ID   CAF2P_MAIZE             Reviewed;         611 AA.
AC   Q84N48;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=CRS2-associated factor 2, chloroplastic;
DE   AltName: Full=Chloroplastic group IIA intron splicing facilitator CRS2-associated factor 2;
DE   Flags: Precursor;
GN   Name=CAF2;
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, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH CRS2.
RC   STRAIN=cv. B73;
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   [2]
RP   INTERACTION WITH CRS2.
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).
CC   -!- FUNCTION: Required for the splicing of group IIB introns in
CC       chloroplasts. Forms splicing particles with CRS2. Interacts with RNA
CC       and confers intron specificity of the splicing particles.
CC       {ECO:0000269|PubMed:12881426}.
CC   -!- SUBUNIT: Interacts with CRS2 and RNA. Part of large ribonucleo-protein
CC       complexes that include group IIB introns, CRS2 and CAF2.
CC       {ECO:0000269|PubMed:12881426, ECO:0000269|PubMed:16379013}.
CC   -!- INTERACTION:
CC       Q84N48; A7UDM2: CFM2; NbExp=2; IntAct=EBI-15761721, EBI-15761773;
CC       Q84N48; B6TTV8: WTF1; NbExp=3; IntAct=EBI-15761721, EBI-15761679;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:12881426}.
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DR   EMBL; AY264369; AAP22136.1; -; mRNA.
DR   RefSeq; NP_001105669.1; NM_001112199.1.
DR   AlphaFoldDB; Q84N48; -.
DR   SMR; Q84N48; -.
DR   BioGRID; 951897; 1.
DR   DIP; DIP-48741N; -.
DR   IntAct; Q84N48; 5.
DR   STRING; 4577.AC199526.5_FGP003; -.
DR   PaxDb; Q84N48; -.
DR   PRIDE; Q84N48; -.
DR   EnsemblPlants; Zm00001eb130860_T001; Zm00001eb130860_P001; Zm00001eb130860.
DR   GeneID; 542682; -.
DR   Gramene; Zm00001eb130860_T001; Zm00001eb130860_P001; Zm00001eb130860.
DR   KEGG; zma:542682; -.
DR   MaizeGDB; 886551; -.
DR   eggNOG; ENOG502QW9P; Eukaryota.
DR   HOGENOM; CLU_012688_1_0_1; -.
DR   OrthoDB; 408261at2759; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   ExpressionAtlas; Q84N48; baseline and differential.
DR   Genevisible; Q84N48; ZM.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0000373; P:Group II intron splicing; IEA:EnsemblPlants.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.110.60; -; 2.
DR   InterPro; IPR044599; CAF1P_plant.
DR   InterPro; IPR001890; RNA-binding_CRM.
DR   InterPro; IPR035920; YhbY-like_sf.
DR   PANTHER; PTHR46247; PTHR46247; 1.
DR   Pfam; PF01985; CRS1_YhbY; 2.
DR   SMART; SM01103; CRS1_YhbY; 2.
DR   SUPFAM; SSF75471; SSF75471; 2.
DR   PROSITE; PS51295; CRM; 2.
PE   1: Evidence at protein level;
KW   Chloroplast; mRNA processing; mRNA splicing; Plastid; Reference proteome;
KW   Repeat; Ribonucleoprotein; RNA-binding; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..611
FT                   /note="CRS2-associated factor 2, chloroplastic"
FT                   /id="PRO_0000283620"
FT   DOMAIN          232..328
FT                   /note="CRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   DOMAIN          350..446
FT                   /note="CRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..509
FT                   /note="CRS2 binding"
FT   REGION          554..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  68069 MW;  587E44D18160AED7 CRC64;
     MPPPPPQRPA SSHVGRANLF SASPPPLSNR RYPHHRSLPL PPVSPRRRDP KKHSQQPSQE
     EPTDSGPTRT VTTNPAFRAA HLRTAYRKPV PPAAAAGEGE ALLAADPTDA ASGRAVVVGP
     SGLSFRLPGA PFDFQFSYSE APRAPPLAIR EPAFLPFAPP TMPRPWTGKA PLLTKEEKAR
     RRGVRLHTPL GQETPQTVSA HGIMMEVRER RKMDLARVSP GDGRSREEVL GEPLTPSEVR
     ALVKPHISHN RQLNIGRDGL THNMLEMIHC HWRRQEICKV RCRGVPTVDM KNLCYHLEEK
     SGGKVIHRVG GVVFLYRGRH YDPKTRPRYP LMLWKPATPV YPKLIKEAPD GFTKEEADEM
     RRKGRDLLPI CKLAKNGIYI TLVKDVRDAF EGSDLVKIDC EGLNPSDYKK IGAKLRDLVP
     CVLLSFDDEQ ILMHRGKEWK SRYSKPLTLI PKVPKNNLAM TSVMNSSDEV SDANTQVAIR
     EVLRPKMFKL WKSAVDSSLA LLLDDAEANN LTPDSLLTLV EEFSVTSQAV EHSFPALLVT
     NGDASTDSLS AEYMNDEPET SVAGNEEGQL EQSPDLRDDE HFDVDMFERL ESSVPLGSLP
     IDSMIERLNS E