ID A0A165FIC5_9APHY Unreviewed; 1704 AA.
AC A0A165FIC5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=LAESUDRAFT_570116 {ECO:0000313|EMBL:KZT09014.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT09014.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT09014.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT09014.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427613; KZT09014.1; -; Genomic_DNA.
DR STRING; 1314785.A0A165FIC5; -.
DR InParanoid; A0A165FIC5; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000076871; 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; 7.
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:UP000076871};
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 239..542
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1704 AA; 190429 MW; 336023F3AB0EE924 CRC64;
MLGHQFAYST APVRKVKEVQ FGILSPEEIK AYSVAKIEFP EVMDETTHKL KTGGLMDPCM
GTIDRNFKCL TCGEGMSECP GHFGHIELAR PVFHPGFIVK VKKILECICV NCGKLKSDST
FADKIRHARD PKVRMQVVWN YCKGKMVCET DEPREETDGL EPEEPKKGHG GCGAVQPLIR
KEGLKLFAQY KRSKDEDEEA KSQPDKRLFP PHEVYTALKK ISDSDLHILG LSDEYARPEW
MILTVLPVPP PPVRPSIAVD GGAMRSEDDL TYKLGDIIKA SANVRRCEQE GAPAHVITEF
EQLLQFHVAT YMDNDIAGIP QALQKSGRPV KAIRARLKGK EGRLRGNLMG KRVDFSARTV
ITGDPNLELD EVGVPKSIAM NLTYPERVTP YNIAYLQELV RNGPTAYPGA RYVVRDTGER
IDLRYNKRAD AFLQYGWIVE RHLKDGDFVL FNRQPSLHKM SMMSHRVKLM PYSTFRLNLS
VTPPYNADFD GDEMNMHVPQ SEETRAELSQ IAWVPRQIIS PQANKPVMGI VQDTLCGVRK
FTLRDTFLDW TQVQNILLWV PDWDGSVPIP AIIKPKPLWT GKQILSMCIP RGINIFRSPD
PKSSNPVFDD GMNIENGEII FGVVEKKTVG ASQGGLVHVC FREKGPEATR TLFTGLQQVV
NYWLFHNGFS IGIGDTIADR KTMEHIQEQI QIRKQNVAQA IDDAAHDRLK PAPGMTIRES
FESRVERELN LARDQNGQYA QKNLKEDNNV KQMVVAGSKG SFINISQMSV CVGQQIVEGR
RIPFGFRHRT LPHFTKDDFS PEARGFVENS YLRGLTPQEF FFHAMAGREG LIDTAVKTAE
TGYIQRRLVK ALEDVMVCYD GTVRNSLGDL IQFVYGEDGM DGAFIERQNI ETFALNNREF
EHNYRVDVTD PSGGFLPGVL QAGLDDSSLE LQAKLDEEFT QLVEDRRNLR EFIFRRQDPN
VPHYLPVNLQ RIVQNAIQIF HIDRRKPSDL EPSYIIDSVR ELVNRLVVVR GNSNISREAQ
ENATLMFRMH LRATFAARRV LEKFHLNREA FEWVLGEIEA KFNQSLAHPG EMCGTLAAQS
IGEPATQMTL NTFHYAGVSS KNVTLGVPRL KEIINVANNI KTPSLSVYLK PELAKDKDLA
HSVQQELAYT SLRTVTAAVE IWYDPDPSST IIEEDAVFVE SFFAIPDEEV EQKLHLQSPW
LLRLELDRAK MIDRKMTMSY VAGRIAESFK TDLFVIWSED NSEKLIIRCR VLGGADKDED
GMDTVEEDIF LRQLENTMLN SISLRGVPGI QRVFLLEHDK VFITEEGSIK AQQEKEWVLE
TDGVNLKTVM CIDGVDFTRT YSNSCVEVFN VLGIEAARAA IMKELRGVIE FDGSYVNYRH
LALLCDLMTH RGTLMAITRH GINRADTGAL MRSSFEETVE ILMEAAAVGE RDDCHGIAEN
VIFGQMAPMG TGAFDVALDI DMLKDVIVDH RLPVQSMMAA QVEGGMTPGQ VAMTPYDSNS
PMWSQDMSFK GETAAFSPLA VNGGEDAASF SYLAYGPSPM GAGSMSPAAP GYSPSSPNVY
SPTSPYVPPS PYGGATSPFG TSPYATSPFY DRGRGPTSPT YSPTSPALNL TSPGYSPTSP
RYSPTSPSFS PTSPRYSPQS PSFSPTSPRY SPTSPSFSPA SPRYSPTPAQ MSPSSPKYSP
TSPASPTSPK YCKLYIRRIA VHLY
//
