ID I6ZHJ5_ENCRO Unreviewed; 1515 AA.
AC I6ZHJ5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN OrderedLocusNames=EROM_030190 {ECO:0000313|EMBL:AFN82638.1};
OS Encephalitozoon romaleae (strain SJ-2008) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=1178016 {ECO:0000313|EMBL:AFN82638.1, ECO:0000313|Proteomes:UP000010094};
RN [1] {ECO:0000313|EMBL:AFN82638.1, ECO:0000313|Proteomes:UP000010094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ-2008 {ECO:0000313|EMBL:AFN82638.1,
RC ECO:0000313|Proteomes:UP000010094};
RX PubMed=22802648; DOI=10.1073/pnas.1205020109;
RA Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L.,
RA Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.;
RT "Gain and loss of multiple functionally related, horizontally transferred
RT genes in the reduced genomes of two microsporidian parasites.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012).
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; CP003520; AFN82638.1; -; Genomic_DNA.
DR RefSeq; XP_009264135.1; XM_009265860.1.
DR GeneID; 20520926; -.
DR KEGG; ero:EROM_030190; -.
DR VEuPathDB; MicrosporidiaDB:EROM_030190; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000010094; Chromosome III.
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; 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; 1.
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; 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 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 203..504
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1462..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1515 AA; 169389 MW; B1E6593D30F3E777 CRC64;
MFEEKVKKQI KSIQFGLFSP EEIRNGSAAL IVHPEVMEGG VPKVGGLIDL RMGTTDRMYL
CQSCGGDNFS CPGHFGHIEL TKPIFHVGYI SKIKKVLECV CFYCSKIKVP KRGVRSTLNN
VWSMSKGKSV CEGEVVGDGR SGCGNRQPVV KKEGLTLVAF MKGEESNEGK VMLNGERVYS
IFKKISDEDC VYMGFDLKYS RPEWMIFTVL LVPPPSVRPS IVMEGSLRGE DDLTHKLADI
IKSNGYLKKY EQEGAPGHIV RDYEQLLQFH VATLIDNDIG GQPQALQKSG RPLKSLSARL
KGKEGRIRGN LMGKRVDFSA RTVITPDPNI SLEEVGVPLE VAKVHTFPEK VTSFNIDKLE
KLVRTGPNEH PGANYVLRSD GQKIDLNFNK SDIRLEEGYI VERHMQTGDV VLFNRQPSLH
KMSMMAHYAR VMDDKTFRLN LSVTSPYNAD FDGDEMNLHM PQSYTSKAEL EELALVSKQI
ISPQSNKPVM GIVQDTLTGL RLFTLRDTFL NEREVMLLLY AVNIEFCDTP PGGTSYMELR
RTKDYDIMKV LKRPAIAKPM KLWTGKQILS FVLPNMNYVG FSSEHNDNDN ENISDTKVII
QDGYIHSGVI DKKAAGATQG GLVHIIFNDF GPKRAAQFFN GVQRMINVFM TGIHTFSIGI
GDTIADAKTV KMVKEAIRKA KEEVSVIIEN ARQNRLERLP GMTMKESFES HLNLVLNRAR
DVSGTSAQRS LSENNNMKTM VLAGSKGSFI NISQVTACVG QQNVEGKRIP FGFSHRTLPH
FVKDDYTGRS RGFVENSYLT GLDPEEFFFH AMGGREGLID TAIKTAETGY IQRRLVKALE
DAIVRQDESV RSGNGLMYQI KYGEDGFDAT FLESQKVDVK NFTKRYYIDM FGSGELAIKQ
DQVSEEVYGM LSSDVDLQKL LDQEYEWLVS EIFEGPSLLS TGEIDIDHDY QVRDIYKNAV
MSPCNFTRLL VTAKRAFHLS TGDVSPYYIL ETQKSLMTSN KILNVLIRTN LNVKRVLLEH
KLNTEAFNWV VEMINAKILQ ARITPNEMVG TLAAQSVGEP ATQMTLNTFH LAGVSSTVTM
GVPRLKEIFN VTKNLKTPSM KIYLDKDHCK TIESAKVIQN EIECLCVKDL CLSSEIYYDP
EITSTEIAED KDFVETYFEF PDDDVDFSCL SPFLMRLIVD RAKLVGRGAN LEYVAESIRK
ELGSGAHVIC SDENAVHMVI RIRVGKSEDE SLNFYMTILN SLLKLQLRGY KSVKKVYISE
DKDKKEWYLQ TDGTCLPQVL GNPAVNSRLT ISNDLIEIAE TLGIEAARES ILRELAMVID
GNGSYVNYRH MSLLADVMTM RGYLCGITRH GVNKAGAGAL KRSSFEETVE ILLDAALVSE
KNLCRGITEN IMMGQLAPMG TGNVEIMLDV KKLDKAIPLS NPVFKPNEPV TPVISTPSSD
SFSISSGNWS PTHLEMAYSR DVDGRLSPTS PSYSPTSPSY SPTSPSYSIS TSGFSNKSKS
KEQDGDKKRR NDNNF
//
