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Database: UniProt
Entry: A0A1X0P2V9_9TRYP
LinkDB: A0A1X0P2V9_9TRYP
Original site: A0A1X0P2V9_9TRYP 
ID   A0A1X0P2V9_9TRYP        Unreviewed;       466 AA.
AC   A0A1X0P2V9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=RNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012724};
DE            EC=6.5.1.3 {ECO:0000256|ARBA:ARBA00012724};
GN   ORFNames=TM35_000061960 {ECO:0000313|EMBL:ORC91191.1};
OS   Trypanosoma theileri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC91191.1, ECO:0000313|Proteomes:UP000192257};
RN   [1] {ECO:0000313|EMBL:ORC91191.1, ECO:0000313|Proteomes:UP000192257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|EMBL:ORC91191.1};
RA   Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA   Matthews J., Matthews K., Carrington M.;
RT   "An alternative strategy for trypanosome survival in the mammalian
RT   bloodstream revealed through genome and transcriptome analysis of the
RT   ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.;
CC         EC=6.5.1.3; Evidence={ECO:0000256|ARBA:ARBA00034038};
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:ORC91191.1}.
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DR   EMBL; NBCO01000006; ORC91191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0P2V9; -.
DR   VEuPathDB; TriTrypDB:TM35_000061960; -.
DR   OrthoDB; 166878at2759; -.
DR   Proteomes; UP000192257; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 1.10.10.1810; RNA ligase; 1.
DR   InterPro; IPR012647; RNA_lig_RNL2.
DR   InterPro; IPR021122; RNA_ligase_dom_REL/Rnl2.
DR   InterPro; IPR041948; Rnl1/2_C_sf.
DR   NCBIfam; TIGR02307; RNA_lig_RNL2; 1.
DR   Pfam; PF09414; RNA_ligase; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ORC91191.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192257}.
FT   DOMAIN          83..295
FT                   /note="RNA ligase"
FT                   /evidence="ECO:0000259|Pfam:PF09414"
SQ   SEQUENCE   466 AA;  52339 MW;  9D05B45229429259 CRC64;
     MTFSRMIARG AEPFLCSGLR RRAIFAAYSN NYFTGRAVTV VTSRRTYMPL PNDQTDFSPY
     IEIDLPSESR IQAIHKSGLG AQDWVACEKV HGTNFGIYLI NQGDKEVVRF AKRSGIMDPN
     ENFFGYHILI DEFTAQVRIL SDLLKQKYGL SRIGRVVLNG ELFGAKYKHP LVPKSEKWCT
     MPNGKRFPIA GVQIQREPFP QYSPELHFFA FDIKYSVSGA EEDFVMLGYD EFVEFCSRVP
     NLLYAKALVR GTLDACLAFD VENFFTPLPA LLGLGNYPLE GNLAEGVVIR HVRRGDPAVE
     KHNVATIIKL RCSSFMELKH PGKQQELKET FIDTVRAGAL RRVRGDVTVV AESMLPQVEA
     AANNLLLNNV SDGRLSNVLS KIGREPLLSG EVKQADVALM LAKDALKDFL KEVDELVLNT
     SLTFRKTLIV NVYFESKKLV EQKWKEILRA EADAKAESEE AAKENA
//
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