ID A0A0N4XGU1_NIPBR Unreviewed; 469 AA.
AC A0A0N4XGU1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=18S rRNA aminocarboxypropyltransferase {ECO:0000256|HAMAP-Rule:MF_03146};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_03146};
GN ORFNames=NBR_LOCUS1744 {ECO:0000313|EMBL:VDL65333.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000174301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000174301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL65333.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It
CC constitutes the last step in biosynthesis of the hypermodified N1-
CC methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
CC {ECO:0000256|HAMAP-Rule:MF_03146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-
CC methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63296, Rhea:RHEA-COMP:11634, Rhea:RHEA-
CC COMP:16310, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03146};
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000256|HAMAP-Rule:MF_03146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03146}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYSL01001553; VDL65333.1; -; Genomic_DNA.
DR STRING; 27835.A0A0N4XGU1; -.
DR WBParaSite; NBR_0000174301-mRNA-1; NBR_0000174301-mRNA-1; NBR_0000174301.
DR OMA; SAHIRME; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR HAMAP; MF_01116; TSR3; 1.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR InterPro; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR NCBIfam; TIGR03724; arch_bud32; 1.
DR PANTHER; PTHR20426:SF0; 18S RRNA AMINOCARBOXYPROPYLTRANSFERASE; 1.
DR PANTHER; PTHR20426; RIBOSOME BIOGENESIS PROTEIN TSR3 HOMOLOG; 1.
DR Pfam; PF06293; Kdo; 1.
DR Pfam; PF04034; Ribo_biogen_C; 2.
DR Pfam; PF04068; RLI; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_03146};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_03146};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03146}; tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 261..469
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03146"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03146"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03146"
SQ SEQUENCE 469 AA; 52620 MW; 0320B098C222CCD6 CRC64;
MGKKGREQHG NKRTNKSRHA DAGDAEPLSS HGEEDSESLD ESRDDHSDSD QTNEMPCKLA
MYDFNQCDPK RCSGRKLLRA GLISEVRLGS RFPGLVLSPT GKTTLAPCDR EFIDQYGLGV
VDCSWKEVER TPLHKATTKA ALFFLIKDGV TRFIALMMGM RFTHSLPTKV KAPEHRLLPY
LVAANSVNYG RPCHLTCAEA LAAGLYIVGH VQAAERVMKQ FTWGPHFIEL NRELLDIYAG
CHTPEENMEW EEQFEQGFDY AIEKDGMRQG AEARVYTCTY LGRPAIMKER FSKKYRHPDV
DEKLNKARLR NELKGIVRAQ EVGVGAPAVF FVDTNNNRII MERIEGLTAN AWIEKRRSEA
SGSNEFKADT LELGKLIGEA IGKMHLSNLV HGDLTTSNII LKNNDLRQPY FIDFGLCALG
KVLPEDKGVD LYVLERAMIS THIDSEDMFK SVLEGYTSVN SKQGSAVIK
//
