P40815
Gene name |
res |
Protein name |
Type III restriction-modification enzyme StyLTI Res subunit |
Names |
Type III R-M system StyLTI, Type III restriction enzyme StyLTI |
Species |
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
KEGG Pathway |
stm:STM0358 |
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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P40815
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P40815-F1 | Predicted | AlphaFoldDB |
7 variants for P40815
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 17 | A>R | strain: LT7 [UniProt] | No | ||
| 293 | K>EINPPT | strain: LT7 [UniProt] | No | ||
| 350 | S>T | strain: LT7 [UniProt] | No | ||
| 420 | L>V | strain: LT7 [UniProt] | No | ||
| 464 | S>R | strain: LT7 [UniProt] | No | ||
| 536 | G>AV | strain: LT7 [UniProt] | No | ||
| 945 | D>IRLFLMRNVNSSICCVGKISMSSLRKDQRAGGIFYDQWLD | strain: LT7 [UniProt] | No |
No associated diseases with P40815
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 |
| MMNILLEELP | HQEQALAAIL | ASFTGIDHAQ | ADHNHYANPL | IKERYDDKAN | IDVKMETGTG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KTYVYTRLMY | ELHQKYGLFK | FVLVVPTPAI | KEGARNFITS | DYARQHFSQF | YENTRMELCT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| INAGDFKVKS | GRKNFPAQLL | SFTDASRRDS | HTIQVLLINA | QMLNSASMTR | DDYDQTLLGG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LTSPVKGLQM | TRPVVIIDEP | HRFARDNKFY | RAIQAIQPQM | IVRFGATFPD | IVEGKGKNKC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VRKDYYRRQP | QFDLNAVDSF | NDGLVKGIDI | YYPNLPEEQA | NNRYIVDSVT | AKKLILRRGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KIAEVGVGEN | LADVDAGFEG | SIEYAGSKML | SNDLELEAGM | ALVPGTFGAS | YQELIIQDAI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DKHFDTEQAN | FLRSNEPENN | APRIKTLSLF | FIDSIKSYRD | DEGWLKVTFE | RLLKKKLTQL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IDDYQRKTLP | REVEYLSFLQ | ATLASLHSDN | QNVHAGYFGE | DRGSGDEAIQ | AEVDDILKNK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EKLLSFSDHH | GNWETRRFLF | SKWTLREGWD | NPNVFVIAKL | RSSGSESSKI | QEVGRGLRLP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VDENGHRVHQ | EEWPSRLSFL | IGYDEKAFAS | MLVDEINRDS | KVQLNEQKLD | EAMITLIVTE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RQKVDPAFTE | LRLLEDLDDK | KLINRSNEFK | PSVTLNGETK | SGFAWLLEFY | PELTQARVRA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DRIRDNKPAS | RLRVRLRKEN | WEQLSSIWEQ | FSRRYMLQFE | RSGASLEQIA | AEVLRDPALY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IRQKPSQVQQ | RLVSNEDNGR | FEVAQREGEL | AASEFMAGMK | YGHFLKQLAL | RTSLPVNVLH |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PVLMAMLRDV | LHGDSRYLSE | ISLDNMTRAL | QTRINAHFAQ | RHDYLPLDFQ | ASTSVFDSTA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RQFREEISAE | IVGKNVDENA | IDDPRSLYQI | PPLRYDSVDP | ELPLLKYDYP | QQVSVFGKLP |
| 910 | 920 | 930 | 940 | 950 | 960 |
| KRAIQIPKYT | GGSTTPDFVY | RIERQDADSV | YLLVETKAEN | MRVGDQVILD | AQRKFFDMLR |
| 970 | 980 | ||||
| RQNINVEFAE | ATSAPAVFST | INGLIEGKAN |