ID A0A1R3HKI1_COCAP Unreviewed; 1084 AA.
AC A0A1R3HKI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=RNA methyltransferase family protein {ECO:0000313|EMBL:OMO70899.1};
GN ORFNames=CCACVL1_18586 {ECO:0000313|EMBL:OMO70899.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO70899.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO70899.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO70899.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO70899.1}.
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DR EMBL; AWWV01011753; OMO70899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3HKI1; -.
DR STRING; 210143.A0A1R3HKI1; -.
DR EnsemblPlants; OMO70899; OMO70899; CCACVL1_18586.
DR Gramene; OMO70899; OMO70899; CCACVL1_18586.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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:0001510; P:RNA methylation; IEA:GOC.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.90.1320.10; Outer-capsid protein sigma 3, large lobe; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004314; Neprosin.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR00479; rumA; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF03080; Neprosin; 2.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000188268};
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}.
FT DOMAIN 605..784
FT /note="Neprosin"
FT /evidence="ECO:0000259|Pfam:PF03080"
FT DOMAIN 872..1077
FT /note="Neprosin"
FT /evidence="ECO:0000259|Pfam:PF03080"
FT REGION 34..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 500
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 373
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 404
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 425
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 473
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 1084 AA; 120408 MW; 12E75BE3CB0D8D91 CRC64;
MATAIPSHAL RHLTVTRPWL RRIRCNASLA LSRQDPHETL PENDSNDNVE IKKPKSSNSQ
AFFPKKNQVL ELECESLAFK GKGVCKAADS GFVLLCDRAL PGERFIGRVT RKKGSYAEVT
KLKTISPHWD FVDAPCEYAS YCGGCKTQNL SYEAQIRAKE QQVRELVINV GKFSDKNSEF
SSLMKPIVPC NVQFHYRNKM EFSFGSQKWL PKELLHEKLD GNENYALGLH APGFFDKILN
VEKCLLQSEP ANKVLETVQD HWKDPELGLS PYNVHSHAGF LKHFVLRTGR DMKTGLPELM
VNFVTSSYKP ELLKPLVEKI SAIPEVVSIM NNVNTSVGNT SVGEEEYTLY GKSTITESLR
GLTFQISANS FFQTNTGQAE VLYKLIEDCA GLRGDGSEVV LDLFCGTGTI GLTLAKMARH
VYGYEVVAQA VADAHRNAKL NGISNATFVQ GDLNKIGEDF GKNFPKPDIV ITDPNRPGMH
MKLIKFLLKL KAPKIVYVSC NPATCARDLD YLCHGVMKPS SYPKGMQVGK FDPKLLQGYI
KCPEGTVPIV RAPINNSTEA NFSHRKYQIK VMAPFHEYAL VSIKNGNYFG ASARLNVWHP
ATFNGELSVA QFWITAGQGT EVNTIEAGWI SNAGDTKTRL FIFWTTDNYR TTGCYNLMCP
GFVQTSNHRL LGTIMNPVSI YGGQQFDILL IVHKDKQSGN WWLRFQDIDL GYWPSSIFTK
LSDRAAEVLW GGEIVNTGGG GRHTTTEMGN GHFPSEGFKF SAFMKNLAYV DESGNFADAG
NIMKPSSYPK GMKVEKFDPN LLQGYIKCPQ GTVPIVRAPI NNSTKANFSH RKYQTQAISG
ALVHEYAQVS AIGNYYGASA RLNVWHPATF NGEFSLAQFW VLGGQGAELN SMEAGWIAIR
KQDFSHFGLT ITMETPVAMI LSPGFVQTSN HRLLGTVIKP ISTYGGKQFD IFLIIHKDKQ
SGNWWLRVQD IDLGYWPSSI FTKFSDSAGV ISWGGEITNS AVKGGRHTIT EMGSGHFPSE
GFKFAAYIGN LAYIDHESGD FVDAKDLVPF VTNAKCYDVK IPKKNKVWGT HIYLGGPGWN
DECP
//