ID A0A0Q9TWW3_9BACL Unreviewed; 1190 AA.
AC A0A0Q9TWW3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Endonuclease {ECO:0000313|EMBL:KRF44011.1};
GN ORFNames=ASG93_03635 {ECO:0000313|EMBL:KRF44011.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF44011.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF44011.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF44011.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF44011.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF44011.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRF44011.1}.
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DR EMBL; LMSP01000001; KRF44011.1; -; Genomic_DNA.
DR RefSeq; WP_056828896.1; NZ_LMSP01000001.1.
DR AlphaFoldDB; A0A0Q9TWW3; -.
DR STRING; 1736411.ASG93_03635; -.
DR OrthoDB; 9801679at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 3.30.1920.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR039975; IFT52.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR12969:SF7; INTRAFLAGELLAR TRANSPORT PROTEIN 52 HOMOLOG; 1.
DR PANTHER; PTHR12969; NGD5/OSM-6/IFT52; 1.
DR Pfam; PF02368; Big_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:KRF44011.1};
KW Hydrolase {ECO:0000313|EMBL:KRF44011.1};
KW Nuclease {ECO:0000313|EMBL:KRF44011.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1190
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038368807"
FT DOMAIN 904..986
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 1190 AA; 124263 MW; 5707AFEA9B61D793 CRC64;
MSRLAGWKTK LFKTTLALTI ALPFQVLATS SWQAVMAEGP TDPAPFIEAK VVNENAGKKV
LFDNTHEQTA GAADWVIDGA FSDFANALAN NGYYVKELRK TTPITLSDLS GYDVFVVAES
NVPYKTSEQA ALEQYVQGGG SIFFIGDHYN ADRNKNRWDG SEVFNGYRRG AWTNPASGMN
AEETASSAMQ DVASSDWLAT QFGLRFRYNA LGDITANQIV APEQAFGITS GVSTVAMHAG
STLAILDPTK AKGIVYLPQT SDAWANAVDQ GVYNGGGIAE GPYVAVAKSG AGKAGFIGDS
SPVEDATPKY VREDTGAKKT TYDGFKEQND GVLLVNMVNW LSKKESYTSL SQVSGLQLDQ
PTALLPFEDP AASTEPQPEP WAAPDAGYKW YDRSTFKAGS YGGPAATASA AYSFVHQATL
PNAVDFPVRV VVDNLPASTT VAGFSMGIYL VSGGTQIAMI QNADGTWPAV YGYSSTFSVT
SDINGHASKD LQVRIKPGTT AAANLRLRQN GTNLKTEAVT LGNVPAEPLP EEQDPIPAKI
TVAEARGKAS GTLVTVEGVV TTEPGSFGGQ SFYLQDASGG LYVFQSLSGF HLGDTMKVTA
STALFNTEFE LTNPVEIAKT GVAAVPIPVA VTAVTYENQG QLVELSNVTI SNIISASPTG
SFEFDAVSGA VSNHVRVDAR TGLTQSAFPY QAGQTVNIQG VAAIFKGVFQ LKPRGLSDFT
KVADTVAPVT TAALSATPNS EGWYKEDVTV TLTAVDESAS AVGTEYSING GTSTAYVAPI
VIQNEGTSTI GYFSTDAAGN VEAAKSLQVK LDKTAPVAVL TESGHPVADV TDADTLRFDL
NSTDAHSGVA AQTLTLDGAV INSGQTIAAG SLALGAHAVQ YSVVDAAGNL VQSTQTFNVS
ASVTFSQATL TADVVSLKPY ETTATHVTGT LSNGAPADLS SAVVAYNTSN GAAATVDATG
KVSALAEGTT QITATVTLNG KTVQTNAVTI TVVKPLSVGA PGKPVLSDNS GRATGLKDGN
YTVTMNMWWG NNGSVFKLYE NGVLISTQTL TDASPAAQVT KVDVKGKANG TYTYTSELIN
SFGTTASSPL VVNITDALPG KPVLSQDNWD GDGNYKVTMN MWWGTNATEY RLYENGILIE
TKSLTAASPN AQSAVSTIAG RAIGVYEYRS ELVNAGGATS SDKITVKVTK
//