ID F0V8J4_NEOCL Unreviewed; 2132 AA.
AC F0V8J4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
DE EC=2.1.1.57 {ECO:0000256|RuleBase:RU368012};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
GN ORFNames=NCLIV_005110 {ECO:0000313|EMBL:CBZ50035.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ50035.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA to produce m(7)GpppNmp (cap1).
CC {ECO:0000256|RuleBase:RU368012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000256|RuleBase:RU368012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR EMBL; FR823382; CBZ50035.1; -; Genomic_DNA.
DR RefSeq; XP_003880070.1; XM_003880021.1.
DR GeneID; 13446093; -.
DR VEuPathDB; ToxoDB:NCLIV_005110; -.
DR eggNOG; KOG3673; Eukaryota.
DR InParanoid; F0V8J4; -.
DR OrthoDB; 205623at2759; -.
DR Proteomes; UP000007494; Chromosome II.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR GO; GO:0097309; P:cap1 mRNA methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.12760; -; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|RuleBase:RU368012,
KW ECO:0000313|EMBL:CBZ50035.1}; mRNA capping {ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012, ECO:0000313|EMBL:CBZ50035.1}.
FT DOMAIN 1082..1193
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2094..2132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2109..2132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2132 AA; 226073 MW; 542DC01F371B5920 CRC64;
MRASGRSHWD TDGHAGRQKG EGRVTPVRRS VDFERTGLGR VDCALLRAEA EDQARLPGTH
LEDECRGLRQ REGLAPESFS PASESNRGSD RCRTASRWHP DNPYAAGFPG PQSDVCLPFS
TPESQHEPTQ LKTEGDECNL TRLEAFYGIS SSPWRATLIS ENEGNTFTAS VPGCTQKPFC
NETSVFAGNT KPSPRDGGDG YVRSSPGLKG ASCAALSLER FATRGNRAND RARPSVISVR
PNFLASQAEH WTGSNAAEWG GDLRSKGERE EEEANAARRE MMEQMLRMEE NDPGMAVGDE
RAQLLHRLLI VPQLEFFKIR VGAAPVPRLT SEATEGSFLG RNEPTGRGVF PVSDGGRGKA
TPGSEDPPAR SNSQREGDRR TPQDDAKNNE KTDCSPAVPV TGAGRRSEKA GPNQDGQESE
AILRATHGVF SRTESSAGPA SAAVGEQEDR PKAGPAAIDG PKSCEKRAKR EGCGASFGVF
KADRNPEAGS EPNENRGVPM QVGASTDSCR FLSGTFCDAD AVRSLWTKKT RLDSIFDEEL
GDEAGKELGG RGDKAQAERD SIVAIKQETE KAKREDDSGN VVFASELMTN GVECRQPQET
CSHGSPETRG GDSTRKDKDE KDHELSASLE RGQIGAGPGE ELQALQIEKV LLSTHGDSVR
LPVGSGPFGG SSRGEKGKSS FVRQQKVSCS IEGEGETCRS PRVSSENEEN LRVFVDICGG
PGAWSLFLLK PIKGQAGPVL QGSAESILRP AMPPLLYAPA EEELEANSLE RGGKVSVDDR
VRSVGAAGAF HGDAKNGVGK TKDGTATEQR EDARASTTSE SLSDFPCAPV VCGFGMTLAT
GAADGDRRKA RTLWYPHLAG NPRWKALWGA DGTGNVYRGK NLAHGKAAVS RWVAEAAKQF
QKKGVRGDHR GSFGDSASVT ETKRSGSAAT GSMETEALLR RADARKDACS GTPVDATAHM
GGTGLADAPE TELKAATVSE RNSFVADRAG ESGKESEQPG SQLWSQESLS TSASSDTFLE
GSHVSAPKAD VPPLPRPDTA WLQAAGAQGS TEAATKETAF LGRGDKNSGE ARKGGTDTRD
TPDTQDAETY QGVPHVCLVV ADGGFHLAID EKTGRHIENY QELLCARLLL SELLFALMLL
EEGGNFVCKI FDTFTHFTAS LVYIVARLFE DCAIIKPIRS RAANSERYLV GLRLKRRSSA
EFRSLFDVVR SVHGMWERHG EVREKLAEDE SPDSLVPVDV LTSDEAFVES LGNACRFLCK
KQTLALDLIY RKYVELKASL QISAVLKPSA DGLFRLPRLV ASRRPPLPFS GGSTGSGEPA
SRNPRECPSE KSVSSAQVAV RWGSAPSQTA HSPCAGGSLV ASSEGLGGAF AWWGGQPQNS
GDSGRESGQR GVPSGVWRTQ KSRACAEAFE SWETPRDRRE GLLSRPEGWL GHESSGGSRW
RSSPVGCCSG EETDRESSSG AGEDADACAY ADVRSASRRG AHVKEEESST SGGSASAVSG
GAREAEAGKE AEEGKMKTPE ELYEERMKQL QSHHERRLRH KAGLASSGRR GGRNGPREAP
RESRDLPPFN CQGQSSCFAE FPGNSLEANL LSLPFAKGGA LHNPISAPAQ RGVRTGGEGV
EERKEAGAHF GSFQRQSGTR RSPGSPLVAM HSEELCPPVG SSEGGVSRTG GSVFVDGSPK
QETDLFSHPF QASSSLQPQF SARPLGIPQL HAHRPNPETM ASSVANLLSA YGSGSSSPLQ
GQAPVASSSE SRQSLPATLF APSASLTISS AQLPHTFPVN LAAALLTRAP VPEGKICAPS
CSPSDGQCNP AAAHGLAQGP FPDLEMDAAK DGTAVTRNHF RSPSAAANLA AQILMTPKRQ
PEAAAGRETA KANSGQMHAC APCQGNVLAE NTVVQGLAGI TGQRGLCGGI SDREASDEKE
ARGRAAQDAH GMQQSPEPVK VSPGGVDYRT QVQLLLEHSR LLLGDGGGFK PSAAAAFKSN
NRFNSLTGIE TPGPLLAFHD PPSEALSPFI QSTSGEREGG KAGAAQQDRA IPSKIAETIA
QKAPVRPEEA SAGGPAPSEA ASGEVARKAE FSGEKNSANS LVMKIFRVET RRAEQTGRMV
TQQREGEGGK EGGIVKAVEE RGEGVDEAVF GK
//
