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Database: UniProt
Entry: M7N8X5_9BACL
LinkDB: M7N8X5_9BACL
Original site: M7N8X5_9BACL 
ID   M7N8X5_9BACL            Unreviewed;      1172 AA.
AC   M7N8X5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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_2 {ECO:0000313|EMBL:EMR05053.1};
GN   Synonyms=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   ORFNames=C772_02975 {ECO:0000313|EMBL:EMR05053.1};
OS   Bhargavaea cecembensis DSE10.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX   NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR05053.1, ECO:0000313|Proteomes:UP000011919};
RN   [1] {ECO:0000313|EMBL:EMR05053.1, ECO:0000313|Proteomes:UP000011919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE10 {ECO:0000313|EMBL:EMR05053.1,
RC   ECO:0000313|Proteomes:UP000011919};
RX   PubMed=23766406;
RA   Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT   from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT   Chagos-Laccadive Ridge System in the Indian Ocean.";
RL   Genome Announc. 1:e00346-13(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:EMR05053.1}.
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DR   EMBL; AOFT01000023; EMR05053.1; -; Genomic_DNA.
DR   RefSeq; WP_008301239.1; NZ_AOFT01000023.1.
DR   AlphaFoldDB; M7N8X5; -.
DR   STRING; 1235279.C772_02975; -.
DR   PATRIC; fig|1235279.3.peg.2973; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000011919; 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:UP000011919}.
FT   DOMAIN          636..797
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          818..972
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1172 AA;  130650 MW;  16F746C72E7A4940 CRC64;
     MEELLDVLAG GGEIADLLGD LKEGRDRQLV TGLAGGARAA LFALAARETG RPVLVVEPNM
     LQAQRTYEDL ARLSGEESVR LYPADELTAA ELSVASPELR AQRIEALDHL MRNGTGIFVT
     PIAGLRKLLP APADWKNAAL SAELGDEIDP ADWAASLVAM GFSRQPMVTS PGEFSLRGGI
     LDIYPLDLEE PVRFELFDTE IDSIRTFSAD DQRSTGRLDT VRILPAHEFS WPAERLAVTA
     DRLEASLAAS LKKVSDEAAR EALLENIGAD IALMKDGEIP EGVMKYASLA GETAFLGDYF
     PEEGILFYNE AGRIIEVAES LERQEGEWHT EMIASGKLVH DARLSHTFKE IDAMAGQKKV
     YLSLFSRSLP GLVLKDTVQI SCKPMQQFHG QMNLLKSEAE RWQAGGFTVL LLAGDRERAE
     KVRSILGDYG MEADIPEEGT VPGSGIHVIE GDLSDGFELP LRQIAVVTDS ELFKQRSRRK
     ARPQKLSNAE RIKSYSEIKP GDYVVHIQHG IGKYIGIETL DVGGTHKDYL HISYRGDDKL
     YVPIDQIDQI QKYVGSEDRE PKIHKLGGTE WKKTKSKVSK AVKDIADDLI KLYAKREAEK
     GFAFSPDDDL MHSFEASFPY DETDDQLRSI EEIKRDMERE RPMDRLLCGD VGYGKTEVAI
     RAAFKAVGDG KQVAFLVPTT ILAQQHFETM KERFAGYPVE VRMLSRFGTR KEHQETVKGL
     KDGTVDVVVG THRLLSKDVE YRDLGLLIVD EEQRFGVTHK ERIKQMKANV DVLTLTATPI
     PRTLHMSMIG VRDLSVLETP PANRFPVQTY VMEFSGPLVR EAIEREMARG GQVFYLYNRV
     EDMARKAEEI QMLVPEARIA TAHGRMSETE LEAVILAFLE GEYDVLVTTT IIETGVDIPN
     VNTLIVHDAD RMGLAQLYQL RGRVGRSNRV AYAYFLYQRN KVLTDVAENR LQAIKEFTEL
     GSGFKIAMRD LSIRGAGNLL GAQQHGFIDS VGFDMYSKML EEAIEEKRGN GKEEEVPDVE
     VTLHTDAYFP DSFIPDGFQK IQMYKRVKAV ATEEDYSELV DEMADRFGDL PLEAEQLLKV
     ALMKVWAREA GVESIKQQGD RVIISFTEAG TQQADGAKIM EDTLQYGRAV GFHVEDGRLL
     LTVDGSKTGK KTLFDVLEGV MKILPDAKKQ EV
//
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