ID A3NWE1_BURP0 Unreviewed; 1189 AA.
AC A3NWE1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
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:ABN90366.1};
GN OrderedLocusNames=BURPS1106A_2402 {ECO:0000313|EMBL:ABN90366.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN90366.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|EMBL:ABN90366.1, ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|EMBL:ABN90366.1,
RC ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) 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; CP000572; ABN90366.1; -; Genomic_DNA.
DR AlphaFoldDB; A3NWE1; -.
DR KEGG; bpl:BURPS1106A_2402; -.
DR HOGENOM; CLU_005122_1_3_4; -.
DR Proteomes; UP000006738; Chromosome I.
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}.
FT DOMAIN 650..811
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 820..986
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1189 AA; 131847 MW; 7BE88F8BDE5615CE CRC64;
MKSKDGFYNT SFAAMRRAEL VRHPAFANQP LVMSDNASPS QSPVALVKAG QRFAFDGAHG
SADALVIARY LAAHRAQVPL LAVICANAVD AQRLAQELAY FAPDARVRVL PDWETLPYDT
FSPHQDLVSE RLATLHDLGE GRCDILLVPA TTALYRMPPA SFLAAYTFSF TQGERLDEAK
LKAQLTLAGY EHVSQVVRPG EYCVRGSLID LFPMGSPLPY RIDLFDDQVD SIRAFDPDTQ
RSLYPVRDVR LLPGREFPFD EAARTAFRSR WRETFEGDPS RAPIYKDIGN GVPSAGIEYY
LPLFFDETAT LFHYLPERAQ LVFTGDLDAA IKRFTADTKQ RYAFLSHDRE RPILEPQRLF
LSDDDFYLLA KPFARIVLPA QPSGGWAAPL PNLALERHAD APLAAFAAYL ETTKNRVLFT
VESAGRRETI AQLFAEHHLR PAGSDSFAAW LASDERFALG VAPLANGFAV PGEGYAIVTE
TELYGALGRR AGRRRQEQAS NVDAMVRDLS ELKVGDPVVH AQHGIGRYMG LVSMDLGEGD
TEFLHLEYAG DSKLYVPVAQ LHVISRYSGA DPDSAPLHAL GSGQWERAKR RAAQQIRDTA
AELLNLYARR AAREGHAFGL DPRDYVKFAD SFGFEETPDQ AAAIAAVIGD MTSGKPMDRL
VCGDVGFGKT EVALRAAFIA VMGGKQVALL SPTTLLAEQH TQTFADRFAD WPVRIVELSR
FKTAKEVNAA IAQINEGSVD IVIGTHKLLS SDVQFKRLGL VIIDEEHRFG VRQKEALKAL
RAEVDVLTLT ATPIPRTLGM ALEGLRDFSV IATAPQKRLA IKTFVRREEE SVIREAMLRE
LKRGGQVYFL HNEVETIENR KAMLEELVPE ARIVIAHGQM HERELERVMR DFVAQRANVL
LCTTIIETGI DVPSANTIIM HRADKFGLAQ LHQLRGRVGR SHHQAYAYLL VHDPQALTKQ
AQRRLEAIQQ MEELGSGFYL AMHDLEIRGT GEVLGDKQSG EIHEIGFQLY TEMLNDAVKA
LKNGKEPDLT APLAATTEIN LHAPAILPAD YCGDVQERLS LYKRLANCEH GDAIDGIQEE
LIDRFGKLPP QAHALVETHR LRLAAKPLGI VKIDASEAAI GLQFVPNPPI DPMRIIDMVQ
KHRHIKLAGQ DKLRIETRTP DLAVRVSTVK ETLRALGQPQ QPRAQAAAR
//
