P25167

PR
Gene name
RpIII128 (RP128, CG8344)
Protein name
DNA-directed RNA polymerase III subunit RPC2
Names
RNA polymerase III subunit C2, DNA-directed RNA polymerase III 128 kDa polypeptide, C128
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG8344
EC number
2.7.7.6: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-49 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P25167

Entry ID Method Resolution Chain Position Source
AF-P25167-F1 Predicted AlphaFoldDB

No variants for P25167

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P25167

No associated diseases with P25167

8 regional properties for P25167

Type Name Position InterPro Accession
domain DNA-directed RNA polymerase, subunit 2, hybrid-binding domain 675 - 1047 IPR007120
conserved_site RNA polymerase, beta subunit, conserved site 900 - 912 IPR007121
domain RNA polymerase Rpb2, domain 7 1049 - 1134 IPR007641
domain RNA polymerase Rpb2, domain 2 188 - 370 IPR007642
domain RNA polymerase, beta subunit, protrusion 46 - 420 IPR007644
domain RNA polymerase Rpb2, domain 3 445 - 509 IPR007645
domain RNA polymerase Rpb2, domain 4 546 - 607 IPR007646
domain RNA polymerase Rpb2, domain 5 628 - 663 IPR007647

Functions

Description
EC Number 2.7.7.6 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
RNA polymerase III complex RNA polymerase III, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces 5S rRNA, tRNAs and some of the small nuclear RNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerase I and others of which are also found in RNA polymerases I and II. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.

4 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-directed 5'-3' RNA polymerase activity Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Utilizes a DNA template, i.e. the catalysis of DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. Can initiate a chain 'de novo'.
metal ion binding Binding to a metal ion.
ribonucleoside binding Binding to a ribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to ribose.

1 GO annotations of biological process

Name Definition
tRNA transcription by RNA polymerase III The synthesis of transfer RNA (tRNA) from a DNA template by RNA polymerase III (Pol III), originating at a Pol III promoter.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVELKMGDHN VEATTWDPGD SKDWSVPIKP LTEKWKLVPA FLQVKGLVKQ HIDSFNHFIN
70 80 90 100 110 120
VDIKKIVKAN ELVTSGADPL FYLKYLDVRV GKPDIDDGFN ITKATTPHEC RLRDTTYSAP
130 140 150 160 170 180
ITVDIEYTRG TQRIKRNNLL IGRMPLMLRC SNCALTGKSE FELSKLNECP LDPGGYFVVR
190 200 210 220 230 240
GQEKVILIQE QLSWNKMLTE DFNGVVQCQV TSSTHEKKSR TLVLSKHGKY YLKHNSMTDD
250 260 270 280 290 300
IPIVVIFKAL GVVSDQEIQS LIGIDSKSQN RFGASLIDAY NLKVFTQQRA LEYMGSKLVV
310 320 330 340 350 360
KRFQSATTKT PSEEARELLL TTILAHVPVD NFNLQMKAIY VSMMVRRVMA AELDKTLFDD
370 380 390 400 410 420
RDYYGNKRLE LAGSLLSMMF EDLFKRMNWE LKTIADKNIP KVKAAQFDVV KHMRAAQITA
430 440 450 460 470 480
GLESAISSGN WTIKRFKMER AGVTQVLSRL SYISALGMMT RVNSQFEKTR KVSGPRSLQP
490 500 510 520 530 540
SQWGMLCPSD TPEGEACGLV KNLALMTHIT TEVEERPVMI VAFNAGVEDI REVSGNPINN
550 560 570 580 590 600
PNVFLVFING NVLGLTLNHK HLVRNLRYMR RKGRMGSYVS VHTSYTQRCI YIHTDGGRLC
610 620 630 640 650 660
RPYVIVENRR PLVKQHHLDE LNRGIRKFDD FLLDGLIEYL DVNEENDSFI AWNEDQIEDR
670 680 690 700 710 720
TTHLEIEPFT LLGVCAGLVP YPHHNQSPRN TYQCAMGKQA MGMIGYNQKN RIDSLMYNLV
730 740 750 760 770 780
YPHAPMVKSK TIELTNFDKL PAGQNATVAV MSYSGYDIED ALILNKASID RGYGRCLVYK
790 800 810 820 830 840
NSKCTVKRYA NQTFDRIMGP MKDALTNKVI FKHDVLDTDG IVAPGEQVQN KQIMINKEMP
850 860 870 880 890 900
AVTSMNPLQG QSAQVPYTAV PISYKGPEPS YIERVMVSAN AEEDFLIKIL LRQTRIPEIG
910 920 930 940 950 960
DKFSSRHGQK GVTGLIVEQE DMPFNDFGIC PDMIMNPHGF PSRMTVGKTL ELLGGKAGLL
970 980 990 1000 1010 1020
EGKFHYGTAF GGSKVEDIQA ELERHGFNYV GKDFFYSGIT GTPLEAYIYS GPVYYQKLKH
1030 1040 1050 1060 1070 1080
MVQDKMHARA RGPKAVLTRQ PTQGRSREGG LRLGEMERDC LISYGASMLI MERLMISSDA
1090 1100 1110 1120 1130
FEVDVCRTCG RMAYCSWCHF CQSSANVSKI SMPYACKLLF QELTSMNVVP KMILENY