ID S7WE52_SPRLO Unreviewed; 1551 AA.
AC S7WE52;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=SLOPH_320 {ECO:0000313|EMBL:EPR80047.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR80047.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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}.
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:EPR80047.1}.
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DR EMBL; ATCN01000027; EPR80047.1; -; Genomic_DNA.
DR STRING; 1358809.S7WE52; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_320; -.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; S7WE52; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000014978; 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; cd02584; RNAP_II_Rpb1_C; 1.
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; 2.
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; 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; 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; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
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; 2.
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:UP000014978};
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 207..508
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1501..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1551 AA; 175653 MW; 613DCF9737292910 CRC64;
MHNEQFLKRR ISSIQFGVLS PEEIRNGSVV AIEHPETMEN GIPKENGLID FRMGTTERGY
LCATCLEGAT DCVGHYGHIE LARPIFHVGY MSKIKKILET VCFYCAKIKI DITDVRLQKN
INSIWSVAKG KTICEGRDIG EGIKSGCGNK QPLIKKEGLG LVAFMKGEEN SEGKVILNGE
KVHNIFKRIP ESDIEAMGFS PKYSRPEWLI LTVLLVPPPP VRPSVLVDGI LRGEDDLTHK
LADIVKANNN LKKYEREGAP GHVIRDYEQL LQFHIATLID NEISGQPQAL QKSGRPLKSI
SARLKGKEGR VRGNLMGKRV DFSARSVITP DSNIGLDEVG VPEQIAKILS FPERVTSFNI
DFLEELVKRG PYNYPGANYV IREDGQRIDL RYNRSEINLT EGCSVERHIV TGDMVLFNRQ
PSLHKMSMMS HKARVLKKLT FRLNLSATSP YNADFDGDEM NLHMPQTYNT KAELQELTYL
PTQIVSPQSN KPVMGLVQDS LLGISKLSSK DTFLKRKEVM QILFSSDFDQ EKVFKTLQRP
AISKPKKLWT GKQLISVLLP KISYKGLNNL YNEYEILSDG SVFIENGILI HGSFDKKIAG
STQGGLIHII KNDYNHKVVL DFINNSQRMV NSYITHIHSF SCGIGDTIAD GNTMKKIMES
ISEAKDSVKA TISDAKRGRL ERLPGMTIKE SIESKIKLSL NKARDVSGTS AQKSLSLSNN
VKNMVLAGSK GSFINISQVT ACVGQQNVEG KRIPFGFNER TLPHFSKGDH GPESRGFVEN
SFLSGLIPEE LFFHTMGGRE GLIDTSIKTS ETGYIQRRLV KSLEDCSIAY DGSVRNGNNN
IFQFLYGEDG FDATFIERNK EQELNKLHKF YVEALKDNNI LEHYANIDNN PVVYAKQDYP
SANTSYSNTE ELKKEYEEIK NIKIDNVVYL PVNFKRIFYN ERVNNRGTIK NYKEISKGRK
EIENYLKELR IENKSLIERI KYSLSIYNIL KNKINLEGYK HIIKRIRNYL QRGKIAYSEM
VGTLASQSIG EPATQMTLNT FHYAGVLSTV TMGVPRLNEI INVAKNIKTP MMELQIKKEH
RNNEMEHIRR VQAALEFITI GNIIEEKYII YDPVIQETNV KEDEEIVQTY FMFPDTEDAS
ESRLSRYIIR LKLSKDKMII KHLKIEEIVE KIKKKYHKDI NIIHSDDNSK NIVIRIRVAI
DCDELFYKKL LEDISTIHLR GYPDIKRSFI VEDKNRMYKD RRLNPEDSDE KEDKNYYIQT
EGCNLLKILK DPYVDVYKIM SNYTIEMCDV LGIEAARESL LIELKRVIEA DGSYVNHRHY
SLLADLMTMK GALSGVTRHG VNRANNSVLM RCSFEETVDI LLDAGLKAEV SECKSVTDNI
MIGDIAPIGT GSTHLLLNTE ALQDAVAVQT REYEFEKEEF MTPNIQSPVS YKSNGESGWS
PVLTYKPTTA SYTPTSGLYS PTTGMYSPMS SFYTPTSPTY NPTSAISRNN TYNPASPIYS
PESPMYSPTS PSYAPTSPAY TPSSPTYIPT TAYNPVKRVK HSKKKKESKK E
//
