ID R6FR17_9BACE Unreviewed; 1131 AA.
AC R6FR17;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=BN744_02643 {ECO:0000313|EMBL:CDB11436.1};
OS Bacteroides sp. CAG:633.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262744 {ECO:0000313|EMBL:CDB11436.1, ECO:0000313|Proteomes:UP000018121};
RN [1] {ECO:0000313|EMBL:CDB11436.1, ECO:0000313|Proteomes:UP000018121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:633 {ECO:0000313|Proteomes:UP000018121};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDB11436.1}.
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DR EMBL; CBDA010000272; CDB11436.1; -; Genomic_DNA.
DR AlphaFoldDB; R6FR17; -.
DR Proteomes; UP000018121; 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; 3.40.50.300; 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:UP000018121}.
FT DOMAIN 578..739
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..914
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1131 AA; 127807 MW; 9A5BD94FAF984C36 CRC64;
MTITELQQLY AAHPNVEGMI RLLKDSSVRH LYCNGLCASS ASLFASTIVQ QAECPFVFVL
GDLEEAGYFY HDLVQILGSD DVLFFPSSFR RAIKYGQKDA ANEILRTEVL SRLEKDGKYV
CVVTYPDALA EKVVSRKELD DKTLKLHVGE KVDMDFVREV LRNYGFEYVD YVYEPGQYAV
RGSIIDVFSF SSEYPFRIDF FGDEVESIRT FEVETQLSKE KKESIVIVPD LSHNLEDGGN
GGMVSLLDFL QADTVLAMRD FLWLRERIQN VHDESLTPQA IAAREAEENG AIRLDGKLID
GGEFTVRALD FRRMEFGNKP TGTPNAVLNF STSAQPIFHK NFDLVAQSFK EYIANGYTIY
ICSDSTRQTD RIRAIFEDRG DNISFTAVER TLHEGFADND LHLCVFTDHQ LFDRFHKYNL
KSDKARGGKV ALSLKELNQF TPGDYVVHTD HGVGRFAGLV RIPNGDTTQE VMKLVYQNDD
VVFVSIHSLH KVSKYKGKEG EAPRLNKLGT GAWEKLKDRT KTKIKDIARD LIKLYSQRRE
EKGFQFSPDS FLQRELEASF LYEDTPDQSK ATAEVKADME SARPMDRLVC GDVGFGKTEV
AIRAAFKAVA DNKQVAVLVP TTVLAYQHFQ TFKERLKELP CKVEYLSRAR TSAQTRAVIK
GLAAGEVNIL IGTHRILGKD VKFKDLGLLI IDEEQKFGVS VKEKLRQLKV NVDTLTMTAT
PIPRTLQFSL MGARDLSVIQ TPPPNRYPVQ TEVHTFNEEV ITDAINFEMS RNGQVFFVNN
RISNLVELKA MIERNIPDCR ICIGHGQMEP AELEKIILDF VNYDYDVLIA TTIIESGIDI
PNANTIIINQ AQNFGLSDLH QMRGRVGRSN KKAFCYLLAP PLSSLTPEAK RRLQAIENFS
DLGSGIHIAM QDLDIRGAGN MLGAEQSGFI ADLGYETYQK ILTEAVRELK NEEFSDLMAE
EQQAADGSGQ ITGEQFVDEC QVESDLELLL PADYVTGSSE RMLLYRELDG LVLDKDVEAF
RSRLEDRFGP IPPETQELLR IVPLRRLAAR LGAEKVFLKG GRMTLFFVSI PDSPYYQSQA
FGKVISYMMK YTRRCDLREQ NGKRSMQVKD VTSVEEAVHV LQEMFAMQVE E
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