A2QQQ8 (A2QQQ8_ASPNC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Putative uncharacterized protein An08g03380 EMBL CAK45374.1
EC=2.1.1.43 EMBL CAK45374.1

Gene names

ORF Names:

An08g03380 EMBL CAK45374.1

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. SAAS SAAS007728 S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. RuleBase RU004542
Subcellular location	Nucleus By similarity RuleBase RU004542.
Sequence similarities	Contains 1 SET domain. RuleBase RU004538 Contains 1 post-SET domain. SAAS SAAS001214 Contains 1 pre-SET domain. SAAS SAAS007728 RuleBase RU004542

Ontologies

Keywords
Cellular component	Chromosome SAAS SAAS007728 Nucleus SAAS SAAS007728 RuleBase RU004542
Molecular function	Methyltransferase SAAS SAAS007728 RuleBase RU004541 EMBL CAK45374.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A2QQQ8 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: E4260D4865A78F04	FASTA	564	63,204
	10 20 30 40 50 60 MVIDLTVDSD SEERNENHVP SSAPPLQNNT PKSPSTLTHR PASSVPLKRK SEDAEELLAS 70 80 90 100 110 120 FLPRRPQSQP RSFSQPQSAN RANQHAISIE IEDDDDDDED VKPVQIRRRV TAARTSSFNP 130 140 150 160 170 180 NAISASKENR PLQIKSNATS TRSSSPFNLT TTNHDHRRSQ DRDEDRKQRS LLSTRRSISF 190 200 210 220 230 240 QTPSPGPISL SVVIPSPSRR QQQELDSAEV ISVPSPIGLS ENFYPTDAYE KRALKGAYPV 250 260 270 280 290 300 ARKVNRAAIP FTIGAPGPLL TSKPDISAQL HQTLQQKLAK IRGPKVTFAS GDQHQLAQFA 310 320 330 340 350 360 ANFEFVNAYK LRQGVTPVPE EFLAGCSCDG FCDPARCLCL SKEEETNDPM VPYKRADDDG 370 380 390 400 410 420 RLLVLTPEFL KRKAMIYECS SRCGCDERCW NRVVQNGRTV RLEIFQTGNR GFGLRSPDHI 430 440 450 460 470 480 RAGQFIDCYL GEVITKEVAD IREDVATSQN RHSYLFSLDF LATGEDSKYV VDGHKFGGPT 490 500 510 520 530 540 RFMNHSCNPN CRMITVTRNH ADDYLYDLAF FAFKDVPPMT ELTFDYNPGW EKVKKVDPNA 550 560 VPCLCGESNC RGQLWPNQRK AKRG

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270165 Genomic DNA. Translation: CAK45374.1.
RefSeq	XP_001392454.1. XM_001392417.1.
3D structure databases
ProteinModelPortal	A2QQQ8.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00006532.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00006657; CADANGAP00006532; CADANGAG00006657.
GeneID	4982652.
KEGG	ang:ANI_1_1828074.
Phylogenomic databases
HOGENOM	HOG000207341.
KO	K11419.
OrthoDB	EOG4H1F4F.
Family and domain databases
InterPro	IPR003616. Post-SET_dom. IPR007728. Pre-SET_dom. IPR001214. SET_dom. [Graphical view]
Pfam	PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
PROSITE	PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A2QQQ8_ASPNC

Accession

Primary (citable) accession number: A2QQQ8

Entry history

Integrated into UniProtKB/TrEMBL:	March 6, 2007
Last sequence update:	March 6, 2007
Last modified:	April 3, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)