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 Q8C5W4

Entry ID Method Resolution Chain Position Source
AF-Q8C5W4-F1 Predicted AlphaFoldDB

65 variants for Q8C5W4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389432612 19 L>Q No EVA
rs3389464049 37 I>M No EVA
rs3389452399 39 N>K No EVA
rs3389412260 71 V>I No EVA
rs3389446488 97 I>N No EVA
rs3389458700 101 G>V No EVA
rs3389457114 124 T>I No EVA
rs3389452343 137 E>G No EVA
rs3389450768 189 T>A No EVA
rs3389447533 230 Q>* No EVA
rs3389402863 231 E>* No EVA
rs3412660074 268 C>* No EVA
rs3389366608 274 P>L No EVA
rs3389447504 280 T>K No EVA
rs257698185 282 H>R No EVA
rs3389446412 300 Q>* No EVA
rs3389470245 311 S>G No EVA
rs3389464107 321 G>C No EVA
rs3407647653 322 G>E No EVA
rs3407506412 323 D>N No EVA
rs3389421376 329 R>G No EVA
rs3389447509 330 V>M No EVA
rs3407582200 332 L>S No EVA
rs3389366654 334 Q>R No EVA
rs3389402835 347 D>N No EVA
rs224888523 358 Q>R No EVA
rs3406677471 391 I>F No EVA
rs3389447528 425 H>R No EVA
rs3389446459 437 R>L No EVA
rs3389464082 468 F>L No EVA
rs3389443499 483 L>* No EVA
rs3389447558 496 T>I No EVA
rs13482953 521 I>V No EVA
rs3413096497 528 N>S No EVA
rs3389402873 573 R>SE* No EVA
rs3389366561 574 K>R No EVA
rs3389401356 579 K>N No EVA
rs3389446448 584 I>T No EVA
rs3389446440 593 L>I No EVA
rs246223033 601 P>S No EVA
rs3389458712 603 S>Y No EVA
rs229039197 618 H>R No EVA
rs260339177 619 V>A No EVA
rs243979134 622 T>M No EVA
rs3389431871 628 P>T No EVA
rs227349207 647 N>D No EVA
rs265274713 652 F>S No EVA
rs33493422 674 L>P No EVA
rs257100768 683 P>T No EVA
rs241687408 700 P>L No EVA
rs222099496 721 V>L No EVA
rs3389464091 732 R>L No EVA
rs3389446478 735 E>G No EVA
rs249108141 749 M>I No EVA
rs262200061 758 K>N No EVA
rs239083917 771 S>A No EVA
rs239083917 771 S>T No EVA
rs52767231 820 E>D No EVA
rs3389421355 830 D>V No EVA
rs3389364377 837 S>R No EVA
rs3389364381 869 Q>E No EVA
rs3389458758 887 D>N No EVA
rs3389458748 906 W>C No EVA
rs3389453087 942 K>T No EVA
rs3389450727 991 I>N No EVA

No associated diseases with Q8C5W4

5 regional properties for Q8C5W4

Type Name Position InterPro Accession
domain Helicase, C-terminal 407 - 567 IPR001650
domain DEAD/DEAH box helicase domain 205 - 384 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 200 - 411 IPR014001
domain RNA helicase, DEAD-box type, Q motif 181 - 209 IPR014014
domain DDX41, DEAD-box helicase domain 192 - 397 IPR044113

Functions

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

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
heterochromatin A compact and highly condensed form of chromatin that is refractory to transcription.
nuclear matrix The dense fibrillar network lying on the inner side of the nuclear membrane.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

7 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.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
identical protein binding Binding to an identical protein or proteins.
magnesium ion binding Binding to a magnesium (Mg) ion.
protein homodimerization activity Binding to an identical protein to form a homodimer.
zinc ion binding Binding to a zinc ion (Zn).

8 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
chromatin remodeling A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication.
double-strand break repair involved in meiotic recombination The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix that contributes to reciprocal meiotic recombination.
gamete generation The generation and maintenance of gametes in a multicellular organism. A gamete is a haploid reproductive cell.
homologous chromosome pairing at meiosis The meiotic cell cycle process where side by side pairing and physical juxtaposition of homologous chromosomes is created during meiotic prophase. Homologous chromosome pairing begins when the chromosome arms begin to pair from the clustered telomeres and ends when synaptonemal complex or linear element assembly is complete.
negative regulation of gene expression, epigenetic An epigenetic process that silences gene expression at specific genomic regions through chromatin remodelling either by modifying higher order chromatin fiber structure, nucleosomal histones, or the DNA.
negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Any process that stops, prevents, or reduces the frequency, rate or extent of single stranded viral RNA replication via double stranded DNA intermediate.
positive regulation of DNA methylation-dependent heterochromatin assembly Any process that increases the rate, frequency, or extent of DNA methylation-dependent heterochromatin formation.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14149 MORC3 MORC family CW-type zinc finger protein 3 Homo sapiens (Human) EV
Q8TE76 MORC4 MORC family CW-type zinc finger protein 4 Homo sapiens (Human) SS
Q9Y6X9 MORC2 ATPase MORC2 Homo sapiens (Human) PR
F7BJB9 Morc3 MORC family CW-type zinc finger protein 3 Mus musculus (Mouse) SS
Q8BMD7 Morc4 MORC family CW-type zinc finger protein 4 Mus musculus (Mouse) SS
Q69ZX6 Morc2a ATPase MORC2A Mus musculus (Mouse) PR
10 20 30 40 50 60
MAFTNYSTLN RAQLTFDYLH TNSTTHAFLF GALAELIDNA RDADATRIDI YAEKREDLQG
70 80 90 100 110 120
GFMLCFLDNG VGMDPNDVIN VIQFGKSAKR TPESTQIGRY GNGLKSGSMR IGKDFILFTK
130 140 150 160 170 180
KENTMSCLFL SRTFHEEEGI DEVIVPLPTW NSQTREPVTD NMEKFAIETE LIYKYSPFHT
190 200 210 220 230 240
EEEVMTQFTK ISGTSGTLVV IFNLKLTDNG EPELDVTSNP KDIRMAEISQ EGVKPERHSF
250 260 270 280 290 300
CAYAAVLYID PRMRIFIHGH KVQTKKLCCC LYKPRKYTFT SHRFKTRAEQ EVKKADQVAQ
310 320 330 340 350 360
LAEEKAREAE SKARTLEIHM GGDITRDSRV MLRQVQNTAI TLRREADVKK RIRDAKQQAL
370 380 390 400 410 420
KEPKELTFVF GVNIEHRDHD GMFIYNCSRL IKMYEKVGPQ LEKGMVCGGV VGVIDVPYLV
430 440 450 460 470 480
LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIEIAQHG IIKFWDEFGY LSANWNRPPS
490 500 510 520 530 540
DELHFKRKRA MQVPTTIQCD LCLKWRTLPF QLSAVEEGYP INWVCSMNPD PEQDQCEAFE
550 560 570 580 590 600
LKQKIPLGIL KKAPKTQEER QKQLTEKIQQ EQRKLKALKK IKPIHSQSDL KKLPLEVTSR
610 620 630 640 650 660
PFSKYPAHIF QGPQSSFHVV KTNARRRPQS RHAPFRQLQR SSIICTNPKP PFLVDKTEAV
670 680 690 700 710 720
LLQPPETPQK SVSLLVKTIP QPPPLVQSLS PSVVPKSNNP WKVETPQIMN TPVAEMPYVP
730 740 750 760 770 780
VNPSLVICDH KRSPEVSDEI EDEDRRKRMC KRGRFTVKKE KIQASELSDS SGEENPVDLK
790 800 810 820 830 840
TAQKDKGLYV EVRMMGECYK GHVTAVEVGD NVVWWKVKFE DMPKDSTPRD CWVEKGSENV
850 860 870 880 890 900
WLVKPSPEYQ STDEQQEDRK GEEDTVVQQA LALQQTSTSE CFCTEPDTTA STANHKTIDL
910 920 930 940 950 960
LVQILWNCLH YFMPLSFPIS KKELGAMNSE ELLSLPLKEC FKQYEVGLQN LCRSYQRCAD
970 980 990 1000 1010 1020
SQAKVSEESL RISQKKLQET EEKLQKLRTN IQTLLQMAQQ GINIRADDEL DAYIEDLVSS
DD