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 Q5H9U9

Entry ID Method Resolution Chain Position Source
AF-Q5H9U9-F1 Predicted AlphaFoldDB

5 variants for Q5H9U9

Variant ID(s) Position Change Description Diseaes Association Provenance
VAR_055897
rs12507582
CA3134966
336 C>Y No ClinGen
UniProt
1000Genomes
ESP
ExAC
TOPMed
dbSNP
gnomAD
CA3134952
rs10029536
VAR_055898
355 N>K No ClinGen
UniProt
1000Genomes
ESP
ExAC
TOPMed
dbSNP
gnomAD
rs13151700
VAR_055899
CA3134905
409 V>L No ClinGen
UniProt
1000Genomes
ESP
ExAC
TOPMed
dbSNP
gnomAD
CA3134745
rs2319850
VAR_055900
583 A>T No ClinGen
UniProt
1000Genomes
ESP
ExAC
TOPMed
dbSNP
gnomAD
CA3134318
rs17540213
VAR_055901
1080 S>C No ClinGen
UniProt
1000Genomes
ESP
ExAC
TOPMed
dbSNP
gnomAD

No associated diseases with Q5H9U9

3 regional properties for Q5H9U9

Type Name Position InterPro Accession
domain Helicase, C-terminal 1205 - 1354 IPR001650
domain DEAD/DEAH box helicase domain 747 - 902 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 740 - 927 IPR014001

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 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.
double-stranded RNA binding Binding to double-stranded RNA.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.
single-stranded RNA binding Binding to single-stranded RNA.

1 GO annotations of biological process

Name Definition
defense response to virus Reactions triggered in response to the presence of a virus that act to protect the cell or organism.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGSKDHAVFF REMTQLILNE MPKAGYSSIL NDFVESNFFV IDGDSLLVTC LGVKSFKWGQ
70 80 90 100 110 120
NLHFFYLVEC YLVDLLSNGG QFTIVFFKDA EYAYFDFPEL LSLRTALILH LQHNTNIDVQ
130 140 150 160 170 180
TEFSGCLSQD WKLFLEQHYP YFLIVSEEGL SDLQTYLFNF LIIHSWGMKV NVVLSSGHES
190 200 210 220 230 240
DTLRFYAYTM ESTDRNQTFS KENETVIQSA YKSLIQHLEE IRVLVLATHF EHLKWNDMME
250 260 270 280 290 300
EAYQTLFLLQ HLWSEGSDIQ RVLCVTSCSL SLRMYHRVLV HSNCLSLQEV EDFCRLRCLC
310 320 330 340 350 360
VAFQLHLPLS QRACSRVITC SWIRNSDSFL KMNKWCEYFI LSNLNVFGCW NLNLNHVSDL
370 380 390 400 410 420
YDEQLLKNIA FYYEFESTQE PHLNLGDSIR RDYEDLWNVV SHLVKEFNVG KSFPLRTTRR
430 440 450 460 470 480
HFLRQEKSVI QEISLEKMPS VGFIPMTSAV IDEFVGDMMK DLPILKSDDP VVPSLFKQKT
490 500 510 520 530 540
SDELLHWHAQ RLLSDDYDRI KCHVDEQSRD PHVLDFLKKI QDYQQFYGKS LESISTKVIV
550 560 570 580 590 600
TQTTRPKEDS SGASGEILQN TKPHQITKKS KKKSFLKEDQ NKAQQNDDLL FSIEEEMKNN
610 620 630 640 650 660
LHSGIRKLED YLTSCASNSV KFGVEMLGLI ACFKAWKKHC RGEGKISKDL SIAVQMMKRI
670 680 690 700 710 720
HSLLERYPEI LEAEHHQYIA KCLKYLGFND LANSLDPTLI GDDKNKKKYS IDIGPARFQL
730 740 750 760 770 780
QYMGHYLIRD ERKDRDPRVQ DFIPNAWQQE LLDVVDKNES AVIVAPTSSG KTYASYYCME
790 800 810 820 830 840
KVLRESDVGV VVYVAPAKSL VGQVAATVEN RFTKTLPAGR TLCGAFTRDY CHNVLNCQVL
850 860 870 880 890 900
ITVPECFEIL LLAPHRQKWV ERIRYVIFDE VHYLGREVGA KFWELLLVII RCPFLVLSAT
910 920 930 940 950 960
INNPNLLTKW LQSVKQYWKQ ADKIMEEKCI SEKQADKCLN FLQDHSYKNQ SYEVRLVLYG
970 980 990 1000 1010 1020
ERYNDLEKHI CSVKHDDVYF DHFHPCAALT TDIIEKYGFP PDLTLTPQES IQLYDTMAQV
1030 1040 1050 1060 1070 1080
WETWPRAQEL CPEEFILFKN KIVIKKLDAR KYEENLKAEL TNWIKNGQVK KVKRVLKNLS
1090 1100 1110 1120 1130 1140
PDSLSSSKDM VKMFPLLVEK LRQMDKLPAI FFLFKNDDVG KRAGSVCTFL EKTETKSHPH
1150 1160 1170 1180 1190 1200
TECHSYVFAI DEVLEKVRKT QKRITKKNPK KAEKLERKKV YRAEYINFLE NLKILEISED
1210 1220 1230 1240 1250 1260
CTYADVKALH TEITRNKDST LERVLPRVRF TRHGKELKAL AQRGIGYHHS SMYFKEKEFV
1270 1280 1290 1300 1310 1320
EILFVKGLIR VVTATETLAL GIHMPCKSVV FAQDSVYLDA LNYRQMSGRA GRRGQDLLGN
1330 1340 1350 1360 1370 1380
VYFFDIPLPK IKRLLASSVP ELRGQFPLSI TLVLRLMLLA SKGDDPEDAK AKVLSVLKHS
1390 1400 1410 1420 1430 1440
LLSFKRRRAM ETLKLYFLFS LQLLIKEDYL NKKGNPKKFA GLASYLHGHE PSNLVFVNFL
1450 1460 1470 1480 1490 1500
KRGLFHNLCK PAWKGSQQFS QDVMEKLVLV LANLFGRKYI PAKFQNANLS FSQSKVILAE
1510 1520 1530 1540 1550 1560
LPEDFKAALY EYNLAVMKDF ASFLLIASKS VNMKKEHQLP LSRIKFTGKE CEDSQLVSHL
1570 1580 1590 1600 1610 1620
MSCKKGRVAI SPFVCLSGNT DNDLLRPETI NQVILRTVGV SGTQAPLLWP WKLDNRGRRM
1630 1640 1650 1660 1670 1680
PLNAYVLNFY KHNCLTRLDQ KNGMRMGQLL KCLKDFAFNI QAISDSLSEL CENKRDNVVL
1690 1700
AFKQLSQTFY EKLQEMQIQM SQNHLE