TM108_YEAST
ID TM108_YEAST Reviewed; 946 AA.
AC P40462; D6VVE9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein TMA108;
DE EC=3.4.11.-;
DE AltName: Full=108 kDa translation machinery-associated protein;
GN Name=TMA108; OrderedLocusNames=YIL137C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP ASSOCIATION WITH RIBOSOMAL COMPLEXES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Putative zinc aminopeptidase which may be involved in
CC ribosome biogenesis.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Associates with ribosomal complexes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86141.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08415.1; -; Genomic_DNA.
DR PIR; S48397; S48397.
DR RefSeq; NP_012129.1; NM_001179485.1.
DR AlphaFoldDB; P40462; -.
DR SMR; P40462; -.
DR BioGRID; 34854; 259.
DR DIP; DIP-5097N; -.
DR IntAct; P40462; 3.
DR MINT; P40462; -.
DR STRING; 4932.YIL137C; -.
DR MEROPS; M01.017; -.
DR iPTMnet; P40462; -.
DR MaxQB; P40462; -.
DR PaxDb; P40462; -.
DR PRIDE; P40462; -.
DR TopDownProteomics; P40462; -.
DR EnsemblFungi; YIL137C_mRNA; YIL137C; YIL137C.
DR GeneID; 854669; -.
DR KEGG; sce:YIL137C; -.
DR SGD; S000001399; TMA108.
DR VEuPathDB; FungiDB:YIL137C; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_3_0_1; -.
DR InParanoid; P40462; -.
DR OMA; WFNEAFA; -.
DR BioCyc; YEAST:G3O-31388-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P40462; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40462; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IDA:SGD.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:1990593; F:nascent polypeptide-associated complex binding; IDA:SGD.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR033514; Yin7.
DR PANTHER; PTHR11533:SF171; PTHR11533:SF171; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Ribosome biogenesis; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..946
FT /note="Protein TMA108"
FT /id="PRO_0000095121"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 293..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 423
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 946 AA; 107723 MW; E14B79A6F6D89F4F CRC64;
MSDNLLSLEN PVVPSHYELR LEIDPKQSSP NFKGSAIIHL KFNPNSTTLA SIEDSFTQFK
LHSKDLIVLS AHATIGSTKF DLKISQDTGK HLSIFNSESP IQLSNDCPLI LSVQYVGKIR
DIKTHHDKTF GIFKTNFMDR KTGTANNHVV ATHCQPFSAS NIFPCIDEPS NKSTFQLNIA
TDAQYKAVSN TPVEMVEALD SSQKHLVKFA KTPLMTTSVF GFSIGDLEFL KTEIKLEGDR
TIPVSIYAPW DIANAAFTLD TVQKYLPLLE SYFKCPYPLP KLDFVLLPYL SDMAMENFGM
ITIQLNHLLI PPNALANETV REQAQQLIVH ELVHQWMGNY ISFDSWESLW FNESFATWLA
CHILEQNGDL SHYWTSEPYL LQQVEPTMCR DAADVNGRSI FQIAQRNTGI DSQTSDIFDP
EAYTKGIIML RSLQLATGES HLQKGLESVF EDTKTFHARS VKPMDIWNHI GKFLKSQNIT
NFVSSWTRTP GLPVVKVEVE EKDGKTQTKL TQHRFINQLS TEEKDQLEDV PYQVPLFGVL
PDGKMDTKNV LLTDRTLKFD YPILVINHLA QGYYRVSYES EECYALINDK ITEETLSEID
LRKIFLDLSQ FIGDEGFQNS IHLHGLFKIL NHIASPSTKI ASKYWDPLSK GLEVLQTIDR
ASLTSSKLQS FLKKKIVIPL FNKIDWPHGE FDKSTNPHEL KVMSQVLFLN KNSAKCAELC
QIYFKHLLQG PRSSVPLELV NSILVVVSQH CANIKQWKKI FDLVKRSSCT GITNHVINMY
DQNSSETAML IQNGAIESLG FCLDSDIVKK TLNFITSNIE SEGMELALFG FNYNFKKRLN
KNEKPQDQVV RETIWEWYMG NFDQWARKAT RKGTTTGDHL HKALRSISLI IFQMFVADEP
QKIEKFINLE KEKLGQSLLS LDDIWASVQQ DEESRKTIRR DLASLV
