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Database: UniProt
Entry: A0A091E5B2_FUKDA
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ID   A0A091E5B2_FUKDA        Unreviewed;      1410 AA.
AC   A0A091E5B2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-APR-2018, entry version 24.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN   ORFNames=H920_08292 {ECO:0000313|EMBL:KFO30261.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Bathyergidae; Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30261.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO30261.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO30261.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000256|RuleBase:RU363031}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000256|RuleBase:RU363031}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000256|RuleBase:RU000434}.
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DR   EMBL; KN122458; KFO30261.1; -; Genomic_DNA.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 3.
DR   Gene3D; 2.40.50.150; -; 2.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR003150; DNA-bd_RFX.
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; 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   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF02257; RFX_DNA_binding; 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; SSF46785; SSF46785; 1.
DR   PROSITE; PS51526; RFX_DBD; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000028990};
KW   DNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363031,
KW   ECO:0000313|EMBL:KFO30261.1};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU363031};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Transcription {ECO:0000256|RuleBase:RU363031};
KW   Transferase {ECO:0000256|RuleBase:RU363031}.
FT   DOMAIN     1301   1393       RFX-type winged-helix.
FT                                {ECO:0000259|PROSITE:PS51526}.
SQ   SEQUENCE   1410 AA;  157859 MW;  1688248CB411D092 CRC64;
     MDVLAEEFGT LTPEQLAAPI STVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK
     ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT
     RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI
     QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIAIIF
     KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG
     PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK
     RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS
     TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC
     PSDTPEGEAC GLVKNLALMT HITTDMEDGP IVKLAGNLGV EDVNFLCGEE LSYPNVFLVF
     LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK
     KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE
     PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV
     KTKTIELIDF EKLPAGQNAT VAVMSYSGYD IEDALVLNKA SLDRGFGRCL VYKNAKCTLK
     RYTNQTFDKV MGPILDAATR KPIWRHEILD ADGICSPGEK VQNKQVLVNK SMPTVTQIPL
     EGSSVAQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR
     HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK AGVLDGRFHY
     GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA YVYFGPVYYQ KLKHMVLDKM
     HARARGPRAV LTRQPTEGRS RDGGLRLGEM ERDCLIGYGA SMLLLERLMI SSDAFEVDVC
     GQCGLLGYSG WCHYCKSSCH VSSLRIPYAC KLLFQELQSM NIIPRLKLSK YNEPLKLSDS
     RNLAALPANS REGAVPGHLW HIRIGLALCW CCQTAGCGLC PKPHNPAEEA KVRQPVGEHW
     ALTTRRLPLS VRRSLGDGHC AGDPQTSGFS GGACAVHGKS MHCGLLEEPD MDSTESWIER
     CLNESENKRY SSHASLGNVS NDENEEKENN RASKPHSTPA TLQWLEENYE IAEGVCIPRS
     ALYMHYLDFC EKNDTQPVNA ASFGKTVALE MPCLQQKTGR DCCGPHPELV ESESQNACGS
     CHLLQRKGLV VPRNSDTIVD SSPSSRAFHT
//
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