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 P33563

Entry ID Method Resolution Chain Position Source
AF-P33563-F1 Predicted AlphaFoldDB

No variants for P33563

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P33563

No associated diseases with P33563

2 regional properties for P33563

Type Name Position InterPro Accession
conserved_site DNA methylase, N-6 adenine-specific, conserved site 140 - 146 IPR002052
domain Type II restriction enzyme and methyltransferase RM.Eco57I-like 140 - 232 IPR011639

Functions

Description
EC Number 2.1.1.72 Methyltransferases
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

2 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).
site-specific DNA-methyltransferase (adenine-specific) activity Catalysis of the reaction: S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

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
MTQILETVDK SRLTVNPLLK NKSELGQFFT PSSISIFMAC LFSEDKLNNA KVLDAGAGIG
70 80 90 100 110 120
SLTSAFLARL ISENIGKADL HLLEIDEMLE PYLSETLALF KDYIEINSQI IIDDFIEWAA
130 140 150 160 170 180
YSLLDEESLL AKDKQRFTHA ILNPPYKKIK SNSKHRKLLR KAGIETVNLY SAFVALTVDL
190 200 210 220 230 240
MSDGGEIVFI IPRSFCNGPY FRHFRQHLLN KTSIKHMHLF ESRDKAFKDD EVLQENVISK
250 260 270 280 290 300
LEKGTVQEDV KISISTDDSF SVIRSYRYPF EKIVQPNDIE KFIHINTTNE ETLIEKHPNV
310 320 330 340 350 360
CYSLEELNIE VSTGPVVDFR VKENLREMPG EGTVPLFYPN HFVGTSLEYP KMMKKPNAII
370 380 390 400 410 420
RNEKVEKWLY PNGHYVVVKR FSSKEEKRRI VAGVLTPESV NDPVVGFENG LNVLHYNKSG
430 440 450 460 470 480
ISKEVAYGLY AYLNSTPVDK YFRIFNGHTQ VNATDLRTMK FPSRDILISL GKWVIENIEN
490 500
VGQVEIDSKL EELLLNDRGN A