ID A0A0D2QKH4_GOSRA Unreviewed; 845 AA.
AC A0A0D2QKH4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=B456_003G141000 {ECO:0000313|EMBL:KJB20259.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB20259.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB20259.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001742; KJB20259.1; -; Genomic_DNA.
DR RefSeq; XP_012471484.1; XM_012616030.1.
DR AlphaFoldDB; A0A0D2QKH4; -.
DR STRING; 29730.A0A0D2QKH4; -.
DR EnsemblPlants; KJB20259; KJB20259; B456_003G141000.
DR GeneID; 105788934; -.
DR Gramene; KJB20259; KJB20259; B456_003G141000.
DR KEGG; gra:105788934; -.
DR eggNOG; KOG1677; Eukaryota.
DR eggNOG; KOG2187; Eukaryota.
DR OMA; RGWRTMS; -.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000032304; Chromosome 3.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:EnsemblPlants.
DR GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR000504; RRM_dom.
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; PF00076; RRM_1; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 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:UP000032304};
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 67..96
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 67..96
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 768
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 768
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 566
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 616
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 740
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 845 AA; 92660 MW; 3B418CBD62ECD4D8 CRC64;
MAASPNNQLS ETKTLDSAAQ TNGQDSPQPS CESIPPSDPQ STADTNPGEK RKRDDDDPTQ
NSSPHPLWKT TLCSYFRRQD GSCTHGSTCK YAHGEEELRP RLDNTWDPTS ERAKKAMKGE
NGEKVAAKEE EEQEVMMTEM VMDGGEDGEE CGDPQLSKCL VHLPRKWHGD NLRKFLSEQG
ITFKSAKKKK GMVVGFVSFE NAEQLKSAVE ELEGKSFGNK NLKVANVIPR PFERKVKSAM
AATLSSQQTI DDASIKENAG VSIASNEVQD GATNCDGSAL DDSTSKAKCA RDAVTPLAHM
PYGDQLEHKK NSVMQMLKKL TRNARKACPN GVSLPQWVLQ SRERGGLPCE VEGIIESPVV
NGYRNKCEFS VGYSQQGKPT VGFMLGNFRE GVTAVEEPVD CPNVSKIACR YASIFQEFLQ
HLSFPIWNRF KNTGFWRQLT VREGRSAGKV ADENFEANIS EVMLIVQVCS VGLDEAQVTN
EFERLAQAFA AGAAANSPPL PLNVFVVQDH QGISNVAPTD APLRSIPIPK TESSLQPETA
NNIIEARIHD CISNLRFSIS PTAFFQVNTL AAEKLYSLAG EWAGLGPDTL LFDICCGTGT
IGLTLAHRVG MVIGIEMNAS AVQDAYKNAE INGIKNCRFI CSKAEDVIES LLKEYLNVSE
KQGQLSSALE SSEKRILTGE EKDTFTTNAR NDGESSCQEP EKCSSENDGK EIQNQLQESS
TSKDGNSSVP QFKNVVAIVD PPRMGLHPTV IKVLRTHAPL RRLVYISCNP ESLVANAIEL
CTPSPEKVEK GKKDNRGWRN MSSAGLARHR AKSMPISEPF QPVKAMAVDL FPHTPHCEMV
MLLER
//