Q4WHD6 (Q4WHD6_ASPFU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
mRNA-capping enzyme subunit alpha PIRNR PIRNR036959
EC=2.7.7.50 PIRNR PIRNR036959

Alternative name(s):
GTP--RNA guanylyltransferase PIRNR PIRNR036959
mRNA guanylyltransferase PIRNR PIRNR036959

Gene names

ORF Names:

AFUA_2G05780 EMBL EAL87669.1

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) EMBL EAL87669.1

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate By similarity. PIRNR PIRNR036959
Catalytic activity	GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. PIRNR PIRNR036959
Subunit structure	The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase By similarity. PIRNR PIRNR036959
Subcellular location	Nucleus By similarity PIRNR PIRNR036959.
Sequence similarities	Belongs to the eukaryotic GTase family. PIRNR PIRNR036959
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Ontologies

Keywords
Biological process	mRNA capping PIRNR PIRNR036959 mRNA processing
Cellular component	Nucleus PIRNR PIRNR036959
Ligand	GTP-binding PIRNR PIRNR036959 Nucleotide-binding
Molecular function	Nucleotidyltransferase PIRNR PIRNR036959 Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mRNA cap methyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q4WHD6 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: CCB9F4A5A2CAF708	FASTA	415	48,321
	10 20 30 40 50 60 MGNPSVPDLD AVGIKAEPEL ADQFRREVAA LLGRNNLNFP GAQPVSFAKR HLLELQREDY 70 80 90 100 110 120 YVCEKTDGIR CLMYFARGEE DSPVPEIHYL IDRKNDYRYV PGLHFPQPDD ETFQSFHVDT 130 140 150 160 170 180 LIDGELVNDT YEDGTQQLKF LVFDCLVLDG QKLMHRTLDK RLAYFKEKVL KPYNALYKKF 190 200 210 220 230 240 PEEKKHRAFA VEDKSTQFSY GIEMMFREII PKVKKIHGND GLIFTCRSTP YRIGTDEHIL 250 260 270 280 290 300 KWKPPSENTI DFRLRLEFPV LEPDTDDEAD GITEPYPDYD AIPICHLFVM LNANEYQHWG 310 320 330 340 350 360 EMYVTESDWE ALKALQVPLD DSIVECFKDE QGRWRFHRLR DDKADANHIS TVEKVLESIE 370 380 390 400 410 DRVTEEDLIR AAPAIKAAWK KRQAQAAAEE EDRRRRARQM PPSANGNGVK RKFEE

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100 and ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000008 Genomic DNA. Translation: EAL87669.1.
RefSeq	XP_749707.1. XM_744614.1.
3D structure databases
ProteinModelPortal	Q4WHD6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WHD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00003652; CADAFUAP00003652; CADAFUAG00003652.
GeneID	3507068.
KEGG	afm:AFUA_2G05780.
Phylogenomic databases
eggNOG	fuNOG04646.
GeneTree	EFGT00050000001354.
HOGENOM	HBG330574.
OMA	GSQPVSF.
OrthoDB	EOG4RV611.
Family and domain databases
InterPro	IPR001339. mRNA_cap_enzyme. IPR013846. mRNA_cap_enzyme_C. IPR017075. mRNA_capping_enz_asu. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K00987.
Pfam	PF03919. mRNA_cap_C. 1 hit. PF01331. mRNA_cap_enzyme. 1 hit. [Graphical view]
PIRSF	PIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q4WHD6_ASPFU

Accession

Primary (citable) accession number: Q4WHD6

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)