ID J9DL48_EDHAE Unreviewed; 1776 AA.
AC J9DL48;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=EDEG_02328 {ECO:0000313|EMBL:EJW03320.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW03320.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW03320.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW03320.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-2015) 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|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:EJW03320.1}.
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DR EMBL; AFBI03000040; EJW03320.1; -; Genomic_DNA.
DR STRING; 1003232.J9DL48; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_02328; -.
DR HOGENOM; CLU_000487_2_2_1; -.
DR InParanoid; J9DL48; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000003163; 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; 2.40.40.20; -; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000003163};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 341..720
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1776 AA; 200225 MW; 6F5045B37DF5ABB2 CRC64;
MGDPFKMDNS IYKINTLELQ FNNENISVCE ITLPISLDTF GHPIPCGLYD LKLGPLSENS
DYCQSCGLNF YSCPGHFGHI NLGYLCLNPL CFDVFVQLMN VFCGRCLRLK ESDFCRFLFV
CECKMFLKGY SNTNFIDLLN EVDCISGNED NNIIINNFNT VKNNKKSRIG NIRKVGNNNH
DTENLNASKK ILLKYSMMDD LSNDNGENSN FDSASTDEHP TKKAKIDKYC ESDSVEENKK
LSSEMLETMT RISSYIDSLE PQRPLYKQHH DHVLQYLKVL SKKRYCPHCN ITSTLYKKGK
NKVVLKEGIV QMPSELREQL ILIFKNDSEL LNAMFRGFFV DMFFLDKLFV PPNKFRPIAF
FDGKPYDCQV NSLYSRIIRI NNVINSNSNS SSNNNSSNSS NNNSNNNINE VTRVNRNISI
NLDFDEKTSD SSDSSETTKT NKTNDSSHYT EKSTDHSEAA IIDKTLNTHE ACQNYCTLQH
HIFTLFDGSG GAEIGYKGVK QKFEKKDGLF RRNMMGKRVN HAARSVISPD PNIHTREIGV
PYVFAENLTF PEIVTVSNYK KLQQMVINGP QYPGAKVLEI HDDMYKVPVT YNLYLLNEQK
RTELSSKLLS SKMCVVHRHI EDKDIVLLNR QPTLHKPSIM AHVVKVLRGE KTIRMHYANC
NSYNADFDGD EMNIHCLQNH LARAEAYMVM SNDHNYVSNT NGNPVRGLVQ DHVVVCARIC
LKEEFMQREE YISYVSACVL AKRDTNNFLL YEGHNIKNIK NSNNVFDNDD SNNEDTIYST
NFNKKNIYSD DSDTSISSDG DTVKYFVDKP TILRPVILYT GKQIVTSILK SLNISIDHTS
KSKTDTDPVI IRDGRLLSGT IDKSQIGPTK NSLVHVCGKK YGFSICNELL TSFGLVINKI
MARQGYGARI SDLLLVESGN QQRGFLCKEG TKAVKNTLLQ SGFIKKCNNN KGGSVNDKET
SVIDHSYSLS DPYFFVDGKS LEYYDSLVKQ TMNKTTSSIY DRTISENQYV PFPFNNYSLM
IKSGAKGSTV NLGQISGLLG QQELEGKRVP YLSSGTTLPC FESTKIAPQI NGYIFGRFLD
GISVAEYFFH CMAGREGLID TAVKTARSGY LQRSLIKALE GLKVEYDYSV TNQGDIVQFL
YGEDAFDTSK DEDNTKIKNI IEGMSNQIEY TTLDKKNKTL KNTRSSSDDS SNVSEEENSK
NTSSISNSTE NDNIKSHTIN ACDNDTNTIS ETNNSDDEDN NTTSESSYEE SIEAVVENTY
KSPSSSQQAK QNTQFEDKFG KYINTLLENK ELCKNMVQPG EAVGIIAAQG VGEPSTQMTL
NTFHLAGVGS KNVTLGIPRL AEILTIASKK IKTPYIKVDL SKPLKNKKQH DDDIDNNLIK
KRGEQLVDML KRITLKDITR KIYIEETGSL FSIVIYLDKK TDVVTVKKLI CRLIDRKLRS
SKVSIGIEII NQPDNTENSV KTHEEHSEND DSVDDSSDKD DINKKNRKNN NDISENDESE
EIDSSEDGSD SEEYSTNKKK KSRKSSSISK DDEESNDSSN SNITSNTSKY DDNDNSTNTI
IHTENNTNLY TLDLSKENKE KKLKKIIRIN LDTKNDKVLL LPILESILPN IVIKEVENIK
GAHTQENDLI IEGSQIENLV GILSNSELMN TYSNDIHNVN LSLGIEACRS VIVNEIKTVF
NAYGITVNIR HLLLIADFMT KEGIYKPFNR YGLAHSQSIL QKMSFESAFK FIKEGVLFNE
KDTLQTPSAN IIVGNAVNLG TDCGFILKEN YSLNKI
//
