ID   TRNL_SCHPO              Reviewed;         787 AA.
AC   Q10313; Q7Z990;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=tRNA ligase 1;
DE            EC=6.5.1.3 {ECO:0000305};
GN   Name=trl1; ORFNames=SPAC17G8.01c, SPAC6C3.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Required for the splicing of precursor tRNA molecules
CC       containing introns. The ligation activity requires three enzymatic
CC       activities: phosphorylation of the 5' terminus of the 3' half-tRNA in
CC       the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of
CC       the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two
CC       tRNA halves in an ATP-dependent reaction. {ECO:0000250}.
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:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: Has three domain each corresponding to an enzymatic activity,
CC       namely in N- to C-terminal order: ligase, kinase and cyclic
CC       phosphodiesterase (CPDase). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRL1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93622.1; -; Genomic_DNA.
DR   PIR; T39034; T39034.
DR   RefSeq; NP_593724.2; NM_001019155.2.
DR   AlphaFoldDB; Q10313; -.
DR   SMR; Q10313; -.
DR   BioGRID; 278634; 1.
DR   STRING; 4896.SPAC17G8.01c.1; -.
DR   MaxQB; Q10313; -.
DR   PaxDb; Q10313; -.
DR   EnsemblFungi; SPAC17G8.01c.1; SPAC17G8.01c.1:pep; SPAC17G8.01c.
DR   GeneID; 2542158; -.
DR   KEGG; spo:SPAC17G8.01c; -.
DR   PomBase; SPAC17G8.01c; trl1.
DR   VEuPathDB; FungiDB:SPAC17G8.01c; -.
DR   eggNOG; ENOG502QQB9; Eukaryota.
DR   HOGENOM; CLU_010316_1_0_1; -.
DR   InParanoid; Q10313; -.
DR   OMA; YNQNHGI; -.
DR   PhylomeDB; Q10313; -.
DR   PRO; PR:Q10313; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0051730; F:GTP-dependent polyribonucleotide 5'-hydroxyl-kinase activity; ISO:PomBase.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019039; RNA_ligase_T4-Rnl1_N.
DR   InterPro; IPR012387; Trl1_fun.
DR   InterPro; IPR015966; tRNA_lig_kin_fungi.
DR   InterPro; IPR015965; tRNA_lig_PDEase.
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; SSF52540; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Ligase; Reference proteome; tRNA processing.
FT   CHAIN           1..787
FT                   /note="tRNA ligase 1"
FT                   /id="PRO_0000116589"
FT   ACT_SITE        117
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   787 AA;  90343 MW;  56B55C14E331A9CB CRC64;
     MTRDQRVCIF GEKKSTVRSV TFKAPKSNYD LTSWRIWEQA FRLNVSNSKK CFDTISGHRI
     TLPTNARGLF TGYDYESKRH RIVIRGYDKF FNIDEVPITT WDALSQHTKG PYELTVKENG
     CIIFIAALPD GQIIVSSKHS LGIVEGQSVS HANVGERWLE KHLQSVGRTK QELAHELLRR
     DMTAVAELCD DEFEEHILPY TGNSRGLYLH GLNRNCPQFI TASSCEVAEF AEQWGFMKVS
     SFFMDSIHEL KAFLENASKD GKWNNRAIEG FVIRCHSDHS SLEQQSSNDF FFKYKFPEPY
     GMFRQWREVT KMLISGKKPS YTKYKKVTAE YITFCDKKFK EDEDAKRLYM SNKGIISLRD
     EFLVLSKLDL MHLSVSNDND CGKEFTLLVP IATIGCGKTT VAKILEKLFG WPVVQNDNLP
     SGKGGPKRFA KAIIEEFRNG HSVVFADRNN HISNMRSTLQ TDILALIDGV RFVALPFKHT
     PEVPEFVQNR VLQRGDRHQS IKVSEGVDKV KAIMNTFYKQ YKPFDPAGNK HDANYDDIIE
     LDPLIGSLEN ARRIVNYFKK NIPELIPNDP SDDDYAAALN YAVNEYVPTY RKTFGNDSKK
     IKNKITAEGI TGSSTCFKKA PRYFGVLLDR KTVESSLVQV LTIANLQWQE AFSRYTLQDS
     FHITMIHESQ KPVNSRIWEQ YLQHMHDKNT TKMGNISFRI THLVWDDRVI CFRVTMNENS
     VWYGKTCNPQ LHITLGTSSS DVKAFESNFL LKKLRWQGDE VDSTDGNVRY LTVLPKIIIE
     GMLEPVY