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

0 structures for Q9WAB1

Entry ID Method Resolution Chain Position Source

No variants for Q9WAB1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9WAB1

No associated diseases with Q9WAB1

1 regional properties for Q9WAB1

Type Name Position InterPro Accession
domain Zinc finger C2H2-type 183 - 203 IPR013087

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Virion
  • Found in the inner capsid (120 copies)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
viral inner capsid The inner layer of a double or triple concentric icosahedral capsid. Inner capsids are part of reoviridae and cystoviridae virions.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
metal ion binding Binding to a metal ion.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

1 GO annotations of biological process

Name Definition
7-methylguanosine mRNA capping Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKRIPRKTRG KSSGKGNDST ERADDGSAQL RDKQSSKVTQ NVKEPGTTLK EQYKTRPSLQ
70 80 90 100 110 120
TVQKATENAE LPMQTNDEGA VDKKGNTKGD KTNEHVEAEV NAADATKRQA KDTDKQKAQV
130 140 150 160 170 180
TYNDTGINNA NELSRSGNVD NEGGDNQKPM TTRIAEATSA IISKHPARVG LPPTASSGHG
190 200 210 220 230 240
YQCHVCSAVL FSPLDLDAHV ASHGLHGNMT LTSSEIQRHI TEFISSWQNH PIVQVSADVE
250 260 270 280 290 300
NKKTAQLLHA DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA
310 320 330 340 350 360
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN NETLSVRGAN PLMFRANVLH
370 380 390 400 410 420
MLLEFVLDNL YINKHTGFSQ DHTPFTEGAN LRSLPGPDAE KWYAIMYPTR MGTPNVSKIC
430 440 450 460 470 480
NFVASCVRNR VGRFDRAQMM NGAMSEWVDV FETSDALTVS IRGRWMARLA RMNINPTEIE
490 500 510 520 530 540
WALTECAHGY VTVTSPYAPS VNRLMPYRVS NAERQISQII RIMNIGNNAT VIQPVLQDIS
550 560 570 580 590 600
VLLQRISPLQ IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY
610 620 630 640 650 660
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM TLANMMVGFE
670 680 690 700 710 720
TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP ILRQWAEIIH RYWPNPSQIR
730 740 750 760 770 780
FGAPNVFGSA NLFTPPEVLL LPIDHQPANV TTPTLDFTNE LTNWRARVCE LMKNLVDNQR
790 800 810 820 830 840
YQPGWTQSLV SSMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR
850 860 870 880 890 900
DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPSDLVTNVW
910 920 930 940 950 960
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LITLVAQISE TQYPVDRYLD WIPSLRASAA
970 980 990 1000 1010 1020
TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMSQLAIQ YQQYNGRTFN VIPEMPGSVV
1030 1040 1050 1060 1070 1080
TDCVQLTAEV FNHEYNLFGI ARGDIIIGRV QSTHLWSPLA PPPDLVFDRD TPGVHVFGRD
1090 1100 1110 1120 1130 1140
CRISFGMNGA APMIRDETGM MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE
1150 1160 1170 1180 1190 1200
MGAYPYMLHY YDPRQYANAW NLTSAWLEEI SPTSIPSVPF MVPISSDHDI SSAPAVQYII
1210 1220 1230 1240 1250 1260
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV VDLYNVVTRY
1270
AYETPPITAV VMGVP