CRS2_MAIZE
ID CRS2_MAIZE Reviewed; 256 AA.
AC Q9M5P4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Chloroplastic group IIB intron splicing facilitator CRS2, chloroplastic;
DE AltName: Full=Chloroplastic RNA splicing factor 2;
DE AltName: Full=Protein CHLOROPLAST RNA SPLICING 2;
DE Flags: Precursor;
GN Name=CRS2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RNA, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11179231; DOI=10.1093/emboj/20.4.872;
RA Jenkins B.D., Barkan A.;
RT "Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II
RT intron splicing in chloroplasts.";
RL EMBO J. 20:872-879(2001).
RN [2]
RP FUNCTION.
RX PubMed=9090875; DOI=10.2307/3870482;
RA Jenkins B.D., Kulhanek D.J., Barkan A.;
RT "Nuclear mutations that block group II RNA splicing in maize chloroplasts
RT reveal several intron classes with distinct requirements for splicing
RT factors.";
RL Plant Cell 9:283-296(1997).
RN [3]
RP FUNCTION.
RX PubMed=10481026; DOI=10.1093/nar/27.19.3866;
RA Vogel J., Boerner T., Hess W.R.;
RT "Comparative analysis of splicing of the complete set of chloroplast group
RT II introns in three higher plant mutants.";
RL Nucleic Acids Res. 27:3866-3874(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH CAF1 AND CAF2.
RX PubMed=12881426; DOI=10.1093/emboj/cdg372;
RA Ostheimer G.J., Williams-Carrier R., Belcher S., Osborne E., Gierke J.,
RA Barkan A.;
RT "Group II intron splicing factors derived by diversification of an ancient
RT RNA-binding domain.";
RL EMBO J. 22:3919-3929(2003).
RN [5]
RP INTERACTION WITH CAF1 AND CAF2.
RX PubMed=16379013; DOI=10.1074/jbc.m508921200;
RA Ostheimer G.J., Rojas M., Hadjivassiliou H., Barkan A.;
RT "Formation of the CRS2-CAF2 group II intron splicing complex is mediated by
RT a 22-amino acid motif in the COOH-terminal region of CAF2.";
RL J. Biol. Chem. 281:4732-4738(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 55-256, INTERACTION WITH CAF1 AND
RP CAF2, AND MUTAGENESIS OF ILE-100; SER-102 AND ILE-108.
RX PubMed=15567410; DOI=10.1016/j.jmb.2004.10.032;
RA Ostheimer G.J., Hadjivassiliou H., Kloer D.P., Barkan A., Matthews B.W.;
RT "Structural analysis of the group II intron splicing factor CRS2 yields
RT insights into its protein and RNA interaction surfaces.";
RL J. Mol. Biol. 345:51-68(2005).
CC -!- FUNCTION: Required for the splicing of group IIB introns in
CC chloroplasts. Forms complexes with either CAF1 or CAF2 which, in turn,
CC interact with RNA and confer intron specificity of the splicing
CC particles. Has no peptidyl-tRNA hydrolase activity.
CC {ECO:0000269|PubMed:10481026, ECO:0000269|PubMed:11179231,
CC ECO:0000269|PubMed:12881426, ECO:0000269|PubMed:9090875}.
CC -!- SUBUNIT: Interacts with CAF1 and CAF2. Part of large ribonucleo-protein
CC complexes that include group IIB introns and either CAF1 or CAF2.
CC {ECO:0000269|PubMed:11179231, ECO:0000269|PubMed:12881426,
CC ECO:0000269|PubMed:15567410, ECO:0000269|PubMed:16379013}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11179231}.
CC -!- SIMILARITY: Belongs to the PTH family. CRS2 subfamily. {ECO:0000305}.
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DR EMBL; AF225708; AAF27939.1; -; mRNA.
DR PDB; 1RYB; X-ray; 1.70 A; A=57-249.
DR PDB; 1RYM; X-ray; 1.80 A; A=57-249.
DR PDB; 1RYN; X-ray; 1.75 A; A=58-250.
DR PDBsum; 1RYB; -.
DR PDBsum; 1RYM; -.
DR PDBsum; 1RYN; -.
DR AlphaFoldDB; Q9M5P4; -.
DR SMR; Q9M5P4; -.
DR BioGRID; 951029; 1.
DR STRING; 4577.GRMZM2G132021_P03; -.
DR PaxDb; Q9M5P4; -.
DR MaizeGDB; 106358; -.
DR eggNOG; KOG2255; Eukaryota.
DR EvolutionaryTrace; Q9M5P4; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9M5P4; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1470; -; 1.
DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR InterPro; IPR001328; Pept_tRNA_hydro.
DR InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; mRNA processing; mRNA splicing; Plastid;
KW Reference proteome; Ribonucleoprotein; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..256
FT /note="Chloroplastic group IIB intron splicing facilitator
FT CRS2, chloroplastic"
FT /id="PRO_0000280532"
FT MUTAGEN 100
FT /note="I->N: Reduced interaction with CAF1 and CAF2. Loss
FT of interaction with CAF1 and CAF2; when associated with F-
FT 102. Loss of interaction with CAF1 and CAF2; when
FT associated with T-108."
FT /evidence="ECO:0000269|PubMed:15567410"
FT MUTAGEN 102
FT /note="S->F: Loss of interaction with CAF1 and CAF2; when
FT associated with N-100."
FT /evidence="ECO:0000269|PubMed:15567410"
FT MUTAGEN 108
FT /note="I->T: Loss of interaction with CAF1 and CAF2; when
FT associated with N-100."
FT /evidence="ECO:0000269|PubMed:15567410"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1RYB"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1RYM"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1RYB"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1RYN"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 213..236
FT /evidence="ECO:0007829|PDB:1RYB"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1RYN"
SQ SEQUENCE 256 AA; 28214 MW; 11D15227394545CB CRC64;
MSLLAAAIPS TSSHFSAPFL PSFRMPRKSL TAPLHRIRRP RPFTVVSSVP DPAAGPVEYT
PWLIAGLGNP GNKYYGTRHN VGFEMVDRIA AEEGITMNTI QSKSLLGIGS IGEVPVLVVK
PQSYMNYSGE AIGPLAAYYQ VPLRHILLIY DDTSLPNGVL RLQKKGGHGR HNGLQNVIEH
LDGRREFPRL SIGIGSPPGK MDPRAFLLQK FSSEERVQID TALEQGVDAV RTLVLKGFSG
STERFNLVQK YKFHRV
