(data stored in ACNUC7421 zone)

SWISSPROT: C8VVA0_DESAS

ID   C8VVA0_DESAS            Unreviewed;       376 AA.
AC   C8VVA0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 70.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930555};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=Dtox_0004 {ECO:0000313|EMBL:ACV60969.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV60969.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV60969.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC       required for DNA replication and normal SOS inducibility. RecF
CC       binds preferentially to single-stranded, linear DNA. It also seems
CC       to bind ATP. {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00032557}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930558}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00365, ECO:0000256|RuleBase:RU000578,
CC       ECO:0000256|SAAS:SAAS00930556}.
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DR   EMBL; CP001720; ACV60969.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0004; -.
DR   EnsemblBacteria; ACV60969; ACV60969; Dtox_0004.
DR   KEGG; dae:Dtox_0004; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269559; -.
DR   KO; K03629; -.
DR   OMA; GQQKSFL; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00365; RecF; 1.
DR   InterPro; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00611; recf; 1.
DR   PROSITE; PS00617; RECF_1; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVA0.
DR   SWISS-2DPAGE; C8VVA0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930557};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|SAAS:SAAS00930531};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354097};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354147};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930553};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930554};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354122}.
FT   DOMAIN        3    358       SMC_N. {ECO:0000259|Pfam:PF02463}.
FT   NP_BIND      30     37       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
FT   COILED      153    173       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   376 AA;  44061 MW;  E2DFD99EE70DE803 CRC64;
     MRIKELFINN FRNYKSLHIK PKENLNIFIG DNAQGKTNIL EAICFLLQGR SFRTSHEKEI
     INFDSEQSKL KTELKAYNQN YSIDISLSRT KPKIIKINNS TTSKPELATN FGTIVFTPDQ
     LSIIKGSPKE RRRFLDLELA SFYPQYKYYF VNYQKVLLQR NNLLKELKEK KQADTFDLLE
     LWDNQLISYG AKILMARMEI LKKLIPMAQQ IHNQITSDKE KLTIRYRSSL NLNSNFREEL
     IYDQFREVIL KNRQQDYLKG QTTVGPHRDD LVFLINNKNI TDFGSQGQQR TIILTLKFAI
     INLWSCELND VPVLLLDDVF FELDSKRQKY IFDLLNKDVQ VFITSTGMAN TEKNLINIKK
     NAIFNVRSGL VCEEEL
//

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