(data stored in ACNUC7421 zone)

SWISSPROT: C8W311_DESAS

ID   C8W311_DESAS            Unreviewed;      1197 AA.
AC   C8W311;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   OrderedLocusNames=Dtox_0214 {ECO:0000313|EMBL:ACV61167.1};
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:ACV61167.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61167.1, 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: Couples transcription and DNA repair by recognizing RNA
CC       polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC       release of RNAP and its truncated transcript from the DNA, and
CC       recruitment of nucleotide excision repair machinery to the damaged
CC       site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969,
CC       ECO:0000256|SAAS:SAAS01144535}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase
CC       family. RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR   EMBL; CP001720; ACV61167.1; -; Genomic_DNA.
DR   RefSeq; WP_015755888.1; NC_013216.1.
DR   STRING; 485916.Dtox_0214; -.
DR   EnsemblBacteria; ACV61167; ACV61167; Dtox_0214.
DR   KEGG; dae:Dtox_0214; -.
DR   eggNOG; ENOG4108JA2; Bacteria.
DR   eggNOG; COG1197; LUCA.
DR   HOGENOM; HOG000216591; -.
DR   KO; K03723; -.
DR   OMA; LDIPRVN; -.
DR   OrthoDB; 234717at2; -.
DR   BioCyc; DACE485916:G1GFV-220-MONOMER; -.
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:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd00079; HELICc; 1.
DR   Gene3D; 2.30.30.840; -; 1.
DR   Gene3D; 3.90.1150.50; -; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR004576; Mfd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037235; TRCF-like_C.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00982; TRCF; 1.
DR   SUPFAM; SSF141259; SSF141259; 1.
DR   SUPFAM; SSF143517; SSF143517; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00580; mfd; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W311.
DR   SWISS-2DPAGE; C8W311.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144540};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144521};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144538};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144510};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN      669    830       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      844   1005       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
SQ   SEQUENCE   1197 AA;  136639 MW;  C8B6CA7621EDDE40 CRC64;
     MNGFVNGIKE WLLQPLINTP EFIDLQNGLA KNRRCQVVSG LSSAQKSFVI AGLVQAMRQT
     ALIITASDQE AAGLTEDLKN LLPDLKVMTF PARRLLPYQV FAYSKEILRQ RMEVLESLCR
     GENPVIIAPV EALMRRLGPC ADFCSARLEL NVGQRYELPQ MVSCLHEHGY ERVNLVESHG
     QFSVRGGILD IYPITGINPV RVEFFDDEVD SIRIFNPGTQ RSEENMSQMQ IFPVREMVVR
     QGDWERAYQA LSQEYQYRRR NLDKKSDSEV LDNLSRCEEV LDNISQAKYF DSIEQYLPYF
     YDEDITLLNY IKAESLVLVD EPSRLQENTD LLQRERTETY SELMKAGRVL PGQFKGYTDW
     AGIHKQITGF RAIYFSFLPR QASLWRSCNT VNFPVKTMQN FMGKVEMLAE EIRHYKMSRY
     GVVLLVKNSD RAAQLVLSLR DYDLEALYLK KDLSEYPHLN VQEDMPDSKT KYKVDRGRGQ
     IVILPMHLSN GFELVSGKLA VITETEIYGH RKKPSVQRQR VQDKMELFAE LKTGDYVVHV
     NHGIGRYDGV VQLTIGDVKR DYLLVKYAGE DKLYIPTDQV EMIQKYLGSE GGTPKLSRLG
     GAEWSRVKSK VKEAVKEMAQ ELLALYAARE AVQGHPFSKD TVWQQEFEAA FPYEETPDQL
     KAIEEVKADM ERPRPMDRLL CGDVGYGKTE VALRAAFKAV MDGKQVAVLV PTTILAQQHF
     NTFKERFAKY PVNIAMLSRF ITARRQRQIV QELLLGQVDI VIGTHRLVQD DIKFKDLGLV
     VVDEEQRFGV THKEKLKQLR QNVDVLTLTA TPIPRTLHMS IVGVRDTSLL ETPPEDRIPV
     QTYVLEEEPV IVREAIRREL GRGGQVYYVH NRVADLDRVA GWLKGLVPDA AIAIGHGQMK
     EDRLENVMLD FMNKKFDILL CTTIIETGLD IQNVNTLIVK DADYMGLAQL YQLRGRVGRT
     NRLAYAYCTF RGDKVMSELA EKRLSAVREF TEFGSGYKIA MRDLEIRGAG NILGPEQHGH
     IAAVGFDLYC RLLEEAVLEA KGGENAKPIE TLVELPVTAY IPDEYVIDLN QKVELYKRMA
     NIRDIKMLSE MEDELIDRFG DIPEPVLNLL AVTRIKALAV NLKIKNISRI NGYYRLQFAA
     SHDLTGEKLI TVSEKYGGKV KFNHAEGEFE IRLQTVSKDQ ETRLTMSRLE SLLMNLL
//

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