ID Q54TL4_DICDI Unreviewed; 647 AA.
AC Q54TL4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=NOL1/NOP2/Sun family protein {ECO:0000313|EMBL:EAL66604.1};
GN Name=nol1 {ECO:0000313|EMBL:EAL66604.1};
GN ORFNames=DDB_G0281685 {ECO:0000313|EMBL:EAL66604.1};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL66604.1, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL66604.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL66604.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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:EAL66604.1}.
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DR EMBL; AAFI02000042; EAL66604.1; -; Genomic_DNA.
DR RefSeq; XP_640577.1; XM_635485.1.
DR AlphaFoldDB; Q54TL4; -.
DR SMR; Q54TL4; -.
DR STRING; 44689.Q54TL4; -.
DR PaxDb; 44689-DDB0237575; -.
DR GeneID; 8623185; -.
DR KEGG; ddi:DDB_G0281685; -.
DR dictyBase; DDB_G0281685; nol1.
DR eggNOG; KOG1122; Eukaryota.
DR HOGENOM; CLU_005316_3_1_1; -.
DR InParanoid; Q54TL4; -.
DR OMA; PIGSWTK; -.
DR PhylomeDB; Q54TL4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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 275..561
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..647
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 390
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 417
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 434
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 647 AA; 72995 MW; EC0067B88055336D CRC64;
MNKKSVAPIK APTGKKLVGA KKTTATPAPL ATKKVTKTVI PSKKPIVQES ESEEEDSDFE
EVSSETPTKK SKLMDSDDDE EEESDDDFNK KNTKGFSDEN QKWLKMKNKG EDDEDEEEED
EEDSDDDDEK TNFDIQSKKL VQKKRKEELD NIKEIQSDFN KEIPEADKFD PTQGDQSSEP
EDTSESEDGS DGDVEEDESE EKKDNLLNVD LPMVYQRIKD VIQTLENFGQ QRKQGISRQT
YMDRLREDIC TYFGYSQWLA EVFLKIFNAS EALEFFEANE THRPLTIRAN TLKVRRKDLA
EALIARGVHL EPIKWSQVGL TIYDTQVAIG ATPEYLAGQY IQQSASSFLP VLALAPQPNE
RVLDMCASPG GKTTYIAAMM KNTGTLVAND VNKDRIKSLV ANIHRLGVKN CMVSNLDGRQ
YPSVLSGFDR VLVDAPCVGL GVISKDPQIK ISKSEQDVIT CTHTQKELLL KAIDSVDASS
PTGGIIVYST CSLTVEENEA VVDYALRNRD VIVVDTTIEF GVDGFTSFRE SRFHPSLALT
KRYYPHTHNM DGFYVAKLKK RSNIIPKDSE EQQQKSNKRK NSDTSSSDSE SKPNKKQQIN
KSNNSNNNNK SNNNNNNNNT TKLSNKKKET KKNRYVKKQQ PQQQKKK
//
