(data stored in SCRATCH zone)

SWISSPROT: C7QFM0_CATAD

ID   C7QFM0_CATAD            Unreviewed;       381 AA.
AC   C7QFM0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00705466};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=Caci_0004 {ECO:0000313|EMBL:ACU68959.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU68959.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU68959.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(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:SAAS00705462}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00365, ECO:0000256|RuleBase:RU000578,
CC       ECO:0000256|SAAS:SAAS00705453}.
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DR   EMBL; CP001700; ACU68959.1; -; Genomic_DNA.
DR   RefSeq; WP_012784254.1; NC_013131.1.
DR   STRING; 479433.Caci_0004; -.
DR   EnsemblBacteria; ACU68959; ACU68959; Caci_0004.
DR   KEGG; cai:Caci_0004; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269561; -.
DR   KO; K03629; -.
DR   OMA; GQQKSFL; -.
DR   OrthoDB; POG091H00U7; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
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:SF15; PTHR32182:SF15; 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; C7QFM0.
DR   SWISS-2DPAGE; C7QFM0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00705458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|SAAS:SAAS00705460};
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:SAAS00705459};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00705438};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00705461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354122}.
FT   DOMAIN        3    356       SMC_N. {ECO:0000259|Pfam:PF02463}.
FT   NP_BIND      30     37       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
SQ   SEQUENCE   381 AA;  41143 MW;  06A4B871DD7CE6C8 CRC64;
     MRVTHLSLAD FRSYASLDVA LGGGVTAFVG PNGQGKTNLV EAIGYIATLD SHRVATDQPL
     VRFGAPRAIV RANVEREGRT QLVEIELNPG GANRARLNRN PVPRPREVLG VLRTVLFAPE
     DLALVKGDPG ERRRFLDELL VARWPRFAGV RADYDRVLKQ RNTLLRTAAM ARRNKASGPN
     ISTLDAWDHH LALAGAELVA ARLALISALS PLVDKCYVEI AEGGQTRIGY RSTISAEPDP
     TAAALTEQFM TALGEARANE LDRGITLVGP HRDEMVLELT SSSGDNMPAR GYASHGESWS
     YALALRLAAY DLLRSDGSDG GEPVLILDDV FAELDAKRRR RLAERVSGAD QVLITAAVDA
     DVPEQLIGQK FTVADGQVSA A
//

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