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; cd02736; RNAP_III_Rpc1_C; 1.
DR   CDD; cd02583; RNAP_III_RPC1_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; 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; 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; IPR035698; RNAP_III_Rpc1_C.
DR   InterPro; IPR035697; RNAP_III_RPC1_N.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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:UP000218811};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          244..546
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1408 AA;  156781 MW;  B3437AE305013322 CRC64;
     MKESVSHQAP KVIKKLQFSL FTNQDAVKVS EFEVTHRDLY TAVDRHPVKN GVLDRRLGTT
     EKSAFCETCG LSSVDCVGHY AYIKLAVPVF HIGYFKHTIS ILQCICKTCA RVLLEEPERR
     TYLKRFRRPN LENIQRQALC KAVNTLARKM VYCPYCAATN GTVKKAGALK IIHDKFRAKK
     TAEEMEKWKM TFAPAVEAQK ELGMYISKAV HEDLNPLKVL NLFKRISDED CELLGLRPTY
     GRPEEYIWQY ISVPPVCIRP SVAQDGASNE DDLTVKLTEI VFTNALIKQG LAKGAPTAQF
     MEQWDFLQIS VAMYINSELP GVPPQMGQKP IRGFCQRLKG KQGRFRGNLS GKRVDFSGRT
     VISPDPNLRI DEVAVPERVA KILTYPERVT SHNIEMLKKA VRNGTDVHPG ANYVTAGSSG
     FKKFLKFGHK EAIADSLRIG DIVERHIIDG DIVLFNRQPS LHKLSIMCHR VKVRPWRSFR
     LNECVCGPYN ADFDGDEMNL HVPQTEEART EALELMSVKH NLVTPRNGEP VIAAIQDFIT
     ASFLLSRKDR FFDRRQFTQI CSYFGDADLQ IDIPPPTIWK PVRLWTGKQI FNVLMRPNKT
     YKVFVNVESK CNKQEKPDPK QYPRMNPALD LSPNDGWLVI VNSEIMCGVM DKATVGSGKK
     KSVFGIIMRD YGPHEAAAAM NRLAKLCARW LANYGFSLGI NDVIPGPKLS LEKNNLVETA
     YAECQDLIMR AKKGLLENKP GCDQEQTLEA MISGVLSKVR DKVGEICLKE LSRHNAPLIM
     ATCGSKGSVI NVAQMVACVG QQIIAGHRVP DGFQDRSLPH FPKKSREPPS KGFVRNSFYT
     GLSPTEFLFH AISGREGLVD TAVKTAETGY MQRRLMKALE DLVTHYDSSV RNAVGGVVQF
     RYGDDGLDPA CLEGDAQPVE FLRAWSHASS IGSRHTRGLL PFEIMELVDS ELSQRKFTSE
     CTAAYLATIR GFISEHVAQK LAGIRKNHGM FDAIERDDEW DAETDLTLGA SGKWLAYADK
     AVVDNKLKVT EDQLRAFLEI CWTKYVKAKI EPGSTVGAVG AQSIGEPGTQ MTLKTFHFAG
     VASMNVTLGV PRIKEIINAA KSISTPIISC KLVTADSEAS ARIVKGRLEK THLGDVAAVL
     EEAWAPEYTY IGIIVDMKTI QDLQLELTLD DIKWGIVAAK KLKIKQESIT VIPRKNRLRV
     YVDGPDKYYR LRELKRALPD VVVKGVSTIR RAIINIKTDD DHRGKKGDKE LLVEGYGLQK
     VMVTQGIVGE QTTSNHIIEV AQVLGIEAAR RTIINEIQYT MASHGMSIDP RHVMLLGDVM
     SYKGEVLGIT RFGVAKMKDS VLMLASFEKT TDHLFDASAY GKTDSIAGVS ESIIMGNPAA
     MTGTSMPALV TPAPPIGKPR KLLFEGAL
//
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