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Protein

tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC

Gene

mnmC

Organism
Yersinia pestis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm5s2U34 to nm5s2U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm5s2U34, to form mnm5s2U34.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate.UniRule annotation

Cofactori

FADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYPES214092:GKDD-2725-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCUniRule annotation
Short name:
tRNA mnm(5)s(2)U biosynthesis bifunctional proteinUniRule annotation
Including the following 2 domains:
tRNA (mnm(5)s(2)U34)-methyltransferaseUniRule annotation (EC:2.1.1.61UniRule annotation)
FAD-dependent cmnm(5)s(2)U34 oxidoreductaseUniRule annotation (EC:1.5.-.-UniRule annotation)
Gene namesi
Name:mnmCUniRule annotation
Ordered Locus Names:YPO2756, y1590, YP_2407
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
Proteomesi
  • UP000000815 Componenti: Chromosome
  • UP000001019 Componenti: Chromosome
  • UP000002490 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 689689tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCPRO_0000095033Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiQ8ZD36. 4 interactions.
STRINGi187410.y1590.

Structurei

Secondary structure

1
689
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 417Combined sources
Turni42 – 498Combined sources
Helixi50 – 545Combined sources
Beta strandi57 – 659Combined sources
Helixi71 – 8616Combined sources
Beta strandi94 – 10310Combined sources
Helixi107 – 1148Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 1299Combined sources
Beta strandi136 – 1438Combined sources
Turni144 – 1474Combined sources
Beta strandi148 – 1558Combined sources
Helixi157 – 1604Combined sources
Helixi161 – 1633Combined sources
Helixi166 – 1683Combined sources
Beta strandi172 – 1776Combined sources
Turni182 – 1843Combined sources
Helixi191 – 20010Combined sources
Beta strandi201 – 21010Combined sources
Helixi214 – 2229Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi238 – 2436Combined sources
Helixi254 – 2563Combined sources
Beta strandi265 – 2706Combined sources
Helixi274 – 28411Combined sources
Turni285 – 2873Combined sources
Beta strandi290 – 2989Combined sources
Helixi303 – 3053Combined sources
Beta strandi309 – 3113Combined sources
Helixi321 – 34222Combined sources
Beta strandi354 – 3574Combined sources
Helixi361 – 37010Combined sources
Turni377 – 3793Combined sources
Beta strandi381 – 3833Combined sources
Helixi385 – 3928Combined sources
Beta strandi400 – 4034Combined sources
Beta strandi407 – 4093Combined sources
Helixi411 – 42414Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi442 – 4498Combined sources
Beta strandi456 – 4638Combined sources
Helixi466 – 4683Combined sources
Turni473 – 4775Combined sources
Beta strandi481 – 49111Combined sources
Helixi496 – 4983Combined sources
Beta strandi501 – 5099Combined sources
Turni514 – 5163Combined sources
Beta strandi517 – 5226Combined sources
Helixi536 – 54914Combined sources
Helixi555 – 5584Combined sources
Beta strandi566 – 5738Combined sources
Beta strandi580 – 5856Combined sources
Helixi587 – 5937Combined sources
Turni594 – 5963Combined sources
Helixi597 – 6004Combined sources
Beta strandi617 – 6259Combined sources
Helixi631 – 64616Combined sources
Beta strandi652 – 6543Combined sources
Helixi655 – 6595Combined sources
Helixi665 – 6717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PVCX-ray2.31A1-689[»]
3SGLX-ray2.70A1-689[»]
ProteinModelPortaliQ8ZD36.
SMRiQ8ZD36. Positions 6-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 245245tRNA (mnm(5)s(2)U34)-methyltransferaseAdd
BLAST
Regioni270 – 689420FAD-dependent cmnm(5)s(2)U34 oxidoreductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.UniRule annotation
In the C-terminal section; belongs to the DAO family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
KOiK15461.
OMAiKSVLCYD.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 4 hits.
HAMAPiMF_01102. MnmC. 1 hit.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8ZD36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQRPIQTAT LSWNEQGTPV SEQFGDIYFS NEDGLEETHH VFLKGNGFPA
60 70 80 90 100
RFASHPQQSC IFAETGFGTG LNFLTLWRDF ALFRQQSPNA TLRRLHYISF
110 120 130 140 150
EKYPLHVADL ASAHARWPEL ASFAEQLRAQ WPLPLAGCHR ILLADGAITL
160 170 180 190 200
DLWFGDVNTL LPTLDDSLNN QVDAWFLDGF APAKNPDMWN EQLFNAMARM
210 220 230 240 250
TRPGGTFSTF TAAGFVRRGL QQAGFNVTKV KGFGQKREML TGTLPQQIHA
260 270 280 290 300
PTAPWYHRPA ATRCDDIAII GGGIVSALTA LALQRRGAVV TLYCADAQPA
310 320 330 340 350
QGASGNRQGA LYPLLNGKND ALETFFTSAF TFARRQYDQL LEQGIAFDHQ
360 370 380 390 400
WCGVSQLAFD DKSRGKIEKM LHTQWPVEFA EAMSREQLSE LAGLDCAHDG
410 420 430 440 450
IHYPAGGWLC PSDLTHALMM LAQQNGMTCH YQHELQRLKR IDSQWQLTFG
460 470 480 490 500
QSQAAKHHAT VILATGHRLP EWEQTHHLPL SAVRGQVSHI PTTPVLSQLQ
510 520 530 540 550
QVLCYDGYLT PVNPANQHHC IGASYQRGDI ATDFRLTEQQ ENRERLLRCL
560 570 580 590 600
PQVSWPQQVD VSDNQARCGV RCAIRDHLPM VGAVPDYAAT LAQYQDLSRR
610 620 630 640 650
IQHGGESEVN DIAVAPVWPE LFMVGGLGSR GLCSAPLVAE ILAAQMFGEP
660 670 680
LPLDAKTLAA LNPNRFWIRK LLKGRPVQTR SPATQESSR
Length:689
Mass (Da):76,671
Last modified:March 1, 2002 - v1
Checksum:i84812EC4DE06A2D4
GO

Sequence cautioni

The sequence AAM85159 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL21375.1.
AE009952 Genomic DNA. Translation: AAM85159.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS62612.1.
PIRiAD0336.
RefSeqiWP_002209716.1. NZ_LQAY01000055.1.
YP_002347703.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM85159; AAM85159; y1590.
AAS62612; AAS62612; YP_2407.
GeneIDi1175587.
KEGGiype:YPO2756.
ypj:CH55_16.
ypk:y1590.
ypl:CH46_2345.
ypm:YP_2407.
ypv:BZ15_769.
ypw:CH59_3643.
PATRICi18595320. VBIYerPes7843_3363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL21375.1.
AE009952 Genomic DNA. Translation: AAM85159.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS62612.1.
PIRiAD0336.
RefSeqiWP_002209716.1. NZ_LQAY01000055.1.
YP_002347703.1. NC_003143.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PVCX-ray2.31A1-689[»]
3SGLX-ray2.70A1-689[»]
ProteinModelPortaliQ8ZD36.
SMRiQ8ZD36. Positions 6-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8ZD36. 4 interactions.
STRINGi187410.y1590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM85159; AAM85159; y1590.
AAS62612; AAS62612; YP_2407.
GeneIDi1175587.
KEGGiype:YPO2756.
ypj:CH55_16.
ypk:y1590.
ypl:CH46_2345.
ypm:YP_2407.
ypv:BZ15_769.
ypw:CH59_3643.
PATRICi18595320. VBIYerPes7843_3363.

Phylogenomic databases

eggNOGiENOG4105CWG. Bacteria.
COG0665. LUCA.
COG4121. LUCA.
HOGENOMiHOG000218142.
KOiK15461.
OMAiKSVLCYD.

Enzyme and pathway databases

BioCyciYPES214092:GKDD-2725-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
3.50.50.60. 4 hits.
HAMAPiMF_01102. MnmC. 1 hit.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR008471. MnmC-like_methylTransf.
IPR029063. SAM-dependent_MTases.
IPR023032. tRNA_MAMT_biosynth_bifunc_MnmC.
IPR017610. tRNA_S-uridine_synth_MnmC_C.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF05430. Methyltransf_30. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR03197. MnmC_Cterm. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMNMC_YERPE
AccessioniPrimary (citable) accession number: Q8ZD36
Secondary accession number(s): Q0WDD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2002
Last modified: September 7, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.