ID E4NLB5_HALBP Unreviewed; 417 AA.
AC E4NLB5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000256|HAMAP-Rule:MF_00411};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00411};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000256|HAMAP-Rule:MF_00411};
GN Name=rpo1C {ECO:0000256|HAMAP-Rule:MF_00411};
GN Synonyms=rpoA2 {ECO:0000256|HAMAP-Rule:MF_00411};
GN OrderedLocusNames=Hbor_28210 {ECO:0000313|EMBL:ADQ68364.1};
GN ORFNames=C499_01025 {ECO:0000313|EMBL:ELY31327.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ68364.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ68364.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC {ECO:0000313|EMBL:ADQ68364.1};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ELY31327.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY31327.1,
RC ECO:0000313|Proteomes:UP000011585};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. Forms part of the jaw domain.
CC {ECO:0000256|HAMAP-Rule:MF_00411}.
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|HAMAP-Rule:MF_00411};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00411}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00411}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_00411}.
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DR EMBL; CP001690; ADQ68364.1; -; Genomic_DNA.
DR EMBL; AOHT01000005; ELY31327.1; -; Genomic_DNA.
DR RefSeq; WP_006053521.1; NZ_AOHT01000005.1.
DR AlphaFoldDB; E4NLB5; -.
DR STRING; 469382.Hbor_28210; -.
DR GeneID; 9994639; -.
DR KEGG; hbo:Hbor_28210; -.
DR PATRIC; fig|469382.19.peg.195; -.
DR eggNOG; arCOG04256; Archaea.
DR HOGENOM; CLU_037097_1_0_2; -.
DR OrthoDB; 372142at2157; -.
DR Proteomes; UP000006663; Chromosome.
DR Proteomes; UP000011585; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06528; RNAP_A; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR012757; RPO1C.
DR NCBIfam; TIGR02389; RNA_pol_rpoA2; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF69; DNA-DIRECTED RNA POLYMERASE SUBUNIT RPO1C; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00411};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00411};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00411};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00411}; Reference proteome {ECO:0000313|Proteomes:UP000006663};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00411};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00411}.
FT DOMAIN 15..344
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46067 MW; 97384214D107DD07 CRC64;
MTEYEHVTED VEALVEDRDI PRRLKIRIYD TIEEREGVSP SQADEIAQAV EARYLDTRVD
PLDPVGTVSA QSIGEPGTQM TMNTFHYAGV AEIDVTQGLP RLIELVDARK TPDTPMMTVF
LEGEYATERE RAHEVVWSME ATKILALGDV STNVADMVVR IDLNEDTLME RWPTVNNVDT
VAQEIAETIE DALGVKTRRS GTVVEFGPES PSYRRLLQLV EELRDIVFKG IEDITRVVIR
KEENDDTGEE EFVLYTEGSA FGDVLSIEGV DASRTTSNNI HEIHRNLGIE AAREAIIDET
MNTLREQGLD DVNVRHLMLV ADIMTNRGEI ESIGRHGISG SKDSVLARAA FEVTVNHLLD
AAIHGEEDDL DGVIENVIVG KPIAIGTGDV DLRMGSIEAS TETEPETDAA APEPSDD
//
