UniProt functional annotation for M4STU1



	UniProt functional annotation for M4STU1

UniProt code: M4STU1.

Organism: Human betacoronavirus 2c Jordan-N3/2012.

Taxonomy: Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; Betacoronavirus; Merbecovirus.

Function: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). {ECO:0000256|ARBA:ARBA00002223}.

Function: 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. {ECO:0000256|ARBA:ARBA00003995}.

Function: 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. {ECO:0000256|ARBA:ARBA00002182}.

Function: 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. {ECO:0000256|ARBA:ARBA00003443}.

Function: May participate in viral replication by acting as a ssRNA- binding protein. {ECO:0000256|ARBA:ARBA00002012}.

Function: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000256|ARBA:ARBA00003115}.

Function: 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. {ECO:0000256|ARBA:ARBA00002840}.

Function: Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'- 3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000256|ARBA:ARBA00002798}.

Function: 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. {ECO:0000256|ARBA:ARBA00002960}.

Function: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000256|ARBA:ARBA00003070}.

Function: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000256|ARBA:ARBA00002697}.

Function: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000256|ARBA:ARBA00003748}.

Function: Responsible for replication and transcription of the viral RNA genome. {ECO:0000256|ARBA:ARBA00003927}.

Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000256|ARBA:ARBA00003368}.

Catalytic activity: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000256|ARBA:ARBA00001665};

Catalytic activity: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00001556};

Catalytic activity: Reaction=TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000256|ARBA:ARBA00001131};

Catalytic activity: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};

Subunit: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1. {ECO:0000256|ARBA:ARBA00011652}.

Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host cytoplasm, host perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum- Golgi intermediate compartment {ECO:0000256|ARBA:ARBA00004452}. Host membrane {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

Similarity: Belongs to the coronaviruses polyprotein 1ab family. {ECO:0000256|ARBA:ARBA00008087}.

Annotations taken from UniProtKB at the EBI.


Organism:		Human betacoronavirus 2c Jordan-N3/2012.
Taxonomy:		Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; Betacoronavirus; Merbecovirus.



Function:		Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). {ECO:0000256\|ARBA:ARBA00002223}.



Function:		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. {ECO:0000256\|ARBA:ARBA00003995}.



Function:		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. {ECO:0000256\|ARBA:ARBA00002182}.



Function:		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. {ECO:0000256\|ARBA:ARBA00003443}.



Function:		May participate in viral replication by acting as a ssRNA- binding protein. {ECO:0000256\|ARBA:ARBA00002012}.



Function:		May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000256\|ARBA:ARBA00003115}.



Function:		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. {ECO:0000256\|ARBA:ARBA00002840}.



Function:		Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'- 3'-cyclic phosphates 5' to the cleaved bond. {ECO:0000256\|ARBA:ARBA00002798}.



Function:		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. {ECO:0000256\|ARBA:ARBA00002960}.



Function:		Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000256\|ARBA:ARBA00003070}.



Function:		Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000256\|ARBA:ARBA00002697}.



Function:		Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000256\|ARBA:ARBA00003748}.



Function:		Responsible for replication and transcription of the viral RNA genome. {ECO:0000256\|ARBA:ARBA00003927}.



Function:		The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000256\|ARBA:ARBA00003368}.


Catalytic activity:		Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000256\|ARBA:ARBA00001665};
Catalytic activity:		Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256\|ARBA:ARBA00001556};
Catalytic activity:		Reaction=TSAVLQ-\|-SGFRK-NH(2) and SGVTFQ-\|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000256\|ARBA:ARBA00001131};
Catalytic activity:		Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000256\|ARBA:ARBA00000707};
Subunit:		Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1. {ECO:0000256\|ARBA:ARBA00011652}.
Subcellular location:		Cytoplasm {ECO:0000256\|ARBA:ARBA00004496}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000256\|ARBA:ARBA00004399}. Host cytoplasm {ECO:0000256\|ARBA:ARBA00004192}. Host cytoplasm, host perinuclear region {ECO:0000256\|ARBA:ARBA00004407}. Host endoplasmic reticulum- Golgi intermediate compartment {ECO:0000256\|ARBA:ARBA00004452}. Host membrane {ECO:0000256\|ARBA:ARBA00004301}; Multi-pass membrane protein {ECO:0000256\|ARBA:ARBA00004301}. Membrane {ECO:0000256\|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256\|ARBA:ARBA00004141}.
Similarity:		Belongs to the coronaviruses polyprotein 1ab family. {ECO:0000256\|ARBA:ARBA00008087}.