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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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000950331 – 689tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCAdd BLAST689

Interactioni

Protein-protein interaction databases

IntActiQ8ZD36. 4 interactors.
STRINGi187410.y1590.

Structurei

Secondary structure

1689
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 41Combined sources7
Turni42 – 49Combined sources8
Helixi50 – 54Combined sources5
Beta strandi57 – 65Combined sources9
Helixi71 – 86Combined sources16
Beta strandi94 – 103Combined sources10
Helixi107 – 114Combined sources8
Helixi118 – 120Combined sources3
Helixi121 – 129Combined sources9
Beta strandi136 – 143Combined sources8
Turni144 – 147Combined sources4
Beta strandi148 – 155Combined sources8
Helixi157 – 160Combined sources4
Helixi161 – 163Combined sources3
Helixi166 – 168Combined sources3
Beta strandi172 – 177Combined sources6
Turni182 – 184Combined sources3
Helixi191 – 200Combined sources10
Beta strandi201 – 210Combined sources10
Helixi214 – 222Combined sources9
Beta strandi226 – 231Combined sources6
Beta strandi233 – 236Combined sources4
Beta strandi238 – 243Combined sources6
Helixi254 – 256Combined sources3
Beta strandi265 – 270Combined sources6
Helixi274 – 284Combined sources11
Turni285 – 287Combined sources3
Beta strandi290 – 298Combined sources9
Helixi303 – 305Combined sources3
Beta strandi309 – 311Combined sources3
Helixi321 – 342Combined sources22
Beta strandi354 – 357Combined sources4
Helixi361 – 370Combined sources10
Turni377 – 379Combined sources3
Beta strandi381 – 383Combined sources3
Helixi385 – 392Combined sources8
Beta strandi400 – 403Combined sources4
Beta strandi407 – 409Combined sources3
Helixi411 – 424Combined sources14
Beta strandi428 – 432Combined sources5
Beta strandi435 – 440Combined sources6
Beta strandi442 – 449Combined sources8
Beta strandi456 – 463Combined sources8
Helixi466 – 468Combined sources3
Turni473 – 477Combined sources5
Beta strandi481 – 491Combined sources11
Helixi496 – 498Combined sources3
Beta strandi501 – 509Combined sources9
Turni514 – 516Combined sources3
Beta strandi517 – 522Combined sources6
Helixi536 – 549Combined sources14
Helixi555 – 558Combined sources4
Beta strandi566 – 573Combined sources8
Beta strandi580 – 585Combined sources6
Helixi587 – 593Combined sources7
Turni594 – 596Combined sources3
Helixi597 – 600Combined sources4
Beta strandi617 – 625Combined sources9
Helixi631 – 646Combined sources16
Beta strandi652 – 654Combined sources3
Helixi655 – 659Combined sources5
Helixi665 – 671Combined sources7

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 245tRNA (mnm(5)s(2)U34)-methyltransferaseAdd BLAST245
Regioni270 – 689FAD-dependent cmnm(5)s(2)U34 oxidoreductaseAdd BLAST420

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_LQBA01000056.1.
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_LQBA01000056.1.
YP_002347703.1. NC_003143.1.

3D structure databases

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

Protein-protein interaction databases

IntActiQ8ZD36. 4 interactors.
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.

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: November 2, 2016
This is version 109 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.