ID   A0A0J8S087_COCIT        Unreviewed;       798 AA.
AC   A0A0J8S087;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=tRNA ligase {ECO:0000256|PIRNR:PIRNR019634};
DE            EC=6.5.1.3 {ECO:0000256|PIRNR:PIRNR019634};
GN   ORFNames=CIHG_08594 {ECO:0000313|EMBL:KMU90790.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU90790.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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}.
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DR   EMBL; DS017026; KMU90790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8S087; -.
DR   STRING; 396776.A0A0J8S087; -.
DR   VEuPathDB; FungiDB:CIHG_08594; -.
DR   eggNOG; ENOG502QQB9; Eukaryota.
DR   Proteomes; UP000054563; 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   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; 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|PIRNR:PIRNR019634, ECO:0000313|EMBL:KMU90790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR019634}.
FT   DOMAIN          64..297
FT                   /note="T4 RNA ligase 1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09511"
FT   DOMAIN          407..513
FT                   /note="tRNA ligase kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08303"
FT   DOMAIN          517..795
FT                   /note="tRNA ligase phosphodiesterase"
FT                   /evidence="ECO:0000259|Pfam:PF08302"
FT   REGION          15..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        115
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019634-50"
SQ   SEQUENCE   798 AA;  90150 MW;  94ED17BFC56D875B CRC64;
     MVQQDSHEVT QLIHSLQAAQ GPKRGGKSFS CKKSTFPVSG SQGTTVDSWK FRDWDYKRDD
     LPTYARGLFT TRTRNGTPEI AIRGYDKFFN VDEVNLTKWE NIEKNTIGPY ELSVKENGCI
     IFMSGLEDGT LLVCSKHSTG PRQDANLSHA VAGQKWVRRH VESVGKTERE LALELRKWNA
     TAVGELCDDS FEEHVLAYDE HSAGIYLHGI NYNVPFFATL SGPEVHKFAD NWGFKKAQFV
     LKNDLSEVRT FLEGCAETGS WGGRDTEGFV VRCKMREAHS GPYVDWFFKY KFEEPYLMYR
     QWRECTKAVI SGRPPKYKKH VKITEEYLQY ARRQLQMNPK LGSLYNQNHG IIAMRDGFLK
     ERGLKGSDII AMETAEGDVA PPISQNIVLV PVASIGCGKT TVALGLAVIA DRNNHQKRER
     KQIIEDIRSI NPDARFVALH YVHEPKGRML DGIRNITRQR VLERGDNHQT IRADSKSPEE
     IIGIMEGFLQ RFEAVDTEHE PDINFDEVID LDIAATSREN LETIVSALYN AYPRLFDGSK
     PSASDLDLAI DAAMKNYTVD VKHDLTFGSK NPSHRQPPSN SGQNQPNTIN GNTIEKLLKR
     IEFFNISLPQ SEINSLAASL FPPSTPPEIS KLYNHLKNSR RIQASFHVTL IHKASAKDRP
     DIWDQYKDLY KNALQRQLQQ PDGHTRNPTP ALGAARVRIE RLVWNDKIMA FVARIMPVDH
     DERLNSHVSR DMGSWECAND IPHVTVGTAA PNIKPKESND LLRHWLEHGA NAETGIMEAE
     IPSVKVLEGI VGVVLSRS
//