ID J9EP13_WUCBA Unreviewed; 1142 AA.
AC J9EP13;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
DE Flags: Fragment;
GN ORFNames=WUBG_05150 {ECO:0000313|EMBL:EJW83938.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW83938.1, ECO:0000313|Proteomes:UP000004810};
RN [1] {ECO:0000313|Proteomes:UP000004810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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:EJW83938.1}.
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DR EMBL; ADBV01001910; EJW83938.1; -; Genomic_DNA.
DR AlphaFoldDB; J9EP13; -.
DR Proteomes; UP000004810; 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 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 Pfam; PF04615; Utp14; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 80..330
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 813..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1142
FT /evidence="ECO:0000313|EMBL:EJW83938.1"
SQ SEQUENCE 1142 AA; 131137 MW; 5054F90E630DC4DD CRC64;
MKNKNSKLEV QTTRQDVVIP KLENDLSNFH IGTTSSVKGR GDVKKQTKLG IEVTKDENYC
EWYVQVITKA EMIEYYDISG CYVLRPWSYA IWEFIQEWFD EKIKKLGVKN CYFPLFVSQS
ALEREKTHIS DFAPEVAWIT RAGQSDLAEA IAIRPTSETV IYPSYAKWVQ SHRDLPIKLN
QWCNVVRWEF KHPTPFLRTR EFLWQEGHTA FQTKAEAEDE VFKILDLYAQ VYTDLLAIPV
IKGRKTEKEK FAGGEFTTTV EAYVPVNGRG IQGATSHHLG QNFSKMFNIS FEDPNGGGKV
YAWQNSWGLS TRTIGALVMI HGDNYGLVLP PRIAAIQMVI VPVGITARTK DEQKTALIEK
AKEVNNVLVD VGIRTELDVR DNISPGWKFN HWELKGVPVR IEIGPKDLAN SQITCVIRYS
GEKRIIPIDV FATKCKDMLD EIHNSIILEV RESHTKIVLE WSDFRSFLDQ KFILLSPFCG
RSECEDEIKK ESVREEENDL SAPSMGAKTL CIPFEQPDIS LPTNCINKNC SEKAQFFALF
GRIKASTMSE DSDFDEEAHT KLLNNINSLG SSVKKGPLIR KCQKKVHIKE LVNLIRSTKN
VDDVKEKLVK KRSKEKRQQK TNRKPCKLHP IDWKDLEEWA PIVKRNRLAE QLVFPLTNDP
PLERTASDLV LFFKPRTPLE IELAKLLKTS KNNLRDGEEY TEAELELIRA MNLKEAKAKW
VQLKKMRALV GYREAKLKRQ AKIKSKSYHR HMKRQKRKQL IREFEEMMVK NPEAAKEKLE
EIDRQRILER ATLKHRNGGK GVQQLARYAN WGENWPKKHG REKNSDSDSE SERTDAVQLT
SAKMLERAAE VLEKEEKERK STKSELKAKL HEMREQEREN LRSSALRAAD AGSVARQRDE
LGTDVADKSM VSIKKVVEIE WGPEDAVNSE EQSNRTEHQQ DISVNSEQDR AEKEVDEQSK
EGHKNLKKKK KSKKMRNKKK SIDIKDMDID QLFDKAEKEL AENALKKCEL LKLEDEENRR
NHSLPIVSDS AGISRQKEKE IATKTEEAAI DISLDPRHFL QIETMALPQV SADFVETLED
TNEQAKDQEE IIAKAFEDVD VIGDFEAEKE AVEAAENPKD IDLTLHGWGS WTGPGITDKK
KI
//