P00652 (RNC2_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanyl-specific ribonuclease C2
Short name=RNase C-2
EC=3.1.27.3

Gene names

ORF Names:

ACLA_055300

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	132 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.
Subcellular location	Secreted.
Sequence similarities	Belongs to the ribonuclease N1/T1 family.
Sequence caution	The sequence EAW13482.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro endoribonuclease activity Inferred from electronic annotation. Source: InterPro ribonuclease T1 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Ref.2
	Chain	27 – 132	106	Guanyl-specific ribonuclease C2		PRO_0000137369
Sites
	Active site	66	1	By similarity
	Active site	84	1	Proton acceptor By similarity
	Active site	118	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	28 ↔ 36		By similarity
	Disulfide bond	32 ↔ 129		By similarity
Experimental info
	Sequence conflict	53	1	Y → E AA sequence Ref.2
	Sequence conflict	98	1	S → G AA sequence Ref.2
	Sequence conflict	124	1	N → D AA sequence Ref.2
	Sequence conflict	130 – 132	3	SGW → Y AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00652 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 3E2B1FEEFE0DBF84	FASTA	132	14,064
	10 20 30 40 50 60 MLYNKLITIA ALLVPALAAP QGLDVRDCDY TCGSHCYSAS AVSDAQSAGY QLYSAGQSVG 70 80 90 100 110 120 RSRYPHQYRN YEGFNFPVSG NYYEWPILSS GSTYNGGSPG ADRVVFNDND ELAGLITHTG 130 ASGNGFVACS GW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.
[2]	"The complete amino acid sequence of ribonuclease C-2 from Aspergillus clavatus." Bezborodova S.I., Khodova O.M., Stepanov V.M. FEBS Lett. 159:256-258(1983) Cited for: PROTEIN SEQUENCE OF 27-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027048 Genomic DNA. Translation: EAW13482.1. Sequence problems.
PIR	NRASTC. A00799.
RefSeq	XP_001274908.1. XM_001274907.1.
3D structure databases
ProteinModelPortal	P00652.
SMR	P00652. Positions 28-130.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4707141.
KEGG	act:ACLA_055300.
Phylogenomic databases
eggNOG	NOG114265.
HOGENOM	HOG000217295.
OrthoDB	EOG4GBBGV.
Family and domain databases
Gene3D	3.10.450.30. 1 hit.
InterPro	IPR000026. Gua-sp_ribonuclease_N1/T1. IPR016191. Ribonuclease/ribotoxin. [Graphical view]
Pfam	PF00545. Ribonuclease. 1 hit. [Graphical view]
SUPFAM	SSF53933. Ribonuclease/ribotoxin. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RNC2_ASPCL

Accession

Primary (citable) accession number: P00652
Secondary accession number(s): A1C9F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 3, 2007
Last modified:	March 6, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program