Q4L2Z3

PR
Gene name
mnmG
Protein name
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
Names
Glucose-inhibited division protein A
Species
Staphylococcus haemolyticus (strain JCSC1435)
KEGG Pathway
sha:SH2675
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

447-525 (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 Q4L2Z3

Entry ID Method Resolution Chain Position Source
AF-Q4L2Z3-F1 Predicted AlphaFoldDB

No variants for Q4L2Z3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4L2Z3

No associated diseases with Q4L2Z3

2 regional properties for Q4L2Z3

Type Name Position InterPro Accession
domain Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal 181 - 322 IPR006109
domain Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal 8 - 161 IPR011128

Functions

Description
EC Number
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.

1 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

1 GO annotations of biological process

Name Definition
tRNA wobble uridine modification The process in which a uridine in position 34 of a tRNA is post-transcriptionally modified.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVQEYDVIVI GAGHAGIEAG LASARRGAKT LMLTINLDNI AFMPCNPSVG GPAKGIVVRE
70 80 90 100 110 120
IDALGGQMAK AIDKTHIQMR MLNTGKGPAV RALRAQADKV LYQQEMKRVI EDEDNLDIMQ
130 140 150 160 170 180
GMVDELIIED NEVKGVRTNI GTEYRAQAVV ITTGTFLRGE IILGNMKYSS GPNHQLPSIT
190 200 210 220 230 240
LADNLRELGF EVVRFKTGTP PRVNAKTIDY SKTEIQPGDD VGRAFSFETT EYILDQLPCW
250 260 270 280 290 300
LTYTNDRTHK VIDDNLHLSA MYSGMIKGTG PRYCPSIEDK FVRFNDKPRH QLFLEPEGRN
310 320 330 340 350 360
TNEVYVQGLS TSLPEHVQRQ MLETIPGLEK ADMMRAGYAI EYDAIVPTQL WPTLETKMIK
370 380 390 400 410 420
NLYTAGQING TSGYEEAAGQ GIMAGINAAG KVLGTGEKIL SRSDAYIGVL IDDLVTKGTN
430 440 450 460 470 480
EPYRLLTSRA EYRLLLRHDN ADLRLTDVGY ELGMISEERY ARFNEKRQQI QDEIQRLTDI
490 500 510 520 530 540
RIKPNEHTQS VIEANGGSRL KDGILAIDLL RRPEMTYNTI LEILEESHQL PEAVEEQVEI
550 560 570 580 590 600
QTKYEGYINK SLQQVEKVKR MEEKKIPEDL DYSKVDSLAT EAREKLAEVK PLNIAQASRI
610 620
SGVNPADISI LLVYLEQGKL QRVKN