ID A0A0L7LXL7_PLAF4 Unreviewed; 2443 AA.
AC A0A0L7LXL7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PFDG_00911 {ECO:0000313|EMBL:KOB85416.1};
OS Plasmodium falciparum (isolate Dd2).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57267 {ECO:0000313|EMBL:KOB85416.1, ECO:0000313|Proteomes:UP000054282};
RN [1] {ECO:0000313|Proteomes:UP000054282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum Dd2.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Kodira C., Zeng Q., O'Leary S., Yandava C., Alvarado L., Wirth D.,
RA Volkman S., Hartl D.;
RT "The genome sequence of Plasmodium falciparum Dd2.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; DS016131; KOB85416.1; -; Genomic_DNA.
DR EnsemblProtists; KOB85416; KOB85416; PFDG_00911.
DR VEuPathDB; PlasmoDB:PfDd2_030023300; -.
DR OMA; MVQYDRT; -.
DR Proteomes; UP000054282; 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; 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; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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; 2.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 2.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
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; 3.
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:UP000054282};
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 266..568
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 627..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2263..2283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2301..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2418..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2443 AA; 277175 MW; 371C7D1914365C0B CRC64;
MTVDLNIPYS ACELKRVKRL ELGVLDPEII KKISVCEIVN VDIYKDGFPR EGGLNDIRMG
TIDYRTLCGT CNMNVKYCPG HFGHIELAKP MYHYGFMNVV LNVLRCVCYH CGRLLCNVNS
SKVKYIEKIK VNSLRLRKLA ELCLGIRACD HSVEEEGLNI NDNSLNNFYN NDLSNLNMNQ
QMLLNKSNYT NIFEMVSKED VDCGCVQPKY SREGPNMYIQ FLHSSEEDID ESKRKLSAEE
ALEILKKIRK EEMSILGFNS DRCVPASLIL TCIPIPPPCA RPYVQYGNQR SEDDLTLKLL
DIVKTNIQLK RQTDRGAKSH VLQDLCSLLQ FHITTLFDND IPGMPIATTR SKKPIKAIRT
RLKGKEGRLR GNLMGKRVDF SARTVITGDP NLNIDYIGVP KSVAMTLTFC ETVTPLNYDN
LKKLVERGPY EWPGAKYIIR DNGTKYDLRH VRRNSEKELE YGYKVERHMT DEDYILFNRQ
PSLHKMSIMG HKAKILPYST FRLNLSVTSP YNADFDGDEM NLHLAQSHET RSEIKHLMIV
QRQIVSPQGN KPVMGIVQDS LLAIRKFTRR DNFLTKEEVM SLLIWIPYWN HVIPTPAIIK
PRALWTGKQI FSMLLQFDDM NIEDDKNDTA NNKVGRDVNT NVNKDSSKMN TSGNYYYGNS
TNDNTDDYLE KGNAYSRSGN NHPNSPLSIG DNINVGNVQQ NDMSSPNNNN NNNNNNNSNN
NNNNIGGGIN SFKRFNMVKI NLMRDSSTSS KDDNPYCSIN DGKVIIKNNE LLSGIICKRT
VGSSSGSLIH VLWHEMGPDK TKDFLSALQK VTNNWLEYVG FTVSCSDIIA SNKVLGKVRE
ILDKSKSEVS KLVEKAQKGE LECQPGKSLY ESFETRVNNE LNCAREMAGK VASESLDERN
NIFSMVASGS KGSIINISQI ISCVGQQNVE GKRIPFGFNH RSLPHFIKFD YGPESRGFVS
NSYLSGLTPQ EVFFHAMGGR EGIIDTACKT SETGYIQRRL IKAMEDVMVQ YDRTVRNSYG
DIIQFLYGED GMAGEYIEDQ IIDLMKLDNK EINKLYKYNF DEEPFGKDYY IGNKNDGSRN
TTYIDYNKQN ILNQEFEELY KCKNYLCKEI FPDGDIRQHL PINMNRLIEY AKSQFPCIPF
VSNNNSTNNN NNNNNNNISN SRKLMDKGNL SSTHNHKESK KRRKRRRRKN KFDKFKNENN
ELMSEIKKEY ENNDLNNMMI SKGDQSPFKG MNEFHMGVAD NDMGSDLGNN NNYNNDDFVD
DDYVDDDDYD DDDDYDDDDD LDDDDLDDDE NYSDNINIGG NRKYYGNTLK NNYDENSMLN
PIDVVHKVNN FLEKLVIIKQ INSNDTLSVE AQNNATILLK AHLRTYLNSK LLTQTHKVSV
KGLDWLLQEI EKIFYKSLCH PGECVGALAA QSIGEPATQM TLNTFHFAGV GSKNVTLGVP
RLKELINIVK NVKTPSTTIY LDDMVSNDQQ KAKDILTKLE YTTLKQLTSH AQIIYDPNTT
TTILEEDKSW VNEFYEFPDE DDTQYSLGEW VLRIQLTNIH VNEKKLTMKE IVYIIYSVFS
SDELDIIYTD DNSEDLVLRI RVKYLNGEYN FMNYDVVDNA NEQVDEQEED EEHLVANDRG
NYDETKNSTH PHHDYNNNTT NIFKSKVKNN ISSDINTKNE DSISINSSNN EQVKNINSSP
VSNNMHNNNN NNNNDSSNIN DIKVKNIKKE DGNEGALRGG GDSNTSALFG NKNSQKEDNI
VNNNNDNNDD DDDEEEEEEE EEEDFLFGDH NVSPKNTKDG KNKNTNNKSN NNENKNKKSG
NNNSNNSNTY DDGDVDNDND DDNDDNKSDI TIKEDNDVAF MKTSTKNAEE DLELKNKNHI
EHNISREDTE DTFLKKLMEQ CLSTLKLRGI ENITKVYMRE ESKITYDSDN GKFVRSSHWV
LDTDGCNLEN IFCAPQVDFK KTVSNDIVEI FEVLGIEAVR RALLKELRTV ISFDSSYVNY
RHLSILCDVM TQKGYLMSIT RHGINRVDKG PLIKCSFEET VEILLEAAAF AQVDNLRGIT
ENIMLGQLCK IGTGSFDIII DNQKLNDANQ NLETIQDLTS AGFTTPDSLH VITPDGLQSP
VAINTINSPL PFSPTYNANL LSPTAPIDNV NNLLSPQYNL QNYGDNVMSP TSKDINNLDT
LKLGGKFSPT QSPKSPTSVM HSPFSPFDHQ NQQPVDATNL LFSPKNNNIM NYNVFSPKPN
INNNVIQSPN IYSPNPMLDI FSPKPQINHN IYSPSYSPTS PTYNANNAYY SPTSPKNQND
QMNVNSQYNV MSPVYSVTSP KYSPTSPKYS PTSPKYSPTS PKYSPTSPKY SPTSPKYSPT
SPVAQNIASP NYSPYSITSP KFSPTSPAYS ISSPVYDKSG VVNAHQPMSP AYILQSPVQI
KQNVQDANMF SPIQQAHVDE AKNDDPFSPM PYNIDEDEMK ENM
//
