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Database: UniProt
Entry: H9GBE5_ANOCA
LinkDB: H9GBE5_ANOCA
Original site: H9GBE5_ANOCA 
ID   H9GBE5_ANOCA            Unreviewed;       701 AA.
AC   H9GBE5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=NOP2 nucleolar protein {ECO:0000313|Ensembl:ENSACAP00000006291.3};
GN   Name=NOP2 {ECO:0000313|Ensembl:ENSACAP00000006291.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000006291.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000006291.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000006291.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000006291.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   RefSeq; XP_008117491.1; XM_008119284.2.
DR   AlphaFoldDB; H9GBE5; -.
DR   SMR; H9GBE5; -.
DR   STRING; 28377.ENSACAP00000006291; -.
DR   Ensembl; ENSACAT00000006431.4; ENSACAP00000006291.3; ENSACAG00000006397.4.
DR   GeneID; 100566323; -.
DR   KEGG; acs:100566323; -.
DR   CTD; 4839; -.
DR   eggNOG; KOG1122; Eukaryota.
DR   GeneTree; ENSGT00940000161554; -.
DR   HOGENOM; CLU_005316_3_0_1; -.
DR   InParanoid; H9GBE5; -.
DR   OrthoDB; 1268at2759; -.
DR   TreeFam; TF105660; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000006397; Expressed in forelimb bud and 13 other cell types or tissues.
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:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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:UP000001646};
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          296..583
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..62
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..701
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        513
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         388..394
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         412
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         439
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         456
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   701 AA;  77449 MW;  72A3890B1914DE31 CRC64;
     MGRKLDPARK VKRGPGRKAR KQRGAEEELA GFLPPDPDDN VRKLSSHARR RAAKRRIKSV
     KLQTNKNSRV LQKVQAAKNL LSEGANKKAK LQVGHQAGFS DENASWLTPG KKRARSKEDE
     SAALSDSDGN EGPWESDGEE GSMDGMVDDY GASSSSDEEE LLPIEKASRK DKLEGEAFNE
     DDSEDEEESP PHQQEEDTDK DADLQLNVET DERFVLPSGQ EIEKEVAQAP DLQLIHQRIK
     DNIEVLQDFS TKREEGHSRQ EYLSLLRRDL AAYYSYSDFL IGKMMDLFPL SELVDFLESN
     EVPRPVTLRT NTLKTRRRDL AQALINRGVN LDPLGKWSKT GLVVYDSSVP IGATPEYLAG
     QYMLQGASSL LPVMALAPQE NERILDMCCA PGGKTSYIAQ LMKNTGVILA NDSNADRLHS
     VVGNLHRLGV TNTVVSHCDG RQFPKVLGGF DRVLLDAPCS GTGVISKDPT VKTNKDEKDI
     LRCAHLQKEL ILSAIDSVNA ASETGGYIVY CTCSVMVEEN EWVVDYALKK RNVRLVPTGL
     DFGKEGFTRF KERRFHPSLK STRRFYPHTH NMDGFFVAKL KKFSNAIPKA VKDEESNGEP
     AVQAEEASSA PAAAEPLPQG RKQVALKAAK KPTAKQGLSA ATPTKAKGSP KGDKQKKQAS
     VSRQGSFQKR TRPSKAARPS PGGLKARPTH SKKRKLHRGH Q
//
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