(data stored in ACNUC7421 zone)

SWISSPROT: A1AZL5_PARDP

ID   A1AZL5_PARDP            Unreviewed;       356 AA.
AC   A1AZL5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Protein RecA {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526, ECO:0000256|SAAS:SAAS00013832};
DE   AltName: Full=Recombinase A {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268};
GN   OrderedLocusNames=Pden_0597 {ECO:0000313|EMBL:ABL68709.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68709.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of
CC       single-stranded DNA, the ATP-dependent uptake of single-stranded
CC       DNA by duplex DNA, and the ATP-dependent hybridization of
CC       homologous single-stranded DNAs. It interacts with LexA causing
CC       its activation and leading to its autocatalytic cleavage.
CC       {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|SAAS:SAAS00013905}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268,
CC       ECO:0000256|SAAS:SAAS00013840}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00268, ECO:0000256|RuleBase:RU004527,
CC       ECO:0000256|SAAS:SAAS00540280}.
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DR   EMBL; CP000489; ABL68709.1; -; Genomic_DNA.
DR   RefSeq; WP_011746942.1; NC_008686.1.
DR   STRING; 318586.Pden_0597; -.
DR   PRIDE; A1AZL5; -.
DR   EnsemblBacteria; ABL68709; ABL68709; Pden_0597.
DR   KEGG; pde:Pden_0597; -.
DR   eggNOG; ENOG4105C68; Bacteria.
DR   eggNOG; COG0468; LUCA.
DR   HOGENOM; HOG000264120; -.
DR   KO; K03553; -.
DR   OMA; DYGEQAL; -.
DR   BioCyc; PDEN318586:G1GW1-605-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd00983; recA; 1.
DR   Gene3D; 3.30.250.10; -; 1.
DR   HAMAP; MF_00268; RecA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013765; DNA_recomb/repair_RecA.
DR   InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45900:SF1; PTHR45900:SF1; 1.
DR   Pfam; PF00154; RecA; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54752; SSF54752; 1.
DR   TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR   PROSITE; PS00321; RECA_1; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZL5.
DR   SWISS-2DPAGE; A1AZL5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00048155};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|SAAS:SAAS00013838};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS01081725};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00289108};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526, ECO:0000256|SAAS:SAAS00013903};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00422436};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527, ECO:0000256|SAAS:SAAS00503978};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526, ECO:0000256|SAAS:SAAS00013834}.
FT   DOMAIN       48    207       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   DOMAIN      212    285       RECA_3. {ECO:0000259|PROSITE:PS50163}.
FT   NP_BIND      78     85       ATP. {ECO:0000256|HAMAP-Rule:MF_00268}.
SQ   SEQUENCE   356 AA;  38177 MW;  AC21FCBD104D646B CRC64;
     MAGATLFDMN DKRSADKQKA LDSALAQIER QFGKGSIMKL GADNPVAEIE ATSTGSLGLD
     IALGIGGLPK GRIIEIFGPE SSGKTTLTLH VVAEEQKKGG VCAFVDAEHA LDPQYAKKLG
     VNLDELLISQ PDTGEQALEI VDTLVRSGAV SLVVVDSVAA LTPKSEIEGD MGDMQMGSQA
     RLMSQAMRKL TASIGRSNCM VIFINQIRMK IGVMFGSPET TTGGNALKFY ASVRLDIRRA
     GSIKDRDEVT GNATRVKVVK NKVAPPFRQV EFDIMYGEGI SKVGELIDLG IKAGVVEKSG
     SWYSYGDERI GQGRENAKQF LRDHPDMAHA IEDKIRASHG LDFGVADDGD EVMAED
//

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