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Database: UniProt/TrEMBL
Entry: A1CQ40_ASPCL
LinkDB: A1CQ40_ASPCL
Original site: A1CQ40_ASPCL 
ID   A1CQ40_ASPCL            Unreviewed;       553 AA.
AC   A1CQ40;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   29-OCT-2014, entry version 49.
DE   SubName: Full=Prolyl-tRNA synthetase {ECO:0000313|EMBL:EAW07761.1};
GN   ORFNames=ACLA_024770 {ECO:0000313|EMBL:EAW07761.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612 {ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|RuleBase:RU003746}.
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DR   EMBL; DS027059; EAW07761.1; -; Genomic_DNA.
DR   RefSeq; XP_001269187.1; XM_001269186.1.
DR   STRING; 5057.CADACLAP00002557; -.
DR   EnsemblFungi; CADACLAT00002604; CADACLAP00002557; CADACLAG00002604.
DR   GeneID; 4701011; -.
DR   KEGG; act:ACLA_024770; -.
DR   HOGENOM; HOG000076895; -.
DR   KO; K01881; -.
DR   OMA; MHQAYCN; -.
DR   OrthoDB; EOG7PGF12; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.800; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF52954; SSF52954; 1.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:EAW07761.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006701};
KW   Ligase {ECO:0000313|EMBL:EAW07761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
SQ   SEQUENCE   553 AA;  61658 MW;  4DA47622403EA4E9 CRC64;
     MLPLGLRVQD KLERLIDKHM QSVGASKVSL SSISSQELWE QSGRLKEGSE VFRFHDRKES
     RFLLAPTHEE EITTLVGSLT KSYRDLPVRV YQISRKYRDE ARPRQGLLRG REFMMKDLYT
     FDYNVEEALK TYNLVKAAYK NLFDELKIPY LVAAADSGNM GGSLSHEFHF PSSKGEDTVI
     SCSRCDHVYN DELADGKAHN LGEQQPHAGQ ASGFDTEGAT AESSPTVSTD LWMAISKDKN
     TLVRGWYPKF SMQQTEQEPV AREVNSHAAK SIATAAGVDI ELSVENPLEQ WVSHVQSNKA
     RGDSSPSQRP QVLDLYDSQV RVYKRPPLSD LLQQASCTAD EIQYSMLNRF PGTNHGLNLV
     KVQDGDKCIK CTEGSLKTHT AVELGHTFHL GTRYSEVLQA SVMVDQSLSG GAAKDQQVPM
     QMGCHGIGVS RMISAVADNL ADSKGLNWPR AMAPYEVVVV PGKGLETEAE KVYDLLASKQ
     SSPIDTILDD REKPMGWKLS DADLIGYPVI IVVGKGWKKQ QTLEVQCRRL DNLREEVPLD
     QLPAFVRSLL ERL
//
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