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Database: UniProt
Entry: E2BRL5_HARSA
LinkDB: E2BRL5_HARSA
Original site: E2BRL5_HARSA 
ID   E2BRL5_HARSA            Unreviewed;      1687 AA.
AC   E2BRL5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, 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=EAI_14335 {ECO:0000313|EMBL:EFN81707.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN81707.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN81707.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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}.
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DR   EMBL; GL449965; EFN81707.1; -; Genomic_DNA.
DR   STRING; 610380.E2BRL5; -.
DR   InParanoid; E2BRL5; -.
DR   OMA; NREDYQQ; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0031981; C:nuclear lumen; 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; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.357.120; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 1.
DR   Gene3D; 6.10.250.2940; -; 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:UP000008237};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          285..620
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1349..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1429
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1687 AA;  193021 MW;  53204866BD298F9E CRC64;
     MFSVFTANDI RNLSVTKIRT PLSFNILGHP LKGGLYDPVL GPLMGNSEPC GTCGGNVHTC
     TGHFGHIELS MPVVNPLFHK VLCMLIKLSC LSCFTFQIPP YVKLLLSAKW KLLYEGQLSD
     IDNLDQEVTS TVAEIPNVLE AQTEYIRDFI DNYIQNIYNR DRFSCGVPQN HENQMNTKNI
     NMQWHMYVDN ILKQYKAVKI CINCHEVIPK ISVMQNKIMT TKLNNSKDSA PKEMVSSTVV
     HKLETVMIMP DQSKEYLRKL WNNEKDFLKL IIPCLDLMDI EYPTDVFFLE VIPVLPPIVR
     PVNILHGQVI EHPQTQVYKN IMQDCLILRN IIQTIQDGGT DQLPQEGRLV FEQIRGLTAI
     EKLHNAWQGL QVNVDHLMDR EMSKTSESVH CQGLKQIIEK KEGIIRMHMM GKRVNFAARS
     VITPDPNLNI DEIGIPEAFA LKLTYPVPVT PWNVVELRRL ILNGPDVHPG AVMVENEDGM
     IQAISSNDST KREAVAKRLF TTNSRTNKFF SGIKVIYRHL QNGDVLLLNR QPTLHKPSIM
     AHKARILKGE KTLRLHYANC KAYNADFDGD EMNAHFPQNE LARSESYNIV SVSNQYLVPK
     DGTPLSGLIQ DHMVSGVRLT SRGRFFSRAD YTQLVYTALS MKQGDIILLP PAIIKPKLQW
     SGKQILSTVI INIIPGNKAR INLTSNTKIS LKEWQVNEPR RWKCGKEFDD PKTMSEMEVI
     IRHGELLCGV LDKMHYGATP YGLIHCIYEL YGGTCASKML SAFGKLFQAF LQWNGFTLGI
     EDILITREAD EKRKEIISNS KIIGSSIQRS AVELSDDTPM DEVRVKTEES YWSNSKFRAQ
     VDRKYKNMLD VYTNDINKTC LPMGLSKKFP DNNLQLMVQS GAKGSTVNTM QISCLLGQIE
     LEGKRPPLMI SGKSLPSFQA YDSTPRAGGY IVGRFMTGIK SQEFFFHCMA GREGLIDTAV
     KTSRSGYLQR CLIKHLEGLV INYDSTVRDS DGSLIQFYYG EDGLDIPGSR FLKKEQIPFL
     VDNKDAIVDA EALENLKTGS SNNEKIMKLI KKIKKWKIKN GPPLQKRRIS EFSKFSMENV
     NQNNNTKKNS VEKNCGRTKA ALSLIKKWMK IDKEMKKMFH IQCVRCPDPI MSKYRQDVEF
     GVLSERLESL LEEYLSHSPN IIKKSLRDLL SMKVMKTICP PGEPVGLLAA QSIGEPSTQM
     TLNTFHFAGR GDMNVTLGIP RLREILMMAS KNIKTPSMEI PFKSNLQKLT KQSKKLRVKL
     TKCVLSDVLK IITISRKMEE APHRRLVHTI KIEFLPYKYY KGEFFVHPQY VIKQTEKTFF
     KNIFKEIKKI AKITGTLLYF EENNRKRTNN EDAMLDQADP DEEESVRRER REDMRGERDL
     GEMHESSDEE RAAEDADATM NRSISRHREN QEYEDPEEEE MEDVMNNENE EADNNANKDL
     GNNQFDEDDD DDDDDDMTEN LNYRKNDKRN SNRRSEVIHM YKNALDYDYD ENKFSWCQFT
     FWLPLKMIKL DLPTIIRNVA SKTVLWETPY IKKAFTFQNN EGEMILKTDG LNIVEMFKYD
     SILNLNKLYS NDIYNISQTY GIEAANRVII KEIRDVFKMY GITVDSRHLS LIADYMTFDG
     TFQPLSRKGM ENSSSPLQQM SFESSLNFLK TATLQGKKDD LLSPSSRLML GQPCKSGTGI
     CSLFVNI
//
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