Q09907 (NTH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endonuclease III homolog
EC=4.2.99.18

Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase

Gene names

Name:	nth1
ORF Names:	SPAC30D11.07

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Possesses glycosylase activity on different types of DNA substrates with pyrimidines damage. It can release both urea and thymine glycol from double-stranded polymers.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Cofactor	Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand By similarity.
Sequence similarities	Belongs to the Nth/MutY family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair, AP site formation Inferred from direct assay PubMed 17641464. Source: PomBase
Cellular_component	mitochondrial matrix Inferred from sequence or structural similarity. Source: PomBase nucleus Inferred from direct assay PubMed 16076563PubMed 16823372. Source: PomBase
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 5-formyluracil DNA N-glycosylase activity Inferred from direct assay PubMed 17641464. Source: PomBase 5-hydroxymethyluracil DNA N-glycosylase activity Inferred from direct assay PubMed 17641464. Source: PomBase 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Inferred from direct assay PubMed 17641464. Source: PomBase DNA binding Inferred from sequence model. Source: PomBase endonuclease activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	Endonuclease III homolog		PRO_0000102226
Sites
	Metal binding	210	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	217	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	220	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	228	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q09907 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: D2E8C93A0DFA60EB	FASTA	355	40,227
	10 20 30 40 50 60 MSKDYGTPPE NWREVYDEIC KMKAKVVAPV DVQGCHTLGE RNDPKKFRFQ TLVALMLSSQ 70 80 90 100 110 120 TKDIVLGPTM RNLKEKLAGG LCLEDIQNID EVSLNKLIEK VGFHNRKTIY LKQMARILSE 130 140 150 160 170 180 KFQGDIPDTV EDLMTLPGVG PKMGYLCMSI AWNKTVGIGV DVHVHRICNL LHWCNTKTEE 190 200 210 220 230 240 QTRAALQSWL PKELWFELNH TLVGFGQTIC LPRGRRCDMC TLSSKGLCPS AFKEKSGITI 250 260 270 280 290 300 TKRKVKTIKR VKKRPASESP PLSPLSLPTD DLYYQSIEDK SLIKLEDLDP VDSISHMNEP 310 320 330 340 350 LKKEPAADID VDQKPPVAFH STTKETRSLR RSKRVAKKSS QYFSQQSLQD IEDLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the Schizosaccharomyces pombe cDNA encoding the endonuclease III homologue, nth1." Sugimoto T., Ikeda S. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III." Roldan-Arjona T., Anselmino C., Lindahl T. Nucleic Acids Res. 24:3307-3312(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB191154 mRNA. Translation: BAD93307.1. CU329670 Genomic DNA. Translation: CAA91893.1.
PIR	S62565. JC6066.
RefSeq	NP_593210.1. NM_001018606.2.
3D structure databases
ProteinModelPortal	Q09907.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC30D11.07-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC30D11.07.1; SPAC30D11.07.1:pep; SPAC30D11.07.
GeneID	2543510.
KEGG	spo:SPAC30D11.07.
Organism-specific databases
PomBase	SPAC30D11.07.
Phylogenomic databases
eggNOG	COG0177.
HOGENOM	HOG000252209.
KO	K10773.
OMA	CSECLNK.
OrthoDB	EOG4T1MWS.
Family and domain databases
Gene3D	1.10.1670.10. 1 hit. 1.10.340.30. 1 hit.
InterPro	IPR011257. DNA_glycosylase. IPR004036. Endonuclease-III_CS2. IPR003651. Endouclease3_FeS-loop_motif. IPR003265. HhH-GPD_domain. IPR000445. HhH_motif. IPR023170. HTH_base_excis_C. [Graphical view]
Pfam	PF00633. HHH. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
PROSITE	PS00764. ENDONUCLEASE_III_1. False negative. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804520.

Entry information

Entry name

NTH1_SCHPO

Accession

Primary (citable) accession number: Q09907
Secondary accession number(s): Q588X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program