ID B3S3V7_TRIAD Unreviewed; 806 AA.
AC B3S3V7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Endonuclease {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_64138 {ECO:0000313|EMBL:EDV22532.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22532.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV22532.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22532.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000256|ARBA:ARBA00010052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS985249; EDV22532.1; -; Genomic_DNA.
DR RefSeq; XP_002115076.1; XM_002115040.1.
DR AlphaFoldDB; B3S3V7; -.
DR STRING; 10228.B3S3V7; -.
DR EnsemblMetazoa; TriadT64138; TriadP64138; TriadG64138.
DR GeneID; 6756109; -.
DR KEGG; tad:TRIADDRAFT_64138; -.
DR CTD; 6756109; -.
DR eggNOG; KOG2645; Eukaryota.
DR HOGENOM; CLU_012256_0_1_1; -.
DR InParanoid; B3S3V7; -.
DR OMA; PFRNRID; -.
DR OrthoDB; 1366859at2759; -.
DR PhylomeDB; B3S3V7; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd16018; Enpp; 1.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF114; ECTONUCLEOTIDE PYROPHOSPHATASE_PHOSPHODIESTERASE C27A7.3; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 2.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..790
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 561..790
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT REGION 61..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 89538 MW; ECC4587F537A0096 CRC64;
MENRIEREKL EVEGLRGSNK ADARRKNIIY VVGGILVIGV VFGLGFMIGW FANQRGVNQG
QQGGNLCPTS SPTAQSTYST KPATTQSTNS ATPEQSTTAP PATTQPATKQ PTTPPATTLP
PITFPPCSIT PAPLLVISLN GFRWDYLNRG QTPNISAFAS KGTQADYMKP VFPTQTLPNL
YSILTGLYPV SHGIVADNFY DPNFQETFDF KGVNGTQEKW WGGEPIWVTA NKNNITTASY
FWPGDQANFQ GYHPNYRFPP NMPQLITMTF DQVQLAGARY GPTSNEVNQE IKNIDNAIGA
ITQGLKQRNA EHCVNVIITS DHGKYIDVDK NQVVNQGAFG GILVNGGNAT EVVSKIKGRS
SKFTVFKKED LPFRFHYRNN TRIPDVIVVM VDGYLVRRIY DANYTACGLA TSGWDNLEKD
MRTIFMASGP GFHSSKKIKP FLNIQLYNVM TKLLGIKPAK NNGVLGSLRA MLRNPGVATP
QAPSQPGPVC RIPADTALFE DRARCSSCVC PYCRSVVKAN LTLYNQALNM TTQEESAAQM
MNFPWGIPEY RVSLDTCILY QNHYITSYSN TYRVPWFVGY EITTKEASGF LKRNDCFRRD
LRLSIASQAS NCTSYSRSGY DRGHMAPNGD MNFDAEAQAN TYLLSNIAPQ IHNFNAGPWL
NLESLTRTWA KKYGSVYVLS GSLVLGDRNK IWSDPSYWIH GAIDTVVLPT HFYKIFVKCQ
TTKKMADSKN EKAIDPCQGK IDVISFVLPH LNSRKPQGQL TDVYLLDHTT SIRDIEALSG
INFFPNLPSQ VQDEIEVPVA SEMWAK
//
