ID A0A093XFT2_TALMA Unreviewed; 1689 AA.
AC A0A093XFT2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=GQ26_0311030 {ECO:0000313|EMBL:KFX44053.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX44053.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX44053.1}.
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DR EMBL; JPOX01000031; KFX44053.1; -; Genomic_DNA.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_4_1; -.
DR Proteomes; UP000029285; 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; -; 2.
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 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 1365..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1689 AA; 188720 MW; 6FCD5805DD0810A9 CRC64;
MASFARPVAS ELASVDFSVY SSEDIKKISV KRIFNTPSLD SLHNPIPHSL YDPALGAWGD
HVCTTCRASS WSCPGHPGHI ELPVPVWNVT FFDQVYRLLR AKCDYCHRLR MPRIEINAFA
CKLRLLQYGL VDQTAKIDMI GEDAQDAAVD ADEKGNVDPQ TKMELRNKFV KKCIREAQKQ
GDGDALFGGA KNPVSAEQRR ELIKEFFKEA AKNPQKPCAN CHYTSPGYRK DRYAKIFRKA
MTTKALVANQ MAGMSAPNPV IVLQEEKRLL NKTKEQDKQN GTAIGDVAEL HGAEEEVVRA
NAAIDQGSLA GGQVGGQQFV SAPEVHAAIC LLFEKEREIL NLVYSSRLGF KINPDMMFVR
NILVPPNRFR PPAQQGGQIM EAQQNTPFTQ ILKTCDLINT ISHSRQTAET DGARMREYRD
LLQAIVTLQE QVNSLIDSDR GPGGMAAARA ANGIKQILEK KEGLFRKNMM GKRVNYAARS
VISPDPSLET HEVGVPMVFA KKLTFPEPVT SFNFHELREA VINGPDKYPG ASAIENESGQ
VVNLKFKNLE ERTALANQLL APSHAKMKGN RNKKVYRHLT TGDYVVMNRQ PTLHKPSMMG
HRARVLPNER VLRLPYPNTN SYNADYDGDE MNMHFPQNTL ARSELLMITD ADRQYISSTD
GKPLRGLIQD HITVSTFLTS RDTFFEEEEY HELLYSCLRP ENANTVTDRI QLVEPAFIRP
RRLWTGKQVI STVLKNIMPP NRRGLNLQGK SSTPGDRWGK GNEEDKVIFK DGELLCGILD
KKQIGASGGG FIDAIHEIYG NTIAGSLLSI LGRLLTRYLN MRAFSCGIED LRLTPEGDQK
RVEILKKAGE LGKNVSLKYV TLDQNPAADQ DAELKRRLED VLRDDQKQSG LDSVYNSQTR
KLTSDITAGC LPHGLIKQFP WNQMQLMTTT GAKGSSVNAN LISCNLGQQV LEGRRVPVMV
SGKTLPSYRA FETHPQAGGY VCGRFLTGIK PQEYYFHTMA GREGLIDTAV KTAKSGYLQR
CLIKGMEAVK VEYDSSVRDT ANGGSVIQFI YGEDGLDVAK QVHLQNFSFL AQNYVSTMAQ
LNMNQDYHKL EKPEVTEWHK DAMKQVKRTG RLDAKDPVLA VYQPGGHFGS VSEAFSQALK
KYEDSNPDKL LKDKKAGIAG ALSKKAFESV MHMKYLNSVI DPGDAVGIVA GQSIGSQTTQ
MTLNTFHLAG HSARNVTLGV PRLREIVMTA SKKPMTPTMT VEVIEELSEE KGESFAKGIS
RLSIAEVIDS LQVRETTSGK DEKFKIYDID MKFFDSKEYE KEYAITKRDL VRALQDEFLP
KFIKKISDEI KRRYDEQNLA GFSAAQPEIG VSIGTTERFE GAIRETQAGG AGDDDDDADE
DNEDDEEDAK RGQSKQNRDN QVSYEAPDDD EDIIRKEQDE SDLEDDDEDN ENKQKQDRKL
EDESESSDSS DDEDEMTEQA KLDRTDVEER TKEILGKYPE ISIFKYNAQE GNSCFIRLQY
KISTPKLLVL PLVEDCARRA VIQAVQDIGS CLYTPADAEN KEPAKIDIEG VNLLAMRDYQ
DYIKPHTIRT NSIHDMLIYY GVEAARSTII REMSDVFSGH SITVDNRHLN LIGDVMTHSG
GFKSYSRNGL IRESNSPFSK SSFETSVGFM RDAVLERDFD DLKSPSSRIV VGRLGNVGTG
AFDIFAPVA
//
