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 P43704

Entry ID Method Resolution Chain Position Source
AF-P43704-F1 Predicted AlphaFoldDB

No variants for P43704

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P43704

No associated diseases with P43704

7 regional properties for P43704

Type Name Position InterPro Accession
domain DNA topoisomerase, type IA, domain 2 128 - 223 IPR003601
domain DNA topoisomerase, type IA, DNA-binding domain 289 - 567 IPR003602
domain TOPRIM domain 1 - 134 IPR006171
domain DNA topoisomerase, type IA, central 98 - 111 IPR013497-1
domain DNA topoisomerase, type IA, central 156 - 612 IPR013497-2
active_site DNA topoisomerase, type IA, active site 326 - 341 IPR023406
domain DNA topoisomerase 3-like, TOPRIM domain 1 - 149 IPR034144

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.
magnesium ion binding Binding to a magnesium (Mg) 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
MRLFIAEKPS LARAIADVLP KPHQRGDGFI KCGDNDVVTW CVGHLLEQAE PDAYDPKFKQ
70 80 90 100 110 120
WRLEHLPIIP EKWQLLPRKE VKKQLSVVEK LIHQADTLVN AGDPDREGQL LVDEVFSYAN
130 140 150 160 170 180
LSAEKRDKIL RCLISDLNPS AVEKAVKKLQ PNRNFIPLAT SALARARADW LYGINMTRAY
190 200 210 220 230 240
TIRGRQTGYD GVLSVGRVQT PVLGLIVRRD LEIEHFQPKD FFEVQAWVNP ESKEEKTPEK
250 260 270 280 290 300
STALFSALWQ PSKACEDYQD DDGRVLSKGL AEKVVKRITN QPAEVTEYKD VREKETAPLP
310 320 330 340 350 360
YSLSALQIDA AKRFGMSAQA VLDTCQRLYE THRLITYPRS DCRYLPEEHF AERHNVLNAI
370 380 390 400 410 420
STHCEAYQVL PNVILTEQRN RCWNDKKVEA HHAIIPTAKN RPVNLTQEER NIYSLIARQY
430 440 450 460 470 480
LMQFCPDAEY RKSKITLNIA GGTFIAQARN LQTAGWKELL GKEDDTENQE PLLPIVKKGQ
490 500 510 520 530 540
ILHCERGEVM SKKTQPPKPF TDATLLSAMT GIARFVQDKE LKKILRETDG LGTEATRAGI
550 560 570 580 590 600
IELLFKRGFL TKKGRNIHST ETGRILIQAL PNIATQPDMT AHWESQLTDI SQKQATYQQF
610 620 630 640 650
MHNLNQILPD LVRFVDLNAL RQLSRIKMIK SDRAKPKSAV KKSSKSNGET D