ID A0A1L4BVQ2_9LACT Unreviewed; 1180 AA.
AC A0A1L4BVQ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BKP56_00570 {ECO:0000313|EMBL:API87918.1};
OS Marinilactibacillus sp. 15R.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Marinilactibacillus.
OX NCBI_TaxID=1911586 {ECO:0000313|EMBL:API87918.1, ECO:0000313|Proteomes:UP000184433};
RN [1] {ECO:0000313|EMBL:API87918.1, ECO:0000313|Proteomes:UP000184433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15R {ECO:0000313|EMBL:API87918.1,
RC ECO:0000313|Proteomes:UP000184433};
RA Wei Y., Cao J., Fang J.;
RT "Genome sequence of Marinilactibacillus sp. 15R.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017761; API87918.1; -; Genomic_DNA.
DR RefSeq; WP_072693228.1; NZ_CP017761.1.
DR AlphaFoldDB; A0A1L4BVQ2; -.
DR STRING; 1911586.BKP56_00570; -.
DR KEGG; marr:BKP56_00570; -.
DR Proteomes; UP000184433; 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; 3.40.50.11180; -; 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:UP000184433}.
FT DOMAIN 636..797
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 822..972
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1180 AA; 134062 MW; 799CE1D02DF0D79D CRC64;
MSTITSFLSE KPSVQKVFST IGQRQTQLIT GIAGSARALL LSSLLKEKQK QIVIIAQNLY
HANQLMADLT GLVPDDQLFV FSVDDMIHAE MAIASPEARA ERVQALDYLL SGKPGIVIIP
LSGIRKLLPP KEIFQASHIN IELGAEIEFD HFAESLIGMG YRREQKVAAP GEFSIRGGII
DVYPLTEENP VRIELFDVEV DSLRFFDADT QRSIENVSKI SLIPATDFLV TKEQMKPAAE
KLKKALSRNL AALTDNEAKQ ILSKQLNSVI RGLETGELTD DLVKFRDFVY EKHSSIIDYM
ADDAILAMDE YPRILEKDAL LNEEEAEWAT SQLSQRLVLQ KQTFSNDFRE ELKKNQHDTL
HFALFQKGMG GLRFDAIHPF QYRNMQQFFG QMHLLKTEMD RWEKLGYTVV VMTADAERAD
KVNRTLLDFE IPSILSGNGE IQEKKIQVIS STVQNGFELP TEKLAVLTEK ELFNRVNRKK
VRRQNITNAE RLKSYTELNP GDFVVHVNHG IGRYTGMETM EIGGVHQDYM SIIYDNDSKL
FIPVTQVNLL QKYVSSEGKT PKINKLGGTA WAKTKRKVAS QVEDIADDLI ELYAERERKT
GFPFSEDNEY QHEFDEAFPY TETDDQLRSI KEVKRDMEKD KPMDRLLVGD VGYGKTEVAM
RAIFKAVQDG KQAAILVPTT VLAQQHYETM LERFSDFPVE IGLMSRFRTG QQMKKLTEEL
RKGQVDVVVG THRILSKDVV FQDLGLLVVD EEQRFGVKHK ERLKQLKNEV DVLTLTATPI
PRTLHMSMLG VRDLSVIETP PANRYPVQTY VMEMNGAVVG EAMKRELARG GQVFYLHNRV
STIDQRAEEL QQLVPDARIG IAHGQMSEGQ LENVLFEFIQ GEFDILVTTT IIETGIDMPN
VNTLLVEDAD RMGLSQLYQL RGRVGRSSRI AYAYFMHQPN KILTEVSEKR LQAIKDFTEL
GSGFKIAMRD LSIRGAGNLL GQQQHGFIDS VGFDLYSQML SEAVARKRGD TAQLQTNVEL
DLSVDAYLPS TYIEDERQKI ELYKRIREFA SDQDYVELQD ELIDRFGDYP QEVSDLLTVG
LLKMYSDRAL IETIKRDKQK VAVTFSKEGT QTLPLPEVFK ALKKISLKTN MNTNDRLSID
FKLPVRLVDN EWLDSLVLFS KNISEFQMNK KEAVAGKGNE
//
