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Database: UniProt
Entry: U1LKN1_9BACL
LinkDB: U1LKN1_9BACL
Original site: U1LKN1_9BACL 
ID   U1LKN1_9BACL            Unreviewed;      1174 AA.
AC   U1LKN1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ORFNames=M467_12580 {ECO:0000313|EMBL:ERG68103.1};
OS   Exiguobacterium chiriqhucha RW-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=1345023 {ECO:0000313|EMBL:ERG68103.1, ECO:0000313|Proteomes:UP000016464};
RN   [1] {ECO:0000313|EMBL:ERG68103.1, ECO:0000313|Proteomes:UP000016464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW-2 {ECO:0000313|EMBL:ERG68103.1,
RC   ECO:0000313|Proteomes:UP000016464};
RX   PubMed=23929485;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "Draft Genome Sequence of Exiguobacterium pavilionensis Strain RW-2, with
RT   Wide Thermal, Salinity, and pH Tolerance, Isolated from Modern Freshwater
RT   Microbialites.";
RL   Genome Announc. 1:e00597-e00513(2013).
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   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERG68103.1}.
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DR   EMBL; ATCL01000010; ERG68103.1; -; Genomic_DNA.
DR   RefSeq; WP_021065744.1; NZ_ATCL01000010.1.
DR   AlphaFoldDB; U1LKN1; -.
DR   STRING; 1385984.GCA_000702565_00024; -.
DR   PATRIC; fig|1345023.5.peg.585; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000016464; Unassembled WGS sequence.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd17991; DEXHc_TRCF; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.11180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR003711; CarD-like/TRCF_RID.
DR   InterPro; IPR036101; CarD-like/TRCF_RID_sf.
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; IPR047112; RecG/Mfd.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   NCBIfam; TIGR00580; mfd; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF02559; CarD_TRCF_RID; 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; CarD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF143517; TRCF domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000016464}.
FT   DOMAIN          634..795
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          816..970
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1174 AA;  131761 MW;  5E543E99F9783573 CRC64;
     MNALEKFMVT LPETNVIRER LPKVDRQLVT GLTTSAKALV LAGLAKNSPR RLVVVTHNMY
     QAQKMYDQLE SLIGPSKTLL YPIDETLAGE LSLTSSPELL AARIEARTRL LDETGGVLVV
     PLGGLRRYIP NPSDWQTSHH HIKPGQELDL KPFAETLITL GYERTATVTA PGEFSVRGSI
     LDVYPLTAAR PYRIDLFDTE VDSIFTFDAE TQRSLGVVGE AVIPPATEFI ASRDQLQQAG
     QALERQYERT LSLIETETIR QALEDGIARD IEQFGRGEVP EKVGKYTPLL YSSTLLDYVG
     AEAVLMLDEV ARIEDAADVQ DREEAEWFSS LIERGESVSN YTLAVPMHKV FRTLKQVAFS
     LLPSRRSGIP ETNTVHLSCR PLPAFHGQMH LLKQEVERWQ QGDHRIVFLA GDQTRADKVV
     ELLDDYGISS TFTNVDGELL PRHVHVMIGQ IEGGFELSTS RLVVVSEEEL FKRVTKRKRQ
     TKNLTNAERI KSYQELKPND HVVHIHHGIG KYLGIKTIEV GGIHQDYLHL VYAGDDALYV
     PVDQIDLVQK YVGAEGKEPK IYKLGGTEWK KVKSKVAKSV EDIADELIKL YAAREASVGY
     AFPGDDEEMS QFESSFPYAE TEDQVRSIAE IKADMERSRP MDRLLCGDVG YGKTEVAIRA
     AFKAVLAGKQ VAFLVPTTVL AQQHYETMLE RFSEFPINVS VMSRFRSKSE MAATKKGLKE
     GTIDVVVGTH RVLSKDVTFA DLGLVIIDEE QRFGVKHKER LKQLKTNIDV LTLTATPIPR
     TLHMSMIGIR DLSVLETPPE NRYPVQTYVM EYDGIVLREA LERELARGGQ AFFLYNRVEG
     IERKAEEIRA LLPEARIATA HGRMTETELE SQLISFLEGE ADVLVSTTII ETGIDIPNVN
     TLIVHDADKM GLSQLYQLRG RVGRSNRIAY AYFTYRKDKR LTEVAESRLQ AIKEFTELGS
     GFKIAMRDLS IRGAGNLLGA QQSGFIDSVG FDLYSQMLSE AIEERKDRMR GQAKQVVFKP
     EIAFQADAYI PDDYLSDSEL KIEMYKRFKY VDTPEALFAL QDELIERFGE FPEPVALLIQ
     LTRLRIYGEM AKVARIKQSP GRIEMVLSLE STTALDVPSF MEWTMPLGRK LGVGQDNGAL
     KLSLSGRMPV VELLNDADTV LEELVKRLAH AVAK
//
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