Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q86AQ5

Entry ID Method Resolution Chain Position Source
AF-Q86AQ5-F1 Predicted AlphaFoldDB

No variants for Q86AQ5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q86AQ5

No associated diseases with Q86AQ5

8 regional properties for Q86AQ5

Type Name Position InterPro Accession
domain RNA polymerase, alpha subunit 351 - 517 IPR000722
domain RNA polymerase, N-terminal 242 - 545 IPR006592
domain RNA polymerase Rpb1, domain 3 520 - 691 IPR007066
domain RNA polymerase Rpb1, domain 1 12 - 349 IPR007080
domain RNA polymerase Rpb1, domain 5 829 - 1385 IPR007081
domain RNA polymerase Rpb1, domain 4 717 - 822 IPR007083
domain DNA-directed RNA polymerase III subunit RPC1, N-terminal 22 - 879 IPR035697
domain DNA-directed RNA polymerase III subunit RPC1, C-terminal 1091 - 1430 IPR035698

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.

3 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.

1 GO annotations of biological process

Name Definition
transcription by RNA polymerase III The synthesis of RNA from a DNA template by RNA polymerase III, originating at an RNAP 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
MIELLKEDDA PKKIGHIQFG LLSEDDIVRL SHVQIVNREL FDLVKRKPTP YGVLDNKLGT
70 80 90 100 110 120
SDKQAMCTTC GLSIVDCVGH FGYIKLQLPV FHIGYLKNIM NILQMICKSC STILLNEEKK
130 140 150 160 170 180
QYYLRKMRNK KMDNLQRKSL LKKIFLECRK TKECLKCGST NGMIKKSGAF KIIHEKYKGK
190 200 210 220 230 240
TESLQDYYAL YDDAIKYNPE MKSHIKKAQD DLNPLVALNL FKKISYQDIE IMNMDPVIGR
250 260 270 280 290 300
PERLILTYML VPPVSIRPSV PMDGGSGTNE DDLTMKLSEI LHINEHIRSN VDRAEMSAIM
310 320 330 340 350 360
EDWDYLQASC AIYINSDVPG LPLQMKPTKA VRGLSQRLKG KTGRFRGNLS GKRVDFSGRT
370 380 390 400 410 420
VISPDPNLNI DEVAVPQLIA LTMTYPERVT DYNIERLQKY VINGPDRHPG ANYIIYADGV
430 440 450 460 470 480
KKWLKFGNRE KFAAELKIGD IVERHIIDGD IMLFNRQPSL HKLSIMSHKA RVMPWRTLRF
490 500 510 520 530 540
NECVCTPYNA DFDGDEMNIH LPQTEEARAE ATILMGVTNN LITPRNGEPL VAATQDFLTA
550 560 570 580 590 600
SYLISRRDAF YERYRFALMC THFADANEHI DLPPPAILKP VELWTGKQIF EVLLRPSVKS
610 620 630 640 650 660
HVLCNFETRS RTYSKNLYMC PKDGYVYFRN SELMCGSIDK SIIGGGNKNS LFHILMRDFS
670 680 690 700 710 720
PTIAANCMTR LAKLCARFLG DQGFSIGIPD IKPAEDLDRK KREIIETAYK KCAVFLKDYE
730 740 750 760 770 780
SGSLQLSSGC SMEQTFEAKM NQTLSQIRDD CGKLCVNDLP NYNSPLIMGL CGSKGSNINI
790 800 810 820 830 840
AQMICCVGQQ IVNGTRIPNG FTNRTTPHFK HFAKNPKSKG FVSNSFYTGM IPTEFFFHTM
850 860 870 880 890 900
GGREGLVDTA VKTAETGYMQ RRLMKALEDL STHYDYTVRD SIGGIVQFIY GDDGLDPAGM
910 920 930 940 950 960
EAKDRPVDFL RAMMSVKSTR QCRNEPEMKP FEIRKLVESI IDSSKFEACT DLFKNEIRVF
970 980 990 1000 1010 1020
FNGNEKTKGY IQELISLRKQ FKLSSFDLND NEDEIIIEDN SPMDISTTTT TTTTTTTNNA
1030 1040 1050 1060 1070 1080
VKITNITTDI EMNESNKEEN DKIEKERIEK EKESKRLKLL GERFANEHVV NQIHRITKTQ
1090 1100 1110 1120 1130 1140
IELFLDICLD KYSRARIEPG TAVGAIGAQS IGEPGTQMTL KTFHFAGVAS MNVTLGVPRI
1150 1160 1170 1180 1190 1200
KEIINAAKNI STPIITASLN CDYDIRSARI VAGRIEKTTL GHVATHIKEV VKRAGCYLSI
1210 1220 1230 1240 1250 1260
KIDKNFVDSL QLEINSKTIS QSIASTKGLK LKPEQITTNG DYKLRIVPPA NIREGSLYYL
1270 1280 1290 1300 1310 1320
QFLKNNLPAV IVKGIPTVNR VVISKVDEKQ ERYQLLVEGY DLRAVMATPG IKGTHTTSNH
1330 1340 1350 1360 1370 1380
IMECENTLGI ETARNTIMSE IDMIMTSHGM SIDIRHVMLL ADLMSFKGEI LGITRFGIAK
1390 1400 1410 1420 1430 1440
MKESVLMLAS FEKTTDHLFD AAVHHRQDDI VGVSECIIMG VVIPLGTGLF KLLRKSNKNN
LPKKSLLLQD