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 Q87AQ6

Entry ID Method Resolution Chain Position Source
AF-Q87AQ6-F1 Predicted AlphaFoldDB

No variants for Q87AQ6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87AQ6

No associated diseases with Q87AQ6

No regional properties for Q87AQ6

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q87AQ6

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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
MPKHLLIVES PAKAKTINKY LGKDFTVLAS YGHVRDLVPK EGAVDPENGF AMRYDLIDKN
70 80 90 100 110 120
EKHVEAITKA AKTADSIYLA TDPDREGEAI SWHISEILKE RGLLKDKPMQ RIVFTEITPR
130 140 150 160 170 180
AIKEAIQKPR MIASDLVDAQ QARRALDYLV GFNLSPVLWR KVQRGLSAGR VQSPALRMIV
190 200 210 220 230 240
EREEEIEAFI TREYWSIHAE CTHPAQHFSA KLIKLDGKKF EQFTITDSDT AAAAQRRIQQ
250 260 270 280 290 300
AAQGRLHITD VTNKERKRRP APPFITSTLQ QEASRKLGFT TRKTMQIAQK LYEGIALGEE
310 320 330 340 350 360
GSVGLITYMR TDSVNLSLDA LSEIRDIIAR DYGTNALPDK PNVYTTKSKN AQEAHEAVRP
370 380 390 400 410 420
TSALRTPTQV APYLSNEEHR LYELVWKRTV ASQMIPAILN TTSVDLAAGN EHVFRATGTT
430 440 450 460 470 480
VVVQGFLAVY EEGKDNKNAE DDDEGRKLPV MKTGENVPLE RILTEQHFTQ PPPRYTEAAL
490 500 510 520 530 540
VKALEEYGIG RPSTYASIIQ TLLFRKYVDM EGRSFRPTDI GRAVSKFLSS HFTQYVDYDF
550 560 570 580 590 600
TAHLEDELDA ISRGEEEWIP LMKKFWVPFK ELVEDKKDSL DKTDAGSVRL LGIDPTSGKE
610 620 630 640 650 660
VSARIGRFGP MVQIGTVDDE EKPRFASLRP NQSIYSISLE EAIELFKMPR VLGEDQSQQV
670 680 690 700 710 720
SVGIGRFGPF AKRGSTYVSL KSEDDPYTID LARATLLINE KEEIARNRII KDFENSQIQV
730 740 750 760 770 780
LNGRFGPYIS DGKLNGKIPK DREPASLTLE EAQQLLINTG KPARKNFSTK KTATKNETRK
790 800 810
QTTKKRTTDA KATKKVSDKP VKKQIKKRIA PNITQ