Q54B14 (QPCT_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaminyl-peptide cyclotransferase
EC=2.3.2.5

Alternative name(s):
Glutaminyl cyclase
Short name=QC
Glutaminyl-tRNA cyclotransferase

Gene names

Name:	qpct
ORF Names:	DDB_G0293986

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation By similarity.
Catalytic activity	L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3.
Cofactor	Binds 1 zinc per subunit By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glutaminyl-peptide cyclotransferase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutaminyl-peptide cyclotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 360	337	Glutaminyl-peptide cyclotransferase		PRO_0000327730
Sites
	Active site	199	1	Proton acceptor By similarity
	Active site	251	1	Proton acceptor By similarity
	Metal binding	165	1	Zinc; catalytic By similarity
	Metal binding	200	1	Zinc; catalytic By similarity
	Metal binding	330	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	135	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54B14 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: B2E05CAADF87D0A9	FASTA	360	42,046
	10 20 30 40 50 60 MKYLKILIIV TIFFFLLINV INCIDRKEIV QKEVKIKFKN LKSTLIKKYS ESNMEKIQKH 70 80 90 100 110 120 LKHILVERVA DTPNHKKVRE YIISQFDQLY WDIELDSFKD NTPFGEKTFT NIIVTSKFVN 130 140 150 160 170 180 DDDEDDIDTK ESNGNISSEP PKTLVLSAHY DSKYFKEFKF FGATDSAVPC SMLIDLAISL 190 200 210 220 230 240 QSEIKKSKKK LMIIFFDGEE AFKEWSDTDS LYGSRHLANL LLDKKVITKD NEDLPISSSF 250 260 270 280 290 300 YNTVEAFILL DLLGTPNPRF YMFNKKTESL FKKLSDIEDK LSLKRFISPK ANKYFQNHFI 310 320 330 340 350 360 GSDIQDDHIP FLNYVPTLHI IPYPFPNVWH TEKDDESCLD KNTIEDLSKI FKIFVGSYLI

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000224 Genomic DNA. Translation: EAL60492.1.
RefSeq	XP_628902.1. XM_628900.1.
3D structure databases
HSSP	HSSP built from PDB template 2AFX based on UniProtKB Q16769.
ProteinModelPortal	Q54B14.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0266352; DDB0266352; DDB_G0293986.
GeneID	8629518.
GenomeReviews	Gene locus qpct in contig CM000155_GR.
KEGG	ddi:DDB_G0293986.
Organism-specific databases
dictyBase	DDB_G0293986. qpct.
Phylogenomic databases
eggNOG	KOG3946.
HOGENOM	HBG314483.
OMA	GYRSFSN.
PhylomeDB	Q54B14.
ProtClustDB	CLSZ2429201.
Family and domain databases
InterPro	IPR007484. Peptidase_M28. [Graphical view]
KO	K00683.
Pfam	PF04389. Peptidase_M28. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

QPCT_DICDI

Accession

Primary (citable) accession number: Q54B14

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)