(data stored in SCRATCH zone)

SWISSPROT: D6Z9G9_SEGRD

ID   D6Z9G9_SEGRD            Unreviewed;       401 AA.
AC   D6Z9G9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 55.
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=Srot_0003 {ECO:0000313|EMBL:ADG96496.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96496.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96496.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96496.1; -; Genomic_DNA.
DR   RefSeq; WP_013136952.1; NC_014168.1.
DR   STRING; 640132.Srot_0003; -.
DR   EnsemblBacteria; ADG96496; ADG96496; Srot_0003.
DR   KEGG; srt:Srot_0003; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269561; -.
DR   KO; K03629; -.
DR   OMA; GQQKSFL; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; SROT640132:G1GLH-3-MONOMER; -.
DR   Proteomes; UP000002247; 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; D6Z9G9.
DR   SWISS-2DPAGE; D6Z9G9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930557};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:UP000002247};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354122}.
FT   DOMAIN        3    363       SMC_N. {ECO:0000259|Pfam:PF02463}.
FT   NP_BIND      30     37       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
SQ   SEQUENCE   401 AA;  43601 MW;  6521ACB285B5027C CRC64;
     MRVSSFEIRD FRSWEHAAMR LDEGCTLFLG RNGYGKTNLV EALGVLSSLS SHRGAQNAAM
     VRRGAAEAFL SAEVLNEGRK LTVGLRIAPG KATKAQLNGV NRPTREVAGI LRTVFFSPED
     LALVRGEPGE RRRFLDETLI VRQPRMAGVK ADFERVLRQR ATLLKSLSGA RGAARNDEAR
     ATLEAWDEQF ASRAAALTVA RLDLVRALSP RVGRCYAAID PLSDDAELRY RMSAEDADQE
     ETGGEAPVGE TSEPQVANAV MERLSQLREE ELRRGQCLVG PHRDDLELRL AGGAARAFVS
     HGEAWSYALA LRVAAFELLR EEGHDPVLVL DDVFAELDGP RREVVAGLAK KAEQTLITAA
     DPATVPDGLV ANVVPVSLGE SRGTKSSRIL VEQTPMGEDD A
//

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