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Protein

Protein TMA108

Gene

TMA108

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Putative zinc aminopeptidase which may be involved in ribosome biogenesis.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi330 – 3301Zinc; catalyticPROSITE-ProRule annotation
Active sitei331 – 3311Proton acceptorPROSITE-ProRule annotation
Metal bindingi334 – 3341Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi353 – 3531Zinc; catalyticPROSITE-ProRule annotation
Sitei423 – 4231Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

  • ribosome biogenesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-31388-MONOMER.

Protein family/group databases

MEROPSiM01.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein TMA108 (EC:3.4.11.-)
Alternative name(s):
108 kDa translation machinery-associated protein
Gene namesi
Name:TMA108
Ordered Locus Names:YIL137C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL137C.
SGDiS000001399. TMA108.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 946945Protein TMA108PRO_0000095121Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP40462.
PeptideAtlasiP40462.
TopDownProteomicsiP40462.

PTM databases

iPTMnetiP40462.

Interactioni

Subunit structurei

Associates with ribosomal complexes.

Protein-protein interaction databases

BioGridi34854. 35 interactions.
DIPiDIP-5097N.
IntActiP40462. 2 interactions.
MINTiMINT-496714.

Structurei

3D structure databases

ProteinModelPortaliP40462.
SMRiP40462. Positions 6-676.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni293 – 2975Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

HOGENOMiHOG000141852.
InParanoidiP40462.
OMAiKGSDWSK.
OrthoDBiEOG75J0WG.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNLLSLEN PVVPSHYELR LEIDPKQSSP NFKGSAIIHL KFNPNSTTLA
60 70 80 90 100
SIEDSFTQFK LHSKDLIVLS AHATIGSTKF DLKISQDTGK HLSIFNSESP
110 120 130 140 150
IQLSNDCPLI LSVQYVGKIR DIKTHHDKTF GIFKTNFMDR KTGTANNHVV
160 170 180 190 200
ATHCQPFSAS NIFPCIDEPS NKSTFQLNIA TDAQYKAVSN TPVEMVEALD
210 220 230 240 250
SSQKHLVKFA KTPLMTTSVF GFSIGDLEFL KTEIKLEGDR TIPVSIYAPW
260 270 280 290 300
DIANAAFTLD TVQKYLPLLE SYFKCPYPLP KLDFVLLPYL SDMAMENFGM
310 320 330 340 350
ITIQLNHLLI PPNALANETV REQAQQLIVH ELVHQWMGNY ISFDSWESLW
360 370 380 390 400
FNESFATWLA CHILEQNGDL SHYWTSEPYL LQQVEPTMCR DAADVNGRSI
410 420 430 440 450
FQIAQRNTGI DSQTSDIFDP EAYTKGIIML RSLQLATGES HLQKGLESVF
460 470 480 490 500
EDTKTFHARS VKPMDIWNHI GKFLKSQNIT NFVSSWTRTP GLPVVKVEVE
510 520 530 540 550
EKDGKTQTKL TQHRFINQLS TEEKDQLEDV PYQVPLFGVL PDGKMDTKNV
560 570 580 590 600
LLTDRTLKFD YPILVINHLA QGYYRVSYES EECYALINDK ITEETLSEID
610 620 630 640 650
LRKIFLDLSQ FIGDEGFQNS IHLHGLFKIL NHIASPSTKI ASKYWDPLSK
660 670 680 690 700
GLEVLQTIDR ASLTSSKLQS FLKKKIVIPL FNKIDWPHGE FDKSTNPHEL
710 720 730 740 750
KVMSQVLFLN KNSAKCAELC QIYFKHLLQG PRSSVPLELV NSILVVVSQH
760 770 780 790 800
CANIKQWKKI FDLVKRSSCT GITNHVINMY DQNSSETAML IQNGAIESLG
810 820 830 840 850
FCLDSDIVKK TLNFITSNIE SEGMELALFG FNYNFKKRLN KNEKPQDQVV
860 870 880 890 900
RETIWEWYMG NFDQWARKAT RKGTTTGDHL HKALRSISLI IFQMFVADEP
910 920 930 940
QKIEKFINLE KEKLGQSLLS LDDIWASVQQ DEESRKTIRR DLASLV
Length:946
Mass (Da):107,723
Last modified:February 1, 1995 - v1
Checksum:iE14B79A6F6D89F4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86141.1.
BK006942 Genomic DNA. Translation: DAA08415.1.
PIRiS48397.
RefSeqiNP_012129.1. NM_001179485.1.

Genome annotation databases

EnsemblFungiiYIL137C; YIL137C; YIL137C.
GeneIDi854669.
KEGGisce:YIL137C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86141.1.
BK006942 Genomic DNA. Translation: DAA08415.1.
PIRiS48397.
RefSeqiNP_012129.1. NM_001179485.1.

3D structure databases

ProteinModelPortaliP40462.
SMRiP40462. Positions 6-676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34854. 35 interactions.
DIPiDIP-5097N.
IntActiP40462. 2 interactions.
MINTiMINT-496714.

Protein family/group databases

MEROPSiM01.017.

PTM databases

iPTMnetiP40462.

Proteomic databases

MaxQBiP40462.
PeptideAtlasiP40462.
TopDownProteomicsiP40462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL137C; YIL137C; YIL137C.
GeneIDi854669.
KEGGisce:YIL137C.

Organism-specific databases

EuPathDBiFungiDB:YIL137C.
SGDiS000001399. TMA108.

Phylogenomic databases

HOGENOMiHOG000141852.
InParanoidiP40462.
OMAiKGSDWSK.
OrthoDBiEOG75J0WG.

Enzyme and pathway databases

BioCyciYEAST:G3O-31388-MONOMER.

Miscellaneous databases

PROiP40462.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH RIBOSOMAL COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTM108_YEAST
AccessioniPrimary (citable) accession number: P40462
Secondary accession number(s): D6VVE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5110 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

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.