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Database: UniProt
Entry: A0A133U4C2_9EURY
LinkDB: A0A133U4C2_9EURY
Original site: A0A133U4C2_9EURY 
ID   A0A133U4C2_9EURY        Unreviewed;       177 AA.
AC   A0A133U4C2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE            EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE   Flags: Fragment;
GN   ORFNames=AKJ57_05965 {ECO:0000313|EMBL:KXA89006.1};
OS   candidate division MSBL1 archaeon SCGC-AAA259A05.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698259 {ECO:0000313|EMBL:KXA89006.1, ECO:0000313|Proteomes:UP000070163};
RN   [1] {ECO:0000313|EMBL:KXA89006.1, ECO:0000313|Proteomes:UP000070163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA259A05 {ECO:0000313|EMBL:KXA89006.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXA89006.1}.
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DR   EMBL; LHXJ01000105; KXA89006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133U4C2; -.
DR   PATRIC; fig|1698259.3.peg.140; -.
DR   Proteomes; UP000070163; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070163}.
FT   DOMAIN          109..177
FT                   /note="Proline-tRNA ligase class II C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00946"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KXA89006.1"
SQ   SEQUENCE   177 AA;  20930 MW;  1F45BAD52A7922F0 CRC64;
     EQMKRILEKA GEISSRLEDS TVDDRENYTP GWKFNEWELK GVPLRIEIGP KEIEENYVTL
     VRRDNQKRIT VAQSKVEEKV KEILQKIQRN LLENARDFLE KNTRETESYE EFKEILEKKG
     GFIKAPWCGK TSCEEKIKNE TTAKITNIPF KYNEPQEKNC IKCGEKAKYW VNFAKSY
//
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