(data stored in SCRATCH zone)

SWISSPROT: C1E1X6_MICCC

ID   C1E1X6_MICCC            Unreviewed;       473 AA.
AC   C1E1X6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACO62243.1};
DE   Flags: Fragment;
GN   ORFNames=MICPUN_68096 {ECO:0000313|EMBL:ACO62243.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62243.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO62243.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA M5U methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01024}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001324; ACO62243.1; -; Genomic_DNA.
DR   RefSeq; XP_002500985.1; XM_002500939.1.
DR   ProteinModelPortal; C1E1X6; -.
DR   GeneID; 8241752; -.
DR   KEGG; mis:MICPUN_68096; -.
DR   HOGENOM; HOG000029870; -.
DR   InParanoid; C1E1X6; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00479; rumA; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E1X6.
DR   SWISS-2DPAGE; C1E1X6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   DOMAIN        1     58       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   ACT_SITE    424    424       {ECO:0000256|PROSITE-ProRule:PRU10015}.
FT   ACT_SITE    424    424       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01024}.
FT   BINDING     301    301       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     332    332       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01024}.
FT   BINDING     353    353       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     397    397       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ACO62243.1}.
FT   NON_TER     473    473       {ECO:0000313|EMBL:ACO62243.1}.
SQ   SEQUENCE   473 AA;  49950 MW;  FCEBF3E072330331 CRC64;
     KSGDVLTLEC TSLAFGGRGV CKLPGGFVVF CDRAVPGETL EARVTSLKGG GRFAEATKVS
     SISPCEHRTA APCPHFERCG GCTWQDIAYA HQLTMKRDQV VDVMTRVAKV DQTRVQNIVG
     DCVPSDKTER YRNKMEFAFG PGANGRGVVI GLRPSGNHSD LVEIGNPDGC LLQHPVADEV
     LRGCRAHLDS NGNSSLLDAF NRRTGEGVLR SLTVRVAVDE NGETIAAVDI AAATRGDDED
     AALRGLAEAI AKVRGVASSG GGDADGEGWS GEDVEVLSGA ATLPMKLRGV TFALSAPSFF
     QTNTDQAEKL VAAVEDACGF SGDGTEVVLD LFCGVGTLGL CVAKKAKHVF GWEVVPEAVK
     DAERNAEANG ITNATFRRGD LAKLKASLPG PDIVIADPAR AGMDESLVKV LRSIGAERIV
     YVSCNPATQA RDLLRLKGGD GGEGARYDVR YCTPVDMFPH TPHVETVVVL DRI
//

If you have problems or comments...

PBIL Back to PBIL home page