ID A0A0V1MEF4_9BILA Unreviewed; 1324 AA.
AC A0A0V1MEF4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 37.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN Name=POLR3B {ECO:0000313|EMBL:KRZ70257.1};
GN ORFNames=T10_4968 {ECO:0000313|EMBL:KRZ70257.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70257.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ70257.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70257.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:RU363031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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:ARBA00048552,
CC ECO:0000256|RuleBase:RU363031};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU000434}.
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:KRZ70257.1}.
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DR EMBL; JYDO01000117; KRZ70257.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR FunFam; 2.40.270.10:FF:000022; -; 1.
DR FunFam; 3.90.1100.10:FF:000009; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000021; DNA-directed RNA polymerase subunit beta; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1100.10; -; 2.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 2.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 212..566
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 373..523
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 598..662
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 699..760
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 782..813
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 828..1176
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1178..1250
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 1324 AA; 150221 MW; 38B3B3E988B1D990 CRC64;
MITLLMHRRN FSKSNRMIAE EYQHTLALNA TKFGVVIKTF IKEYERIHDL VNVRMNCGQV
ISGSEYAELV LKMSDAISKI FKPGMQLVEM GNELLDTINK MEQLNLFSLG NASYPFSMWI
FGIAVSIKDI SKSLTVLEVN FLEFLSAVRR AKIMIKQENQ PVSFNNIKVK TESRCSSTYG
NTLDRKGEHL GLPVDSLEQK WTIIPHYLRT KGLINQHIDS FDYFINSEIK EIVKANDMVR
CTADPSFYIK YIDIRVGFPK AEEADCLKTS VTPHECRLRD ITYAAPIFVD IEYTRGKEKV
LRKNFQIGRM PIMLRSSRCV LKGKSEKELI KMNECPLDPG GYFIIRGTER VVLIQEQMSK
NRMLVAMDKA DEISCGVLTM THVSRGKTYV VYKKDIFFMR NNRLDISMAI VFRAMGILSE
REMLHLVSGE QDSCLIFLNT LQDLHKREIF TQKDVIVALI FVGNRIKGNP FFTSKNNSTV
NKDELALSFL ADVVCAHVPR IIQVMLGKAA VDDPDYYGNK RLELAGSMLA LLFEDLFKRF
NQEISLLTDR TIQRLRTALF DFVKHAPKDL ITNGLFNAIA TGNWVIRRYR MDRHGVTQIL
SRMSYIAMLG MMTRINSQFE HTRKMGGPRS LQPSQWGMLC PADTPEGEPC GLIKSLALLS
HITTDSEELP VKKAFCNLGV EDVNYLSTEV LLHPSTSFVF LNGVLFGITR DVVQLYNSLR
YMRRHGFLNK FVNLFLNEEQ RTLYVSCDGG RICRPYIIVE NGKSLLQNHH LRELASGKRD
LEDFFKDGLI EYLDVSEEES ALIAVYDSEI TEKTTHLEIE PFALFGVCAG LIPYPNHNQS
PRNTYQCAMG KQAMGIIAYN QSIRMDSLLY GLVYPQRPLV KTKTIELINF ECLPAGQNAI
VAVMSYSGFG RCHVYRSSKC FVKTYGNMDS DRIMGPLMDV TTGKAVFRHM ALDAEGIVKP
GNVVKVGQVL VNKVAPRSTL FNGEEPTVLS ESDFREEPLV WMGAADAYAE RVLVTSNLDN
QCLIKVLLRQ TRRPELGDKF SSRHGQKGVV GLIVQQEDMP FSSEGIVPDL IMNPHGYPSR
MTVGKLLELI NGKGGTFTGT PRYGTAFCGD KIEEIAKDLM QHGFSINTKM QCAMQFGCDE
VYLLQKLKHM VLDKVHARGK GPMENLTRQP TEGRSRDGGL RLGEMERDCF IAYGASAILV
ERLMVSSDAF EATVCQNCKS SQALATVSMP YACKLLFQEL QAMNVTPQMK LRDANLPRSF
KTTVEPTKEE NNVTLNTDEV INFPIRKLNY SEELQLDDPV MKIIKYYLYN TQHDYHSRRN
VENT
//
