NucEnvDB

NucEnvDB

A database of Nuclear Envelope Proteins and their Interactions

2'-O-methyl transferase - Avian infectious bronchitis virus (strain Beaudette) - NucEnvDB

2'-O-methyl transferase (Avian infectious bronchitis virus (strain Beaudette))

FASTA TEXT XML

Subcellular Location Biology & Function Interactions Cross-References

General Information

Protein Information
Protein Name	2'-O-methyl transferase
Accession Code	P0C6Y1
Gene	rep
Organism	Avian infectious bronchitis virus (strain Beaudette) (Taxonomy: 11122)
Part of Reference Proteome?	Yes
Sequence (Length: 6629)
MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL RQPKSSVQSVAGASDFDKNYLNRVRGSSEARLIPLASGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQELRDTEDGNL EYLDSYFVVKQTTPSNYEHEKSCYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEILV TYGCIEDYHPKWFEENKDWYDPIENSKYYVMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGDFQ KTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQELFQKYFKYWDQEYHPNCRDCSD DRCLIHCANFNILFSTLIPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALLVG TSNNLVDLRTSCFSVCALTSGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRPTM FDICQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFEITKKNVLPTITQMNL KYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNASVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKCDR AMPNLLRIAASLVLARKHTNCCSWSERIYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSANV ARLLSVITRDIVYDNIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGFRE VLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPKYLPYPDPSRILGACVFVDDVDKTEPVAVMERYIALAI DAYPLVHHENEEYKKVFFVLLAYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNSQT ILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQLGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVFGI YRANCAGSENVDDFNQLATTNWSIVEPYILANRCSDSLRRFAAETVKATEELHKQQFASAEVREVFSDRELILSWEPGKT RPPLNRNYVFTGYHFTRTSKVQLGDFTFEKGEGKDVVYYKATSTAKLSVGDIFVLTSHNVVSLVAPTLCPQQTFSRFVNL RPNVMVPECFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAVYFSSARVVFTACSHAAVDALCEKAFKFLKVDDCTR IVPQRTTVDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRTLL NGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRECFKVIVNNGNSDVGHESGSAYNT TQLEFVKDFVCRNKQWREAIFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRAKR GILVVMRQRDELYSALKFTELDSETSLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITYKH LISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGNNF EPVNSKAPPGEQFNHLRVLFKSAKPWHVIRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKEQVCSCGSRA TTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASVDAIMTRCLAINNAFCQDVNWDL TYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDVNFRFYDKNPIVRNVKQFEYDYNQHKDKF ADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFYTPKFDRISFRNLKAMPFFFYDSSPCETIQV DGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYAEFVTSYNAAVTAGFTFWVTNKLNPYNLWKSFSALQSIDNIAYNMYK GGHYDAIAGEMPTVITGDKVFVIDQGVEKAVFVNQTTLPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYANQ TPLYRNTVKVCAYTDIEPNGLVVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGMPLKDGANLYVYKR VNGAFVTLPNTINTQGRSYETFEPRSDIERDFLAMSEESFVERYGKDLGLQHILYGEVDKPQLGGLHTVIGMYRLLRANK LNAKSVTNSDSDVMQNYFVLSDNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMTWFEDGSIK TCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGITLPSGILMNVAKYTQLCQYLSKTTICVPHNMRVMHFGAGSD KGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYNTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDVFI YLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLIGVNYLGASEKVKVSGKTLHANYIF WRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM

Structure Viewer (PDB: 5BZ0)

Subcellular Location

Description
[Papain-like protease]: Host endoplasmic reticulum membrane {By SimilarityUniProtKB:P0C6Y3}; Multi-pass membrane protein {Curator Inference}. Host cytoplasm {By SimilarityUniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {By SimilarityUniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {By SimilarityUniProtKB:P0C6Y3}; Multi-pass membrane protein {Curator Inference}. Host cytoplasm {By SimilarityUniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {By SimilarityUniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {By SimilarityUniProtKB:P0C6Y3}; Multi-pass membrane protein {Curator Inference}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {By SimilarityUniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {By SimilarityUniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {Curator Inference}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}.
Position in the Nuclear Envelope
Location	Location ID	Description
Host Perinuclear Region	SL-0382	The host perinuclear region is the host cytoplasmic region just around the host nucleus. Note: This location is defined for viral proteins that appear in the perinuclear region of infected host cells
Membrane Topology
Topology	Source	Annotation Type
Transmembrane	UniProt	Sequence Analysis {ECO:0000255}
Assigned Ontology terms

Cellular Component	Host Cell Endoplasmic Reticulum Membrane (GO:0044167) Host Cell Endoplasmic Reticulum-Golgi Intermediate Compartment (GO:0044172) Host Cell Perinuclear Region Of Cytoplasm (GO:0044220)

Biology & Function

Description
[Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {Curator Inference}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {By SimilarityUniProtKB:P0C6X7}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:25609249). {By SimilarityUniProtKB:P0C6X7, Experimental EvidencePubMed:25609249}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {By SimilarityUniProtKB:P0C6Y3}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255\|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {By SimilarityUniProtKB:P0C6Y3}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {By SimilarityUniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {By SimilarityUniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {By SimilarityUniProtKB:P0C6X7}. [Proofreading exoribonuclease]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity). {By SimilarityUniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {By SimilarityUniProtKB:P0C6X7}. [2'-O-methyl transferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {By SimilarityUniProtKB:P0C6X7}.
Assigned Ontology terms

Biological Process	DNA-Templated Transcription (GO:0006351) Induction By Virus Of Host Autophagy (GO:0039520) Proteolysis (GO:0006508) Viral Protein Processing (GO:0019082) Viral RNA Genome Replication (GO:0039694)
Molecular Function	3'-5'-Exoribonuclease Activity (GO:0000175) ATP Binding (GO:0005524) ATP Hydrolysis Activity (GO:0016887) Cysteine-Type Endopeptidase Activity (GO:0004197) DNA Helicase Activity (GO:0003678) Endonuclease Activity (GO:0004519) Lyase Activity (GO:0016829) MRNA (Guanine-N7-)-Methyltransferase Activity (GO:0004482) MRNA (Nucleoside-2'-O-)-Methyltransferase Activity (GO:0004483) Omega Peptidase Activity (GO:0008242) RNA Binding (GO:0003723) RNA Helicase Activity (GO:0003724) RNA-Dependent RNA Polymerase Activity (GO:0003968) Zinc Ion Binding (GO:0008270)

Protein-Protein Interactions

Interactions with Nuclear Envelope proteins (6 interactors)

Partner (NucEnvDB)		IntAct	Confidence score
K9N7C7	2'-O-methyltransferase	EBI-25758616	0.44
P0C6X7	2'-O-methyltransferase nsp16	EBI-25758560	0.44
P0C6Y1	Self	EBI-25757817	0.44
P0C6Y0	2'-O-methyl transferase	EBI-25758438	0.44
P0C6Y5	Putative 2'-O-methyl transferase	EBI-25758315	0.44
Q98VG9	Putative 2'-O-methyl transferase	EBI-25758391	0.44
Interactions with other proteins (1 interactors)

Partner (UniProt)		IntAct	Confidence score
Q92499	ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1) (DEAD box protein retinoblastoma) (DBP-RB)	EBI-25826987	0.54

Cross-References

Database	Links
UNIPROT	P0C6Y1 P26314 P27920 Q4ZJT1 Q4ZJT2
PDB	3EJF 3EKE 4X2Z 5BZ0
Pfam	PF06471 PF06460 PF09401 PF19215 PF19216 PF19219 PF19218 PF16348 PF19217 PF19213 PF08716 PF08717 PF08710 PF08715 PF06478 PF01661 PF17896 PF05409 PF00680 PF01443
PROSITE	PS51961 PS51952 PS51954 PS52000 PS51948 PS51960 PS51992 PS51943 PS51944 PS51946 PS51949 PS51950 PS51951 PS51653 PS51442 PS51154 PS51958 PS51947 PS51955 PS51953 PS51124 PS51657 PS50507

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