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Database: UniProt
Entry: B8P466_POSPM
LinkDB: B8P466_POSPM
Original site: B8P466_POSPM 
ID   B8P466_POSPM            Unreviewed;       814 AA.
AC   B8P466;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=tRNA ligase {ECO:0000256|PIRNR:PIRNR019634};
DE            EC=6.5.1.3 {ECO:0000256|PIRNR:PIRNR019634};
GN   ORFNames=POSPLDRAFT_100403 {ECO:0000313|EMBL:EED84337.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED84337.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(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}.
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DR   EMBL; EQ966251; EED84337.1; -; Genomic_DNA.
DR   RefSeq; XP_002470448.1; XM_002470403.1.
DR   AlphaFoldDB; B8P466; -.
DR   KEGG; ppl:POSPLDRAFT_100403; -.
DR   HOGENOM; CLU_010316_1_0_1; -.
DR   InParanoid; B8P466; -.
DR   OMA; FQDWDYK; -.
DR   OrthoDB; 1405617at2759; -.
DR   Proteomes; UP000001743; 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:UP000001743};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR019634}.
FT   DOMAIN          80..326
FT                   /note="T4 RNA ligase 1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09511"
FT   DOMAIN          429..568
FT                   /note="tRNA ligase kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08303"
FT   DOMAIN          624..811
FT                   /note="tRNA ligase phosphodiesterase"
FT                   /evidence="ECO:0000259|Pfam:PF08302"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019634-50"
SQ   SEQUENCE   814 AA;  91357 MW;  54BC58BE4721D595 CRC64;
     MAALPTSEPA AELEKLSISK HGSEKDSELI DELLALSKKN PKLVRSTEYT APADPNINVR
     SWKMNEFKYY DVPSPFPTLA RGLFTQDVQT NDRVKHRIVA RGYDKFFNIG EVPWTTWASL
     ESHTGAPYIL TLKSNGCIIF IAALTPDKLL ITSKHALGPS NNAEYKSHAQ FGEQWLRKHL
     LDAGKTEEQL AATLWEKNWT AVAELCDDSF EEHVLPYGPE KTGLHLHGLN ECTRQFKTMD
     QPVVDAFAKE WGFIQTLSTV LDTVPQVREF TEAIGRTGKW NGEALEGFVV RTRVVDPPTK
     GGQPAAASPY RAGSSFFFKV KFDEPYMMYR DWREVTKALL SKGPSMGNVP KSKLRRPETR
     VYINWVIDEI KRDREQFATY THGKGIIATR ERFLNWLRSE EGSKAVKRQD ELPAERGLIR
     EGEKFGKTII APIAVPGVGK TSIAVALSHL FGFGHIQSDD IKAKKAAPIF IKNVVNALKT
     NDVVIADKNN HLIQHRQQLR EAVRTFKPPV RLMALNWSFD QPLSTIHRIC GDRVLQRGEN
     HQSLHGDPLA KSHEDVIWQF MNQAEELADE EVDVAVEMDW EETLEDALTR AVDACVRILG
     MPRPDQEKVG EALAIARGYA PSTKANKADS AKAKKQAVRY YAILAEVDLQ DVLGKRFAEA
     GIPRDGKTFW ENLKAQKRIA PRPHITLVHQ KALPGETALW ERCKELHLHS NPPLFSFRLS
     NLVWNDRVMA ATVSDFAIST DGSHQDAKGL DLVLKLPFEV QNRLHVTVGT RDGVPPVEAK
     ALVESWKKNK HISGVGSLEL DNVWVKGSVK GLVN
//
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