CFM3_MAIZE
ID CFM3_MAIZE Reviewed; 842 AA.
AC A7XN92;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=CRM-domain containing factor CFM3, chloroplastic/mitochondrial {ECO:0000305};
DE AltName: Full=Protein CRM FAMILY MEMBER 3 {ECO:0000303|PubMed:18799595};
DE Short=ZmCFM3 {ECO:0000303|PubMed:18799595};
DE Flags: Precursor;
GN Name=CFM3 {ECO:0000303|PubMed:18799595};
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18799595; DOI=10.1261/rna.1223708;
RA Asakura Y., Bayraktar O.A., Barkan A.;
RT "Two CRM protein subfamilies cooperate in the splicing of group IIB introns
RT in chloroplasts.";
RL RNA 14:2319-2332(2008).
CC -!- FUNCTION: Binds specific group II introns in chloroplasts and
CC facilitates their splicing. Acts on subgroup IIB introns. The
CC substrates of the subgroup IIB also require the CRM domain proteins
CC CAF1 or CAF2, with a simultaneous binding of CFM3 and CAF1 or CAF2
CC (PubMed:18799595). May influence the biogenesis of the mitochondrial
CC small ribosomal subunit (By similarity). {ECO:0000250|UniProtKB:F4J2U9,
CC ECO:0000269|PubMed:18799595}.
CC -!- SUBUNIT: Interacts with RNA. Part of large ribonucleo-protein particles
CC that contain CAF1 and/or CAF2, and RNC1. {ECO:0000269|PubMed:18799595}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18799595}. Mitochondrion
CC {ECO:0000269|PubMed:18799595}.
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DR EMBL; EU084957; ABU96081.1; -; mRNA.
DR RefSeq; NP_001106061.1; NM_001112591.1.
DR AlphaFoldDB; A7XN92; -.
DR SMR; A7XN92; -.
DR DIP; DIP-48745N; -.
DR IntAct; A7XN92; 4.
DR STRING; 4577.GRMZM2G436001_P02; -.
DR PaxDb; A7XN92; -.
DR EnsemblPlants; Zm00001eb114780_T001; Zm00001eb114780_P001; Zm00001eb114780.
DR GeneID; 100126360; -.
DR Gramene; Zm00001eb114780_T001; Zm00001eb114780_P001; Zm00001eb114780.
DR KEGG; zma:100126360; -.
DR eggNOG; KOG1990; Eukaryota.
DR eggNOG; KOG2492; Eukaryota.
DR OMA; DLYNHTD; -.
DR OrthoDB; 505933at2759; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; A7XN92; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.110.60; -; 3.
DR InterPro; IPR033262; CFM3.
DR InterPro; IPR045278; CRS1/CFM2/CFM3.
DR InterPro; IPR001890; RNA-binding_CRM.
DR InterPro; IPR035920; YhbY-like_sf.
DR PANTHER; PTHR31846; PTHR31846; 1.
DR PANTHER; PTHR31846:SF19; PTHR31846:SF19; 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 Chloroplast; Coiled coil; Mitochondrion; mRNA processing; mRNA splicing;
KW Plastid; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..82
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 83..842
FT /note="CRM-domain containing factor CFM3,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000435534"
FT DOMAIN 167..263
FT /note="CRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 371..468
FT /note="CRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 582..682
FT /note="CRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT REGION 49..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 703..732
FT /evidence="ECO:0000255"
FT COMPBIAS 266..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..814
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 94060 MW; E58230C8375B8B26 CRC64;
MAMASSPACH FRHPPRLRLL LPLSTSAPHP WLYSWSHPRQ RGRLRAPPAA LDLRPEPSPS
SDSDDEDAVG ASRSSGRSTM SLILSRLRRA GYSGEDPRAA APPHPPRGSV EDVFRADDGV
LPNARGGFDA DDEERALGDA RFPWERPMPP PEAAPRSARS PTWMAELTLP AAELRRLRHA
AIRIKSRTKV GGAGVTREIV EKIKEKWKTE EVVRVKVSGT PALNMRLFHE ILERKTGGLV
IWRSGTSVSL YRGVDYDEPE PTKKSKKNSQ SLAMDFPIKG SSNPSLLPTE TANSVRDSNV
ALVSNAAKEE LVVQAPEIKY EDEIDKLLDE LGPRYTDWPG SDPLPVDADL LPANMPGYKP
PFRVLPYGVR PSLSRRDTTN LRRLARGLPP HFALGRSRQL QGLANAMVKL WEKSSIAKIA
LKRGVQLTTS ERMAEDIKKL TGGVMLSRNN EFIVFYRGKD FLSSELAEVL LERERLAKSL
QDEEEARRKA ASYFSSAETY AQPTVAGTLG ETLEANSKYG TKHDENHADK MARTIEAARH
ADLVRKLEWK LSLAQKKMEK AERVLGKVET ALRPTEDSRP PETITDEERF MFRKLGLRMK
AFLLLGRRGV FDGTIENMHL HWKYRELVKI LVKAKSFADV KRIALSLEAE SGGILVSVDK
VSKGYAIVVF RGKNYRRPSS LRPRNLLSKR KALARSIELQ RHQALSRHFA KLNRKVERLK
AELVQMEDVK EQGDEELYAK LDAAYSSDDE DMEDEDDEAY LKRFDNEVAG ATADDDGSDD
YTSAADEADY PDSDDEAGDC SEDEGEDDED EAAAGVSDAG FHGEVVGFSS DTDRRNHDVN
EY
