ID A0A0A7CLG2_9STRA Unreviewed; 706 AA.
AC A0A0A7CLG2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Secreted protein {ECO:0000313|EMBL:AIG55592.1};
GN ORFNames=THRCLA_06335 {ECO:0000313|EMBL:OQR99921.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:AIG55592.1};
RN [1] {ECO:0000313|EMBL:AIG55592.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:AIG55592.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SIMILARITY: Belongs to the nuclease type I family.
CC {ECO:0000256|ARBA:ARBA00009547}.
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DR EMBL; KM038131; AIG55592.1; -; Genomic_DNA.
DR EMBL; JNBS01001775; OQR99921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7CLG2; -.
DR STRING; 74557.A0A0A7CLG2; -.
DR OrthoDB; 90104at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR CDD; cd11010; S1-P1_nuclease; 1.
DR Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR003154; S1/P1nuclease.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR33146; ENDONUCLEASE 4; 1.
DR PANTHER; PTHR33146:SF26; ENDONUCLEASE 4; 1.
DR Pfam; PF02265; S1-P1_nuclease; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..706
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002036890"
FT REPEAT 467..500
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 640..673
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 706 AA; 77641 MW; 037BAEAAFA0995B5 CRC64;
MKTSLTALVV FATASTTQGW WDTGHMTTAE IASQLMKPDD VKTINTILSR WDGQFPNTGE
ITTAAIWPDL IKCSSKSAIC PSPAVPSLAM GDNWHFVNLP LYTNGSDWHG LTSKDGAKLI
QASFGGFGLN TLNNALSTVQ KSGSNWSVNY LVRYLLHVFG DMHQPLHAVT GISSDFPNGD
LGGNSYALRQ PCVATNLHAY WDGVGNLYPG NWSPTMSGND PARVELTKNA TALIQKFQGQ
ADPLNFQQYS SLSWKDFVSA MSKVGYLSLV LESYDLARNV VYKDIDLTVD GSKKIACPSS
DYQKKVLDTV QLRFYLGGSR LAVILTQVAA QLRQSTLVTN VHTMMIRGGK PLVPPIAIEP
PAQVEEGSQL AEATPQIDLP QRMDAPIMMN TPERVPSMTR DARVRQLIFS ARAIGQRKYK
EIHTYDVPPN KVDLDHPLET AHEAKLLKDY TMLAASSKRA GKSEAEATAY FAMGIIFDNL
DEFERAIEVY KKALVLLKDS EKVAFRGLVH SCIGVDYQLL SSGNVAYSGR FVAASSTELE
HALTYHKNHL DLNTDDAGTF VAHTNIGLTL GSLARFTEAA KHHQEALRLA IRLNSAYGQS
IAVGNLGLLA SRQGDLATAR ACMDQHLQLI QTVQDRSAEV NAWMQLGFLS MREQEYEKAS
RYFEQAYELA KELNEIGVMK QASCYLGIAR GCQRLPALFS CVNPKK
//
