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CFM9_ARATH
ID   CFM9_ARATH              Reviewed;         491 AA.
AC   Q9LT57;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=CRM-domain containing factor CFM9, mitochondrial {ECO:0000305};
DE   AltName: Full=Protein CRM FAMILY MEMBER 9 {ECO:0000303|PubMed:31359042};
DE   Flags: Precursor;
GN   Name=CFM9 {ECO:0000303|PubMed:31359042};
GN   OrderedLocusNames=At3g27550 {ECO:0000312|Araport:AT3G27550};
GN   ORFNames=MMJ24.10 {ECO:0000312|EMBL:BAB01285.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31359042; DOI=10.1093/pcp/pcz147;
RA   Lee K., Park S.J., Park Y.I., Kang H.;
RT   "CFM9, a mitochondrial CRM protein, is crucial for mitochondrial intron
RT   splicing, mitochondria function, and Arabidopsis growth and stress
RT   responses.";
RL   Plant Cell Physiol. 60:2538-2548(2019).
CC   -!- FUNCTION: Involved in the splicing of group II introns in mitochondria
CC       (PubMed:31359042). Required for the splicing of mitochondrial introns
CC       found in nad1, nad2, nad4, nad5, nad7, rps3 and cox2 genes
CC       (PubMed:31359042). Splicing of mitochondrial introns is crucial for
CC       mitochondrial biogenesis and function, plant growth and development,
CC       and plant response to abiotic stresses (PubMed:31359042).
CC       {ECO:0000269|PubMed:31359042}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:31359042}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and meristemic regions of
CC       young seedlings (PubMed:31359042). Expressed at low levels in stems,
CC       trichomes and stigma (PubMed:31359042). {ECO:0000269|PubMed:31359042}.
CC   -!- DISRUPTION PHENOTYPE: Delayed seed germination, retarded growth and
CC       reduced size and height. {ECO:0000269|PubMed:31359042}.
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DR   EMBL; AB025626; BAB01285.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77336.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65985.1; -; Genomic_DNA.
DR   RefSeq; NP_001319656.1; NM_001338891.1.
DR   RefSeq; NP_189392.1; NM_113671.3.
DR   AlphaFoldDB; Q9LT57; -.
DR   SMR; Q9LT57; -.
DR   STRING; 3702.AT3G27550.1; -.
DR   iPTMnet; Q9LT57; -.
DR   PaxDb; Q9LT57; -.
DR   PRIDE; Q9LT57; -.
DR   ProteomicsDB; 181725; -.
DR   EnsemblPlants; AT3G27550.1; AT3G27550.1; AT3G27550.
DR   EnsemblPlants; AT3G27550.3; AT3G27550.3; AT3G27550.
DR   GeneID; 822377; -.
DR   Gramene; AT3G27550.1; AT3G27550.1; AT3G27550.
DR   Gramene; AT3G27550.3; AT3G27550.3; AT3G27550.
DR   KEGG; ath:AT3G27550; -.
DR   Araport; AT3G27550; -.
DR   TAIR; locus:2091458; AT3G27550.
DR   eggNOG; KOG1990; Eukaryota.
DR   HOGENOM; CLU_032610_0_0_1; -.
DR   InParanoid; Q9LT57; -.
DR   OMA; CSRTCKW; -.
DR   PhylomeDB; Q9LT57; -.
DR   PRO; PR:Q9LT57; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LT57; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR   GO; GO:0140040; P:mitochondrial polycistronic RNA processing; IMP:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR   Gene3D; 3.30.110.60; -; 1.
DR   InterPro; IPR040286; At3g25440-like.
DR   InterPro; IPR001890; RNA-binding_CRM.
DR   InterPro; IPR035920; YhbY-like_sf.
DR   PANTHER; PTHR31426; PTHR31426; 2.
DR   Pfam; PF01985; CRS1_YhbY; 1.
DR   SMART; SM01103; CRS1_YhbY; 1.
DR   SUPFAM; SSF75471; SSF75471; 1.
DR   PROSITE; PS51295; CRM; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; mRNA processing; mRNA splicing; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..491
FT                   /note="CRM-domain containing factor CFM9, mitochondrial"
FT                   /id="PRO_0000448354"
FT   DOMAIN          90..187
FT                   /note="CRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  57003 MW;  39C405151A36DA40 CRC64;
     MNQVFKGWSR GMSTSRGRSM RSKVESRMRK ESGKTLREIR RAKKLKKKLM TDEERLIYNL
     KRAKKKVALL LQKLKKYDLP ELPSPVHDPE LFTSEQVQAF KKIGFKNKNY VPVGVRGVFG
     GVVQNMHMHW KFHETVQVCC DNFPKEKIKE MASMIARLSG GVVINIHNVK TIIMFRGRNY
     RQPKNLIPVN TLTKRKALFK ARFEQALESQ KLNIKKTEQQ LRRMGVNPED PVAMASIHRV
     ASTFFNAIDK KEGTPYVFHG DKQSERGTSV DNREESEPGD EDSDQEELDR FIAEIEEAAD
     KEWEEEEAAE QEESGRIRYW NREEFAGRSR TPELRSYGDA SHGFRRNDRD THSQRRPNDS
     DDDDDDGELD SEDDEIPKRF DRARSSNTNT RRPREDFKRR SPDPRPRPRA QVRSDDDVLS
     DLDNTMWDSE DEEDAPPANY ISSSDDDEDE NRTVSASSSK QSRFRNNSSR DGINNSKSKS
     GKQRDEDWDS D
 
 
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