CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005071
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase III subunit RPC2 
Protein Synonyms/Alias
 RNA polymerase III subunit C2; C128; DNA-directed RNA polymerase III 130 kDa polypeptide 
Gene Name
 RET1 
Gene Synonyms/Alias
 RPC128; RPC2; YOR207C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
957PSRMTVGKMIELISGubiquitination[1]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). 
Sequence Annotation
 ZN_FING 1095 1110 C4-type (By similarity).
 METAL 1095 1095 Zinc (By similarity).
 METAL 1098 1098 Zinc (By similarity).
 METAL 1107 1107 Zinc (By similarity).
 METAL 1110 1110 Zinc (By similarity).  
Keyword
 Complete proteome; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1149 AA 
Protein Sequence
MVAATKRRKT HIHKHVKDEA FDDLLKPVYK GKKLTDEINT AQDKWHLLPA FLKVKGLVKQ 60
HLDSFNYFVD TDLKKIIKAN QLILSDVDPE FYLKYVDIRV GKKSSSSTKD YLTPPHECRL 120
RDMTYSAPIY VDIEYTRGRN IIMHKDVEIG RMPIMLRSNK CILYDADESK MAKLNECPLD 180
PGGYFIVNGT EKVILVQEQL SKNRIIVEAD EKKGIVQASV TSSTHERKSK TYVITKNGKI 240
YLKHNSIAEE IPIAIVLKAC GILSDLEIMQ LVCGNDSSYQ DIFAVNLEES SKLDIYTQQQ 300
ALEYIGAKVK TMRRQKLTIL QEGIEAIATT VIAHLTVEAL DFREKALYIA MMTRRVVMAM 360
YNPKMIDDRD YVGNKRLELA GQLISLLFED LFKKFNNDFK LSIDKVLKKP NRAMEYDALL 420
SINVHSNNIT SGLNRAISTG NWSLKRFKME RAGVTHVLSR LSYISALGMM TRISSQFEKS 480
RKVSGPRALQ PSQFGMLCTA DTPEGEACGL VKNLALMTHI TTDDEEEPIK KLCYVLGVED 540
ITLIDSASLH LNYGVYLNGT LIGSIRFPTK FVTQFRHLRR TGKVSEFISI YSNSHQMAVH 600
IATDGGRICR PLIIVSDGQS RVKDIHLRKL LDGELDFDDF LKLGLVEYLD VNEENDSYIA 660
LYEKDIVPSM THLEIEPFTI LGAVAGLIPY PHHNQSPRNT YQCAMGKQAI GAIAYNQFKR 720
IDTLLYLMTY PQQPMVKTKT IELIDYDKLP AGQNATVAVM SYSGYDIEDA LVLNKSSIDR 780
GFGRCETRRK TTTVLKRYAN HTQDIIGGMR VDENGDPIWQ HQSLGPDGLG EVGMKVQSGQ 840
IYINKSVPTN SADAPNPNNV NVQTQYREAP VIYRGPEPSH IDQVMMSVSD NDQALIKVLL 900
RQNRRPELGD KFSSRHGQKG VCGIIVKQED MPFNDQGIVP DIIMNPHGFP SRMTVGKMIE 960
LISGKAGVLN GTLEYGTCFG GSKLEDMSKI LVDQGFNYSG KDMLYSGITG ECLQAYIFFG 1020
PIYYQKLKHM VLDKMHARAR GPRAVLTRQP TEGRSRDGGL RLGEMERDCV IAYGASQLLL 1080
ERLMISSDAF EVDVCDKCGL MGYSGWCTTC KSAENIIKMT IPYAAKLLFQ ELLSMNIAPR 1140
LRLEDIFQQ 1149 
Gene Ontology
 GO:0005666; C:DNA-directed RNA polymerase III complex; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032549; F:ribonucleoside binding; IEA:InterPro.
 GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IDA:SGD. 
Interpro
 IPR015712; DNA-dir_RNA_pol_su2.
 IPR007120; DNA-dir_RNA_pol_su2_6.
 IPR007121; RNA_pol_bsu_CS.
 IPR007644; RNA_pol_bsu_protrusion.
 IPR007642; RNA_pol_Rpb2_2.
 IPR007645; RNA_pol_Rpb2_3.
 IPR007646; RNA_pol_Rpb2_4.
 IPR007647; RNA_pol_Rpb2_5.
 IPR007641; RNA_pol_Rpb2_7.
 IPR014724; RNA_pol_RPB2_OB-fold. 
Pfam
 PF04563; RNA_pol_Rpb2_1
 PF04561; RNA_pol_Rpb2_2
 PF04565; RNA_pol_Rpb2_3
 PF04566; RNA_pol_Rpb2_4
 PF04567; RNA_pol_Rpb2_5
 PF00562; RNA_pol_Rpb2_6
 PF04560; RNA_pol_Rpb2_7 
SMART
  
PROSITE
 PS01166; RNA_POL_BETA 
PRINTS