ID   SEN2_NEUCR              Reviewed;         633 AA.
AC   Q9P6Y2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable tRNA-splicing endonuclease subunit tsp-2;
DE            EC=4.6.1.16;
DE   AltName: Full=tRNA-intron endonuclease sen2;
DE   AltName: Full=tRNA-splicing protein 2;
GN   Name=tsp-2; Synonyms=sen2; ORFNames=13E11.340, NCU01115;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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. This subunit may anchor the
CC       endonuclease complex to the nuclear membrane. Probably carries the
CC       active site for 5'-splice site cleavage (By similarity). {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       tsp-2/sen2, tsp-1/sen15, tsp-4/sen34 and tsp-5/sen54. Interacts
CC       directly with tsp-5/sen54 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AL353820; CAB88602.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31786.1; -; Genomic_DNA.
DR   PIR; T48786; T48786.
DR   RefSeq; XP_961022.1; XM_955929.3.
DR   AlphaFoldDB; Q9P6Y2; -.
DR   SMR; Q9P6Y2; -.
DR   STRING; 5141.EFNCRP00000004401; -.
DR   EnsemblFungi; EAA31786; EAA31786; NCU01115.
DR   GeneID; 3877201; -.
DR   KEGG; ncr:NCU01115; -.
DR   VEuPathDB; FungiDB:NCU01115; -.
DR   HOGENOM; CLU_012847_1_0_1; -.
DR   InParanoid; Q9P6Y2; -.
DR   OMA; LPAFYPN; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
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   PANTHER; PTHR21227; PTHR21227; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   SUPFAM; SSF53032; SSF53032; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..633
FT                   /note="Probable tRNA-splicing endonuclease subunit tsp-2"
FT                   /id="PRO_0000109460"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        535
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        543
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        586
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   633 AA;  70104 MW;  F7536C1E5E62563E CRC64;
     MAENMTIATM AQPSESPSKS GEEAPASTNP AATSAPPRPP RVPYHQIYKL PAPIRTFPLP
     TFYPSNPLSL FHLAVAWLRQ VLLPPPAEPS VIHEGIWDPD TRSVHVKDPK SIRALWEQGF
     YGKGSLSRSE PNWFKRELSR RGLDGTTVSE ERTASRREER RQVKWERAKA ELEAIEKQKH
     EEAKLNSETV NAAIPEPPAA EIEPEPEVLL SSLPDHVLSA TSTIPLSRAA PTNEFVPKTV
     AHGHVEPKPP VGPLELLALP NSYALVRGEE LALSQPEPAP TEENVRKELK APVGPIELLA
     LPNSLVDLVA LSVVSVLSED AGVDEDESST EDQLEASALT NDEPETSATE ANDSTSSSSP
     PHTDGLPDSQ PTQENVPATP ERRKSVRFSS TVESTTFQHT DAASEVKNNN GSSDVEVFSS
     FVSAVEKPVI LNVEPTVISQ ELVDKEHFQL APEEAFFLTF GLGALRVVDP VTEAPISNEQ
     LLIKLRANSY FPPRSVDNLS PEDPFLVQYA VYHHFRSLGW VPRHGIKFGV DWIIYQRGPV
     FDHSEFGIMV VPSFSDPRWS EFEHEESKKT WSWLMGVNRV LSHVLKSLVL VYVDVPPPPV
     FDEEMKKGGI AAALKKFTIR EVMVRRFSVN RNR