ID A0A2U3ABG2_9BACL Unreviewed; 1169 AA.
AC A0A2U3ABG2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:STX08424.1};
GN ORFNames=NCTC10597_00066 {ECO:0000313|EMBL:STX08424.1};
OS Kurthia zopfii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1650 {ECO:0000313|EMBL:STX08424.1, ECO:0000313|Proteomes:UP000254330};
RN [1] {ECO:0000313|EMBL:STX08424.1, ECO:0000313|Proteomes:UP000254330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10597 {ECO:0000313|EMBL:STX08424.1,
RC ECO:0000313|Proteomes:UP000254330};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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:STX08424.1}.
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DR EMBL; UGNP01000001; STX08424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3ABG2; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000254330; 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}.
SQ SEQUENCE 1169 AA; 133186 MW; A612842E4DC80BA5 CRC64;
MEILHQLFMN DAEIEKFIND LKNGQRSQLV TGLSGSARPT MIGTAFEETK KSMYIIAPNM
LQAQNLYEDL SKLIGEELVH YYPADEFIAA DMTVASPELR AQRIETINHM LNDQRGIYII
PAAGMRKIMP PKDLWKELNV QIELGEELDT ELLLSNLVTM GYSRNGMVTT PGEFALRGGI
IDIYPPYYEN PVRIELFDTE VDSIRTFSAD DQRSIDKLTQ LTILPASEFV LSKENRVALA
LRLEDGLAQS LKQVQSDSVK TTLLENVQSD ITLLKEGQLP EFTNRYGSLL YENPTFLGDY
FQKDGVVIFE EIARIQEVMD AWEKEEKDWM LEMIEIGKMV HSVKPSFSFQ EILANIPQQK
VFFTLFTRGF TGIKFTETYN FSCKPMQHFH GQIDLLQSEI KRWQSSNFTV IFMTDVKERT
GILQDLLEEH GVKVQIGTPN GAGVFILSGH LTSGFELPMQ KIAVVTEEEL FKQQKKRKTR
PKTMTNAERI KSYTEIKPGD YIVHVHHGIG KYIGIETLEI NGNFKDYLQI RYRADDKLFV
PIDQIDLIQK YVGSEDKEPK LHKLGGVEWK KTKTKVAKAV QDIADDLIKL YAEREAAKGF
AFSPDDAQMR EFEESFPYEE TEDQLRTIQE VKIDMERERP MDRLVCGDVG YGKTEVAIRA
AHKAVLDGKQ VAFLVPTTIL AQQHYETMIE RFQDTPVNIG VLSRFRSKKQ QNETLAALHE
GKIDILVGTH RILSKDVAYK DLGLLIVDEE QRFGVTHKEK IKTLKTNVDV LTLTATPIPR
TLHMSMVGVR DLSVIETPPA NRFPVQTYVM EHNGALIREA IEREMARGGQ VFYLHNRVDD
MGKQIDLIQT LVPEARIARA HGKMTESELE SVILAFLDGE YDVLVTTTII ETGIDIPNVN
TLIVNNADRM GLSQLYQLRG RVGRSNRVAY AYFMYQRDKV LTEVAEQRLQ AVKEFTELGS
GFKIAMRDLS IRGAGNLLGA QQHGFIDSVG FDLYSQMLEE AVEEKQTGEK KVEEHNIEIL
IPFDAYLPDE YIPDGYQKIQ MYKRIRSIQT EKDYSEIIDE LVDRFGDLPT EVDRLMRIAR
MKAWGKEVGL NSVKYKNKMY KIELSPEGTA QIDGSKMVSD SMSLGRAVGF TMENNMLALT
VDERKVSKSQ DLFELVEAVV KLLPDALKE
//
