Q03R49

PR
Gene name
mutS2
Protein name
Endonuclease MutS2
Names
Species
Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis)
KEGG Pathway
lbr:LVIS_1217
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

575-737 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q03R49

Entry ID Method Resolution Chain Position Source
AF-Q03R49-F1 Predicted AlphaFoldDB

No variants for Q03R49

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q03R49

No associated diseases with Q03R49

4 regional properties for Q03R49

Type Name Position InterPro Accession
domain DNA mismatch repair protein MutS, C-terminal 327 - 512 IPR000432
domain Smr domain 707 - 785 IPR002625
domain DNA mismatch repair protein MutS, core 10 - 314 IPR007696
domain MutS2 and Smr-associated SH3 domain 641 - 680 IPR046893

Functions

Description
EC Number
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

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent DNA damage sensor activity A molecule that recognises toxic DNA structures, and initiates a signalling response, driven by ATP hydrolysis.
endonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks.
mismatched DNA binding Binding to a double-stranded DNA region containing one or more mismatches.

2 GO annotations of biological process

Name Definition
mismatch repair A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
negative regulation of DNA recombination Any process that stops, prevents, or reduces the frequency, rate or extent of DNA recombination.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNQKTLKIME YERIKQALRG YLVSAAGQHE LAELAPTADA KQLQIWLDES RDGADIYRLE
70 80 90 100 110 120
NGIPLPKLDD IRPHLHRLAM EAALNGLELA QISRVLWTTS SVVKFFRDLT EKEITLRRLD
130 140 150 160 170 180
RVVKELVTLP DVTRRLRTSL EGDGHITDEA SPALRQIRQH IAQTEVAIRQ TMDQYTRGKD
190 200 210 220 230 240
AKYLSETIVT IRDERYVIPV RAEYKQRFGG IVHDQSASGQ TLFIEPQAVV GLNNRLRQNQ
250 260 270 280 290 300
IDERHEEQRI LAELTALLDP YQAEILRNSE ILGHFDFINA KAKYAHQLKA TEPKLSEDNQ
310 320 330 340 350 360
VNLRQARHPL IDPKKVVAND ITIGRDYKTI IVTGPNTGGK TITLKTLALV QLMGQSGLFI
370 380 390 400 410 420
PANENSVIGI FDDIFADIGD EQSIEQSLST FSGHMENIVA ILRQADERSL IVVDELGAGT
430 440 450 460 470 480
DPQEGAALAI AILDQMGTLG SYVMASTHYP ELKAYGYNRP ETINASMEFD GETLQPTYHL
490 500 510 520 530 540
LIGIPGRSNA LDIAARLGMP EQVVAAARGL TDQDSQDLNA MISDLTEQKR HADADAERLR
550 560 570 580 590 600
QELAEADELH AQLKKQFDAY QHQKDQLMTD AKREANRLVD ESRKRANQII SDLRKKQLAA
610 620 630 640 650 660
GKSVVKEDEL IAAQGALNAL QQDSKLKKNR VLRREKAKLD FHKGDSVLVK SYGQVGVLME
670 680 690 700 710 720
QLDDQHWEVQ LGILKMKIAT NDLEKAQDPA KSAKQPRASV KRSGSSGMSA TLDLRGHRYE
730 740 750 760 770 780
EAMAEVDRYI DSALLAGYPS VTIIHGKGTG ALRKGVTDYL KRNNRIKSFG FSPANAGGDG
STVVHFK