CFM2_ARATH
ID CFM2_ARATH Reviewed; 1011 AA.
AC Q8L7C2; Q9SGI0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=CRM-domain containing factor CFM2, chloroplastic {ECO:0000305};
DE AltName: Full=Protein CRM FAMILY MEMBER 2 {ECO:0000303|PubMed:18065687};
DE Short=AtCFM2 {ECO:0000303|PubMed:18065687};
DE Flags: Precursor;
GN Name=CFM2 {ECO:0000303|PubMed:18065687};
GN OrderedLocusNames=At3g01370 {ECO:0000312|Araport:AT3G01370};
GN ORFNames=T13O15.1 {ECO:0000312|EMBL:AAF24608.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18065687; DOI=10.1105/tpc.107.055160;
RA Asakura Y., Barkan A.;
RT "A CRM domain protein functions dually in group I and group II intron
RT splicing in land plant chloroplasts.";
RL Plant Cell 19:3864-3875(2007).
CC -!- FUNCTION: Binds specific group II introns in chloroplasts and
CC facilitates their splicing. Acts on both subgroup IIA and subgroup IIB
CC introns. The substrates of the subgroup IIB also require the CRM domain
CC proteins CAF1 or CAF2, with a simultaneous binding of CFM2 and CAF1 or
CC CAF2. Can bind to and promote the splicing of the single group I intron
CC in chloroplast tRNA transcript of trnL-UAA gene.
CC {ECO:0000269|PubMed:18065687}.
CC -!- SUBUNIT: Interacts with RNA. Part of large ribonucleo-protein particles
CC that contain CAF1 and/or CAF2. {ECO:0000269|PubMed:18065687}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18065687}.
CC -!- DISRUPTION PHENOTYPE: Albino seeds that germinate poorly and die soon
CC after germination. {ECO:0000269|PubMed:18065687}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010870; AAF24608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73657.1; -; Genomic_DNA.
DR EMBL; AY136347; AAM97013.1; -; mRNA.
DR EMBL; BT010594; AAQ89616.1; -; mRNA.
DR RefSeq; NP_186786.2; NM_111003.5.
DR AlphaFoldDB; Q8L7C2; -.
DR SMR; Q8L7C2; -.
DR IntAct; Q8L7C2; 5.
DR STRING; 3702.AT3G01370.1; -.
DR iPTMnet; Q8L7C2; -.
DR PaxDb; Q8L7C2; -.
DR PRIDE; Q8L7C2; -.
DR ProteomicsDB; 241228; -.
DR EnsemblPlants; AT3G01370.1; AT3G01370.1; AT3G01370.
DR GeneID; 821288; -.
DR Gramene; AT3G01370.1; AT3G01370.1; AT3G01370.
DR KEGG; ath:AT3G01370; -.
DR Araport; AT3G01370; -.
DR TAIR; locus:2096662; AT3G01370.
DR eggNOG; KOG1990; Eukaryota.
DR HOGENOM; CLU_006310_4_0_1; -.
DR InParanoid; Q8L7C2; -.
DR OMA; HRVSGSK; -.
DR OrthoDB; 505933at2759; -.
DR PhylomeDB; Q8L7C2; -.
DR PRO; PR:Q8L7C2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L7C2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009532; C:plastid stroma; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000372; P:Group I intron splicing; IMP:TAIR.
DR GO; GO:0000373; P:Group II intron splicing; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.110.60; -; 4.
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; 4.
DR SMART; SM01103; CRS1_YhbY; 4.
DR SUPFAM; SSF75471; SSF75471; 4.
DR PROSITE; PS51295; CRM; 4.
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..1011
FT /note="CRM-domain containing factor CFM2, chloroplastic"
FT /id="PRO_0000435531"
FT DOMAIN 164..260
FT /note="CRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 376..473
FT /note="CRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 577..677
FT /note="CRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 873..972
FT /note="CRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113663 MW; 11CBAEA3D46CED80 CRC64;
MLLPLFHQQP LILAKTFPDR IFPPFLVPNT LVSRRNVSRA NSGIFCSSAS GRKTLPQSAI
QRIAEKLRSL GFVEEKHDSP TRRITGEESG KNSPGEIFVP LPKQLPIHRV GHTIDTSWST
PSYPVPKPGS GTAISRYHEL KRVWKKETEM ERKKEEKVPS LAELTLPPAE LRRLRTVGIR
LTKKLKIGKA GITEGIVNGI HERWRTTEVV KIFCEDISRM NMKRTHDVLE TKTGGLVIWR
SGSKILLYRG VNYQYPYFVS DRDLAHEAAS GASSMDQGVV DSREKQSIAE SSAPSITNKM
VKPMLTQGVG SPDKVRFQLP GEVQLVEEAD RLLEGLGPRF TDWWAYDPLP VDGDLLPAVV
PDYRRPFRLL PYGVSPKLTD DEMTTIRRLG RPLPCHFALG RNRNLQGLAV AIVKLWEKCE
LAKIAVKRGV QNTNSELMAE ELKWLTGGTL ISRDKDFIVL YRGKDFLPSA VSSAIEERRR
QTMIMENSSV HGNKLTENEE EIKPRAVKED IELEAKDQKD HIQTHQMKSR QRNSPEAILE
KTSMKLSMAL EKKANAEKVL ADLENRESPQ LSDIDKEGIT NDEKYMLRKI GLKMKPFLLL
GRRGVFDGTI ENMHLHWKYR ELVKIICNEY SIEAAHKVAE ILEAESGGIL VAVEMVSKGY
AIIVYRGKNY ERPQCLRPQT LLSKREALKR SVEAQRRKSL KLHVLKLSNN IEELNRQLVE
DSATNETWSD GESSNMMVEE ETENQHTEPE KAREKIELGY SSDLSVPSSG EENWEDDSEG
EVDPLTTSSQ EYQEDESESA SSQRHEGNSL DSTANLSVFA ETGSANASSF HDRSLPHNSF
LNANRKLPGS STGSGSQISA LRERKSENDG LVTDLSNRER LILRKQALKM KKRPPFAVGR
SNVVTGLART LKMHFQKNPL AIVNVKGRAN GTSVQEVIAK LKEETGALLV SQEPSKVILY
RGWGAEEEMK SFYPNNNVKS SINLPSTRSF VDDPPHVSPA LIEAIRLECG L
