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Database: UniProt
Entry: A0A1Y1UNR6_9TREE
LinkDB: A0A1Y1UNR6_9TREE
Original site: A0A1Y1UNR6_9TREE 
ID   A0A1Y1UNR6_9TREE        Unreviewed;       429 AA.
AC   A0A1Y1UNR6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=mRNA-capping enzyme subunit alpha {ECO:0000256|ARBA:ARBA00019171, ECO:0000256|PIRNR:PIRNR036959};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475, ECO:0000256|PIRNR:PIRNR036959};
DE   AltName: Full=GTP--RNA guanylyltransferase {ECO:0000256|ARBA:ARBA00029909, ECO:0000256|PIRNR:PIRNR036959};
DE   AltName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00030702, ECO:0000256|PIRNR:PIRNR036959};
GN   ORFNames=BD324DRAFT_227683 {ECO:0000313|EMBL:ORX39688.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX39688.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX39688.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX39688.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Second step of mRNA capping. Transfer of the GMP moiety of
CC       GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction
CC       intermediate. {ECO:0000256|PIRNR:PIRNR036959}.
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   -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR036959}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR036959}.
CC   -!- SIMILARITY: Belongs to the eukaryotic GTase family.
CC       {ECO:0000256|ARBA:ARBA00010237, ECO:0000256|PIRNR:PIRNR036959}.
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:ORX39688.1}.
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DR   EMBL; NBSH01000002; ORX39688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1UNR6; -.
DR   STRING; 4999.A0A1Y1UNR6; -.
DR   InParanoid; A0A1Y1UNR6; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000193218; Unassembled WGS sequence.
DR   GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; 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:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07895; Adenylation_mRNA_capping; 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   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR   InterPro; IPR017075; mRNA_cap_enzyme_alpha.
DR   InterPro; IPR013846; mRNA_cap_enzyme_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR   PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR   Pfam; PF03919; mRNA_cap_C; 1.
DR   Pfam; PF01331; mRNA_cap_enzyme; 1.
DR   PIRSF; PIRSF036959; mRNA_cap_alpha; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|PIRNR:PIRNR036959};
KW   mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW   ECO:0000256|PIRNR:PIRNR036959};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR036959};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036959};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR036959};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR036959};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT   DOMAIN          134..288
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          375..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ   SEQUENCE   429 AA;  49094 MW;  35043F92B909CF26 CRC64;
     MPSQSSSEPW PVPDPPGERL TDPAIHHFLL ARVAELCGLS RAKFPGSQPV SFNVSSIEEK
     LMKYDFWTCE KSDGQRLLIV IVVNSATEEQ ETWLLDRKEQ FYKVSGLHFP YWESPDLPLR
     DTIIDGELVI DEDPKTKERT LRYYAFDCLV VNGMNVTGRP LLKRFGRLRE WVVAPFERIL
     KQIPEWRDEL PFEVIVKKQE LSYHIAQVLN VHIPSLLHGH DGIIFTNAES PYVFGTDENI
     LKWKKPSENT IDFKLNLRFP PSPADPSEPD FYAKPVFLLS VWHGGSRGQD KYQFFDELEV
     DDDEWEKFKE MGQIDDTIVE CFWDTERGAW RYFRHRNDKE NGNHASVVQK VLASIEDGVE
     IETLLSKSDA IRAAWKAREQ SRRGEQTPAP PQHRSSAPQQ GPRGSVPPIT PGPGAYPATT
     PGVMAGLRR
//
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