ID A0A2H3ID56_9EURO Unreviewed; 1686 AA.
AC A0A2H3ID56;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PENO1_048580 {ECO:0000313|EMBL:PCH00290.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH00290.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH00290.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH00290.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCH00290.1}.
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DR EMBL; NPFK01000122; PCH00290.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3ID56; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000218381; 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; -; 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; 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; 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:UP000218381};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 355..679
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1360..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 188315 MW; 57D350F815E64EF3 CRC64;
MSSFARPVAS ELASVDFSVY TSEDIKKISV KRIFNTPSLD SLHNPIPNSL YDPALGAWGD
HVCTTCRASS WSCPGHPGHI ELPVPVWNVT FFDQVYRLLR AKCDYCHRFR IARIEIHAYT
CKLRLLQYGL VDQTANIDLI GEDPQDAAVD ADEKGNIDSQ TKMELRNKFV KKCIREAQKQ
GDSDAFFGGA KNPVAAEQRK ELIKEFFHAV AKSPQKPCTN CHYTSPGYRK DRYSKIFRKA
LSPKASIGNS MAGMTAPNPV IVLQEDKKLL NKFKEQGKQN GVAVGDVSEL HGAEEEVVRA
NAAIDQGSLP GEKTGGQQFV SAPEVHAAIC LLFEKEREIL NLVYSSRRGI KINPEMMFVR
NILVPPNRFR PPAQQGGQIM EAQQNTPFTQ ILKTCDLINM ISHSRQTAET DGARMREYRD
LLQAIVTLQE QVNSLIDSDR GPGGMAAARA ANGVKQLLEK KEGLFRKNMM GKRVNYAARS
VISPDPSLET HEVGVPMVFA KKLTFPEPVT SFNFHELREA VINGPDKYPG AAAIENESGQ
VVNLKFKNLE ERTALANQLL APSHAKMKGN RNKKVYRHLT TGDYVVMNRQ PTLHKPSMMG
HRARVLPNER VLRLPYPNTN SYNADYDGDE MNMHFPQNTL ARSELLMITD ADRQYISSTD
GKPLRGLIQD HITVSTFLTS RDTFFEEEEY HQLLYSCLRP ENANTVTDRI QLMEPAFIRP
RRLWTGKQVI STVLKNIMPP NRRGLNLQGK SSTPGDRWGK GNEEDKVIFK DGELLCGVLD
KKQIGASGGG FIDAVHEIYG NTVAGSLLSI LGRLLTRYLN MRAFSCGIED LRLTPEGDRK
RVEILKKATE LGKNVSLKYV TLDQNPVADQ DAELKRRLED VLRDDQKQSG LDSVYNSQTR
KLTSDITAGC LPHGLIKQFP WNQMQLMTTT GAKGSSVNAN LISCNLGQQV LEGRRVPVMV
SGKTLPSYRA FETHPQAGGY VCGRFLTGIK PQEYFFHTMA GREGLIDTAV KTAKSGYLQR
CMIKGMEAVK VEYDSSVRDT ANGGAVIQFI YGEDGLDVGK QVHLQNFSFL AQNYVSTMAQ
LNMSMDYHML EKPEVTQWHK DAMKQVKRTG RIDAKDPALA IYQPGGHFGS VSEAFSQALK
KYEDSNPDKL LKDKKAGIAG ALSKKAFESV MHMKYLNSVI DPGDAVGIVA GQSIGSQTTQ
MTLNTFHLAG HSAKNVTLGV PRLREIVMTA SKKPMTPTMT VEVIEELSEE KGQSFAKGIS
RLSIAEVIDT LQVRESITDI KGKKYKIYDI EMKFFDAKEY EEEYAITKRD LVRAIQDDFL
PIFMKKMSNE EERRRDEQNL SAFSAAQPEI GVSIGTTERF EGAARETQAS GAGNDDDDSD
NEDDEEDAKR AQSKQNRDNQ VSYEAPDEDE DMIRKEQDES DMEDDDDEDD ENKKGQEQTA
DEESDSSDDE DEMTEEVKLA RTDVAERTKE ILGKWPQINA FKFNALEGNS CFIRLHYDIE
TPKLLVLPLV EDSARRAVIQ AVKDIGACLY TPADPENKEP AKIDIQGVNL LAMRDYQEYI
NPHTIRTNSI HDTLIYYGVE AARSTIIREM SDVFSGHSIT VDNRHLNLIG DVMTHSGGFK
SYSRNGLIRD SNSPFSKSSF ETSVGFMRDA VLERDFDDLK SPSSRIVVGR LGNVGTGAFD
ILAPVA
//
