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Database: UniProt
Entry: R7QNV2_CHOCR
LinkDB: R7QNV2_CHOCR
Original site: R7QNV2_CHOCR 
ID   R7QNV2_CHOCR            Unreviewed;       351 AA.
AC   R7QNV2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CHC_T00000277001 {ECO:0000313|EMBL:CDF39453.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF39453.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase NEP1 family.
CC       {ECO:0000256|ARBA:ARBA00008115}.
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DR   EMBL; HG002033; CDF39453.1; -; Genomic_DNA.
DR   RefSeq; XP_005719364.1; XM_005719307.1.
DR   AlphaFoldDB; R7QNV2; -.
DR   STRING; 2769.R7QNV2; -.
DR   EnsemblPlants; CDF39453; CDF39453; CHC_T00000277001.
DR   GeneID; 17327083; -.
DR   Gramene; CDF39453; CDF39453; CHC_T00000277001.
DR   KEGG; ccp:CHC_T00000277001; -.
DR   OMA; ITHAFED; -.
DR   OrthoDB; 275493at2759; -.
DR   PhylomeDB; R7QNV2; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
DR   GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:InterPro.
DR   CDD; cd18088; Nep1-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR12636; NEP1/MRA1; 1.
DR   PANTHER; PTHR12636:SF5; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE NEP1; 1.
DR   Pfam; PF03587; EMG1; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..87
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  38817 MW;  2629239A509A95F7 CRC64;
     MVTQLDAAER RKRKSSKSRD GPKRKQKRRR PTDDEPQQVD QRLLELLTGK NEEEDLKKID
     SENSSESEEE ESGSSSGEDE ASDADEKPAE ENETAAGAAA ASGATNDTWP RRISDAHAKK
     VNVTVLLERA NLETVKQSGR SGGMVLLNCE DHRHVLKKSG RDANDARPDI THQCLLALMD
     SPLNKAGRLK VYIRTAKNVL IEVHPQTRVP RTIRRFSGLM AELLEKFKVR GTSGSTPLLK
     VIRNPITSHL PVGTRKVVCT YNTDNIVDMR EHAAKMAALA IPEGLNVGED EEAIEEQAEE
     VNVLYVIGAM AHGKVSEDWA DDNICVSEYP LSAATVCSRL TYTYECLFGI L
//
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