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Database: UniProt
Entry: Q0MVS8_9EURO
LinkDB: Q0MVS8_9EURO
Original site: Q0MVS8_9EURO 
ID   Q0MVS8_9EURO            Unreviewed;      1007 AA.
AC   Q0MVS8;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE   Flags: Fragment;
GN   Name=RPB1 {ECO:0000313|EMBL:ABH09098.1};
OS   Pyrenula reebiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Pyrenulales; Pyrenulaceae; Pyrenula.
OX   NCBI_TaxID=1776377 {ECO:0000313|EMBL:ABH09098.1};
RN   [1] {ECO:0000313|EMBL:ABH09098.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AFTOL-ID 387 {ECO:0000313|EMBL:ABH09098.1};
RX   PubMed=17051209; DOI=10.1038/nature05110;
RA   James T.Y., Kauff F., Schoch C.L., Matheny P.B., Hofstetter V., Cox C.J.,
RA   Celio G., Gueidan C., Fraker E., Miadlikowska J., Lumbsch H.T., Rauhut A.,
RA   Reeb V., Arnold A.E., Amtoft A., Stajich J.E., Hosaka K., Sung G.H.,
RA   Johnson D., O'Rourke B., Crockett M., Binder M., Curtis J.M., Slot J.C.,
RA   Wang Z., Wilson A.W., Schussler A., Longcore J.E., O'Donnell K.,
RA   Mozley-Standridge S., Porter D., Letcher P.M., Powell M.J., Taylor J.W.,
RA   White M.M., Griffith G.W., Davies D.R., Humber R.A., Morton J.B.,
RA   Sugiyama J., Rossman A.Y., Rogers J.D., Pfister D.H., Hewitt D., Hansen K.,
RA   Hambleton S., Shoemaker R.A., Kohlmeyer J., Volkmann-Kohlmeyer B.,
RA   Spotts R.A., Serdani M., Crous P.W., Hughes K.W., Matsuura K., Langer E.,
RA   Langer G., Untereiner W.A., Lucking R., Budel B., Geiser D.M., Aptroot A.,
RA   Diederich P., Schmitt I., Schultz M., Yahr R., Hibbett D.S., Lutzoni F.,
RA   McLaughlin D.J., Spatafora J.W., Vilgalys R.;
RT   "Reconstructing the early evolution of Fungi using a six-gene phylogeny.";
RL   Nature 443:818-822(2006).
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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; DQ840558; ABH09098.1; -; Genomic_DNA.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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; cd02733; RNAP_II_RPB1_N; 1.
DR   Gene3D; 1.10.132.30; -; 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; IPR007075; RNA_pol_Rpb1_6.
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   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};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          159..467
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          71..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          613..640
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        71..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABH09098.1"
FT   NON_TER         1007
FT                   /evidence="ECO:0000313|EMBL:ABH09098.1"
SQ   SEQUENCE   1007 AA;  113173 MW;  556E7D3A9E23472A CRC64;
     HIELAVPVYH HGFLKMVKKI LETVCHNCGK VKAIDVSGEE LRLAKAIPNK RTRFEKVWQL
     SKKHRICEAD ISEEGDQEFS KEKGPPRPKH GGCGNAQPEI RLSGLNLMTS WKPTKDGDNE
     PVQAETRPLT PPTALNILRL MNDEEMEEIG LDTKNARPEW MILSVLPVPP PPVRPSISMD
     GSGQGARGED DLTFKLGDIV RANQNVRRVQ QEGSPEHILN EHVQLLQWHV ATYMNNDIAG
     MDGLKAQHKT GRPIKSIRAR LKGKDGRLRQ NLMGKRVDFS ARTVITGDPN LSLDEVGVPR
     SIARNLTYPE VVTPFNVDKL KRLVANGPTE HPGARFVVRD DGTRIDLRHH KRTSELTLQF
     GWKVERHISH GDIILFNRQP SLXXXXXXXX RVRVMPYSTF RLNLSVTTPY NADFDGDEMN
     LHVPQSEEAR AELANLCMVP LNIVSPQRNG PLMGIVQDTL CGIYKICRRD VFLSREQVMN
     TMLWVPDWDG VIPQPAVLKP RPRWTGKQVI SMVLPPNLNL VRIDKDSGEE YERFSPLADG
     GLFVDRGELM FGLFNKKSVG TSAGGIIHTV FNEFGPETAM AFFNGAQTVV NYWLLHYGFS
     IGIGDTVPDN ATVESIKEQV NQRKSEVESI TQKAQNQELE AQPGMNVRET FESKVAKALN
     DARDGAGGAT ESSLKDLNNA IQMARAGSKG STINIAQMTA IVGQQSVEGK RIPFGFKYRT
     LPHFAKDDYS AQSRGFVENS YLRGLTPSEF FFHAMAGREG LIDTAVKTAE TGYIQRRLVK
     ALEETTVRYD NTVRDARGNV VQFIYGEDGL DGAHIENQRV DVITMSDEAF NKRYRVDLME
     KAPQFPKGRL ETDFRADVER QQLLDEEYDQ LREDRAFLRS FRKGSDEMMQ LPLNILRIID
     QAKTTFKVDA TQTCNLDPKH VIPEVQRLLR ELVVVRGDDT ISDEAQTNAT LLFKAQLRSR
     LAFKRLVNEN RLSTVAFNHV IGNVKSRWVK AQAQPGEMVG VLAAQSI
//
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