ID A0A0C9M758_9FUNG Unreviewed; 1337 AA.
AC A0A0C9M758;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE SubName: Full=Aspartyl-tRNA synthase {ECO:0000313|EMBL:GAN02749.1};
GN ORFNames=MAM1_0027d02196 {ECO:0000313|EMBL:GAN02749.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02749.1};
RN [1] {ECO:0000313|EMBL:GAN02749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02749.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR EMBL; DF836316; GAN02749.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9M758; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00777; AspRS_core; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 1.20.120.20; Apolipoprotein; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR047090; AspRS_core.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55261; GAD domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT DOMAIN 880..1315
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 212..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 149646 MW; 01F1BBB33C7BBC6C CRC64;
MNQFNLNKAS PLMRRQSALM MMNNRRFMSS QYRQPVRQGG ISKGLVATLV IAAAGFAYYK
RTVDEKKFYN GDSDPYEKTK KNVAQFGDKV AKDAEPEARG AVDEINAAGR HIKKSANLAG
QAAQDAYQSA TSSAKKEGEH VVSTFKKESG ELASEVDKFR QEHHLKEGDR TPEDVLSHKY
NQAADKVSSK ANELKQDANE AAFKAADKFK TAKNSASSGS NVEHNPMVNE KVSADKTKSS
YERSLEHHAK ENVRDTSNLV GKDTDKVKKV WDDKHSQEHS TEEKSKGFWS SLVGGNGASN
EAAPPKSTTH SGTPSVPHGQ PEKRVYDTAP TDHGNPMVHE KHNFDKTKPG WESRLENYAE
KNVHDTSTLV GKDTEKVRGV WDEKHVRDNG GVPVAQENTN SFWSSLFGQA KDAEHKVEER
LEEGWEDVKS KVGLSAHDVK KDASGAYQDA KGKASAEASR LKRSASNAAD DLSHKAGQEA
NRVESKWNNL KSQVKGDAQS AYDNAADTAS NVSDKLQRET SRATSETQRK AEELKRTASD
RLEAEKNRAS SNLKDLHNEV SSNAEKWKDQ TEQTAKSWYQ KGTEQIKSGL ETVKTTADKD
LHWAEDKVSE GLSTAKTEVD RLLGKEVPKE PGYTGHVIRG EKFAEEEEGM LRHTRPNTKA
KPAEVVVGNA DGKEIFGRVV LLANRASLLR HAQRSTAFHL TRATAACQAR KIATTAAVRE
QYLHGYKDNE RYHGEYPGRT HYCGELRASN EGEKVVLCGW AQSSRDMSQD LIFLPLRDHS
GVTQLVYRNS NDEHLKSQIQ SLSAESVVCV EGVVKKRPEG MANTTQAAGD IEVEITKIYC
LNPATPSLPF WPNQAQLPNE EVRLRYRYLD LRRQELQHNI RLRSLTANTV RNYLTENGFT
EIETPTLFKS TPEGAREFIV PTRKRGAFYA LPQSPQQHKQ MLMAAGFDRY FQIARCFRDE
DLRADRQPEF TQIDLEMSFI KIKDIQQIIE GMVTSIWDKA LGKKLTKEHF PHMTYNEAMS
KYGSDKPDIR FDMKINDIGS FAKDVAGDGS IDCMVVKKGS ALTGGELKAM QKVLDLTDDK
NFAFVKINDN NIHSWSSKCN SLRHSQHISQ PQQLEQLNQS LDIEQGDLVL VYKRPSYLYG
GNTTMGRVRL HVSDLMQKKG LLTLDQNEKH KFLWVESFPL FTPDEQGIRT WQATHHPFTA
PYDEDIPLLA TEPEKVRGQH YDLVLNGMEI GGGSIRIHSP VMQTFILEKV LQLEKYEYKR
FDHLIDALGG GCPPHGGIAL GFDRLMAILC ESTSIRDVIA FPKAAGGKDF VVNSPSEVTT
AQLNEYCLQL ANVDEKK
//
