ID A0A7J7Q4A0_9CHLO Unreviewed; 855 AA. AC A0A7J7Q4A0; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 03-AUG-2022, entry version 6. DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475}; DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475}; GN ORFNames=COO60DRAFT_1639382 {ECO:0000313|EMBL:KAF6258115.1}; OS Scenedesmus sp. NREL 46B-D3. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Sphaeropleales; Scenedesmaceae; Scenedesmus; OC unclassified Scenedesmus. OX NCBI_TaxID=2650976 {ECO:0000313|EMBL:KAF6258115.1, ECO:0000313|Proteomes:UP000588193}; RN [1] {ECO:0000313|EMBL:KAF6258115.1, ECO:0000313|Proteomes:UP000588193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NREL 46B-D3 {ECO:0000313|EMBL:KAF6258115.1, RC ECO:0000313|Proteomes:UP000588193}; RG DOE Joint Genome Institute; RA Calhoun S., Bell T.A., Dahlin L.R., Kunde Y., Labutti K., Louie K., RA Kuftin A., Treen D., Daum C., Bowen B., Northen T.R., Guarnieri M.T., RA Starkenburg S., Grigoriev I.V.; RT "A multi-omic characterization of temperature stress in a novel RT halotolerant Scenedesmus strain for algal biotechnology."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000588193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NREL 46B-D3 {ECO:0000313|Proteomes:UP000588193}; RX PubMed=33712730; DOI=10.1038/s42003-021-01859-y; RA Calhoun S., Bell T.A.S., Dahlin L.R., Kunde Y., LaButti K., Louie K.B., RA Kuftin A., Treen D., Dilworth D., Mihaltcheva S., Daum C., Bowen B.P., RA Northen T.R., Guarnieri M.T., Starkenburg S.R., Grigoriev I.V.; RT "A multi-omic characterization of temperature stress in a halotolerant RT Scenedesmus strain for algal biotechnology."; RL Commun. Biol. 4:333-333(2021). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate; CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; CC Evidence={ECO:0000256|ARBA:ARBA00024520}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; CC Evidence={ECO:0000256|ARBA:ARBA00024520}; 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:KAF6258115.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JACERP010000085; KAF6258115.1; -; Genomic_DNA. DR Proteomes; UP000588193; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR CDD; cd07895; Adenylation_mRNA_capping; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation. DR InterPro; IPR013846; mRNA_cap_enzyme_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; Tyr_Pase_dom. DR Pfam; PF03919; mRNA_cap_C; 1. DR Pfam; PF01331; mRNA_cap_enzyme; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. PE 4: Predicted; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}; KW Reference proteome {ECO:0000313|Proteomes:UP000588193}. FT DOMAIN 136..188 FT /note="TYR_PHOSPHATASE_2" FT /evidence="ECO:0000259|PROSITE:PS50056" FT REGION 646..778 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 796..855 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 670..686 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 698..732 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 742..758 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 855 AA; 96417 MW; 48D21E8D66F2D212 CRC64; MARAPPYNPI PPGWFDCPDI GEVSTLHHMI PMKVPLGNSH RNPHMESITS GQWTPLEALT AAHHKIVDVD KEGQVGMVLD LSNSDRYYDP GVITANCVRY VKVPCRGRGV SPDPLAVNMA VWEIRKALAV NKNFYILVHC THGFNRSGFI IVCAAMRLLA DKGYCVERGI RYFREQRTPG IYKHEYINDL FNLEACDDED EDERLGYNMN PAQLQAAAAH GRMTHSDKVG EPVCLEEARY YINTAYDILA GQDNMLRGLP FTGGYPHESM AGRGPGDLFM GSQPVSLDLD NLDLVRSKRY FVTWKADGTR YLMLLTREGV YLIDRAGEVR RMHMRFPTLL QQQQPKGAHP VGPPHHWTLL DGEMVVDDIE MAGDKQRRRF LVYDCMMLAG EGISDLRFEL TCILSATAVL GRQDRYQIVD KQVMRPVALE KDHYMRHPNP KFLYDWSLEV CSVRRKEFWP LFKARKLLEQ FIPTLCHESD GLILQVGSGR ADDALGRPYI QRTYPHLLKW KFRHMNSVDF KLAALPGQPP KLLLNCATRR KHGNADINHL SLQDIGLGEQ RLEFPADVDP TSLHGKVIEC SFDVERRTWL YMRDRPDKLT ANHRSVFDKV MTSISDNITE EVLLNVFDEA LQSDIYTQEQ DWIKNPQPAK QQQQAAPEGA DAEAEQQAKP PVLHQQQQQQ QQTNELLHQE QHHHKQGQLQ QQHSQQQQQQ QQRQQMPEVQ QQQFSGQGMQ GPSPILTPPP GLTAQELQQQ QQQNGHHTAA AGDGFADDDM PGTGEGHVAV DHSAYGLMGG VGNVGDLGAL GDHDNMEQQD DDDDGGDGGG SDYRVTEAGD GEGSDGNYND MELEDQGAAM EEEQF //