ID F4WLL9_ACREC Unreviewed; 926 AA.
AC F4WLL9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN ORFNames=G5I_06647 {ECO:0000313|EMBL:EGI64955.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI64955.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; GL888208; EGI64955.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WLL9; -.
DR STRING; 103372.F4WLL9; -.
DR EnsemblMetazoa; XM_011057006.1; XP_011055308.1; LOC105146621.
DR EnsemblMetazoa; XM_011057008.1; XP_011055310.1; LOC105146622.
DR eggNOG; KOG2096; Eukaryota.
DR eggNOG; KOG2386; Eukaryota.
DR InParanoid; F4WLL9; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine 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 CDD; cd17664; Mce1_N; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 110..177
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REPEAT 756..788
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 887..923
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 209..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 105277 MW; 028783D717D56C59 CRC64;
MSSENRIGRG VPPRWLDCPR KAMRLIQGKF LAFKTPLSSA YDSQVPEGCR FTVDMFFENL
KSQKLKMGLW IDLTNTSRFY DKDTIEDYNC SYVKLQCRGH GETPSEEQTR AFVQLCSSFI
AHNPLEIIGV HCTHGFNRTG FLIISYLVEI DNTSVDAGLA EFATARPPGI YKADYIKELY
KRYDDEADAP PPPARPAWCL EYDDSNIPDT DEGPSRENED CQDEKGKRKR REIFNKNPIF
MAGVPGVTPI LEKKKLFGIQ RRVQDICGWK DSGFPGSQPV SMDCDNIMLL HTKPYRVSWK
ADGTRYMMLV QGDGEIFFID RENSVFEVTG LTFPHVRENR NLRDTLMDGE MVIDKDRGKN
IPRYLVYDVI MYDGQDVSKL PFHPDRYSII ENKIIAGRLR AMKEGRLIKE REPFSVRLKY
FWDVTQSKNL LGEKFAKQLS HEPDGLIFQP AKEKYCSGVC IEVLKWKPLS LNSVDFKLKI
VTESGMGILP RKIGHLFVGG LNTPYGTIKI TKHMRDLDNA IVECKFENGQ WVFMRQRIDK
SFPNSIKTAE SVCKSINKPV TKERLLDYIE KYRFARDDSE LMPPPNKKPN LHRTVLLWYT
KDFTSKDRKS LRINIEFDHA TLIRWSPDGK AFIIHKAVAN AIEVYKIAKK SDGHLASATK
ALEFPQHHTE DVVGMDIACT GKYIITCSKM NDLIIWDLKG QTLATVEMHL GSTYRARISP
CGRFVAASGF TPDVNVWEVV FSKSGEFKTV AKAFDLAGHS SGVHDFGFSA DTSHMATVSK
DGTYRFYNTK IEFEKGEDPH VLMTGTWNTT APASLALSPN AEVLVIAHGS SISFYSTITG
VLDTTIEDIF LGSITCLVFD AMGEYLLAAG DKHIKIFRNV TGYRTTIESA KRKLEQRQTQ
ATKERLEKMI RDNKELLEKI GEKCSE
//
