UniProt: F0SV72

Database: UniProt
Entry: F0SV72_SYNGF

LinkDB:  F0SV72_SYNGF 
Original site:  F0SV72_SYNGF

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Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   F0SV72_SYNGF            Unreviewed;       391 AA.
AC   F0SV72;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|ARBA:ARBA00013365, ECO:0000256|RuleBase:RU363069};
GN   Name=sbcD {ECO:0000256|RuleBase:RU363069};
GN   OrderedLocusNames=Sgly_1258 {ECO:0000313|EMBL:ADY55572.1};
OS   Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Syntrophobotulus.
OX   NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY55572.1, ECO:0000313|Proteomes:UP000007488};
RN   [1] {ECO:0000313|EMBL:ADY55572.1, ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX   PubMed=21886864;
RA   Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA   Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT   (FlGlyR).";
RL   Stand. Genomic Sci. 4:371-380(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC       inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double strand
CC       exonuclease that can open hairpins. It also has a 5' single-strand
CC       endonuclease activity. {ECO:0000256|RuleBase:RU363069}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|ARBA:ARBA00011322,
CC       ECO:0000256|RuleBase:RU363069}.
CC   -!- SIMILARITY: Belongs to the SbcD family. {ECO:0000256|ARBA:ARBA00010555,
CC       ECO:0000256|RuleBase:RU363069}.
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DR   EMBL; CP002547; ADY55572.1; -; Genomic_DNA.
DR   RefSeq; WP_013624442.1; NC_015172.1.
DR   AlphaFoldDB; F0SV72; -.
DR   STRING; 645991.Sgly_1258; -.
DR   KEGG; sgy:Sgly_1258; -.
DR   eggNOG; COG0420; Bacteria.
DR   HOGENOM; CLU_038045_0_1_9; -.
DR   OrthoDB; 9773856at2; -.
DR   Proteomes; UP000007488; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041796; Mre11_N.
DR   InterPro; IPR004593; SbcD.
DR   InterPro; IPR026843; SbcD_C.
DR   NCBIfam; TIGR00619; sbcd; 1.
DR   PANTHER; PTHR30337; COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE; 1.
DR   PANTHER; PTHR30337:SF0; NUCLEASE SBCCD SUBUNIT D; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF12320; SbcD_C; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   DNA recombination {ECO:0000256|RuleBase:RU363069};
KW   DNA replication {ECO:0000256|RuleBase:RU363069};
KW   Endonuclease {ECO:0000256|RuleBase:RU363069};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU363069};
KW   Hydrolase {ECO:0000256|RuleBase:RU363069};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU363069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007488}.
FT   DOMAIN          1..217
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          266..367
FT                   /note="Nuclease SbcCD subunit D C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12320"
SQ   SEQUENCE   391 AA;  42767 MW;  540AAD3AA3BE6051 CRC64;
     MKLLHLADLH IGKRLNEFSL LEDQKHILKE ILDLTEDIRP AGILIAGDVY DKSVPAGEAV
     EILDDFLTEL VALRAPVFLV SGNHDSPERL NFGSRILAPN GVHIAGTFEG ALKQVTLRDE
     YGPAHIYLLP FIKPAMARPH FPDRNIESYE DAVRAVIEAA PIDSGERNLL VAHQFVTSGT
     TEPERSDSET IAVGGLDNID ASVFAPFDYV ALGHLHAPQS IGRETVRYAG SPLKYSFSEV
     RGQKSATLVE LAQKGTSRIE TVNLTPRRDL REIKGPLAEL LRAGAAGSPA DTLSGGLCQD
     YIRAVLTDED EVLDAIGRLR QVYPHIMRLD FENSRTKQGT EAAAAAAGDA AQKSPLDLFA
     EFYLRQNNRE MTEEQGRIMR EVLEQAGGGG Q
//

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