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Database: UniProt
Entry: A0A1S2Y9D2_CICAR
LinkDB: A0A1S2Y9D2_CICAR
Original site: A0A1S2Y9D2_CICAR 
ID   A0A1S2Y9D2_CICAR        Unreviewed;       505 AA.
AC   A0A1S2Y9D2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Probable 28S rRNA (Cytosine-C(5))-methyltransferase {ECO:0000313|RefSeq:XP_004501444.1};
GN   Name=LOC101505034 {ECO:0000313|RefSeq:XP_004501444.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004501444.1};
RN   [1] {ECO:0000313|RefSeq:XP_004501444.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004501444.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   RefSeq; XP_004501444.1; XM_004501387.3.
DR   AlphaFoldDB; A0A1S2Y9D2; -.
DR   STRING; 3827.A0A1S2Y9D2; -.
DR   PaxDb; 3827-XP_004501444-1; -.
DR   GeneID; 101505034; -.
DR   KEGG; cam:101505034; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR049561; NSUN5_7_fdxn-like.
DR   InterPro; IPR048889; NSUN5_RCM1_N.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF21148; NSUN5_fdxn-like; 1.
DR   Pfam; PF21153; NSUN5_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        109..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..447
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         251..257
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   505 AA;  56936 MW;  A31DD1C0A81A7443 CRC64;
     MRMKRERKKK KSDGGRQQNE EKKTTLKGAE RSAYFARREA AKVLKTVLVG DAKRRALASI
     KTLVYHPSVR NKKATFALIC QTLKHLPIIN DVLQAASIIN SKWKRQQELI YIIVYDILFG
     QGVPLVGDAE KYLMRHKDAL HSTLKQILSR KNVKTVKELF ALHEVPDVSV PRNVRVNTLK
     LDVDSALVEL RKKYTVQKDD LIPDLLILPP GTDLHDHPLV KNGSIFLQGK ASSMVAPALS
     PEPGWEVLDA CSAPGNKTVH LAALMKRKGR IIACELQKER IKRLNDTIKL SGASNIQVLN
     EDFLNINPKD PSYSKIKAIL LDPSCSGSGT AASRLDHLLP SKAAGQDIDM ERLNKLAAFQ
     RKALQHAFLF PAVERIVYST CSINQIENED VVKSVLPLAE SYGFQLAKPF PEWQCRGLPV
     FEGSEHLVRT DPAKHGEGFF IALFSKKDAK LSVRSNNNDN RNIHSSTRTR NLRRKKPMLI
     HTNLFRMWLY GHLNRCRIQD KSFSG
//
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