ID A0A096LS01_POEFO Unreviewed; 1490 AA.
AC A0A096LS01;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000021942.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000021942.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AYCK01003344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01003345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000031475.1; ENSPFOP00000021942.1; ENSPFOG00000017972.2.
DR GeneTree; ENSGT00550000074815; -.
DR Proteomes; UP000028760; 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:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd10309; GST_C_GluProRS_N; 1.
DR CDD; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR CDD; cd00936; WEPRS_RNA; 3.
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; 3.
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; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; 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; 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; 3.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 3.
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; 3.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 3.
DR PROSITE; PS51185; WHEP_TRS_2; 3.
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:UP000028760}.
FT DOMAIN 55..191
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 728..784
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 806..862
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 878..934
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1023..1274
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 184..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1490 AA; 166040 MW; 8EB1DDB215840C6C CRC64;
SMALNLTINS NNPPLVCRDD SKRNAWVLSI ISMFLKGALL TAEHVKDTVQ VSVEEGKDNS
LQISDSVQFS DTNSISRYLA RVAPALGLYG ANLMEQTEVD HWLEFSARRV CDQPDLTLAL
GDLDKVLSLR TFLVGHALTL ADLSVWAALK NQSSWPSQSK AFPHVSRWFF FLNSQVPFSS
VGSKYASKKP VKNNSNSGEK KPDVGKFVDL PGAEMGKVVV RFPPEASGYL HIGHAKAALL
NQHYQVTFKG KLIMRFDDTN PEKEKEDFEK VILEDVAMLQ IHPDQFTYTS DHFPVIMRMA
EKLLAEGKAY IDDTPPEQMK QETVEQNMKM WAEMKAGTEY GQSCCMRAKI DMSSNNGCLR
DPTLYRCKNA PHPRTGTTYK VYPTYDFACP IVDSLEGVTH ALRTTEYHDR DEQFYWFIEA
LGIRKPYIWE YARLNLNNTV LSKRKLTWFV DQGYGGSRSV VNMEWDKIWS FNKKVIDPVA
PRFTALSSSY VVPVSVPEAT EEMKEVAKHP KNEEVGLKEV WYGPRVLIEG ADAETLTEGE
TVTFINWGNL IITKINKAPD SKVASIEARL DLDNKDYKKT TKITWLAETS SAPLLPVICV
NYQHLITKAV ITKDDDFKEY INKNSKLEEK MLGDPCLKSL KKGDIIQLQR RGFYICDQPY
EPISPNSCKE SPCVLFYIPD GHTKEMPTAG SKDKSKSQAS SNTKSMAPPT SAPATPAASA
PVAPAPEATA CPYTRVSQQG ELVRKLKAEK APKDKIDAAV KQLLALKEEY KQATGQDYKP
GAGPAPSPTQ KTAAPTQNST SPSPAAATGL YGKVAEQGEL VRKLKTEKAP KDQVDAAVKQ
LLALKAEYKQ QTGQEYKPGL QAPAGPAQTG AQSSTPPQAQ ELYALVAQQG ELVRKLKTEK
ASKEQVDEAV KTLLDLKGKY KSLTGEDYKP VAAAGATGGE DKNRKAERVE ERAKAPRSRH
GGAGEETESR ESTKGTKSGG GEGQGPKKQT RLGLEAKKEE NLADWYSQVI TKAEMIEYYD
VSGCYVLRPW AYSIWEAIKD FFDREIKKLG VENCYFPMFV SQAALEKEKS HIADFAPEVA
WVTRSGKTEL AEPIAVRPTS ETVMYPAYAK WVQSHRDLPI KLNQWCNVVR WEFKHPQPFL
RTREFLWQEG HTAFATKEEA AEEVLQILDL YARVYEELMA IPVVKGRKTE KEKFAGGDYT
TTVEAFISAS HRAIQGATSH HLGQNFSKMF EIAFEDPKKP GEKQLAFQNS WGITTRTIGV
LTMVHGDNMG LVLPPRVACL QVVIIPCGIT ASLPEQDKEA LLAQCSKYLS RLLDAGVRVK
SDTRDNYSPG WKFNHWELKG VPIRLEVGPK DMQQKQCVAV RRDTGAKVTI PEAEVEKRLL
GMLEDIQNNL FKKASDDLKS HMVAVDTMEA FQKELDQGKI VQIPFCGGIE CEDWIKKTTA
KDQDLEPGAP SMGAKSLCIP FSPIKTLQPG QMCVSGKEPA QFYTLFGRSY
//
