CRS1_MAIZE
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 03-AUG-2022, entry version 78.
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.GRMZM2G078412_P01; -.
DR PaxDb; Q9FYT6; -.
DR PRIDE; Q9FYT6; -.
DR GeneID; 541870; -.
DR KEGG; zma:541870; -.
DR MaizeGDB; 106357; -.
DR eggNOG; KOG1990; Eukaryota.
DR OrthoDB; 505933at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9FYT6; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0000373; P:Group II intron splicing; IEA:EnsemblPlants.
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; -; 3.
DR InterPro; IPR045278; CRS1/CFM2/CFM3.
DR InterPro; IPR001890; RNA-binding_CRM.
DR InterPro; IPR035920; YhbY-like_sf.
DR PANTHER; PTHR31846; PTHR31846; 1.
DR Pfam; PF01985; CRS1_YhbY; 3.
DR SMART; SM01103; CRS1_YhbY; 3.
DR SUPFAM; SSF75471; SSF75471; 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
