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Database: UniProt
Entry: A0A0F9XSL1_TRIHA
LinkDB: A0A0F9XSL1_TRIHA
Original site: A0A0F9XSL1_TRIHA 
ID   A0A0F9XSL1_TRIHA        Unreviewed;       795 AA.
AC   A0A0F9XSL1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=tRNA ligase {ECO:0000256|PIRNR:PIRNR019634};
DE            EC=6.5.1.3 {ECO:0000256|PIRNR:PIRNR019634};
GN   ORFNames=THAR02_00401 {ECO:0000313|EMBL:KKP07480.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP07480.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
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|PIRNR:PIRNR019634};
CC   -!- SIMILARITY: Belongs to the TRL1 family.
CC       {ECO:0000256|PIRNR:PIRNR019634}.
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:KKP07480.1}.
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DR   EMBL; JOKZ01000006; KKP07480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9XSL1; -.
DR   OMA; FQDWDYK; -.
DR   OrthoDB; 1405617at2759; -.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051730; F:GTP-dependent polyribonucleotide 5'-hydroxyl-kinase activity; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019039; T4-Rnl1-like_N.
DR   InterPro; IPR012387; Trl1_fun.
DR   InterPro; IPR015966; tRNA_lig_kin_fungi.
DR   InterPro; IPR015965; tRNA_lig_PDEase.
DR   PANTHER; PTHR32004; TRNA LIGASE; 1.
DR   PANTHER; PTHR32004:SF1; TRNA LIGASE; 1.
DR   Pfam; PF09511; RNA_lig_T4_1; 1.
DR   Pfam; PF08302; tRNA_lig_CPD; 1.
DR   Pfam; PF08303; tRNA_lig_kinase; 1.
DR   PIRSF; PIRSF019634; tRNA_lig_yeast; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|PIRNR:PIRNR019634};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR019634}.
FT   DOMAIN          68..302
FT                   /note="T4 RNA ligase 1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09511"
FT   DOMAIN          393..550
FT                   /note="tRNA ligase kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08303"
FT   DOMAIN          553..792
FT                   /note="tRNA ligase phosphodiesterase"
FT                   /evidence="ECO:0000259|Pfam:PF08302"
FT   REGION          595..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        119
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019634-50"
SQ   SEQUENCE   795 AA;  90586 MW;  E8BA85FD078EA402 CRC64;
     MAAPYVEQDV SAVSQMLSAL EAARKDKRHG GFSCKKTTFK IKSSRDGIEV DSWRMQDWDY
     KKKGLPTYAR GLFTTKTSRN VPEIAVRGYD KFFNVSEVNE TKWDVILKNT KGPYELTLKE
     NGCIIFVAGL EDDTLLVCSK HSTGDRSDVE LSHARAGEIR LEKQLAAVGK TKEDLARELR
     SRNITAVAEL CDDSFEEHIL AYENDKAGLY LHGINLNLPE FATYPSNLVQ EFADRWGFIK
     TDLLVMEDVN EVKTFLEDVA KTGSYSGRDV EGFVIRCKMS HNHTALPYQD WFFKFKFEEP
     YLMYRQWREC TKAMISGKQP KFKKHIKITE EYLQYAKKQL VANPNLSKLY NQNHGIIKLR
     DDFLAYKNLK GSDAANLDLL DRVVMSEVIK DVILSPIATI GCGKTTLALA LKHLFGWGHI
     QNDNISGKGR PPRFVKALMD ELQEHPVVYA DRNNAQRHER KQLIGDVKAQ NVEARIVCLN
     FRHDEETIDE IRRITQDRII ERGDNHQTIH AATDKDKYLD VMEGFIKRFE ECNPNSPPDA
     GFDLVIDLDP TAGSRVNLET LVNELHLSLP NVVKEVPSPE KLDEAMEYAL SYTPDFKHTI
     PDRGSKKDAK QGQRQQQQAQ PKKKGLEYMS VHVPRDQIDK VLDKAFKGVG PEISRFFWQL
     KNTRRVQRQF HVTLMHKATA AQYPELWKRY TELHDAAGGG DTILGECDVL LERVVFDDRI
     MAIVVRLFDA ENKWECVNKI AHITVGTRDA AVKPKESNDL LAKWLEVGAG NEGIQEVVFA
     DKPTLKGHVK GVTSR
//
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