ID A0A1Y2GXA7_9FUNG Unreviewed; 1892 AA.
AC A0A1Y2GXA7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN ORFNames=BCR41DRAFT_347099 {ECO:0000313|EMBL:ORZ26938.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ26938.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ26938.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ26938.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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};
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:ORZ26938.1}.
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DR EMBL; MCFF01000005; ORZ26938.1; -; Genomic_DNA.
DR STRING; 64571.A0A1Y2GXA7; -.
DR InParanoid; A0A1Y2GXA7; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000193648; 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:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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; IPR001339; mRNA_cap_enzyme_adenylation.
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 SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..223
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 239..340
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 385..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1892 AA; 208337 MW; 33AA829576CACC85 CRC64;
MPFEFGVPID PTFRKTLQAK IRSLLQGKSE GFPGSYPVNF ESSHLQLLAK EEYFVTEKVP
GVRYMLLSTH TPKGPACFLI DRHYEISFVP HLLLPLRDNP SKYQNETLLD GEMIVEGDGS
KKTLRFLVFD LMALNGIVVT QRSYSTRLGM MDQDVLAVQA SKSSEIRSKE PFTIERKTMQ
RSYGLNIILS GSKRHKHGGE GLIFMPVRQP YVPGTSPKLL KWKSHTTAQF LIKVAMSKER
KPMYSIHVKH GGGTKFYDYV TPEPQLASEW HNSSPDGKVA EFWWDAQWPT QMFEKGYGLE
TRTGGWRFYR TREDKKDVDD EATVQALVKG IETAVTKEQL ESQIEHIRTQ WKAREAGLPT
NGNNQSPHST SQRPAIRQLS IVSTHSENHP PPMTPSHTSS QYLQSPSVAN HPGSHGYFSK
KGERKSSVDE HGSSSHHPIT APGTFSHPLP PKPQSFQARH SSVEQSQSQS AKNADQEQTS
SSSSSTPSTS VIQTPDRKST PPPTSTPTSS VASPSSTSGV KNPLKLSQVP AHLQPIKSWM
TASPVPRAPP LDKGVKGVKN ERRDSRDSIV SSGSNSPKSA PSRKSSMSIA DVPKETVVGS
ISKANEAGDA NGNQSTTTSS SISISQEAPS QTPTPAHTPI PSGISRPTTV PALPPTTSSA
STDIALSGVA LETNDNKDSD EKRHEDSSAS ADHVRMPSVI PVTTTTPSGS AAVKTSVDED
ITLKAPTPVL GKRMADLSES EGERSEDSIV QRRKISDGVG PSFKTEAVMT GIGTLKLIAS
QSPKPSFSSP LAVQDSTTMS PLSPLSSPDR AAVVTSDDNK QASPRSQHPI GSRTTISSKL
LHEVTAQLGQ ETNEHDALET HENVEKVDQV EPTAAILKED VVMKEDNMGS AVTTGPLPTP
ALTVMEQTAY DLPSEGEKAQ ALARAREEAI SRMAVQREHQ EAIQMKLKED VEVFKEKSLI
RKDKAQKRKM QEVNETPVQD RRAQPVRQIN QQQGRQVNND APVLRGQSQA AQRQLASPQD
QQQRLGYTTR LSKAASRTEA QQNAQNNVKG QSHVEPSTGN SKEQIGCIVE PVAPITTQRE
ERSSINRPMS LHHGQLNDQI VSVPNPALLH PEGPSRNHRR INSTEDHHHS LDSVRADAST
PDQQELPKQY DQTHSIRQDI DEHFEPNHRR LHSDVGALYK PIMNTTAQPQ MITPGQLPHK
GALEVRDQPG SPYSPQPPGM LTAVYHPEAD SPRVSKNSSF STTVKEDVPM KRESKTRLQF
ILNDDDAGPE SGNEDDSQER RLSPERAQWN DQRPPIQETP QRTNVSQEEY GLRPPIPEEY
NAYEYQGFRS PPNTSASAME INSAQRQQAK KQKLPQEGTG SEHYGNRVDE YEYHVRQSQI
QPMLSRAAAQ PSQRSVSQVD RWPQQQHQQQ HHPLPPSPSQ QTMSGPTQVA GRRLPGDSQA
LSPHLQITHS PARPVYQSSE QQPHGNQIGK PTHHDQYGLT GPVPSPEGPR PTSDRPTHSR
HSSSSTPGPG PENPHPQGLP YQINRGKAPQ GPVQVEMYGR GYPSPSTVHA PVQARVANSV
QHMQQSSQQA SPQFHHQQVQ SQQQQQASAN AFTRKKVPVE HHAGAYGPPP PSSIHPGFES
RASHTQHSHS HQQLPHQHLN RHSEQEPVHD LDPAPGHHKQ TPPQYRVPHH EQVSGPSGPS
YYEQEAPPPA GTFGSSRSSI YGSQPLHPSP VQERQPQPYP SHPGAGQQHD PSYRSYTGSS
ARPGPGNDMG SKDEHMRGRA HITAPALGHG GRGSMGHLPS DHPSSQRQHQ QQYLPQQMPM
QHDYRHSSAS YHHHQQQQST QYASQKSMHL QDHSPYPPPP HHTASPTIPS PRHGQPHSGR
PNEHDPNYRP MPHGQQSHGH GHGHGHGHGG PW
//
