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 Q6FY76

Entry ID Method Resolution Chain Position Source
AF-Q6FY76-F1 Predicted AlphaFoldDB

No variants for Q6FY76

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FY76

No associated diseases with Q6FY76

6 regional properties for Q6FY76

Type Name Position InterPro Accession
domain SNF2, N-terminal 421 - 828 IPR000330
domain Helicase, C-terminal 978 - 1146 IPR001650
domain Zinc finger, RING-type 896 - 944 IPR001841
domain Helicase superfamily 1/2, ATP-binding domain 414 - 723 IPR014001
domain HIRAN domain 167 - 278 IPR014905
conserved_site Zinc finger, RING-type, conserved site 915 - 924 IPR017907

Functions

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

4 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
chromosome, telomeric region The end of a linear chromosome, required for the integrity and maintenance of the end. A chromosome telomere usually includes a region of telomerase-encoded repeats the length of which rarely exceeds 20 bp each and that permits the formation of a telomeric loop (T-loop). The telomeric repeat region is usually preceded by a sub-telomeric region that is gene-poor but rich in repetitive elements. Some telomeres only consist of the latter part (for eg. D. melanogaster telomeres).
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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-dependent chromatin remodeler activity An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling.
four-way junction DNA binding Binding to a DNA segment containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices.
four-way junction helicase activity Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis.
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Catalysis of the hydrolysis of any acid anhydride which contains phosphorus.
Y-form DNA binding Binding to a DNA segment shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end.
zinc ion binding Binding to a zinc ion (Zn).

6 GO annotations of biological process

Name Definition
double-strand break repair The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
error-free postreplication DNA repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.
error-free translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
error-prone translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
free ubiquitin chain polymerization The process of creating free ubiquitin chains, compounds composed of a large number of ubiquitin monomers. These chains are not conjugated to a protein.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDQNANQKKR FFKDELESSI ETTLTDKSSF LFEPQVDAIQ EENANDPEEQ IAQGTQESPF
70 80 90 100 110 120
IEQLRAVLPT IRLEVALALE EKYRDIDDGL DLAISEYFDQ YQTGNDDAPP SSLELQHSQE
130 140 150 160 170 180
VLTVPDNEEK DTDLQLVSVK RKREDDFMQS SQSKKPQRAN SSWKKFVGSL QVTVMVTRPT
190 200 210 220 230 240
MRPVPYGTPL IFKRSNNNVP LKKIYEQLNK KKTGLAAFVK IYSANDEREI GRVPEDIARI
250 260 270 280 290 300
VFPLLHRNEV HFKLTMIYPG DKRLSIGDNI IIQMDSFLTS TLFNRKENPT FSTQNGNGRE
310 320 330 340 350 360
RFGAIVETEQ ELEERNIRMG LIMLFDKIKL RPVKDEAKFL EKLKQDGDDN EIVDLEDDES
370 380 390 400 410 420
FGNFLSQEPL NDELPTQHQE DTMNINQLTS FYKATQSSKQ LNSLIPTTPP PELVKVELRK
430 440 450 460 470 480
YQKQGLTWML RREGISIGHD NEDKSEDDTT LLNPLWRQFQ WPRNMSWHNQ STGSENDNSN
490 500 510 520 530 540
PKLIFFYGNL HTGEFSLERP TMNSFKNGGI LSDEMGLGKT ISALSLVLMR PKDEHTTSQS
550 560 570 580 590 600
LFHQESSNLS SDDVIEIKEP ERSYAYKTTL IIVPMSLLTQ WRDEFDKVNN NAGLTCELYY
610 620 630 640 650 660
GGNVSSLKSL LIKRKNPPTV VLTTYGIVQN EWTKLSKDGT NIRSLGRTSG IFSIEFFRII
670 680 690 700 710 720
LDEGHTIRNK STITSKAVLE LSSKYRWILT GTPIINRLDD LYSLVKFLKL EPWSQIGYWK
730 740 750 760 770 780
QFITNPFEER NFKQAFDVVN AIMEPVLLRR TKQMKDTDGN PLVQLPPKEI VIEKLQLSKK
790 800 810 820 830 840
QKLIYEEFLQ RAEKTFRSGL QSGDLLKKYS TILVHILRLR QVCCDSNLIG TLDENDEDLS
850 860 870 880 890 900
SGNNKLITES VDVKTLIPDT EEEEDEVPPF ENDELDKLIE SVEAKFIDSN QLIPVECSIC
910 920 930 940 950 960
TAEPIESSSA VVTECEHVFC KECLEEYGNF QKEKSLQQKC PNCRRDINLN RCLAFEKGSD
970 980 990 1000 1010 1020
GILKLIHFDR KERPAKLNAL IRHLQQLQDS SAGEQVVVFS QFSSYLDILE SQLNEVYSSN
1030 1040 1050 1060 1070 1080
KLKVYKFDGR LSLKERTAVL EDFKVKDYAV QKVLLLSLKA GGVGLNLTCA SYAFMMDPWW
1090 1100 1110 1120 1130 1140
SPSMEDQAID RIHRIGQTNS VKVIRFVIDG SIEEKMLRIQ DRKRTLGEAM DTDEDERRKR
1150
RIEEIQMLFE S