ID A0A1H6AE11_9ACTN Unreviewed; 1167 AA.
AC A0A1H6AE11;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN04489712_105373 {ECO:0000313|EMBL:SEG46612.1};
OS Thermomonospora echinospora.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=1992 {ECO:0000313|EMBL:SEG46612.1, ECO:0000313|Proteomes:UP000236723};
RN [1] {ECO:0000313|Proteomes:UP000236723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43163 {ECO:0000313|Proteomes:UP000236723};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNVO01000005; SEG46612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6AE11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000236723; 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:UP000236723}.
FT DOMAIN 628..789
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 807..964
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1167 AA; 128862 MW; FED39D803C209729 CRC64;
MTLTGLLDVA VRDRALAEAL ARARVDHDVV APAPLWPILA AALARTAGSG TLLAVTATGR
EAEDLEAALT CFLDPHRVAH FPAWETLPHE KLSPRSDTVG RRLAVLRRLA HPDPDDPAGG
PLDVVVAPVR AVLQPIVTGL GDLEPVRLRA SEDADPGDVV RRLADAGYHR VDLVEKRGEF
AVRGGILDVF PPTEEHPLRV EFWGDTVEEV RYFKAADQRS LEAARDGLWA PPCRELPLTE
TVRERARELA EQHPALQEIL TRIADGEAVE GMEAFSPVLA DRMELLVDLL PPESALLVCE
PERIRTRAHE LVRTSQEFLE ASWVNAAAGG QVPIDLGAAA FRTLEEVREQ AARLGLPRWT
VTALNPEGEA LGLDVHAAEQ YRGDTARVIG DIKRWVDDQW RVVLVTAGHG PAERLVEVLR
EEGLGARLAD LPEPPEPSVV NVTTGMLDNG FVWPAARLAV LTETDLSGQR ASTKDMRRLP
SRRRGGIDPL RLRVGDYVVH EQHGVGRYVE MVSRTVQGAT REYLVLEYAR GDRLFVPTDQ
LEEVTRYVGG EAPTLHRLGG ADWQKSKSKA RKAVKQIAGE LIRLYSARMA TPGHAFAPDT
PWQRELEDAF PYVETADQLA AIDEVKGDME KPVPMDRLIC GDVGYGKTEI AVRAAFKAIQ
DGKQVAVLVP TTLLVQQHLS TFSERFAPFP VVVKPVSRFQ TDAEITETLR GAADGTVDLV
IGTHRLFAAQ SRFKNLGLVI IDEEQRFGVE HKEELKRLRT QVDVLAMSAT PIPRTLEMGL
TGIREMSTIL TPPEERHPIL TFVGPYDDKQ IAAAIRRELL REGQVFFVHN RVRSIDRVAA
TLQQLVPEAR IATAHGQMNE QQLEAVMVDF WEKNYDVLVA TTIVESGLDI PNANTLIVDR
ADTYGLSQLH QLRGRVGRGR ERGYAYFLYP PETPLTETAH ERLATIAQHT EMGAGMYVAM
KDLEIRGAGN ILGVEQSGHV AGVGFDLYVR MVGEAVRELK AKAGGEAEPA ELPETKVELP
VDAHLPHDYV PGERLRLDAY RRIAAITSDE EIAGVLEELT DRFGTPPEPV LNLLEVARFR
ARARRAGLTE VTVQGNHVKF APVQLPDSKQ VRLQRLYPRS IYKPTTNTLL VPAPKTAPLG
GRPLRDTALL KWATDLVEAM FLEPART
//
