ID G2NHL3_STREK Unreviewed; 1046 AA.
AC G2NHL3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Type III restriction protein res subunit {ECO:0000313|EMBL:AEN10224.1};
GN ORFNames=SACTE_2333 {ECO:0000313|EMBL:AEN10224.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN10224.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN10224.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN10224.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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DR EMBL; CP002993; AEN10224.1; -; Genomic_DNA.
DR RefSeq; WP_014046209.1; NC_015953.1.
DR AlphaFoldDB; G2NHL3; -.
DR STRING; 862751.SACTE_2333; -.
DR REBASE; 40025; SspAAEORF2333P.
DR KEGG; ssx:SACTE_2333; -.
DR PATRIC; fig|862751.12.peg.2427; -.
DR eggNOG; COG1061; Bacteria.
DR eggNOG; COG3886; Bacteria.
DR HOGENOM; CLU_005588_1_1_11; -.
DR OrthoDB; 9776021at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd09203; PLDc_N_DEXD_b1; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR021835; DUF3427.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR47962; ATP-DEPENDENT HELICASE LHR-RELATED-RELATED; 1.
DR PANTHER; PTHR47962:SF7; MITOCHONDRIAL ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR Pfam; PF11907; DUF3427; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT DOMAIN 215..246
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 335..490
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 546..703
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1046 AA; 117114 MW; E7E2E87AF017C214 CRC64;
MANDFSNAAP VVGLYETLIT RRLAKRIEEL KAEGWRPRTE PVGQESTPHV LARHVGDTVR
QVLQGLSASE QVIAANHILE SLNTIEGATQ WVDLVTEGPK QLLAIPQQEA PGVYAMLRPT
TPLSDTALIT NSPGDPSLGA ELRAELATAD RVDLLCAFVK WHGLRVLEES LASAHARGVP
IRVLTTTYIG ATERRALDRL VRDFGAEVKV NYELRSTRLH AKAWLFRRES GFDTAYVGSS
NLSKAALLDG LEWNVRLSSV ATPSVLRKFE ATFDAYWSEQ AFEPYDPDID AQRLDEALAQ
AGGSAPLGRG GITLSGLEIR PHPYQRDMLE RLEVERTVHN RHHNLLVAAT GTGKTVMAAL
DYKHLRQRLG RDLRLLFVAH RKEILEQSLR VYQDVLVDAN FGELFVAGEI PDHWTHVFAS
VQSLNTRALD RLATDHFDVI VIDEFHHGTS PTYRKLLDHF APGELLGLTA TPERTDGLNI
QDEFFDGRIA AEMRLWEALE NELLSPFHYF GITDNTDMTA VAWKRGAYDS TALSNLFTGN
DARARLVVQA VKDKVSDPRI MRALGFCVSV AHAHFMADFF RRAGLNAVAL SGETPRHERK
SALDDLRAGT VQVIFSVDLF NEGLDVPDVD TLLLLRPTSS ATVFLQQLGR GLRRTQGKAV
LTVLDFIGQH RKEFRFESQF RALTNLTRNR LEKSIEDGFP QLPSGCQIIL EAKARQLILN
NIRNQINVNV TQLAREVAEY AQPRLADFLE ESGRELKELY RGNGNSWTGL LRRSKLLDAV
GPEGEAALVK RVPAFSHVDD PLRVNTYTKL LEDDAPTYDA LSEKEQAYAR MLFFSLWPLG
GGFTSYQEGF DTLHHLGALR DEIRQVLAYA LNRADHVPVP LLGTHASLPL AVHASYSREE
ILPALGQSTA NAFMPGHFRE GVKWCENIQT DALFITLEKD EKDFSPETRY KDYALNDFQF
HWETQHRTSE SSSTGIRYQT HKEMGTHVLL FVRRFKNTDI GGPQPWMLLG PGEYVKHYGS
KPMGIVWNLR HEIPADVLTY SAIAAG
//
