ID   A0A671X9B6_SPAAU        Unreviewed;       816 AA.
AC   A0A671X9B6;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=NOP2/Sun RNA methyltransferase family member 7 {ECO:0000313|Ensembl:ENSSAUP00010045500.1};
GN   Name=nsun7 {ECO:0000313|Ensembl:ENSSAUP00010045500.1};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010045500.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010045500.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A671X9B6; -.
DR   Ensembl; ENSSAUT00010047831.1; ENSSAUP00010045500.1; ENSSAUG00010018989.1.
DR   GeneTree; ENSGT00940000157352; -.
DR   InParanoid; A0A671X9B6; -.
DR   OMA; TMHSEHG; -.
DR   Proteomes; UP000472265; Unplaced.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR049561; NSUN5_7_fdxn-like.
DR   InterPro; IPR042620; NSUN7.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14663:SF2; METHYLTRANSFERASE NSUN7-RELATED; 1.
DR   PANTHER; PTHR14663; UNCHARACTERIZED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF21148; NSUN5_fdxn-like; 1.
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:UP000472265};
KW   RNA-binding {ECO:0000256|PROSITE-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          219..533
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          14..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..631
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..658
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         351
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   816 AA;  90110 MW;  14F1AA440EB5F612 CRC64;
     MSCVAPVRRI VNDKVGSSED VNTSSVTEEI FTSSHQDQRT NKEPLSFLPP LPRLHSSLPS
     PVSPPSDEVY LQAAAIFQQL RTEKTVTQQP LLYGKKTDTP QPESKDKTTQ RQAYQLAFNT
     LKYQDLLEDI IADSCFHTSQ NISRDVLPLA LVMLFDFQDR RFFVREHSLK DEEEALQEVR
     VLESSLHRCK TKLAASLARC RVKHHLHSVS CFLSDPVRAK QHRAKCLPLY GWVNTLKTSV
     EEVCEALRSA GLCEVKNIAD LRGPTFCRDP LCPDTLVFTQ QLHALLQQLL TAPPALYMQD
     RSVCVAVSVL RPLLFENGDV LVAGSFSAVT VAHVAVVAAA RSGRVLVCGA DHTPSHIEEI
     QELLTQMDLK NVRVLSEAFC GLDEWDAAVQ KLKVIIVLPQ CSSTALNDPV PTIHSEHGDW
     DLLPDLSQGP VSKSRIHTMA AKQARLLSQA LSFPKVQTVV YCTRSVYPEE NEQLVKRVLE
     KTHTHPKLLP FRVNGPIFPD DSQSGDATTD SRFFRLEQSQ FTNGCFVARL SRQADPTKVE
     TVQDVLARAA AKGLLGGVIS EQPKNVKKGK GNKNRGTSAS SRPSSPSSQE RQDPASEHEE
     KNGECDEEVK EGGKKKKVLK GSKRKVKQRP KQSNRATAVS KPHKKKPTKR RVKTKPRRIP
     RLTLTLMSSA KPSNRLSPIT ALAHKLSDNT SIKSQQTVFS TRAPASPAPP APHAASKQVK
     RQNPEPERAE KTQKDATKPE SQFKTESKTV RAKTEVVTQN RSKAADSVLP PISFPSPRSL
     SSRSGSSHSQ RLSRASSSHL TQITASCAST ISLPGL
//