ID   SEN2_CHICK              Reviewed;         461 AA.
AC   Q5ZIN2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=tRNA-splicing endonuclease subunit Sen2;
DE            EC=4.6.1.16;
DE   AltName: Full=tRNA-intron endonuclease Sen2;
GN   Name=TSEN2; ORFNames=RCJMB04_24m3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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. Probably carries the active site
CC       for 5'-splice site cleavage. The tRNA splicing endonuclease is also
CC       involved in mRNA processing via its association with pre-mRNA 3'-end
CC       processing factors, establishing a link between pre-tRNA splicing and
CC       pre-mRNA 3'-end formation, suggesting that the endonuclease subunits
CC       function in multiple RNA-processing events (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC       SEN2, SEN15, SEN34/LENG5 and SEN54. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000305}.
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; AJ720752; CAG32411.1; -; mRNA.
DR   RefSeq; NP_001025765.1; NM_001030594.2.
DR   AlphaFoldDB; Q5ZIN2; -.
DR   SMR; Q5ZIN2; -.
DR   STRING; 9031.ENSGALP00000073696; -.
DR   PaxDb; 9031-ENSGALP00000007969; -.
DR   GeneID; 415965; -.
DR   KEGG; gga:415965; -.
DR   CTD; 80746; -.
DR   VEuPathDB; HostDB:geneid_415965; -.
DR   eggNOG; KOG4685; Eukaryota.
DR   InParanoid; Q5ZIN2; -.
DR   PhylomeDB; Q5ZIN2; -.
DR   PRO; PR:Q5ZIN2; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0000214; C:tRNA-intron endonuclease complex; IBA:GO_Central.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR   CDD; cd22363; tRNA-intron_lyase_C; 1.
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; IPR006678; tRNA_intron_Endonuc_N.
DR   InterPro; IPR006676; tRNA_splic.
DR   InterPro; IPR016589; tRNA_splic_SEN2.
DR   PANTHER; PTHR21227; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1.
DR   PANTHER; PTHR21227:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   Pfam; PF02778; tRNA_int_endo_N; 1.
DR   PIRSF; PIRSF011789; tRNA_splic_SEN2; 1.
DR   SUPFAM; SSF53032; tRNA-intron endonuclease catalytic domain-like; 1.
PE   2: Evidence at transcript level;
KW   Lyase; mRNA processing; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..461
FT                   /note="tRNA-splicing endonuclease subunit Sen2"
FT                   /id="PRO_0000109455"
FT   REGION          140..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  52134 MW;  69108F9DAE6EC982 CRC64;
     MAEAAFHPPR RKRRVFECYQ APFPVGPGAG DFRMCRADMV NNCVVVRSPE DMDQLYNKGY
     FGKGILSRSR PVYSISDPSL VSKWQGANLN VPIITSKKYQ QRVQWAKSAL QEQGFDGCSV
     TKILENYTRP LEFPFLEKGG AEQTGDSCDT VCPNTENTEL SGQSSTDTGN IATSSPECQK
     EVCQKAYAEG DPASDSMVGS KEQEPADVKE TAQTSCQMHG SCMHCGCKAK GAPDRESCNM
     AKSRERAPEY VLVQEEEESS LCPEEGSARE QENFVKKEKL VCRRNPFRIF EYLQLSLEEA
     FFLVYALGCL TVYYGEEPLT ILKLWEIFSE VKPSFKTTYM AYHYFRSKGW VPKVGLKYGT
     DLLLYRKGPP FYHASYSVIA ELVDDNFEGS LRRPLSWMSL SGLNRTTVNA SKELLLCYLI
     KPSDMTEEEM ATPECLKRIK VQELIVTRWV SSRERSEQDD L
//