ID W7APK5_9APIC Unreviewed; 2334 AA.
AC W7APK5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=C922_02052 {ECO:0000313|EMBL:EUD67346.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD67346.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD67346.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD67346.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) 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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI965466; EUD67346.1; -; Genomic_DNA.
DR RefSeq; XP_008815873.1; XM_008817651.1.
DR EnsemblProtists; EUD67346; EUD67346; C922_02052.
DR GeneID; 20037326; -.
DR VEuPathDB; PlasmoDB:C922_02052; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000030640; Unassembled WGS sequence.
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; 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; 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; 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.
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};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 268..570
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1125..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2304..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1151
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2334 AA; 261452 MW; 3260754A47B33442 CRC64;
MTVDLNVPYS ACELKRVKRL ELGVLDPEII KKIGVCEIVN IDLYKDGLPR EGGLNDIRMG
TIDYKTLCGT CNMNVKYCPG HFGYIELAKP MYHYGFMNVV LNVLRCVCYH CGRLLCNTSN
SKVKYIEKIK VNSLRLKRLS EVCQTIKVCD HSSPQEEDTL HLNENAVDNF YNNNLSNLNV
NQQMLLNPNS YSNIFEMVNK EDVDCGCVQP KYSREGPNMF IQFLHSSDED IDESKRKLSA
EEALEILKKI RKEEMPILGF NSDRCIPASL ILTFIPIPPP CARPYVQYGN QRSEDDLTLK
LLDIVKTNIQ LKRQTDRGAK SHVLQDLCAL LQFHITTLFD NDIPGMPIAT TRSKKPIKAI
RTRLKGKEGR LRGNLMGKRV DFSARTVITG DPNLNIDYIG VPKSVAMTLT FCETVTPLNY
DDLKKLVERG PYEWPGAKYI IRDNGTKYDL RHVRKNSERE LEYGYKVERH MTDEDYILFN
RQPSLHKMSI MGHKAKILPY STFRLNLAVT SPYNADFDGD EMNLHLAQSH ETRSEIKHLM
IVQKQIVSPQ GNKPVMGIVQ DSLLAIRKFT RRDNFLTKEE VMSLLIWIPY WNHVIPTPAI
MKPKALWTGK QIFSMLLQFE DLERLNDPLG NANMMIGGGG GATHGSGFRI EDEMGRANNT
SGAHLHPHSP LAIGDTLNSN VKNQFIGNEV TGTNGPDGIF KGVSGWRRNV KINLMRDSST
SCKDDNPYCS INDGKVIIKN NELLCGIICK RTVGSSSGSL IHILWHEMGP DKTKDFISAL
QKVTNNWLEY VGFTVSCSDI IASNKVLDKV KDILSKSKKE VSKIVKKAQR GELECQPGKS
LYESFETRVN NELNCAREMA GKVASESLDE RNNIFSMVAS GSKGSIINIS QIISCVGQQN
VEGKRIPFGF NHRSLPHFIK FDYGPESRGF VSNSYLSGLT PQEVFFHAMG GREGIIDTAC
KTSETGYIQR RLIKAMEDVM VQYDRTVRNS YGDIIQFLYG EDGMAGEYIE DQIIDLMKLD
NKEVKKLYKY NFDDDEDDNH DDRYGKDFYL DRGQNRKNSY IDYNKQNVLN QEFQELLRCK
NNICKEIFPD GDVRQHLPIN MNRLIEFAKS QFPFVPVVGS KVKDPISANR MRPKMSSTQR
RRKKGKKARP RAERKATADV ALEDPNEELR NSEFMSEIKK EYETNDLASA MKGQGTYSGF
EPFDEDLAEG TRRDGSDEGS ADEDEEEASH SDSGVESDGE SHGEDRSFVN PVDIVHKVNR
FLEKLVIIKQ INSNDTLSLE AQNNATVLLK AHLRTYLNSK LLIQTHKISM KGIDWLLQEI
EKNFYKSLCH PGECVGALAA QSIGEPATQM TLNTFHFAGV GSKNVTLGVP RLKELINIVK
NVKTPSTTIY LDDVVSNDQQ KAKDILTKLE YTTLKQLTSH AQIIYDPNTT TTILEEDKMW
VDEFYEFPDE DDTQYTLGEW VLRIQLTNIH VNEKKLTMKE IVYIIYSVFS SDELDIIYTD
DNSEDLILRI RVKYLNGEYN FLNDDAEQAQ EDEYEEEEEE EEEEENYNNI GKTFKTKKNV
DADDNQATQN RKNDKDDNQS VSSSRSRQNS VNSENRFGSA TGSASGTHMD DGDGMGNHNR
DEAVGKDKTS KDKSAAKMKK LKEESANRTD SNYVEGYEET DLFAKGEGRS GVGSGIGSGL
VNGLGSGKSS GTAEDMFGKA NSKHAEEDAH TTKGRNNISG PNVGGGGITS GNAPNANNTS
SVDRNSMRNV NNLSNPIYMK EDTEDTFLKK LMEQCLSTLK LRGIENITKV YMREESKITY
DSNNGKFVRS SHWVLDTDGC NLEHIFCASH VDYKKTVSND IVEIFEVLGI EAVRRALLKE
LRTVISFDSS YVNYRHLSIL CDVMTQRGYL MSITRHGINR VDRGPLVKCS FEETVEILLE
AAAFAQVDNL KGITENIMLG QLCKIGTGVF DIIIDNQKLS DANQNLETMM DITSAGFTTP
DSHHGITPDG LQSPVAINTL NSPLPFSPTY NVNLLSPTAP LGSVNGILSP QCLQDYGDAN
SGGMGGSGGE NIMSPSKNDF NNLDTLKLGG KFSPTQSPRS PTSVIHSPFS PFDNHNQQAL
DPSMLFSPKN NNSGGISGSS NSMSMMNYNI FSPKANLNSI QSPAMLYSPN RALDIFSPKQ
QTQNNIYSPS YSPTSPTYHL SNNANAGGSS GLNGTKAFYS PTSPTNQVDD MNPNMMKYHS
VVSPVYSYSP TSPVPNNPNS PHYSPYAIAS PKFSPTSPAY SISSPVYDRS SNARNKSQHA
LSPAYILQSP VQVKQHIQDV SIFSPIQQAN ADEAQNDDPF SPMPYNMEED EMEQ
//
