ID A0A0S1XV67_9BORD Unreviewed; 1157 AA.
AC A0A0S1XV67;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ASB57_00880 {ECO:0000313|EMBL:ALM81710.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM81710.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM81710.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM81710.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) 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}.
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DR EMBL; CP013111; ALM81710.1; -; Genomic_DNA.
DR RefSeq; WP_057649747.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1XV67; -.
DR STRING; 1746199.ASB57_00880; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000064621; 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: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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000064621}.
FT DOMAIN 630..791
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 812..966
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1157 AA; 127930 MW; 0157DC2029A30323 CRC64;
MSAESSSTIA APTAPLVPAT ATLLAALKPG TRYAHPRPPG SGDAWLLADL ARQAGRPLVI
LSADPLEAQR LAEEIHLFAP TLRVRQLPDW ETLPYDAFSP HHDLISQRLQ TLDALMHQAV
DVLTVPITTA LYRLPPPAFM AAYTFSFKQR DKLDEAALRA QLTLANYTHV TQVTAPGEFC
LRGGLIDLFP MGSIVPYRID LFDDEIESIR AFDVDTQRSL YPVNNVQLLP GREFPMDEDA
RNRFRARFRE LFEGDPSRAL PYRDIGAGIA FAGVEYYLPL FFDEVATLFD YLAPGTITVT
LGDIEEAMRR FNQDTTSRYE FLKSDRERPV LPPPSLFLDG EGLFGHLKQF ERLALTADAA
HPDIGPAPDV AVTRRADDPV SRLRAVVDSG KWRVLLCADS AGRRETLSQM LAEFDLRPDA
EPASIDDFRA SHAELALMPA PLTAGFSLPG ERVALITEND LYPGQTATGR RGHRAQERAS
NVEAMVRDLS ELREGDPVVH AQHGIGRYHG LVNMDMGEGV MEFLHLEYAN GSTLYVPVSQ
LHVIARYSGA DPDAAPLHQL GSGQWDKARR KAAKQVRDTA AELLDLYAKR AAREGYSFKL
PLNDYEAFAE GFGFEETVDQ SAAIQAVILD MTSGKPMDRL VCGDVGFGKT EVALRAAFLA
VANGKQVALL CPTTLLAEQH AQTFSDRFAD WPVRVVELSR FRSAKEISAA IQGINSGGVD
IVIGTHKILS KDVQFKQLGL VIIDEEHRFG VRQKEALKSL RAEVDVLTLT ATPIPRTLGM
SLEGIRDFSV IATAPQKRLA IKTFVRREDG STIREALLRE LKRGGQAYFL HNEVETIHNR
RARLEELVPE ARIAVAHGQM AERELEQVMK GFYQQRYNVL LCTTIIETGI DVPSANTIVI
HRSDRFGLAQ LHQLRGRVGR SHHQAYAYLL TPGEDAITTN AKKRLEAIQA MEELGSGFYL
AMHDLEIRGT GEVLGDSQSG NIQEVGFSMY TEMLNEAVRA LKAGEEPDLD APFNSACEVN
LHAPALLPAD YCADVHARLA VYKRLSHAQD DDELIRIQEE LIDRFGKLPE AATTLLATHR
LRLGAVALGI VKIDASESQA LVQFGPKPSV DPLRIIELVQ KQRHIKLAGQ DKLRVEIKGQ
QVPARVEAVR TVLRALA
//
