ID V7AJH6_PHAVU Unreviewed; 862 AA.
AC V7AJH6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=PHAVU_011G078600g {ECO:0000313|EMBL:ESW04241.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW04241.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
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DR EMBL; CM002298; ESW04241.1; -; Genomic_DNA.
DR RefSeq; XP_007132247.1; XM_007132185.1.
DR AlphaFoldDB; V7AJH6; -.
DR STRING; 3885.V7AJH6; -.
DR EnsemblPlants; ESW04241; ESW04241; PHAVU_011G078600g.
DR GeneID; 18615499; -.
DR Gramene; ESW04241; ESW04241; PHAVU_011G078600g.
DR KEGG; pvu:PHAVU_011G078600g; -.
DR eggNOG; KOG1677; Eukaryota.
DR eggNOG; KOG2187; Eukaryota.
DR OMA; RGWRTMS; -.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000000226; Chromosome 11.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:EnsemblPlants.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR45904:SF2; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG A; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 66..95
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 66..95
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 785
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 519
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 569
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 757
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 862 AA; 93809 MW; 6523DA27278481B9 CRC64;
MAEPVTNIQL SPSKTLGSIN GHDSIVEPNQ TLSQDAQLNQ ENDVVVPTGK RNREDNDGEE
SSLHPMWKTS LCSFYRSHNN TCNHGDTCRY AHGEEELRPR PDNTWDPTSE RAKKALKTET
GEKCAVSEDV MMTEAVVDDD DYGSNHALSK CLVHLPRKWS SENLRNFLNE QGIAFKHAKK
KKGMMIGFVT FEDEEQLKSS SKDLEGKTIG NKTVKVADVI PRSFEKKSNP SVASHQELDE
GVDVPSSGAL DAENNDKLAV DGSVSKSRSL RDTRNARKAC PNGVSLPDWI LKSREIGGLP
CKLEGIIASP IVNGYRNKCE FSVGYSLEGK VTVGFMMGNF REGVTAVGEP IECPNVSNIA
CKYATIFQEF LQDSDLPVWN RFKNTGFWRQ LTVREGRTSG NTDPAVTFGG IAEVMLIVQV
STANFDDALV AAEFKRLAQA FVAGGATSQC PTLPLTALIV QDHQGISNVA PADAPLHLLT
LPKAGGDPEI GENNNAMDVR IHDYINNLQF SISPTAFFQV NTLAAEKLYS LAGDWACLGP
DTLLFDICCG TGTIGLTLAH RVGMVIGIEM NASAVSDAHK NAEINGIKNI RFICSKAEDV
MGSLLREYLN MTKKEDDSNT PKSGNDIPED NACPEAENGE MASHCPENNN AEVGSEVQKD
STSEQVDGIS EQAENVTGSQ LRDDVNVPKE QSDDPNVCGS GNDIPGDSTC PGPETSEMTS
RSENNNAEVG SEVQKGNSSE NGNTSMQQFK NIVAIVDPPR AGLHPTVIKA LRTHPRLRRL
VYISCNPESL VANAIELCTP SPLKIEKGNK DNRGWRNMSS AGLARHRAKS MPISEAFHPV
KAMAVDLFPH TPHCELVMLL ER
//
