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 Q8CSU3

Entry ID Method Resolution Chain Position Source
AF-Q8CSU3-F1 Predicted AlphaFoldDB

No variants for Q8CSU3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8CSU3

No associated diseases with Q8CSU3

No regional properties for Q8CSU3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8CSU3

Functions

Description
EC Number 5.6.2.1 Enzymes altering nucleic acid conformation
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.

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 topoisomerase type I (single strand cut, ATP-independent) activity Catalysis of a DNA topological transformation by transiently cleaving one DNA strand at a time to allow passage of another strand; changes the linking number by +1 per catalytic cycle.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
DNA topological change The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADNLVIVES PAKAKTIEKY LGKRYKVIAS MGHVRDLPRS QMGVDTEDNY EPKYITIRGK
70 80 90 100 110 120
GPVVKDLKKH AKKAKKIFLA SDPDREGEAI AWHLSKILEL EDSKENRVVF NEITKDAVKD
130 140 150 160 170 180
SFKHPRGIEM DLVDAQQARR ILDRLVGYNI SPVLWKKVKK GLSAGRVQSV ALRLVIDREN
190 200 210 220 230 240
EIRNFKPEEY WSIEGEFRYK KSKFTAKFLH YKNKPYKLNN KDDVQRITEA LNGDQFEITN
250 260 270 280 290 300
VNRKEKTRYP AHPFTTSTLQ QEAARKLNFK ARKTMMLAQQ LYEGIDLKRQ GTVGLITYMR
310 320 330 340 350 360
TDSTRISTSA KSEAQQYIND KYGEQYVSQR KSSGKQGDQD AHEAIRPTST MRTPDDMKAF
370 380 390 400 410 420
LTRDQHRLYK LIWERFVASQ MAPAILDTVA LDVTQNDIKF RANGQTIKFK GFMTLYVEAK
430 440 450 460 470 480
DDKENDKENK LPQLDKGDKV TATKIEPAQH FTQPPPRYTE ARLVKTLEEL KIGRPSTYAP
490 500 510 520 530 540
TIDTIQKRNY VKLESKRFIP TELGEIVYEQ VKEYFPEIID VEFTVNMETL LDKIAEGDMN
550 560 570 580 590 600
WRKVIGDFYN SFKQDVERAE SEMEKIEIKD EPAGEDCEVC GSPMVIKMGR YGKFMACSNF
610 620 630 640 650 660
PDCRNTKAIV KTIGVTCPKC NEGDVVERKS KKNRIFYGCS RYPECDFISW DKPVGRDCPK
670 680
CHHYLVNKKK GKSSQVVCSN CDYEEEVQK