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 O67137

Entry ID Method Resolution Chain Position Source
AF-O67137-F1 Predicted AlphaFoldDB

No variants for O67137

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O67137

No associated diseases with O67137

6 regional properties for O67137

Type Name Position InterPro Accession
domain DNA gyrase B subunit, C-terminal 579 - 640 IPR002288
domain Histidine kinase/HSP90-like ATPase 40 - 184 IPR003594
domain TOPRIM domain 429 - 543 IPR006171
domain DNA topoisomerase, type IIA, subunit B, domain 2 232 - 401 IPR013506
conserved_site DNA topoisomerase, type IIA, conserved site 433 - 441 IPR018522
domain DNA gyrase subunit B, TOPRIM domain 430 - 542 IPR034160

Functions

Description
EC Number 5.6.2.2 Enzymes altering nucleic acid conformation
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2.
metal ion binding Binding to a metal ion.

2 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.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKRQSQTPQ EYTAEAIKAV SGLEHVRLRP AMYIGDIGER GLHHLIWEIL DNAVDEAVAG
70 80 90 100 110 120
YARNISVTIH RDNSVTVEDD GRGIPVDIHP ETGKPAVEMV FTMLGAGGKF EKKVYTYSGG
130 140 150 160 170 180
LHGVGASVVN ALSEWLIVEV YRDGKIYRMA FKRGEVVEPL HVVGETKKRG TKVSFKPDPE
190 200 210 220 230 240
IFETTEIKFD IVEKRVRELA YLNPEVKFEL TDERLGKHLI YKFDRGIEEL VKYLNEGKEP
250 260 270 280 290 300
LFKDIIRIQG EKEGVIVDIA FQYVKDYKER IESFVNNIKT VEGGTHVTGF RSGLSKAVIR
310 320 330 340 350 360
MAQGLKLAKE LKKSFTGEDV REGLTAVVAC KVPNPQFEGQ TKTKLGNQNV KQIVESITYD
370 380 390 400 410 420
FLTSYFEKKR DVLKAIVEKA IEAALAREAA KKAKELVRRK SPLEEGVLPG KLADCSETDP
430 440 450 460 470 480
SKCEIFLVEG DSAGGSAKQA RDRRYQAILP LRGKIINVEK ARIDKVLSND EIKAIVSALG
490 500 510 520 530 540
CGIGEDLDLK KLRYHKIILM TDADVDGSHI RTLLLTFFYR FMPKLVEEGY VYIAEPPLYR
550 560 570 580 590 600
VKKGKKEIYI KDDKEFEHFL LNEIREKGRL VDAREKEFKG EELVRLLIDL KDYEDAYRAL
610 620 630 640 650 660
VKSKGENLVN FLLTHRVREE DLRNPARVKE ITHLMEEELG DYRVDTKYNE LEGAYDIIFY
670 680 690 700 710 720
DDKLGTKTII DVNFLSSLSY REVLEGIHLH LPVQVFFENK KVEINSLGEI YDKFMDFARS
730 740 750 760 770 780
GMEVQRYKGL GEMNPEQLWE TTMNPKTRRL KKVKIEDAAE ADRIFTILMG EQVEPRREFI
790
EAYAKEVKHL DV