ID A0A267ERY6_9PLAT Unreviewed; 968 AA.
AC A0A267ERY6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BOX15_Mlig024670g1 {ECO:0000313|EMBL:PAA63637.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA63637.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA63637.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA63637.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA63637.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- 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:PAA63637.1}.
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DR EMBL; NIVC01001827; PAA63637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267ERY6; -.
DR STRING; 282301.A0A267ERY6; -.
DR Proteomes; UP000215902; 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; cd02733; RNAP_II_RPB1_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; 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; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 249..552
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 968 AA; 108871 MW; 7FD3D12AAFA7597F CRC64;
MLMYEVADST APLRTVKRVQ FGILSPDEIK RMSVTEGGIL YPETMEAGKP KLGGLMDPRQ
GVIDRMSRCQ TCAGNMSQCP GHFGHIELAK PVFHVPMMTK IVKILRCVCF FCSKLLIDPQ
SEKVKEILIK TANHPQRRLN YIYDECKGKS ICEAPSTGGQ QDQPDAEAGG AAFSEGIGGE
VTVRSGCSRY QPKIRKTGLD LSAEWNKVND ESQERKIALS AERVLEIFKR ISDDDCHVLG
MNVRFARPDW MITTVLPVPP LPVRPAVVMH GAAKNQDDLT HKLSDIIKAN NQLRRNEQSG
AAAHIIQEDT KMLQYHCTTL IDNEIPGLPK ATQKSGRPLK SVKQRLKGKE GRIRGNLMGK
RVDFSGRTVI TADPNIGIHQ VGVPRTIALN LTFPEVVTPF NIEWLQELVR NGANHYPGAK
YIIRDNGDRI DLRYHPKAAD LTLQIGYIVE RHMMDDDYVV FNRQPTLHKM SMMCHRVKVL
PWSTFRLNLS VTTPYNADFD GDEMNLHMPQ SLETKAEIAQ LATVPRMIIT PQSNRPVMGI
VQDTLTAVRK MTKRDVFITR AEMMNLLMYL PSWDGRMPNP AILKPQPLWT GKQLFSLIIP
PRINCVRTHF THPDEEDNGP YKWISPGDTK VLVEDGQLLS GILCKKSLGA SAGSLVHIVA
LECSHMDAGR FYGEIQTVVN NWLLIEGHTI GIGDTIADNK TYSDIRETIK KAKENVEDVI
NQAHHDELTP TPGNTLRQTF ENMVNKILND AREKTGSCAQ KSLSEFNNFN AMVVSGAKGS
KINISQVIAC VGQQNVEGKR IPFGFCHRTL PHFIKDDYGP ESRGFVENSY LAGLTPTEFY
FHAMGGREGL IDTAVKTAET GYIQRRLIKA MESVMVKYDN TVRNQIEQVI QLRYGEDGLD
ACHVEFQAVP IIKPSNPAFE RNFRFDLSNE RMLRRCMTEE QMRRVLHDNN CQQELERSGI
SCRQIAKS
//
