ID A0A346NIM2_9ALTE Unreviewed; 1475 AA.
AC A0A346NIM2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Endonuclease I {ECO:0000313|EMBL:AXR05379.1};
GN ORFNames=D0Y50_02745 {ECO:0000313|EMBL:AXR05379.1};
OS Salinimonas sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR05379.1, ECO:0000313|Proteomes:UP000262073};
RN [1] {ECO:0000313|EMBL:AXR05379.1, ECO:0000313|Proteomes:UP000262073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N102 {ECO:0000313|EMBL:AXR05379.1,
RC ECO:0000313|Proteomes:UP000262073};
RA Cao J.;
RT "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT deep-sea sediment sample from the New Britain Trench.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the EndA/NucM nuclease family.
CC {ECO:0000256|ARBA:ARBA00006429}.
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DR EMBL; CP031769; AXR05379.1; -; Genomic_DNA.
DR KEGG; salm:D0Y50_02745; -.
DR OrthoDB; 9800417at2; -.
DR Proteomes; UP000262073; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd10283; MnuA_DNase1-like; 1.
DR CDD; cd04486; YhcR_OBF_like; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR007346; Endonuclease-I.
DR InterPro; IPR047971; ExeM-like.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR NCBIfam; NF033681; ExeM_NucH_DNase; 1.
DR PANTHER; PTHR42834; ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR PANTHER; PTHR42834:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF04231; Endonuclease_1; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00932; LTD; 2.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51841; LTD; 2.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:AXR05379.1};
KW Hydrolase {ECO:0000313|EMBL:AXR05379.1};
KW Nuclease {ECO:0000313|EMBL:AXR05379.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016847653"
FT DOMAIN 8..185
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 647..765
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 172..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 156089 MW; B11CF033C9546220 CRC64;
MKKIALLPFA FCLSSAASAD LLISQYIEGS SNNKAIELYN TSDSAVDLGE YTLSFYFNGS
TSAGTVIELS GSLAAGQTYI IADDSADGSI TALANLNSSH SFFNGDDAII LKAGSQIIDS
LGQLGVDPGS QWGSGLTSTQ DNTLIRLESV ASGDTDPSDS FDPATEFRGL EKDDFSGLGE
HTYTPTDGGG DGDTGGEDGD LAGVCTNCPA LDKVADASTF DPAIYYSAVQ SEIDAGSDVS
ILRQRISETL ASGHRQLTYS QVWTALTETD EDPANSDNVI LFYSNRSLAK ASNGSGSASS
NPDNWNREHS WPKSHGFSGT SNEAYTDIQH LRATDISVNG SRASLDFDYS DAPLAEAPEN
RVDGDSFEPR DAIKGDVARM MMYMDVRYEG SSADITPDLM LVNRLTSGDE AALGKLCVLL
EWHNNDPVDN AELTRQNTIY EYQGNRNPFV DHPDWAALLY PASSCEDSEP TEPPTDPDPS
EPAAAASLML TAIFDGPLSG GVPKGIELLV TQDTDDLSVC GVGSANNGGG SSGEEFVFPA
VSARAGDYIY IASEADGFTS FFGFAPDYTS NAMSINGDDA VEVFCHGELI DIYGDANTDG
TGEAWEYTDS FAYRNSGSAS VIFEVNNWQV PGTDTLDGQT SNSSATTPIP VGTYALTPAT
LFFSEYVEGS SFNKALELVN VGGTEIDLSE YAVQVFANGN TTGNSIIALS GSLAAGGVYV
LANDGADSAI TAVANALTGE VNFNGDDAVV LLQNGEIVDA IGQIGVRTEW GSGDTSTKDN
TLRRKAGITS GDSNAFDTFD PAFEWDGFAN NSFDNLGRYG DATGGGSDDS LGVCADEATY
IHTVQGAESA SALAGKTVVV EGVVTHITPA LSGYFVQEEA ADTDNDDNTS EGIFVKADGS
DLKPGDVVRV LGSVEEQYGR TQLVAQQDPL LCGSGTVVPV VINLPKTAQD SFEAVEGMLV
TNATDWIINN VYNYGSYGEV AVSSQRLYVP TQLYGSDSEE AAALSAANAL DQVLIDDNSD
GSDTTEHLLM PGEFGPYNSV RSGDTVTSVV GVMDYGFSAY RIRPVEVADV INSNARTEQP
EIEPGSLRIA SFNVLNLFNG DGEGAGFPTS RGADSFAEYQ RQLDKIVAAM SELDADVIGL
LELENDGFGQ TSTLAQLTAA MNDAAGDERY AYVDANVTTI GSDEITSGII YRQDKVTTKG
GAAILSEANS IADENGPLFA WNNRPSLAQK FSLNSTGNEF VVDVNHFKSK GSSCGTGDDD
PLGGNCNLTR TRAAIALTAW LAETYGDTPT VVVGDLNAYA QEDPIRYLTG AGFTDTLAQT
DGLKTYSYTF QGAAGTLDYQ LANAPMAQYL VDATVWHVNA DESPALDYNS EYKPDSWLNT
LVYRASDHDP VLATYQFALI GDWDGDNDVD YLDSRALLNA ILRRQPIDDS FDINGDGKIN
TRDVAALGKL CTRRACATGE TSNRGNSPFA GLFSR
//