ID A0A016W1P4_9BILA Unreviewed; 586 AA.
AC A0A016W1P4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=Acey_s0002.g663 {ECO:0000313|EMBL:EYC33202.1};
GN ORFNames=Y032_0002g663 {ECO:0000313|EMBL:EYC33202.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC33202.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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};
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:EYC33202.1}.
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DR EMBL; JARK01001338; EYC33202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016W1P4; -.
DR STRING; 53326.A0A016W1P4; -.
DR Proteomes; UP000024635; 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:InterPro.
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 Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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 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; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 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 SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 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:UP000024635}.
FT DOMAIN 3..60
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 120..370
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 54..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 66319 MW; 0FE8D5F39B208153 CRC64;
MANELEIEKE IVAQGDLVRK LKGDASASED MKKEAIEKLL RLKLTYKEIT GKEYAAPGGR
QQKEKKPAAE KKQDKKAEPK ADGKKQTKLG IEISKDENYS EWYSQVITKA EMIEYYDVSG
CYVLRPWSYA IWEGIQAWFD SGIKKLGVKN CYFPMFVSNA ALEREKTHIA DFAPEVAWVT
RAGSSEMAEP IAIRPTSETV MYPSYKKWVQ SHRDLPIKLN QWCNVVRWEF KHPTPFLRTR
EFLWQEGHTA FATPEEAVRE VFQILDLYAG VYTDLLAIPI VKGRKSEKEK FAGGDFTTTV
EAYVPCNGRG IQGATSHHLG QNFSKMFDIS FEDPNTGGKA YAWQNSWGLS TRTIGAMVMI
HADDSGLVLP PRVAAIQAII LPVGITAQTT EEQRKHLMDS ADELAKILVD ADVRAEADLR
DNYSPGWKFN HWELKGVPIR IEIGPKDLAA DQVTAVLRYN GKKMAIKRAD LVNEIKRLLE
VIHEEMYNKV LTARDAHMKV CYDFEEFKQL LDEKFILLSP FCGEIACEDE IKKASTRDDA
EAGAAQMGAK TLCIPLEQPK ETLPEKCLFP ACKNKAKFFA LFGRSY
//
