P25241

PR
Gene name
res (t3res)
Protein name
Type III restriction-modification enzyme BceSI Res subunit
Names
Type III restriction enzyme BceSI, Type III restriction-modification enzyme Bce10987IP Res subunit
Species
Bacillus cereus (strain ATCC 10987 / NRS 248)
KEGG Pathway
bca:BCE_1019
EC number
3.1.21.5: Endodeoxyribonucleases producing 5'-phosphomonoesters
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

421-513 (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 P25241

Entry ID Method Resolution Chain Position Source
AF-P25241-F1 Predicted AlphaFoldDB

No variants for P25241

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P25241

No associated diseases with P25241

3 regional properties for P25241

Type Name Position InterPro Accession
domain Helicase/UvrB, N-terminal 6 - 231 IPR006935
domain VRR-NUC domain 872 - 975 IPR014883
domain Type III restriction enzyme, C-terminal endonuclease domain 869 - 970 IPR045572

Functions

Description
EC Number 3.1.21.5 Endodeoxyribonucleases producing 5'-phosphomonoesters
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

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).
helicase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
type III site-specific deoxyribonuclease activity Catalysis of the endonucleolytic cleavage of DNA to give double-stranded fragments with terminal 5'-phosphates. ATP hydrolysis is required. Cleavage is dependent on the presence of two copies of a specific recognition sequence in an inverse orientation in the DNA. Cleavage occurs at a specific distance from one of the recognition sites.

1 GO annotations of biological process

Name Definition
DNA restriction-modification system A defense process found in many bacteria and archaea that protects the organism from invading foreign DNA by cleaving it with a restriction endonuclease. The organism's own DNA is protected by methylation of a specific nucleotide, which occurs immediately following replication, in the same target site as the restriction enzyme.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKILLEELPH QEESLKAILE NFTGIDNAAN DSDVDYVYAN PLIRGRYNEI SNIDVKMETG
70 80 90 100 110 120
TGKTYVYTRL MYEMHQQYGI FKFVIVVPSP AIKEGAKNFI QSDYAKQHFS QFYENVRIEL
130 140 150 160 170 180
NVINAGDFKS KSGRRNFPAQ LLNFVEGSRQ NSNTIEVLLI NADMLRSKSM RNNDYDQTLI
190 200 210 220 230 240
GGTTSPIEAI QDTRPVVIID EPHRFPRDKA NYQSIEAIKP QVIIRFGATF PEVTTGKGSN
250 260 270 280 290 300
KITKKDYYRK KPQFDLNAIE SFNNGLVKGI DIYYPNLTEE QAKNRYVVDS VKAKELVLKQ
310 320 330 340 350 360
NSKSWILHVG DNLAEVDSGF EGDIEYAGSK MLSNELELEK GMTLIPGTYR STYQELIIKD
370 380 390 400 410 420
AIDKHFEIEQ ANFLRANQRE NNVPRIKTLS LFFIDSITSY RQDDGWLKAT FERLLKEKLS
430 440 450 460 470 480
RLVAEYEFKR LPREKEYLEF LRATQSSLAS DNQNVHAGYF GEDRGSGDES IQAEVDDILK
490 500 510 520 530 540
NKEKLLSFKD ENGNWQTRRF LFSKWTLREG WDNPNVFVIA KLRTSGSDNS KIQEVGRGLR
550 560 570 580 590 600
LPVDETGHRI QQDEWPTRLA FLIGYDEKDF AQKLIGEINS DAKLQLNEEK LTEDMIQLIV
610 620 630 640 650 660
TKRKKVNPEF TDERLLEHLD NLGIINRKNE FKESIDIGGV QKSGFEWLVE LYPELNTNRL
670 680 690 700 710 720
REGKVIDTKK HSIKVRVKLR KENWEKVKEL WQQFSNRYML EFQRIPETIS FMAEQIVGNH
730 740 750 760 770 780
SLYEREVPMQ MKESLHASDD NESVVLREQE NEYQRIYLPG MAYGKFVKRI NIATGIPIKE
790 800 810 820 830 840
IHANLFKLMK SSLKGDARYL SELSLNNIIR EFKKRFDEIF AQAYEYKKLD FQARTAIYNP
850 860 870 880 890 900
EMDSFVDDIN AEVIGVNIDE QAQEDNRYLY ELPPMRYDSV TPERDLLRHG YNDKVTVFGK
910 920 930 940 950 960
LPRRAIQVPK YTGGSTTPDF IYMIEKDNDS SVYVLVETKA ENMRLEDQRI IDIQKKFFDT
970 980
LKEHHIEFIE ATSAQQVYSI IRKLSEE