CFM3B_ARATH
ID CFM3B_ARATH Reviewed; 907 AA.
AC F4JVH1; O23307;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=CRM-domain containing factor CFM3B, chloroplastic {ECO:0000305};
DE AltName: Full=Protein CRM FAMILY MEMBER 3B {ECO:0000303|PubMed:18799595};
DE Short=AtCFM3b {ECO:0000303|PubMed:18799595};
DE AltName: Full=Protein SUPPRESSOR OF RFC THREE 2 {ECO:0000303|PubMed:32143506};
DE Flags: Precursor;
GN Name=CFM3B {ECO:0000303|PubMed:18799595};
GN Synonyms=SPRT2 {ECO:0000303|PubMed:32143506};
GN OrderedLocusNames=At4g14510 {ECO:0000312|Araport:AT4G14510};
GN ORFNames=dl3295c {ECO:0000312|EMBL:CAB10230.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RFC3, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=32143506; DOI=10.3390/plants9030328;
RA Nagashima Y., Ohshiro K., Iwase A., Nakata M.T., Maekawa S., Horiguchi G.;
RT "The bRPS6-family protein RFC3 prevents interference by the splicing factor
RT CFM3b during plastid rRNA biogenesis in Arabidopsis thaliana.";
RL Plants (Basel) 9:328-328(2020).
CC -!- FUNCTION: Binds specific group II introns in chloroplasts and
CC facilitates their splicing (PubMed:18799595, PubMed:32143506). Exhibits
CC non-specific action during plastid rRNA biogenesis; RFC3 prevents
CC unaccurate splicing to improve the accuracy of plastid rRNA processing
CC (PubMed:32143506). Acts on subgroup IIB introns (PubMed:18799595). The
CC substrates of the subgroup IIB also require the CRM domain proteins
CC CAF1 or CAF2, with a simultaneous binding of CFM3B and CAF1 or CAF2
CC (PubMed:18799595). Required for seed development (PubMed:18799595).
CC {ECO:0000269|PubMed:18799595, ECO:0000269|PubMed:32143506}.
CC -!- SUBUNIT: Interacts with RNA (By similarity). Part of large ribonucleo-
CC protein particles that contain CAF1 and/or CAF2, and RNC1 (By
CC similarity). Interacts with RFC3 in plastids (PubMed:32143506).
CC {ECO:0000250|UniProtKB:A7XN92, ECO:0000269|PubMed:32143506}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18799595}. Plastid {ECO:0000269|PubMed:32143506}.
CC Note=Localized to root plastids. {ECO:0000269|PubMed:32143506}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots and shoots.
CC {ECO:0000269|PubMed:32143506}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the seeds of the double mutant plants cfm3a-4 and
CC cfm3b-2 fail to germinate (PubMed:18799595). The double mutant rfc3-2
CC sprt2-1 is rescued for primary and lateral root development,
CC intracellular distributions of plastids in roots, as well as for
CC plastid rRNA level compared to the single mutant rfc3-2
CC (PubMed:32143506). {ECO:0000269|PubMed:18799595,
CC ECO:0000269|PubMed:32143506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10230.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78493.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97336; CAB10230.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78493.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83453.1; -; Genomic_DNA.
DR PIR; D71407; D71407.
DR RefSeq; NP_193187.3; NM_117531.4.
DR AlphaFoldDB; F4JVH1; -.
DR SMR; F4JVH1; -.
DR STRING; 3702.AT4G14510.1; -.
DR PaxDb; F4JVH1; -.
DR PRIDE; F4JVH1; -.
DR ProteomicsDB; 241230; -.
DR EnsemblPlants; AT4G14510.1; AT4G14510.1; AT4G14510.
DR GeneID; 827098; -.
DR Gramene; AT4G14510.1; AT4G14510.1; AT4G14510.
DR KEGG; ath:AT4G14510; -.
DR Araport; AT4G14510; -.
DR TAIR; locus:2129840; AT4G14510.
DR eggNOG; KOG1990; Eukaryota.
DR HOGENOM; CLU_006310_3_0_1; -.
DR InParanoid; F4JVH1; -.
DR OMA; SSRNENW; -.
DR OrthoDB; 505933at2759; -.
DR PRO; PR:F4JVH1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JVH1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0042794; P:plastid rRNA transcription; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0048316; P:seed development; IMP:UniProtKB.
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; 2.
DR PANTHER; PTHR31846:SF18; PTHR31846:SF18; 2.
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; mRNA processing; mRNA splicing; Plastid;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..907
FT /note="CRM-domain containing factor CFM3B, chloroplastic"
FT /id="PRO_0000435533"
FT DOMAIN 220..316
FT /note="CRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 421..518
FT /note="CRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT DOMAIN 663..763
FT /note="CRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00626"
FT REGION 62..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 621..654
FT /evidence="ECO:0000255"
FT COMPBIAS 62..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..857
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 102031 MW; 1EB91B66EADE32C2 CRC64;
MAINSSHHFC PMTTTTTTSA KFVDSLGSSF CKFHGTSSSI SLRSYRFGFS FMKNVKRLSC
EGSSSSSSSR NENWNRTQKQ NQFRPSKVVL NRRKDERFSD LGVISGENSS RSGDVGGGSG
SSSTMEKIVE KLKKYGFVDE DQFQDKEVEQ ERRIEKSSVE ERFYVEERRG GFSEESPFGV
YGGNDEVKFP WEKVSSMEKK ELVNGEWTAK KESRYSLAEM TLSEFELNRL RNVMFRTKSK
MRVTGAGVTQ AVVDAIQEKW KGSEIVRLKI EGSSALNMRR MHEILERKTG GLVIWRSGTS
IALYNYKGGS NRDGSGNMNK QVYRRAERLP SSLPTSTVDQ SVQLVNLPQL EKEPTVVGNK
DRTSPQEVEY EDEINELLEG LGPRYTDWQG GYPLPVDADL LPGIVPGYEP PFRALPYGVR
STLGTKEATS LRRIATVLPP HFALGRSRQL QGLATAMVKL WQKSLIAKVA LKRGVQLTTS
ERMAEDIKRL TGGMLLSRNK DFLVFYRGKS FLSLEVGEAL MEKEMLVRTL QDEEEQARLR
ASSALVVPSI KANQQLARTL QDKEEQARPS ALVLPSTKAN QNLVSAGTLG ETLDATGKWG
KNLDNDDHVE EMKQEVEKVR SAKLVRKLER KLAFAEKKLL KAERALAKVE ESLKPAEQRT
DLEGITEEER FMFQKLGLKM KAFLLLGRRG VFDGTVENMH LHWKYRELIK ILVKAKTLEG
AQKVAMALEA ESGGILVSVD KISKGYAVIV YRGKDYKRPT TLRPKNLLTK RKALARSLEL
QKREALIKHI EAIQTRSEQL RAEIEQVELV KDKGDETLYD KLDMAYSSDE ETEETDGEED
DVYLDTYEDE GEDDEEGGIQ ANGSLSETDV EFGSDESDTD FGDNSASSTT PETTFVELQN
EELDVQP
