A8GJW6

PR
Gene name
rlmG
Protein name
Ribosomal RNA large subunit methyltransferase G
Names
23S rRNA m2G1835 methyltransferase, rRNA (guanine-N(2)-)-methyltransferase RlmG
Species
Serratia proteamaculans (strain 568)
KEGG Pathway
spe:Spro_4312
EC number
2.1.1.174: Methyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-54 (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 A8GJW6

Entry ID Method Resolution Chain Position Source
AF-A8GJW6-F1 Predicted AlphaFoldDB

No variants for A8GJW6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8GJW6

No associated diseases with A8GJW6

2 regional properties for A8GJW6

Type Name Position InterPro Accession
conserved_site DNA methylase, N-6 adenine-specific, conserved site 303 - 309 IPR002052
domain Methyltransferase small domain 201 - 371 IPR007848

Functions

Description
EC Number 2.1.1.174 Methyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
23S rRNA (guanine(1835)-N(2))-methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + guanosine(1835) in 23S rRNA = N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine.
nucleic acid binding Binding to a nucleic acid.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQLDLGTQQ LELERYPQQE ESTQLQAWEA ADEYLLQQLE NVNIGDRPVL IFNDNFGTLA
70 80 90 100 110 120
CALHSHQPYS ISDSYMSQLA TRHNLKLNEL DPQQVTLLDT LAELPASPAV VLIRIPKALA
130 140 150 160 170 180
LLEQQLRALR DVVAPDTVII AGAKARDVHT STMQLFEKVL GPTRTSLAWK KARLIHCEVA
190 200 210 220 230 240
DIVPPAAPVT TNWVLDGTDW VIHNHANVFS RSNLDIGARL FLDHLPHDIE GHIIDLGCGN
250 260 270 280 290 300
GVIGMAALMQ NPQAQVSFVD ESYMAVASSE LNVEHNLPQD MDRCQFEVNN SLAGIERESV
310 320 330 340 350 360
QAVLCNPPFH QQHAITDHTA WQMFCDAKRC LQVGGELRIV GNRHLDYHQK LKRLFGNCTL
370
IASNKKFVIL KAVKSGARY