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 Q07736

Entry ID Method Resolution Chain Position Source
AF-Q07736-F1 Predicted AlphaFoldDB

No variants for Q07736

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q07736

No associated diseases with Q07736

5 regional properties for Q07736

Type Name Position InterPro Accession
domain Helicase, C-terminal 412 - 526 IPR001650
domain Helicase/UvrB, N-terminal 169 - 326 IPR006935
domain EcoEI R protein C-terminal domain 648 - 803 IPR013670
domain Helicase superfamily 1/2, ATP-binding domain 166 - 361 IPR014001
domain Type I restriction enzyme R protein, N-terminal domain 35 - 118 IPR029464

Functions

Description
EC Number 3.1.21.3 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

3 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).
type I site-specific deoxyribonuclease activity Catalysis of the endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5' or 3' protrusions, driven by ATP hydrolysis. Cleavage is dependent on the presence in the DNA of a specific recognition site. Cleavage may occur hundreds or thousands of base pairs away from the recognition site due to translocation of DNA.

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
MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK VAARRTVKSA
70 80 90 100 110 120
DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV PFVFATNGDG FIFRDATAAE
130 140 150 160 170 180
GECLEKQITL DDFPSPAELW QKFCLWKGYT QAQLPVITQD YYDDGSGKSP RYYQLQAINK
190 200 210 220 230 240
TIEAVSNGQN RVLLVMATGT GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF
250 260 270 280 290 300
QPFGTAMTKV SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA
310 320 330 340 350 360
SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI EDGFLAPYKV
370 380 390 400 410 420
VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM VIDERTELVA RTITDYLKRT
430 440 450 460 470 480
NPMDKTIVFC NDIDHAERMR RALVNLNPEQ VKKNDKYVMK ITGDDEIGKA QLDNFINPKK
490 500 510 520 530 540
PYPVIATTSE LMTTGVDAKT CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF
550 560 570 580 590 600
KKATELFADE RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY
610 620 630 640 650 660
QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF KDYTRKTLLK
670 680 690 700 710 720
EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG KDLDPFDMLC HVVYGQPPLT
730 740 750 760 770 780
RKERAENVRK RNYFTKYSEA AQAVLDNLLD KYADAGVQEI ESIQVLKLKP FDSMGTLPEI
790 800
IKTGFGDRNG YNQALSELEN EIYQLPPRSA