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Q29PG5

- MOC32_DROPS

UniProt

Q29PG5 - MOC32_DROPS

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Protein
Adenylyltransferase and sulfurtransferase MOCS3-2
Gene
GA12041
Organism
Drosophila pseudoobscura pseudoobscura (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions By similarity.UniRule annotation

Catalytic activityi

ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP.UniRule annotation
[Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + cysteine desulfurase.UniRule annotation

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991ATP; via amide nitrogen By similarity
Binding sitei120 – 1201ATP By similarity
Binding sitei144 – 1441ATP By similarity
Metal bindingi229 – 2291Zinc By similarity
Metal bindingi232 – 2321Zinc By similarity
Active sitei246 – 2461Glycyl thioester intermediate; for adenylyltransferase activity By similarity
Metal bindingi304 – 3041Zinc By similarity
Metal bindingi307 – 3071Zinc By similarity
Active sitei408 – 4081Cysteine persulfide intermediate; for sulfurtransferase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1315ATP By similarity
Nucleotide bindingi188 – 1892ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. molybdopterin-synthase adenylyltransferase activity Source: UniProtKB-EC
  4. molybdopterin-synthase sulfurtransferase activity Source: UniProtKB-EC
  5. thiosulfate sulfurtransferase activity Source: UniProtKB

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB
  2. enzyme active site formation via L-cysteine persulfide Source: UniProtKB-HAMAP
  3. tRNA wobble position uridine thiolation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis, tRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00344.
UPA00988.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylyltransferase and sulfurtransferase MOCS3-2
Alternative name(s):
Molybdenum cofactor synthesis protein 3-2
Including the following 2 domains:
Molybdopterin-synthase adenylyltransferase 2 (EC:2.7.7.80)
Alternative name(s):
Adenylyltransferase MOCS3-2
Sulfur carrier protein MOCS2A adenylyltransferase 2
Molybdopterin-synthase sulfurtransferase 2 (EC:2.8.1.11)
Alternative name(s):
Sulfur carrier protein MOCS2A sulfurtransferase 2
Sulfurtransferase MOCS3-2
Gene namesi
ORF Names:GA12041
OrganismiDrosophila pseudoobscura pseudoobscura (Fruit fly)
Taxonomic identifieri46245 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000001819: Partially assembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0072089. Dpse\GA12041.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Adenylyltransferase and sulfurtransferase MOCS3-2UniRule annotation
PRO_0000369208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphothreonine By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi7237.FBpp0279121.

Structurei

3D structure databases

ProteinModelPortaliQ29PG5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 44997Rhodanese
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG0476.
InParanoidiQ29PG5.
KOiK11996.
OMAiTDYVFFC.
OrthoDBiEOG776SQ3.
PhylomeDBiQ29PG5.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_03049. MOCS3_Uba4.
InterProiIPR028885. MOCS3/Uba4.
IPR007901. MoeZ_MoeB.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR001763. Rhodanese-like_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF05237. MoeZ_MoeB. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q29PG5-1 [UniParc]FASTAAdd to Basket

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MIDSEALESE RVKLKRDIAD LRANLNRKEQ CLRELEAAIA AGEDSDEAEE    50
SSNDMPTPQT KLTNDDIARY SRQLILQDFG VQGQLKLKNS SVLIVGMGGL 100
GCPAAQYLVA AGCGHLGLID YDEVERSNLH RQILHSEHRC GMSKAESARI 150
ALLELNSHCQ IRCHSRLINS MNAMHIIRPY DVVLDCSDNV ATRYLLNDAC 200
VMLRKPLVSG SALKMDGQLT VYGYGQGPCY RCIYPVPPPP EAVTNCGDGG 250
VLGAVTGIIG AMQALEAIKV IIGLGDVMSG RLLIFDGSSF MFRNIRIRTK 300
RPNCHVCSAQ PLITELIDYE MFCGMHATDK DNPLDLLEPD QRLEVKEYHQ 350
KLQSQPHLLL DVRPPAEFEI CQLPRSINVP LSEILDDSYL KRFAKQLEDK 400
ELPIVLLCRR GNDSQIAVQH ITNRFPAHSI RDLVGGLHAW TGSVDATFPI 450
Y 451
Length:451
Mass (Da):50,086
Last modified:April 4, 2006 - v1
Checksum:i31E6FDE5E76538E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH379058 Genomic DNA. Translation: EAL34328.1.
RefSeqiXP_001357259.1. XM_001357223.2.

Genome annotation databases

EnsemblMetazoaiFBtr0280683; FBpp0279121; FBgn0072089.
GeneIDi4817985.
KEGGidpo:Dpse_GA12041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH379058 Genomic DNA. Translation: EAL34328.1 .
RefSeqi XP_001357259.1. XM_001357223.2.

3D structure databases

ProteinModelPortali Q29PG5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7237.FBpp0279121.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0280683 ; FBpp0279121 ; FBgn0072089 .
GeneIDi 4817985.
KEGGi dpo:Dpse_GA12041.

Organism-specific databases

FlyBasei FBgn0072089. Dpse\GA12041.

Phylogenomic databases

eggNOGi COG0476.
InParanoidi Q29PG5.
KOi K11996.
OMAi TDYVFFC.
OrthoDBi EOG776SQ3.
PhylomeDBi Q29PG5.

Enzyme and pathway databases

UniPathwayi UPA00344 .
UPA00988 .

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPi MF_03049. MOCS3_Uba4.
InterProi IPR028885. MOCS3/Uba4.
IPR007901. MoeZ_MoeB.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR001763. Rhodanese-like_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view ]
Pfami PF05237. MoeZ_MoeB. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view ]
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
    Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L.
    , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A.
    Genome Res. 15:1-18(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MV2-25 / Tucson 14011-0121.94.

Entry informationi

Entry nameiMOC32_DROPS
AccessioniPrimary (citable) accession number: Q29PG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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