ID A0A5J5N2P9_MUNRE Unreviewed; 1025 AA.
AC A0A5J5N2P9;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
DE Flags: Fragment;
GN ORFNames=FD755_001732 {ECO:0000313|EMBL:KAB0386776.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0386776.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0386776.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0386776.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0386776.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:ARBA00047768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000256|ARBA:ARBA00047768};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KAB0386776.1}.
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DR EMBL; VCEB01000001; KAB0386776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5N2P9; -.
DR Proteomes; UP000326062; Chromosome 1.
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: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:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.50.150:FF:000003; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1070.20:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000004; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1110.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1800.10:FF:000003; DNA-directed RNA polymerase subunit beta; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1070.20; -; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 2.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1.
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; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
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; 2.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000326062};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 17..327
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 101..278
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 353..417
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 454..515
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 536..568
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 583..824
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 832..933
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 935..1020
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAB0386776.1"
SQ SEQUENCE 1025 AA; 115683 MW; 4572D9B2DCB734DF CRC64;
LQDIREAFGR FWWVSCCRLR DMTYSAPITV DIEYTRGSQR IIRNALPIGR MPIMLRSSNC
VLTGKTPAEF AKLNECPLDP GGYFIVKGVE KVILIQEQLS KNRIIVEADR KGAVGASVTS
STHEKKSRTN MAVKQGRFYL RHNTLSEDIP IVIIFKAMGV ESDQEIVQMI GTEEHVMAAF
GPSLEECQKA QIFTQMQALK YIGNKVRRQR MWGGGPKKTK IEEARELLAS TILTHVPVKE
FNFRAKCIYT AVMVRRVILA QGDNKVDDRD YYGNKRLELA GQLLSLLFED LFKKFNSEMK
KIADQVIPKQ RAAQFDVVKH MRQDQITNGM VNAISTGNWS LKRFKMDRQG VTQVLSRLSY
ISALGMMTRI SSQFEKTRKV SGPRSLQPSQ WGMLCPSDTP EGEACGLVKN LALMTHITTD
MEDGPIVKLA SNLGVEDVNL LCGEELSYPN VFLVFLNGNI LGVIRDHKKL VNTFRLMRRA
GYINEFVSIS TNLTDRCVYI SSDGGRLCRP YIIVKKQKPA VTNKHMEELA QGYRNFEDFL
HESLVEYLDV NEENDCNIAL YEHTINKDTT HLEIEPFTLL GVCAGLIPYP HHNQSPRNTY
QCAMGKQAMG TIGYNQRNRI DTLMYLLAYP QKPMVKTKTI ELIEFEKLPA GQNATVAVMS
YSGYDIEDAL VLNKASLDRG FGRCLVYKNA KCTLKRYTNQ TFDKVMGPML DAATRKPIWR
HEILDADGIC SPGEKVENKQ VLVNKSMPTV TQIPLEGSNV PQQPQYKDVP ITYKGATDSY
IEKVMISSNA EDAFLIKMLL RQTRRPEIGD KFSSRHGQKG RCSLKSVHIT QVGKLIELLA
GKAGVLDGRF HYGTAFGGSK VKDVCEDLVR HGYNYLGKDY VTSGITGEPL EAYIYFGPVY
YQKLKHMVLD KMHARARGPR AVLTRQPTEG RSRDGGLRLG EMERDCLIGY GASMLLLERL
MISSDAFEVD VCGQCGLLGY SGWCHFCKSS CHVSSLRIPY ACKLLFQELQ SMNIIPRLKL
SKYNE
//
