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 Q1RIM1

Entry ID Method Resolution Chain Position Source
AF-Q1RIM1-F1 Predicted AlphaFoldDB

No variants for Q1RIM1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1RIM1

No associated diseases with Q1RIM1

2 regional properties for Q1RIM1

Type Name Position InterPro Accession
domain Helicase, superfamily 3, single-stranded DNA/RNA virus 168 - 264 IPR000605
domain Viral replication-associated protein, N-terminal 4 - 82 IPR003365

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
MKLVIVESPA KAKTINKYLG DEFKVIASFG HIRDLPSKKG SVIPDENFSM KYDISEKAGK
70 80 90 100 110 120
YVDAIIKDAK KAESVYLATD PDREGESISW HIAEVIKEKN KVKSDDFFKR VAFNEITKKA
130 140 150 160 170 180
ITHAIENPRK LDNNLVNAQQ ARRALDYLVG FTLSPLLWRK LPGCKSAGRV QSVALRLICE
190 200 210 220 230 240
REDEIERFKS EEYWDISLKM LNSNNELFTA KLTHINDQKL EKFSITNDKE AKDLTEKLKS
250 260 270 280 290 300
QNFHVDKIEK KQQKRQPQPP FITSSLQQEA ARKLGFSAKK TMQIAQKLYE GVDIGKETIG
310 320 330 340 350 360
LITYMRTDGV TLSNDAVDEI RKLINKDYGD KYLPSSPRIY KSKVKNAQEA HEAIRPTNIN
370 380 390 400 410 420
YIPNDLKEKL EKDYYKLYEL IWKRTIACQM ENVIMDLVNA TLASENKEYL ARANGSTIAF
430 440 450 460 470 480
DGFYKVYRES IDDEAEEENK MLPPLKEQEH LKTKEIIPNQ HFTEPPPRYS EASLVKKLEE
490 500 510 520 530 540
LGIGRPSTYA TILSVLQDRK YVTLEKKRFI PEELGRLVTV FLVGFFKKYV EYDFTAGLEN
550 560 570 580 590 600
ELDEIAAGKL EWKSALGNFW NGFNHNIESV NKQNITEIIS YVQQALDYHI FGENKDSKVC
610 620 630 640 650 660
PSCKTGELSL KLGKFGAFLA CSNYPECNFR KSIVSGNDNN EADGEAKDIV NENKVLGKDK
670 680 690 700 710 720
EGIEIYLKKG PYGPYIQYGE QVDSKIKPKR SPLPAGLNQN DITLDMALKL LSLPLKIGNH
730 740 750 760 770 780
KESGEEVLVG YGKFGPYIKY MGKFISIPKK YDFLNLSLDD AMKLIEEKLN AIAAKQPNPL
790
NMDEVTNLVD KKIKVKKTKK