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Database: UniProt
Entry: X8HDV3_9FIRM
LinkDB: X8HDV3_9FIRM
Original site: X8HDV3_9FIRM 
ID   X8HDV3_9FIRM            Unreviewed;      1096 AA.
AC   X8HDV3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
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:EUB26055.1};
GN   ORFNames=HMPREF1504_1815 {ECO:0000313|EMBL:EUB26055.1};
OS   Veillonella sp. ICM51a.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=936591 {ECO:0000313|EMBL:EUB26055.1, ECO:0000313|Proteomes:UP000020651};
RN   [1] {ECO:0000313|EMBL:EUB26055.1, ECO:0000313|Proteomes:UP000020651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICM51a {ECO:0000313|EMBL:EUB26055.1,
RC   ECO:0000313|Proteomes:UP000020651};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) 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:EUB26055.1}.
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DR   EMBL; JAPX01000029; EUB26055.1; -; Genomic_DNA.
DR   RefSeq; WP_038123896.1; NZ_JAPX01000029.1.
DR   AlphaFoldDB; X8HDV3; -.
DR   PATRIC; fig|936591.3.peg.951; -.
DR   Proteomes; UP000020651; 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}.
FT   DOMAIN          563..724
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          742..899
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1096 AA;  124632 MW;  76798C69E6E400DF CRC64;
     MDTSIDTLLS QNPSMTDGLK AFRQKGKSVI YGLSGSQKSF LLSCAVPEEQ VQSIIIVVHD
     KEHKELWERD LAFFWPNVQV LPFPITERVE FTTVARSLEG QGAQMRALSM LAWNRPVVVL
     ATIEEATQYV VSPQYVISQS VHLEVSQSIE RDELLEKLVK IGYERVDQVE QRGHFSVRGD
     IFDIFPVNSD DPIRMEFFGD EIDTMRHFSV DTQRSIETVD AYTVTPFFLT SDDADSTLLS
     YAKDGLIIYD EPVRIQEALK KFLKEDTTHR KQHCEWSELQ RSVDAKIEVA FTFMQQRSIG
     LAGFYPIGIQ GKTMTSFERQ IPLLMDEIKQ WQKLGNQVVL VINNLQRREG IEKTLHGDAI
     PYKLCESWDF EPNTVHVMQG LLTDGFELPH SHLVVVVEGN IYGQQKRKLR NKPKKGQEIN
     YFTDLSVGDY VVHSMHGIGK YVGLKTIETE GIHRDYIEIA YAGTDRLYLP ASNLDQLQKY
     IGNEGDVPRI HKMGGSDWRK AVTKAQKSID DLADKLVELY AKREITEGFA FLPDQPWQQE
     FEDAFPYEET EDQLQATREI KESMERPTPM DRLLAGDVGF GKTEVAMRAI FKAVVSGKQV
     AVLVPTTVLA QQHYQTFLNR FNPFGVKVDV LNRFRSTAEK KEVLKGVENG SIDILIGTHS
     LLNKKVKFKD LGFLVVDEEQ RFGVAQKEKW KEWASNIDVL TLSATPIPRT LHMSLVGVRE
     MSVISTPPED RLPVQTYVVE YDMNLIADAI KRELARGGQV YFVYNRVASI NHMGELLEQA
     LPDLRYAIAH GQMTGRQIEE IMTDFYEGHY DVLLSTSIIE TGLDIPNANT IIIYDADRLG
     LSQLYQMRGR VGRSRRRAYA YFMYRPDKML SEAAEKRLKA IEEFTELGAG FKLAMRDLEI
     RGAGNLLGSQ QHGNIASVGF GMYVSMLEEA IAKAQNKEVV KEIVPDPAID LEIDAFIDDA
     YIKDSARKIS VYQRMLQIKN KAQLDDLTDE LIDRFGTPTD PVDRLLRVAQ IKEQARLLGI
     KSIVHREGQL IIHWQDDSKM ADWDMGAVRE DLWKKMKFMD TKPASLYISL NGLKGSILTI
     TEAVMKELSK KSKGGL
//
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