ID A0A0V1LHB7_9BILA Unreviewed; 1850 AA.
AC A0A0V1LHB7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Ribosomal RNA methyltransferase NOP2 {ECO:0000313|EMBL:KRZ58893.1};
GN Name=Nop2 {ECO:0000313|EMBL:KRZ58893.1};
GN ORFNames=T02_645 {ECO:0000313|EMBL:KRZ58893.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ58893.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ58893.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ58893.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735}.
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:KRZ58893.1}.
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DR EMBL; JYDW01000050; KRZ58893.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00899; b4GalT; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
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; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19300:SF57; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE BRE-4; 1.
DR Pfam; PF02709; Glyco_transf_7C; 2.
DR Pfam; PF13733; Glyco_transf_7N; 2.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 2.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1520..1805
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1829..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1850
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1735
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1612..1618
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1636
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1663
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1678
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1850 AA; 211531 MW; BE8CE3BCA854C681 CRC64;
MLYVSEKAGD CCTLERNVAF KQTANKNKIP PNDGDSDSLE ISGAVGLGHL TNCCSKTALT
ELSIDVRFFR LRPWALIFST GFWLQTELSA SSSHFCSNGF NLHMFLKLSC KASNRHIVVW
LNTLPYSVPR ARPTSAWVKP SLIRRCLNCL ANASKLLTSI CPSSPQLISV GCTHEPNSPA
ANGRQGRRPV YVSTKPNRRV SNGTTVYCLF ILTIDDGLEP AIQIVVLYKV GFCYVAHFFT
VLTALRVKRQ TFNRGKLMNV GFLEAMRLHN WTCFVFHDVD LLPENDLNPY SCLDTPRHLS
VAVDKFNYRL PYASIFGGVT ALTAEQFRRI NGFSNEYWGW GGEDDDFYIR VNLGKYVVHR
HPEQIGRYKM IKHSSELLNE ANPCRYRLLR EASRRWRMDG LNSIRYAILN ITEHQLFTRI
LVDLRELLWP RTCGETYEIG RRQIRASCKP PPRGSKHENV KYLCTTNDPV IMPMNLCFRC
RRKRANKEIY KKVNQEARNT TTMDDSQVYS KEARCGFTSW PHCLQVTFAS LLVLCIFCIY
VLYPSNSFLN FQDDFKQITL SSSPSLSVSV IRSKEICRPT SLRYDGKLNV EFSSPEFSQL
EALYPEVNNG GSFYPQDCIP PDDVAVIIPY RDRDLHLRTF LLNIHSFLMR QKLHYQIFVV
EQVANQTFNR GKLMNVGYVE AQRLFNWSCL VFHDVDLLPE NDLNPYWCVD TPRHLSAAVD
KFQYKLPYQT IFGGVSALTA SQFEVINGFS NNFWGWGGED DDMYSRVLLG RFSVHRHPGK
YARYKMIKHQ QESMNNANAC RFNLLKFTNM LWRRSGLSNL NYRLLNISVN RLYTKMTVDL
YEEQSRREIR RFLVGGKGSS DVLPPSVPAS REISIHELKM PNEQSKMNEE STYIDEVDAF
LAAEHGYIIM LRRLPIRCIP NRIVIMFQQL FAGFGISPND FFFQRRFDER YTGNAFVRIS
DSRIVDELRE RDKIIVEGRE VTIMMISDVG MRRFMECGYE MGTNSTTTFR KLFAGYFTID
AGVAWAQQLL ESENESCFIL IKALPINITP YQVFSCLGKF CLHLRLGGVL DVELFSSHIF
ILCMKSSTFA TIGAEVLRTQ IVGGTLIDAS GELIAQHCIG EILEYLKEMK MRFCGVSYSN
AIGNSGIDST SGSIVYHNLL QPPEEQNLIA YSNPRSYMPT FVEGGDTMQI ERPLPSMCSS
RYFIIGCLPH NVQNRDMELL FSILKFALVG GIRCVHDGYG VFHSEAEVYF TDEAMADWIR
QRFGQLNSFL ATLRLSSAIT NSKHRLLSQE VTHKEAAADL ATIQPWACGA TDNASVYGTE
DCRFESCHAR ESFLANCIFK TLSSLNVEDM STSVTKISDR KVIGKLKINN DDSDEYIEDD
NFLNDESDAD SEKELSFEHE PSVKFENNVH AEEMLSDDET DFNMTESDSN EEFTNSDSLY
DRIKEIVNKL NKFKDVSNTN RLISHHQPIF PSLKGRFYYV EKLKNYLCSF YGYNEFMMEK
LIHIFKINEV MFSFLPFGKF LQANESQRPL VIRCNTLKIR RKDLAQSLTS RAVNLQPLGE
WSKVGLVVYG SQVPIGATPE YMFGFYILQG ASSFMPVLAL DPQEDEIILD LCAAPGGKSS
YISALMKNTG ILMANDISRD RCKAITSNFH RLGVRNAMVT CLDGRRFKRI FFDRVLLDAP
CSGSGVISKD ASVKVSKDLL DIKRCVTLQK QLILAAIDRL DARSRTGSIL VYSTCSIFVE
ENEAVIDYAL RNRNVKLVDT GLPFGIEGFV RFREYRFHPN MKYCRRFYPH KHNMDGFFVA
KLKKFSNELP GEKKGEWKMA HSNVGKVAQS ARKKNGMQLH KTRLPKRRKF
//
