ID Q4FS67_PSYA2 Unreviewed; 516 AA.
AC Q4FS67;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN OrderedLocusNames=Psyc_1291 {ECO:0000313|EMBL:AAZ19141.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ19141.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ19141.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC Evidence={ECO:0000256|RuleBase:RU004355};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family.
CC {ECO:0000256|RuleBase:RU004355}.
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DR EMBL; CP000082; AAZ19141.1; -; Genomic_DNA.
DR RefSeq; WP_011280563.1; NC_007204.1.
DR AlphaFoldDB; Q4FS67; -.
DR STRING; 259536.Psyc_1291; -.
DR KEGG; par:Psyc_1291; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_4_0_6; -.
DR OrthoDB; 7235451at2; -.
DR Proteomes; UP000000546; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR CDD; cd04489; ExoVII_LU_OBF; 1.
DR InterPro; IPR003753; Exonuc_VII_L.
DR InterPro; IPR020579; Exonuc_VII_lsu_C.
DR InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR NCBIfam; TIGR00237; xseA; 1.
DR PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU004355};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004355};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU004355};
KW Reference proteome {ECO:0000313|Proteomes:UP000000546}.
FT DOMAIN 47..150
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 174..496
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT COILED 342..402
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 516 AA; 57606 MW; 361E9CB5DA8B0D21 CRC64;
MRKPNLSSTK HTKVLAPAKD LATLEAELAE KENSLEGNLE DTVLCLSDYL SAVDMVIKQT
FNHRVWVKAE IRNLSSKGGH YYFELAEKDD DGKVIASCRG NLWRFKAVRV LAKFERATGM
PLDRDLTVLL KVSAGFHAQY GFSLTIEDID PSYTLGDLAR QYAEMVDRLA GEGLLHLNQQ
LPTPFDIEHV LVIAPEKAAG LGDFQADANR LASTGACHFH YHNATFQGNH APAEIRQAII
SAQQQFQDIY QRLPDLLVII RGGGAVGDLA YLNDYELAAL VAEQPIPVWV GIGHERDKVI
LDEVAHTSFD TPSKVIAAIS AHLAQLVAQT LQYQMQIKQA AQRQLNTAMQ QTSRQLSQIQ
SQTIGQLTAL QKDSAYAWRS IQQSANRQVK QAARQASELH TQTQSSVYQQ LSLASTYSKS
HQKTMMQSAQ QQLIQAQRNS EHLRDIVLLH RPSRVLKQGY SILTDEKDKR ILTSSNQLYP
EQTIHIALKD GKAKAQIIDI KMNKKPTEST EVSTYS
//
