#=GF ID   ProRS-C_2
#=GF AC   PF09181.14
#=GF DE   Prolyl-tRNA synthetase, C-terminal
#=GF AU   Sammut SJ;0000-0003-4472-904X
#=GF SE   pdb_1nj8
#=GF GA   25.00 25.00;
#=GF TC   27.70 94.40;
#=GF NC   21.20 19.00;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   12578991
#=GF RT   The structural basis of cysteine aminoacylation of tRNAPro by
#=GF RT   prolyl-tRNA synthetases. 
#=GF RA   Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Soll D, Steitz
#=GF RA   TA; 
#=GF RL   Proc Natl Acad Sci U S A. 2003;100:1673-1678.
#=GF DR   INTERPRO; IPR015264;
#=GF DR   SCOP; 1nj8; fa;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Members of this family are predominantly found in prokaryotic
#=GF CC   prolyl-tRNA synthetase. They contain a zinc binding site, and
#=GF CC   adopt a structure consisting of alpha helices and antiparallel
#=GF CC   beta sheets arranged in 2 layers, in a
#=GF CC   beta-alpha-beta-alpha-beta motif [1].
#=GF SQ   5
#=GS SYP_METMP/394-460     AC Q6LZD3.1
#=GS SYP_META3/395-456     AC A6UTK4.1
#=GS F6BAN8_METIK/395-458  AC F6BAN8.1
#=GS SYP_METJA/394-455     AC Q58635.1
#=GS D7DTC8_METV3/417-481  AC D7DTC8.1
SYP_METMP/394-460                ITVLDFENdVNSLSEKVKAKLLENKGIILIPFNESIYNEEFEELIDASVLGLTTYEGKEYISVARTY
SYP_META3/395-456                ITILDNHD.----VNNIKETLSTKKGVVLVPYDENIYTEEFEEEIDASVLGTTEYDGKKYISIAKTY
F6BAN8_METIK/395-458             IKIVEFDE.--SKIDEIKNILSEKRGVILIPYSDDIYNEELEDKVEASVLGVTEYKGNKYIAIARTY
SYP_METJA/394-455                ITILEDIN.----PDEIKNILSEKRGVILVPFKEEIYNEELEEKVEATILGETEYKGNKYIAIAKTY
D7DTC8_METV3/417-481             IEILEAVE.SNLLLENIKEAINNRK-VVLIPFNEELYNEEFEEETGASILGECEFEGNKYISIAKTY
#=GC seq_cons                    ITILEsc-....hl-cIKstLSEKKGVILIPFsE-IYNEEFEEcl-ASVLGpTEY-GNKYISIAKTY
//