Q6F7Y9

PR
Gene name
mnmC
Protein name
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
Names
tRNA mnm(5)s(2)U biosynthesis bifunctional protein
Species
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
KEGG Pathway
aci:ACIAD3135
EC number
2.1.1.61: Methyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

264-335 (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 Q6F7Y9

Entry ID Method Resolution Chain Position Source
AF-Q6F7Y9-F1 Predicted AlphaFoldDB

No variants for Q6F7Y9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6F7Y9

No associated diseases with Q6F7Y9

4 regional properties for Q6F7Y9

Type Name Position InterPro Accession
domain FAD dependent oxidoreductase 264 - 586 IPR006076
domain MnmC-like methyltransferase 124 - 242 IPR008471
domain tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal 264 - 617 IPR017610
domain tRNA mnm(5)s(2)U biosynthesis bifunctional protein MnmC, N-terminal 23 - 242 IPR047785

Functions

Description
EC Number 2.1.1.61 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.

3 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.
oxidoreductase activity, acting on the CH-NH group of donors Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate.

1 GO annotations of biological process

Name Definition
tRNA wobble base modification The process in which the nucleotide at position 34 in the anticodon 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
MCVSSSIQTA ILDWQCVDGI DIPVSRQFGD VYFSKDNGLL ETRHVFLNGN NLTERLADLK
70 80 90 100 110 120
PYQYFCVGET GFGTGLNILA VWQLWQQVRP DNHSHLHVIS VEKFPLSKSD LERALRAWPE
130 140 150 160 170 180
LIILAEQLIE QYPFPIAGCH RLNFPDERFS LDLWLGDAHD VFPSIVKTHS VDAWFLDGFA
190 200 210 220 230 240
PSCNPELWET QVLNQIVRLS DYGTTFASFS VAGILKRGLK AHGIHISRPR GFGHKREMLK
250 260 270 280 290 300
AIWPFPDHES TTTVKGNQPS TQQHFAVIGA GIAGLHCAWS LAQRGHRVTL VDQSQPLSGA
310 320 330 340 350 360
SGNPLALLNP KLCPITQCHD HLMVLCWQYA RRFYQNFEAF RLIQVNQLAL KASDSLLNLA
370 380 390 400 410 420
EQYPKDVLDA HSAQQSPLET QYDYLTLHYA GVISPQLFCN QVLQHPLIEF KQFKINQIIE
430 440 450 460 470 480
IDGTVQLLSS EQAILESNAA IVCCARESGK LFEQYPTLKP IRGQVSWFEQ HTFPFAPDQA
490 500 510 520 530 540
FSYGGYCMQL HPQQLILGAS FHPQRDDDEV LLEDHVHNFN LIHSVFPAYA QTLPPVEEWH
550 560 570 580 590 600
GRASVRAQSP DYFPLVGQLQ DHSKLFTLAG LGSKGYLFAP LNSEILVAHI LGEACPVSAN
610 620
LLQKLNPQRF LKKVKIKKPY YSS