ID   SYP2_ANADE              Reviewed;         510 AA.
AC   Q2ILX2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Prolyl-tRNA synthetase 2;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase 2;
DE            Short=ProRS 2;
GN   Name=proS2; OrderedLocusNames=Adeh_0024;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC       diphosphate + L-prolyl-tRNA(Pro).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the anticodon-binding domain and the C-terminal extension
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 3 subfamily.
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DR   EMBL; CP000251; ABC79802.1; -; Genomic_DNA.
DR   RefSeq; YP_463239.1; -.
DR   GeneID; 3890389; -.
DR   GenomeReviews; CP000251_GR; Adeh_0024.
DR   KEGG; ade:Adeh_0024; -.
DR   HOGENOM; Q2ILX2; -.
DR   OMA; Q2ILX2; CIEAMMQ.
DR   BioCyc; ADEH290397:ADEH_0024-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_01571; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR004499; Pro-tRNA-synth_IIa_pro-type.
DR   InterPro; IPR016061; Pro-tRNA_synth_II_C.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Gene3D; G3DSA:3.30.110.30; Pro-tRNA-synth_II_C_arc/euk; 1.
DR   PANTHER; PTHR11451:SF6; ProS_fam_I; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    510       Prolyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000249114.
SQ   SEQUENCE   510 AA;  57291 MW;  5E835CE43B0EED0B CRC64;
     MSDASAETAI RPTRAENFSE WYLEVIKAAD LAESSSVRGC MVIKPWGYAL WEHVQRVLDG
     MFKATGHVNA YFPLFIPLSL LEKEAAHVEG FAKECAVVTH HRLEARDGKL VPVGELEEPL
     IVRPTSETII GESFARWVQS YRDLPLLINQ WANVVRWEMR TRMFLRTAEF LWQEGHTAHA
     TEPEAIDETM QMLGIYARFA EEWMALPVVQ GEKTESERFP GAVRTYCIEA MMQDRKALQA
     GTSHFLGQNF AKASGIQFQD EKGTLTHAWT TSWGLSTRMI GAMIMTHGDD DGMVCPPRLA
     PQQVVIIPVI QKPEVREQVL AWCTALKREL EAQTYAGAPV RVHLDARDLQ GAKKSWEWIK
     KGTPVRLEVG PRDIEKGAVF MGRRDRKPRE KQSVPRAELV AGVGALLQEI QDALLERART
     MRAAHTRVID TKDEFYAYFT PPPTRRPNDP TPIHGGFALA HFAGDPAVEA RIKEDLGVTV
     RCIPLEPGEP GTCAFTGQPS PKRVVWAKSY
//