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Database: UniProt
Entry: Q5CRA7_CRYPI
LinkDB: Q5CRA7_CRYPI
Original site: Q5CRA7_CRYPI 
ID   Q5CRA7_CRYPI            Unreviewed;       745 AA.
AC   Q5CRA7;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=CNcl1p/MJ0026/YebU-like. SUN family methylase {ECO:0000313|EMBL:EAK88233.1};
DE   Flags: Fragment;
GN   ORFNames=cgd5_3560 {ECO:0000313|EMBL:EAK88233.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK88233.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK88233.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:EAK88233.1}.
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DR   EMBL; AAEE01000007; EAK88233.1; -; Genomic_DNA.
DR   RefSeq; XP_626279.1; XM_626279.1.
DR   AlphaFoldDB; Q5CRA7; -.
DR   STRING; 353152.Q5CRA7; -.
DR   EnsemblProtists; EAK88233; EAK88233; cgd5_3560.
DR   GeneID; 3373081; -.
DR   KEGG; cpv:cgd5_3560; -.
DR   InParanoid; Q5CRA7; -.
DR   OMA; DTRRAHM; -.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000006726; Chromosome 5.
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   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; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006726};
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}.
FT   DOMAIN          35..439
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          517..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        297
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         154..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAK88233.1"
SQ   SEQUENCE   745 AA;  86203 MW;  6FE604008E5691C8 CRC64;
     KMSNKGYSDL VKESKLFEKY YKEQNIVPVE EWELFMEYLK QDLPSTFRVV GVSPYSSSIK
     EFAKETESVT VYLNENSEEM DNLIKEIKWY PKGLAFQITK SRDKLRRSSG VSKEFHSKLV
     MMSDGGSIMR QEAVSMLPVL FLDVKPNHYV LDLCSAPGSK TSQIIEILQS EQAVTGEYPK
     GFVIANDLDT RRAHMLIHHT RHLNSPSLIV TTHSADHFPD IYLSNPSSES LKEKFYFDRI
     LCDVPCSSDG TLRKNPNLFA KWSISFSLGL HRLQRNILLR ALSILKPKEG LLVYSTCSFN
     PLENEAVVSS VISSLANRGI HVEIVDPLTI SEISKDVISK TKFGRGISTW RVPIPRKQLK
     KNKNKKNKCE ETNVELLSQE PKEFFDNYEE VPFQSRESIF PSMFPPEDPK IKESLSKCIR
     ISPHQENTGG FFVSVLRITS SEKEDHKVDN FQLEIQDDYL TLADNPNKKN IIKMLFNPYG
     ISNFNEEKIL NTLIYRNPKG DFNRACTNKK SLEELNKKEK ENKEGSTDKI EDDFDSINNT
     TDDLSNQELE DSKFPRKMWQ VSESVSKFLF SAKSKNPLRV IHAGFPGVEL SRYRKGPISI
     EDNQIIDVNF PPIYRFNCGF NSYLHYSHGL SLDDTPRCRE FPIKYILKLL QTIEKPTENT
     EEVKEFHPYR IPRHHLKEEE YPEFKGIFDL PGSIIIKLDM KKFGGNKPIF LPAHVGRHHI
     ELLLDKFLRF CVKFHIEWLY KHQNH
//
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