ID   CRS1_MAIZE              Reviewed;         715 AA.
AC   Q9FYT6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic;
DE   AltName: Full=Chloroplastic RNA splicing factor 1;
DE   AltName: Full=Protein CHLOROPLAST RNA SPLICING 1;
DE   Flags: Precursor;
GN   Name=CRS1;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH RNA.
RX   PubMed=11565746; DOI=10.1017/s1355838201010445;
RA   Till B., Schmitz-Linneweber C., Williams-Carrier R., Barkan A.;
RT   "CRS1 is a novel group II intron splicing factor that was derived from a
RT   domain of ancient origin.";
RL   RNA 7:1227-1238(2001).
RN   [2]
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   [3]
RP   FUNCTION, HOMODIMER, AND INTERACTION WITH ATPF INTRON.
RX   PubMed=15598799; DOI=10.1105/tpc.104.027516;
RA   Ostersetzer O., Cooke A.M., Watkins K.P., Barkan A.;
RT   "CRS1, a chloroplast group II intron splicing factor, promotes intron
RT   folding through specific interactions with two intron domains.";
RL   Plant Cell 17:241-255(2005).
CC   -!- FUNCTION: Required for the splicing of group IIA introns in
CC       chloroplasts, and especially for atpF, by regulating the intron
CC       folding. Forms splicing particles with RNA. Also involved in
CC       chloroplast protein translation. {ECO:0000269|PubMed:10481026,
CC       ECO:0000269|PubMed:11565746, ECO:0000269|PubMed:15598799}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-7.5.;
CC       Temperature dependence:
CC         Optimum temperature is 25-30 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. Interacts with RNA, specifically with atpF intron.
CC       Part of large ribonucleo-protein complexes that include group IIA
CC       introns and CRS1. {ECO:0000269|PubMed:11565746,
CC       ECO:0000269|PubMed:15598799}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:11565746}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FYT6-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: More expressed in leaves than in roots.
CC       {ECO:0000269|PubMed:11565746}.
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DR   EMBL; AF290414; AAG00595.1; -; mRNA.
DR   RefSeq; NP_001105008.1; NM_001111538.2. [Q9FYT6-1]
DR   AlphaFoldDB; Q9FYT6; -.
DR   SMR; Q9FYT6; -.
DR   DIP; DIP-48743N; -.
DR   IntAct; Q9FYT6; 1.
DR   STRING; 4577.Q9FYT6; -.
DR   PaxDb; 4577-GRMZM2G078412_P01; -.
DR   GeneID; 541870; -.
DR   KEGG; zma:541870; -.
DR   MaizeGDB; 106357; -.
DR   eggNOG; KOG1990; Eukaryota.
DR   InParanoid; Q9FYT6; -.
DR   OrthoDB; 1215318at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9FYT6; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0000373; P:Group II intron splicing; IEA:UniProt.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.110.60; YhbY-like; 3.
DR   InterPro; IPR045278; CRS1/CFM2/CFM3.
DR   InterPro; IPR001890; RNA-binding_CRM.
DR   InterPro; IPR035920; YhbY-like_sf.
DR   PANTHER; PTHR31846:SF10; CHLOROPLASTIC GROUP IIA INTRON SPLICING FACILITATOR CRS1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31846; CRS1 / YHBY (CRM) DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01985; CRS1_YhbY; 3.
DR   SMART; SM01103; CRS1_YhbY; 3.
DR   SUPFAM; SSF75471; YhbY-like; 3.
DR   PROSITE; PS51295; CRM; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Coiled coil; mRNA processing;
KW   mRNA splicing; Plastid; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding; Transit peptide; Translation regulation.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..715
FT                   /note="Chloroplastic group IIA intron splicing facilitator
FT                   CRS1, chloroplastic"
FT                   /id="PRO_0000283625"
FT   DOMAIN          168..265
FT                   /note="CRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   DOMAIN          350..447
FT                   /note="CRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   DOMAIN          562..662
FT                   /note="CRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          448..473
FT                   /evidence="ECO:0000255"
FT   COILED          502..550
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  81406 MW;  9ADC6ECE35F6C55F CRC64;
     MAPPPLPLFS PSLKAPPPPP WLHGSSTQSR DSAPPVPPLP AEATPSKFRI DSPKPAPARK
     NTKTAAKPLT AGVPGGRTHR AVLGIIRRVR SLELSDAPSP NSVHTSNSGA AAAAFHLTIE
     LSPPREPGQY VVEKEKSRAV PWAAARDEGL KVALRREKKP REPTRAETEL ETHELRRLRR
     LARGIGRWAR AKKAGVTDEV VKEVRREWAS GEELAAVRIV EPLRRSMDRA REILEIKTGG
     LVVWTKGDMH FVYRGSKYQQ NAKHSHTFLT NVHKDDAFQE NDQSICGQKD EEPVKGTLYE
     REVNRLLDTL GPRFVDWWWD TPLPVDADLL PEFVPGSKTP YRLCPPGVRP TLADEELTYL
     RKLARLLPTH FALGRNTRLQ GLAAAILKLW EKSLIAKIAV KIGIQNTNNE QMAWNLKHLT
     GGTVILRNKD FIILYRGKDF LPGGVAQTVI QREAQVHDEQ VKEEEARLKA VDSLQMVGEL
     SEESSLGTFR EYQGFHAKFV HENTENSNTM IELEAEKYRL EKELKDHEWK LSVLNKKIER
     SNQALAKLHS SWSPSEQSAD REHLTEEEKI MFRRIGRKMD GLVLLGRRGI FDGVIEEIHQ
     HWKHKEVVKV ITKQNQTRQI MYAASLLEVE TGGILIAVEK LTTSHAIILY RGKNYRRPAK
     SSFSNLLTKR EALRRSIEVQ RRGSMKYFVR ERQKSILELK RKLRYVTRQI RYRTP
//