(data stored in SCRATCH zone)

SWISSPROT: C7QHI7_CATAD

ID   C7QHI7_CATAD            Unreviewed;       198 AA.
AC   C7QHI7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
DE            Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
GN   Name=pth {ECO:0000256|HAMAP-Rule:MF_00083};
GN   OrderedLocusNames=Caci_0171 {ECO:0000313|EMBL:ACU69126.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69126.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69126.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA. {ECO:0000256|HAMAP-Rule:MF_00083,
CC       ECO:0000256|RuleBase:RU000673}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00083, ECO:0000256|RuleBase:RU004320}.
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DR   EMBL; CP001700; ACU69126.1; -; Genomic_DNA.
DR   RefSeq; WP_012784421.1; NC_013131.1.
DR   STRING; 479433.Caci_0171; -.
DR   EnsemblBacteria; ACU69126; ACU69126; Caci_0171.
DR   KEGG; cai:Caci_0171; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; POG091H02CU; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00462; PTH; 1.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QHI7.
DR   SWISS-2DPAGE; C7QHI7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00083,
KW   ECO:0000256|RuleBase:RU000673, ECO:0000313|EMBL:ACU69126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
SQ   SEQUENCE   198 AA;  21461 MW;  81ED71E227C72B2E CRC64;
     MTTTEARDQL WLIAGLGNPG PGYAGNRHNA GFMVVDLLAA RVGGKFKSHK ARADVVEGRL
     GVGGPRVVLA KPKTFMNLSG GPVKALRDFY KIEPAQIIAV HDELDVDYGV LRLKLGGGDN
     GHNGLRSITS SLGTKEYHRV RFGVGRPPGR QDPADFVLKD FSSTEKKDLD YNVDRAADAV
     EDLIRRGLVE AQNIYHAA
//

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