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 Q9LAI2

Entry ID Method Resolution Chain Position Source
AF-Q9LAI2-F1 Predicted AlphaFoldDB

No variants for Q9LAI2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9LAI2

No associated diseases with Q9LAI2

No regional properties for Q9LAI2

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9LAI2

Functions

Description
EC Number 2.1.1.113 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

3 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).
N-methyltransferase activity Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.
site-specific DNA-methyltransferase (cytosine-N4-specific) activity Catalysis of the reaction: S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine.

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
MNWIFNTLIQ FLEDLNIDPS VVSLIDEDAK KLEEQFPKAL KHPVVDEEIV YKILCEKYNL
70 80 90 100 110 120
NALNVKTISE TLNKEYKFGR NSKTALKKYL DYGKEEYLIQ FFNTLMLENN TYIDREYIES
130 140 150 160 170 180
VLAFCEPVSK EKIKNEFIKL WNEANEVNEY GKLKDYLLGI YSKLFSMGLE NLRLIEIYNS
190 200 210 220 230 240
NESLIKKVFK YESTIKELKE YCLSNQESIT AGLAIKMFNE KYMELMKKEY QQDAIALKLE
250 260 270 280 290 300
EHMNQLYVDN NINEYPYIFD RGNDILLLPT EEYDFVYFHI DQDFFNRFQD ENKFLDYVLS
310 320 330 340 350 360
SIKQIYRVLA NEKVFALKID NIYNNEKNLK WELYPKLTIY SEHFIQTKET ARFYKAYDIA
370 380 390 400 410 420
KDLLSKHEFR LLENDSEKNR ENILKEYFSG KISEDELFSL VHVNMKKEHF FEFLNRFKYV
430 440 450 460 470 480
HYGFTFNDCL VLDRVDKSFA NGELENVISN ATEILLIFYK FRADQRRIPC PSCGSLNISG
490 500 510 520 530 540
NSYPEINNRS WECKSPYCPD RSKSNRGKRY SKKSNYMQWG AIYPKSHDII PRELIKKWRR
550 560 570 580 590 600
DIIVINNEQE IFEMLVKYFS FTDEKLLFIN TNELPSVVTE RENRKVVILS QKLKEKAYTS
610 620 630 640 650 660
NVVVKESLEG EIEFFKNGLY LKNFTELYLP EDQRRVSPEI NNFLNSGGRL KLIQGDSYEV
670 680 690 700 710 720
LKSVEDNTFA AAVTSPPYYN AREYSQWPNL YLYFNDMYNI IKECFRTLKP GSVFLYNIAD
730 740 750 760 770 780
IVDNENIIVK SSMGNKRIPL GAYTIYFFQK AGFELLDNII WDKGEPQSNR QKNDGKFTPH
790 800 810 820 830 840
YQKPLNAYEH MFIFKKTGAP LTLSDDWQSK RGSWIKNIVP FQPVFKINSK GENILGHTAP
850 860 870 880 890 900
FPEDIPRFVA NVFTKHDNDI ILDPFSGSLT SAIASYKSNR IGLGIELSPD YVELSRDRAL
910
LEGVTTKILN FN