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Database: UniProt
Entry: A0A0C4EFA0_MAGP6
LinkDB: A0A0C4EFA0_MAGP6
Original site: A0A0C4EFA0_MAGP6 
ID   A0A0C4EFA0_MAGP6        Unreviewed;       561 AA.
AC   A0A0C4EFA0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE            EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN   ORFNames=MAPG_11439 {ECO:0000313|EMBL:KLU92494.1};
OS   Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS   fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_11439T0, ECO:0000313|Proteomes:UP000011715};
RN   [1] {ECO:0000313|Proteomes:UP000011715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KLU92494.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU92494.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KLU92494.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU92494.1};
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Magnaporthe poae ATCC 64411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblFungi:MAPG_11439T0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_11439T0};
RX   PubMed=26416668; DOI=10.1534/g3.115.020057;
RA   Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA   Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA   Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA   Ma L.-J., Dean R.A.;
RT   "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT   family of fungi.";
RL   G3 (Bethesda) 5:2539-2545(2015).
RN   [5] {ECO:0000313|EnsemblFungi:MAPG_11439T0}
RP   IDENTIFICATION.
RC   STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_11439T0};
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000256|ARBA:ARBA00000857};
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DR   EMBL; ADBL01002820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL876981; KLU92494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4EFA0; -.
DR   STRING; 644358.A0A0C4EFA0; -.
DR   EnsemblFungi; MAPG_11439T0; MAPG_11439T0; MAPG_11439.
DR   VEuPathDB; FungiDB:MAPG_11439; -.
DR   eggNOG; KOG4163; Eukaryota.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 2733051at2759; -.
DR   Proteomes; UP000011715; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
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   InterPro; IPR033721; ProRS_core_arch_euk.
DR   NCBIfam; TIGR00408; proS_fam_I; 1.
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   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
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.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:KLU92494.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT   DOMAIN          101..337
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  62903 MW;  2234855FD2E20037 CRC64;
     MADNEQQPPA AEQSAEPSKS ALKKAAKAAQ KGAEKAAKAA KQMPVQTKKT DDIIGITVSK
     DDNFAQWYQE VVLKAEMIEY YNEISGFYIL RPAAMFVWTQ IRKWFQERID LMGVEETSFP
     MFLSSKSLEK EKDHVEGFAP ELAWVTKAGD KDLEVPVAVR PTSEAVMYPY YAKWIRSHRD
     LPLRLNQWNS VVRWEAKQTT PFLRAREFLW QEGHTAHLSE ELAGKEVLEI LELYAGVYEQ
     LLAVPVVRGK KTENEKFAGG YYTTTVEGYI PSNGRGIQGA TSHCLGQNFS KMFDITVEDP
     AKQGGHLHVW QNSWGLSTRV IGVMVMIHGD DKGLVLPPRI ARIQTVLIPV GLTAKTTPEE
     RTKHGEKVEE IRKTLKDAGL RVEADLREGY TPPWKFNDWE LKGVPLRLEF GPKDAAKDVV
     SYARRDTGEK GTIPIAELAT KVPELLETIQ KAMYDKADAA FRSHRLVLSE WDEVVPALDS
     KNVVLIPHCL DGKCEDHIKD ITKGSGMELM ADGQKAPSMG MKSLCIPFEQ PEGGIVKGET
     KCLSPDCDKL AETFVMFGRS Y
//
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