ID A0A1D2MRC6_ORCCI Unreviewed; 1793 AA.
AC A0A1D2MRC6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000313|EMBL:ODM95546.1};
GN ORFNames=Ocin01_11134 {ECO:0000313|EMBL:ODM95546.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM95546.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM95546.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM95546.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM95546.1}.
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DR EMBL; LJIJ01000655; ODM95546.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2MRC6; -.
DR OMA; WDPKGNN; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00807; GlnRS_core; 1.
DR CDD; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR CDD; cd00936; WEPRS_RNA; 5.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 6.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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 InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00463; gltX_arch; 1.
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; PF08263; LRRNT_2; 3.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 6.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 6.
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 SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 6.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 4.
DR PROSITE; PS51185; WHEP_TRS_2; 6.
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, ECO:0000313|EMBL:ODM95546.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527}.
FT DOMAIN 794..850
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 866..922
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 942..998
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1024..1080
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1102..1158
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1181..1237
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1333..1575
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 180..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1793 AA; 198542 MW; 930C5886CC30E04B CRC64;
MELEVCLDSN NPPMGLRMAA TLAEETGVRA NWTNETKLSW NNGIAVSSST IYRILARRFP
ALYCNTAYER TEVDYWLGFA ESQLVKPTAE NLQKLDGILK LSSFLVGNQL TVADLAVFDK
LAGRREALVK FLNINRYYNF IEAAIVDTIP RSDVSKMKDL KTVPIEVGAG DAGKRFVGFT
NIKKEGQQKP GKQAGGGEGE SKKKPEKASG NKDNGKGEDK NNQPGGGDKG KKKDEGKFVE
LPGAEMGKVV VRFPPEASGY LHIGHAKAAL LNQYYQLMFN GKLIMRFDDT NPAKEKEAFE
EVILQDLEML QVKPDRFTYT SDYFELMLEL CEKLLKADKA YVDDTEAEVM KDERMKRIES
KNRSNAIDKN LQMWNEMKNG TAYGQKCCVR AKIDMNAANG CMRDPTIYRC KPEHHPRTGN
KYKVYPTYDF ACPIVDSIEG VTHALRTTEY HDRDDQFFWF IDALGLRKPY IYEYSRLNLT
NTVLSKRKLT WFVDEGAVDG WDDPRFPTVR GVLRRGMTVE GLKQFIVAQG SSRSVVMMSW
DKIWAFNRQV IDPIAPRHTG LMQGFLIPVN VKGAAEIVDV ADAHPKNPEV GKRNVWKSGK
VLVEEDDAVL FKEGENVTFV NWGNIKIEKI NRKGDKIESV DASLNLDDKD FKKTMKITWL
AETAKSPLTP IEAVYYDHII SKPVLNPDED FKQFLGQNTK VKVDMVGDAD MRNLKKGDIV
QLQRKGFFIC DVPYKPRSAH TCKETPLVLF AVPDGKTKEN PTVRIPGKQG QNLAGQIEPK
KEAGSGLDSN VSSAAASLDA QIIAQGNKIR DLKSQKATKD VIEVEVKALL AFKTEFKSVV
GKDWDPKGNN VPKTEAAPVA AVPNNAIASL DAQIVAQGNK IRDLKGQKAA KDVIEGEVKA
LLALKVDFKK AAGKDWDPKG NNVPKSEPAA AQITSSASSS DSLVSLDNQI TEQGGKIRDL
KSQKAAKDVL DVEVKKLLAL KAEFKKVAGK DWDPKGNNVP KTSSSSVTAP APTTTSSSSS
NNSELVSIDA QITAQGSKIR DLKSQKAGKD VIDAEVKKLL GLKADFKKAA GKDWDPKGNN
VPQNTTAPAP TTASSSTSNN SELGSLDAQI TAQGNKIRVL KSQKAAKDVL DAEVKTLLSL
KADFKKVAGK DWDPKGNNIS KSQTVASQAS AQSSMSESDS ALASIDAQIT AQGNRVRELK
GQKATKDAID AEVKALLALK AEFKKVAGRD WDPKGNNTGG ASKPSAENTS GSSGGNQKSK
GKENKPAKPS KDTPKPAAAK ESQADAGKKQ TRLCVEAKKS ENLAEWFSQV ITKSEMIEYY
DVSGCYIFRP WSFAIWEAIK DWFDGEIKKL GVQNCYFPMF VSQAALQKEK DHIADFAPEV
AWVTKSGDSD LAEPIAIRPT SETVMYPSFA KWVQSHRDLP IKLNQWNNVV RWEFKHPQPF
IRTREFLWQE GHSAFATYEE AEEEVYAILC LYERVYTELL AIPVIPGRKT EKEKFPGGDY
TTTVEAYISA SGRGLQGATS HHLGQNFSKM FKISFEDPKS PEKECFAYQN SWGLSTRTIG
AMVMVHGDDQ GLVLPPRVAA TQVVIVPCGI TASLKDDERE ALYAECKSYE TRLSKLGLRV
KGDYRENYSP GWKFNHWELK GVPLRIEVGP RDLKESQYVA VQRHDGSKGT YKNASLERDV
KNLLDDIHNA MFQKAQKEMD ANITVTEDWQ ALCADLDKKH IIMAPFCGRV ECEENIKKDS
AKDEPSEPGA PAMGAKSLCI PFKQPKDLQS STKCIHPKCN QKPKSYTLFG RSY
//
