| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA-directed RNA polymerase subunit beta' |
Protein Synonyms/Alias | RNAP subunit beta' |
Gene Name | rpoC2 |
Gene Synonyms/Alias | SYNPCC7002_A2043 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | | 74 | IKRQMLDSAEQEIKT | S | HTP | [1] | | 222 | VREEDCGTARGLKLR | T | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity) |
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| Completeproteome; DNA-directedRNApolymerase; Nucleotidyltransferase; Transcription; Transferase |
Protein Sequence | MTKEKPAVFY NRIIDKGRLK KLMSWAYTSF GSAHCATMAD ELKTLGFRYA TQAGVSISVD 60
DLQVPPIKRQ MLDSAEQEIK TTEARYSRGE ITEVERFQKV IDTWNSTSES LKDEVVKNFR 120
ETNPLNSVYM MAFSGARGNL SQVRQLVGMR GLMADPQGEI IDLPIKTNFR EGLTVTEYII 180
SSYGARKGLV DTALRTADSG YLTRRLVDVS QDVIVREEDC GTARGLKLRA MTDGEREQIS 240
LEDRLFGRVL NADVVDPKTG EVIAQRNQDI DADLAKKIAT TVAEVEVRSP LTCEAARSVC 300
RKCYGWSLAH GHMVDMGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTKEA ARTIKASKAG 360
TIQFKDGLST RRMRTPHGDE VEQVEVAGTL VLKPSDNGKM VSHALSPGSF VLVAEGASVK 420
KGDLLVEVGA GQKTQKSTER ATKDVSSDLA GEVLFDNLIA EEKTDRQGNT TRSAQRSGLM 480
WVLAGDVYNL PAGAEPVVEN GTHVNVGDIL AETKLVSLSG GVVRLIPNSR EIEIVTASVL 540
LDEAKVLHET GGGSEQYIIE TSKGDQFLLK TAPGTKVQNN ANIAELIDDR YRTTTGGIIK 600
YSGVEVAKGT KKQGYEVLKG GTLLWIPEET HEVNKDSSLR IVEDGQYVEA GTEVVKDIFS 660
QSAGVAEVIE KNDILREVII KPGELHLTEE AIADKYHEQL IQPGEEVIPG VTIDKLSYGE 720
KVISTEGVAL LVRPVEEFQV EDTPVEPSQG SINEQGAGRN IELHAVQRLF FKDGERVKSV 780
DGVSLLSTQL IIEIGAIEGE DEDVLANLYA DIELQDDPTD DEVKRLQLVI LESLILRRDS 840
DSDPFGGQVQ TRLMVEDGQE IVPGAVVART EIQCKEPGEV RGIRSGQEAI RRLLIVRDSD 900
RQTLAIDGKA KVKENTLVVA GTEIAEGVVI EDSAQVLKVS DKEIVLRHAR PYRVSGGAVL 960
HIDEGDLVQR GDNLVLLVFE RAKTGDIIQG LPRIEELLEA RKPKEAAVLA RRPGTCQVEY 1020
LDDETVDVKV IEDDGVISEY PVSLNQSVMV VDGQRVGPAE PLTDGLNNPH EILEIFFDYY 1080
AESKGIYEAA LIGLRESQRF LVEEVQRVYQ SQGIDISDKH IEVIVRQMTA KVRIDDGGDT 1140
TMLPGELIEL RQVEQVNEAM SITGGAPARY TPVLLGITKA SLNTDSFISA ASFQETTRVL 1200
TEAAIEGKSD WLRGLKENVI IGRLIPAGTG FASQNDFVDE GTSRSPNGYS NVVTNDNGAG 1260
LSSRTYDDLD GSEILDDQTA RAFTEGKSNR KDIISGDELI SDDTPIPSDV QGKAPVIDDD 1320
AMIDDNWMKD Q 1331 |
| GO:0003677 F:DNA binding IEA:UniProtKB-HAMAP GO:0003899 F:DNA-directed RNA polymerase activity IEA:UniProtKB-HAMAP GO:0006351 P:transcription, DNA-templated IEA:UniProtKB-HAMAP |
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