ID F6FTF2_ISOV2 Unreviewed; 906 AA.
AC F6FTF2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Endonuclease/exonuclease/phosphatase {ECO:0000313|EMBL:AEG43145.1};
GN OrderedLocusNames=Isova_0346 {ECO:0000313|EMBL:AEG43145.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG43145.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002810; AEG43145.1; -; Genomic_DNA.
DR RefSeq; WP_013837540.1; NC_015588.1.
DR AlphaFoldDB; F6FTF2; -.
DR STRING; 743718.Isova_0346; -.
DR KEGG; iva:Isova_0346; -.
DR eggNOG; COG2374; Bacteria.
DR eggNOG; COG3979; Bacteria.
DR HOGENOM; CLU_006338_2_0_11; -.
DR Proteomes; UP000009236; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd10283; MnuA_DNase1-like; 1.
DR CDD; cd04486; YhcR_OBF_like; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR047971; ExeM-like.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR006311; TAT_signal.
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; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR PROSITE; PS51841; LTD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:AEG43145.1};
KW Exonuclease {ECO:0000313|EMBL:AEG43145.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000313|EMBL:AEG43145.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..906
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003336003"
FT DOMAIN 26..171
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 201..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 93672 MW; E058A6D5A1E97329 CRC64;
MSTTHPSPRR RGSATAALLA ALALPASAAL AAPAVAVPSV DAPVVIDEVY GGGGNSGAVL
DRDYVELHNP TDAPVSLDGW SIQYGSATGT AWASQTDLTG VIPAGGSFLV GQAYGSNRDL
PDLPTPDVEG SIAMSGTGGK VALVSSTQRL TCLGAACADA TDVVDLVGWG ATTNTFLGSG
PAPGTTNATA VARVEHANTV DNAADFRAGV PDPQNSGSTG GGEDPDPEPE PGEVVPIAEI
QGTGAASPLV GQTVTTRGVV TAAYPTGGFD GVYVQTEGTG GDPADDPTPG ASDAVFVYSS
AAAQQLRIGD HVEVTGQVHE HFGLTQVSAT SWTVLDEPAQ EVKPTTTTWP ATEAEREALE
GMLLAPQGDF TVTDNYSTNY YGTIGLAAGT TPLVQPTSVG RPLSPEYHAQ VADNAARAVL
LDDGATTNYS TSANSSKPLP WLTGGDPVRV GAAVTFTTPV ILDYRYDAWA FQPLTHLTPD
VADTVQQAVF EDTREASPAD VGGNLRVGTF NVLNYFTTTG DQLSGCTYYT DRVGDPVTVR
GGCLARGAAE AEDLERQEAK IVAAISGLGA DVVALEEIEN SVHFGKPRDQ ALSDLVDALN
EHDGAGTWAY VPSPAEVPAD EDVIRNAFVY RTAAAEPVGE SRILVGSDAF VNAREPLAQV
FQPAGGVDAD TGDDVLVVTN HFKSKGSAGP WPGDADQGDG QGASNESRVR QATALLAFAD
EVAADAGTDK VLLVGDFNAY EKEDPIVVLT DAGYTDLGPA TGKYTYMFEG KVGSLDHVLA
SPAAAEVVTG ADIWNINAYE PIANEYSRHN YNVSLLYDTT PFRSSDHDPF LVGLDLAPSA
PAWDAGTVYV AGDRVVHDGA ATTWTASGLY VRGDVVVHEG HLWEAQRRSR GVEPGTSNAW
AGLGAA
//
