ID A0A1A9VJL9_GLOAU Unreviewed; 618 AA.
AC A0A1A9VJL9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT039444-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT039444-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT039444-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000256|ARBA:ARBA00006711}.
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DR AlphaFoldDB; A0A1A9VJL9; -.
DR STRING; 7395.A0A1A9VJL9; -.
DR EnsemblMetazoa; GAUT039444-RA; GAUT039444-PA; GAUT039444.
DR VEuPathDB; VectorBase:GAUT039444; -.
DR OrthoDB; 1475382at2759; -.
DR Proteomes; UP000078200; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; 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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd03023; DsbA_Com1_like; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 3.90.940.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR003716; DNA-dir_RNA_pol_omega.
DR InterPro; IPR011740; DUF2460.
DR InterPro; IPR039554; HigA2-like_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02217; chp_TIGR02217; 1.
DR NCBIfam; TIGR00690; rpoZ; 1.
DR PANTHER; PTHR34476; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR PANTHER; PTHR34476:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR Pfam; PF09343; DUF2460; 1.
DR Pfam; PF13744; HTH_37; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 88..197
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
FT DOMAIN 431..482
FT /note="HigA2-like helix-turn-helix"
FT /evidence="ECO:0000259|Pfam:PF13744"
FT REGION 584..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..618
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 69727 MW; 002D3271D1ED817D CRC64;
MTLTSTPRSL ALIKDFATAP RVLLLPQSAS RDEIACFFQY TVIASLPIIN NWLSNRSQML
SDDYIGEKLD NYISRNFDKI DQIFDLTYPY SGNENSSVVA VGFFDYSCGY CKTIKDDIKQ
LINDGKIKYI FRDSPILGHD SLRAAKSALA VYFIDKEKYF DFHYAALSHK GGFSDESILD
IVKSIGIDED DFNSSMKNNA DKIEQMINGR GHMSFTEIRF PENISYGSAG GPEFSTDVVT
THNGCEQRNI NWSRARARYN IAYGVRSSEQ LTELITFFHA RKGKAIGFRF KDWSDFIAIN
QKIGIGDNKK TTFQLIKTYV SGEDKHIRMI KKPVHGTVKI YLNGKEESEY SVNYSTGEIT
FMKPPVKDAI ITASFEFDVP VRFDTDYLNA SIDNYGSNSW NNIPLVEPKP DLPLQGTPIT
GKQVSDATIP EKNAWTQAFA AEKLGIDQPK VSQIKNGKID GFSLERLLGF LKKLDHEITI
TMTESQEIKS EAEKYLMAES IVEKCTEQVS NRFKLVLLAS QRTHDLNTGA SNPVQTAQFK
DHKNTIVSLH EIAEKQADTH ELFNLLVGRC KEYMKGNMNN VYSSNTNLDA SQESQDYEVD
GEIDDEINDQ DGDEEVSV
//
