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 Q9CP53

Entry ID Method Resolution Chain Position Source
AF-Q9CP53-F1 Predicted AlphaFoldDB

No variants for Q9CP53

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9CP53

No associated diseases with Q9CP53

7 regional properties for Q9CP53

Type Name Position InterPro Accession
domain DNA topoisomerase, type IA, domain 2 128 - 223 IPR003601
domain DNA topoisomerase, type IA, DNA-binding domain 294 - 572 IPR003602
domain TOPRIM domain 1 - 135 IPR006171
domain DNA topoisomerase, type IA, central 98 - 111 IPR013497-1
domain DNA topoisomerase, type IA, central 156 - 617 IPR013497-2
active_site DNA topoisomerase, type IA, active site 331 - 346 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 KCGADDYVTW CIGHLLEQAE PDAYDPKFKQ
70 80 90 100 110 120
WRLEHLPIIP EKWQLIPRKD VHKQLTIVEK LIHQADILIN AGDPDREGQL LVDEVFSYAN
130 140 150 160 170 180
LSVDKLNQIQ RCLISDLNPS AVEKAVNKLQ SNRNFIPLAT SALARARADW LYGINMTRAY
190 200 210 220 230 240
TLRGRQAGYQ GVLSVGRVQT PVLGLIVRRD LEIENFKPQD FFEVLAHIQA ETPEKITALS
250 260 270 280 290 300
AQEKANIPQF KALWQPSKAC EDYQDEEGRV LSLGLVENVV KRIAQQPAEV VEYVDKREHE
310 320 330 340 350 360
SAPLPYSLSA LQIDAAKRYG LSAQEVLDIC QRLYETHRLI TYPRSDCRYL PEEHFGERTK
370 380 390 400 410 420
VFQAISRHIS DYQPLPDILN PEQKNRCWND KKVEAHHAII PTAKNTPVNL NQREWQIYHL
430 440 450 460 470 480
IARQYLMQFC PDAEYRKSKI TLNIAGGTFI AQARNLQVAG WKQLLGKEDS DEQQEPLLPV
490 500 510 520 530 540
VKKGQILFCE KGEIVSKKTQ PPKPFTDATL LSAMTGIARF VQDKELKKIL RETDGLGTEA
550 560 570 580 590 600
TRAGIIELLF KRGFLYKKGR NIHSTETGRI LIQALPDVAT QPDMTAHWES QLTSISQKEM
610 620 630 640
SYQQFMSTLT NFLPELMRYV NFAALRQLSQ VEKPQSFSKK MSAKSKKRPT