ID Q5BDT4_EMENI Unreviewed; 810 AA.
AC Q5BDT4; C8VS89;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=tRNA ligase {ECO:0000256|PIRNR:PIRNR019634};
DE EC=6.5.1.3 {ECO:0000256|PIRNR:PIRNR019634};
GN ORFNames=ANIA_01296 {ECO:0000313|EMBL:CBF87771.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF87771.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001308; CBF87771.1; -; Genomic_DNA.
DR RefSeq; XP_658900.1; XM_653808.1.
DR AlphaFoldDB; Q5BDT4; -.
DR STRING; 227321.Q5BDT4; -.
DR EnsemblFungi; CBF87771; CBF87771; ANIA_01296.
DR GeneID; 2877064; -.
DR KEGG; ani:AN1296.2; -.
DR eggNOG; ENOG502QQB9; Eukaryota.
DR HOGENOM; CLU_010316_1_0_1; -.
DR InParanoid; Q5BDT4; -.
DR OMA; FQDWDYK; -.
DR OrthoDB; 1405617at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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, ECO:0000313|EMBL:CBF87771.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR019634}.
FT DOMAIN 55..288
FT /note="T4 RNA ligase 1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09511"
FT DOMAIN 373..534
FT /note="tRNA ligase kinase"
FT /evidence="ECO:0000259|Pfam:PF08303"
FT DOMAIN 537..806
FT /note="tRNA ligase phosphodiesterase"
FT /evidence="ECO:0000259|Pfam:PF08302"
FT REGION 583..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR019634-50"
SQ SEQUENCE 810 AA; 91356 MW; DE7D0F91533C616F CRC64;
MAKALEGARL ENKGAKKKTF NCRKSTFKVG KAGDISADSW KFMDWDYKRR DLPTYARGLF
TAKRKDGTTE IVTRGYDKFF NVDEVSATQW RNIEAYTEGP YELSVKENGC IIFISGLEDG
SLLVCSKHST GARADTDRSH AQVGEEWIER HVATVGKSTA ELAKQLREMN ATAVGELCDD
SFEEHVLAYD SAAAGIYLHG INYNLPEFAT LPSSEVHRFA DAWGFKKANF VVYDDLSTVK
KFLEKCAETG SWDGRDTEGF VIRCKMSENG HGPYRDWFFK YKFEEPYLMY RQWRECTKAI
LSGKAPKIKK HKKITEEYLA YARQQFALHP KLREQYQHNH GIISMRDGFL KERGLNGAQI
IQMEAENVTR DVVLVPIASI GCGKTTVGLA LTKLFGWGQV QNDNIPKQKN KPKQFVANIL
NLLMDKPAVI ADRNNHQRRE RSQLINDIVA GSPNARFVAL HYVHEPKDMM LPLIREVTRK
RVLDRGDNHQ TIRAGTKDTD EVLGIMEGFL RRFETVDVDH EPDQNFDEVI DLDVTASSRE
NLEKVVNALH SAYPQLVTKV PSAQELDDAI NYATSEYSVE VDHSASYGQS KPSKQSNKSN
SNKNGGSEIN IEAKVRKIEY FGISLPTSSV TDLLHSLFAN PAITPEKARL YHHLVNSRRV
QPAFHVTLIH KALKTAHPDV WEDLVNRYVG QMKKNPPKDH ALTPPLGSAR VRLERLIWDD
KIMTFVARIM PGEPENSGDN AEPQPDWICV NPLPHVTVGT VSPAVKPKES NDLLQRWLQE
GSQGTGIWEM EIPGVKVVNG TVNVTMSRGK
//
