ID Q0CQ34_ASPTN Unreviewed; 816 AA.
AC Q0CQ34;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=tRNA ligase {ECO:0000256|PIRNR:PIRNR019634};
DE EC=6.5.1.3 {ECO:0000256|PIRNR:PIRNR019634};
GN ORFNames=ATEG_04200 {ECO:0000313|EMBL:EAU36002.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU36002.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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|PIRNR:PIRNR019634};
CC -!- SIMILARITY: Belongs to the TRL1 family.
CC {ECO:0000256|PIRNR:PIRNR019634}.
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DR EMBL; CH476598; EAU36002.1; -; Genomic_DNA.
DR RefSeq; XP_001213378.1; XM_001213378.1.
DR AlphaFoldDB; Q0CQ34; -.
DR STRING; 341663.Q0CQ34; -.
DR EnsemblFungi; EAU36002; EAU36002; ATEG_04200.
DR GeneID; 4318562; -.
DR VEuPathDB; FungiDB:ATEG_04200; -.
DR eggNOG; ENOG502QQB9; Eukaryota.
DR HOGENOM; CLU_010316_1_0_1; -.
DR OMA; FQDWDYK; -.
DR OrthoDB; 1405617at2759; -.
DR Proteomes; UP000007963; 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:UP000007963};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR019634}.
FT DOMAIN 66..299
FT /note="T4 RNA ligase 1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09511"
FT DOMAIN 385..546
FT /note="tRNA ligase kinase"
FT /evidence="ECO:0000259|Pfam:PF08303"
FT DOMAIN 549..813
FT /note="tRNA ligase phosphodiesterase"
FT /evidence="ECO:0000259|Pfam:PF08302"
FT REGION 598..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR019634-50"
SQ SEQUENCE 816 AA; 92357 MW; EA4E48CB3E231539 CRC64;
MVRQDPTEVG DLIAALETAS KRTKREGKKT FSCKKSTFPV AGSDHISVDS WRFMDWEYKR
SDLPTYARGL FTTIRKDGTP EIAVRGYDKF FNVDEVNATK WRNIENNTRG PYELSVKENG
CIIFISGLED DTLLVCSKHS TGVRSDAAVS HAQAGEQWVE RHLAATGRSV KDLARELRSM
NATAVGELCD DQFEEHVLAY DENAAGIYLH GLNYNVPYFA TCSGAEVHAF ADKWGFKKAK
YVVYEDLDAV KKFLEQCAET GSWDGRETEG FVVRCQMNQG GVGPYMDWFF KYKFEEPYLM
YRQWRECTKA VISGKVPNIK KHKKITEEYL QYARRQFAQN PGLAKQYQQN HGIIALREGF
LRERGLKGSE IIAMATENEV TRDVILCPIA SLGCGKTTVA LALTKLFGWG HIQNDNIPKQ
KNKPKKFALD ITMQLADKPV VIADRNNHMR RERQQLMDDI FPVIPAARFV ALQYVHEPKG
VLLPGIREVT RKRVLDRGDN HQTIRAGSKD SSEIIGIMEG FLNRFEAVDT DREPDKSFDE
VIDLDVAASS RENLEKVVTA LHSFYPEVVK QVPSAQELDD AIEWAMSEYE VQLDLSHQYS
SKQNQKQKNK GNKDHGGPPQ APPSPEVLAK NIEYFCISLP AAEVSSVLHS LFPPSTAPEK
ARLYHQLVNS RRVQPTFHVT LIHRASKKDQ PEVWEQYVRL YIEKMHQKPE SDPTVTPVLA
PARVRLERLV WDDRLMTFVA RIMPPEDQDQ ADWPCANALP HVTVGTVSPD VKPKESNDLL
QRWLENGSGA DKGIWEAEIP GVKVVSGSVG LVMSRR
//
