(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7W9_ASPNC

ID   A2Q7W9_ASPNC            Unreviewed;       276 AA.
AC   A2Q7W9;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 72.
DE   RecName: Full=tRNA-splicing endonuclease subunit Sen34 {ECO:0000256|PIRNR:PIRNR017250};
DE            EC=4.6.1.16 {ECO:0000256|PIRNR:PIRNR017250};
GN   ORFNames=An01g02220 {ECO:0000313|EMBL:CAK43592.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43592.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-
CC       splicing endonuclease complex, a complex responsible for identification
CC       and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at
CC       the 5'- and 3'-splice sites to release the intron. The products are an
CC       intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and
CC       5'-OH termini. There are no conserved sequences at the splice sites,
CC       but the intron is invariably located at the same site in the gene,
CC       placing the splice sites an invariant distance from the constant
CC       structural features of the tRNA body. {ECO:0000256|PIRNR:PIRNR017250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC         half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC         a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017250};
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000256|PIRNR:PIRNR017250}.
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DR   EMBL; AM269955; CAK43592.1; -; Genomic_DNA.
DR   PaxDb; A2Q7W9; -.
DR   EnsemblFungi; CAK43592; CAK43592; An01g02220.
DR   HOGENOM; HOG000175584; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0000214; C:tRNA-intron endonuclease complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000213; F:tRNA-intron endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR   InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR   InterPro; IPR006676; tRNA_splic.
DR   InterPro; IPR016690; tRNA_splic_SEN34.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   PIRSF; PIRSF017250; tRNA_splic_SEN34; 1.
DR   SUPFAM; SSF53032; SSF53032; 1.
DR   TIGRFAMs; TIGR00324; endA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7W9.
DR   SWISS-2DPAGE; A2Q7W9.
KW   Lyase {ECO:0000256|PIRNR:PIRNR017250};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR017250}.
FT   DOMAIN          179..250
FT                   /note="tRNA_int_endo"
FT                   /evidence="ECO:0000259|Pfam:PF01974"
FT   REGION          128..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017250-50"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017250-50"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017250-50"
SQ   SEQUENCE   276 AA;  30699 MW;  D5AEF13C71B9FE04 CRC64;
     MDIEPTLPIP ISYIGGSYFL FSIDAVTYVR REYHICGVLS GTLPQIPQQN VFLGLPLKLM
     PEEARLLVEK GVACIVDEVK VQKDGMRALM EEDRKKYLRE LESQGQHAMR LQNDRKEQQR
     EKALKKIEEK KAAKAKKSAE RQQEQQPAPL NNEAAAQDPV VDLFANDQEA TASDVPSSYP
     LFAHLHSEGY FLSPGLRFGC QYLAYPGDPL RFHSHFLSVS ADWDEELDLM SIVAGGRLGT
     GVKKGFLIGG AEKKIEGSDA GDPSSVRTFS IEWGGM
//

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