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Database: UniProt
Entry: A0A073ILR8_9BACT
LinkDB: A0A073ILR8_9BACT
Original site: A0A073ILR8_9BACT 
ID   A0A073ILR8_9BACT        Unreviewed;      1049 AA.
AC   A0A073ILR8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=EH55_11265 {ECO:0000313|EMBL:KEJ91273.1};
OS   Synergistes jonesii.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Synergistes.
OX   NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91273.1, ECO:0000313|Proteomes:UP000027665};
RN   [1] {ECO:0000313|EMBL:KEJ91273.1, ECO:0000313|Proteomes:UP000027665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=78-1 {ECO:0000313|EMBL:KEJ91273.1,
RC   ECO:0000313|Proteomes:UP000027665};
RA   Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT   "Draft Genome Sequence of Synergistes jonesii.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KEJ91273.1}.
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DR   EMBL; JMKI01000053; KEJ91273.1; -; Genomic_DNA.
DR   RefSeq; WP_051682891.1; NZ_JQEL01000053.1.
DR   AlphaFoldDB; A0A073ILR8; -.
DR   STRING; 2754.EH55_11265; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000027665; 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; 2.
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:UP000027665}.
FT   DOMAIN          525..686
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          707..861
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1049 AA;  116813 MW;  B6A0605072DFF6DD CRC64;
     MTENKKNISA GALVELDEEL WLRNKGVHVA SKGAMRPWVC RGIEEPLLAL LPDARQARDF
     AADAAALGVF ENVKVLPEIT LADDTSKSGA QRFARGDALE NFKYRGGVLA ATPASLMAPF
     STGADYLELE CGKEAGRDRL ADWLAQKGYE RCDLVWTPGQ YAVRGSVVDI FSPSDDYPLR
     IEFFDDDVEN IRFFLPESQM SLRRLRRCSV QSLVSKSESR LEKFFPDDMR ALLFDPAALD
     VTAENALWLS RSINAQSGEE LQWRAWNDIL SVLTRFKRLR ILPDVKNCIA RMPVAQFPNF
     RGKLKNVEYY CLSLLKEGYK INVVSETARN LEWARVNSFG AKSGVLSEGF IDAASKTAVL
     TELELSGITV ARRGIENRAP SDWGSGLMRG QWVVHDDYGV ALYMGSERVK TSEGEQEYLV
     LQFAEERRLL IPVMQFYKIS PWSPLPGQEP KPDNLKTSHW KKAAAKAKAM AEQAAAALVK
     IYAEREVSGG FAFPENGAMM RELEESFSYK ETKDQLQAID DVMRDMASGV PMDRLVVGDV
     GFGKTEIAIR AAGTAVFAGK QTAIMTPTTL LARQHFETFS ARFANTAVRV EVVSRFIAVS
     KQKKILQELA EGKVDILIGT HRLLADDVKF KDLGLVIVDE EHRFGVMHKE HMKKLAPGVD
     VLMLSATPIP RSLSLSLSGL RDMSVLETPP QRRLPVITVV RPFSEELLKS AVLREKNRGG
     QIFYVHNRIS DLQERAVMLK RLFPKLTIAV AHSKMAEASL EKTMADFSAG KVDMLVCTTI
     VESGLDIPAA NTLIVDDAQE LGLAQMYQLR GRVGRREDQA YAFLFYPPEA HISVESSERL
     EAIADLDELG AGYQLAQRDL QIRGGGDLIG ISQHGNASKI GYQKYCDLLA DEIAKIKGRY
     HEQLAVEISF PVSIPGDYLP QENLRVTLYR RLLKVDSAEE ATALREETED RFGKIPNELD
     FLFSLAAIRG ASYALGITKL ICSRYELVLQ GRPDAAWEGL KFPPRWRRRL DGFIGPGGFA
     GIKEAARTII EQNAHLSDKI LQSGSDRNG
//
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