ID A0A261Q7U6_9BACT Unreviewed; 1134 AA.
AC A0A261Q7U6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:OZI08183.1};
GN ORFNames=BWI93_10735 {ECO:0000313|EMBL:OZI08183.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI08183.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI08183.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI08183.1,
RC ECO:0000313|Proteomes:UP000215802};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Draft genome of Siphonobacter sp. BAB-5385.";
RL Submitted (JUN-2017) 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:OZI08183.1}.
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; NMPS01000103; OZI08183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261Q7U6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000215802; 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:UP000215802}.
FT DOMAIN 585..746
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 767..921
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1134 AA; 129260 MW; 41AD9A2DC202957C CRC64;
MLIKDLLTLY RNDAFIRLMG ERLQSKQPDD YHLQIKGITG SLDAVLVAAH YQNHPAASLV
VLSDKEEAAY FYNDLQNLLG EDHVLLFPMS YKKPYEYEEI DNANVLMRSE VLNRINDKSN
KTLIVTYPEA LSEKVINRRS LVKNTFTISV GEKLDTEFLT EFLLSQDFEG TDFVYEAGQF
AVRGGIIDVY SYANEFPYRI DLFGDEVESI RTFDPDTQLS KESVSRINII PDVQTKLIQE
SRDSFLSFFP ETTRIWFKDV ELTLELIGIC FENVEKSFQS ILERSGGIKV IHEPSQLFET
RRGFLNQIKE FPSVEFGKRF YFKPADGSTL PASELRINYA SKPQPSFNKD FNRLIETLHE
QQYRGYTNVV VSETQKQLER LSSIVGEAND SVRFQGVNVS LREGFIDDTL KIACFTDHQI
FDRFYRYRIK DKFSKSKALT LRELKTLAPG DYVTHIDHGI GRFAGLVKID IGDHQQEGIR
LVFRDNDTVV VNVQSLHKIA KYTGKEGTQP SLSKLGSPEW ENKKAKVRRQ VKDIAAELIE
LYAKRRLAPG YPYSRDTFLQ VELESSFLYE DTPDQAKATS AVKEDMEKPH PMDRLVCGDV
GFGKTEVAMR AAFKAASDNK QVAVLVPTTV LAMQHYRTFR DRFERFPVKV EYINRFKTTQ
QIKETLKRVE SGETSILIGT HRIVGKDVKF KALGLLIVDE EQKFGVKVKD RLKEFKLNVD
VLTLTATPIP RTLHFSLMGA RDLSVIATPP PNRQPVTTEL MVFDELKIRD AVMREMKRGG
QVFFVHNRIG DLESLGNMIL KLVPDAKIGI AHGQMDGDRL EKVMMKFIEG EYDVLISTNI
IEAGLDIPNA NTILINQAQL FGLSDLHQMR GRVGRSNKKA YCYLLTPALS LLSTDSRKRL
QALEEFTELG DGFKVAMRDL DIRGAGNLLG AEQSGFINDL GFETYHKILD ETVRELKETQ
FKDLFADELA RAANNLRVEC QIETDLPVLI PENYVSNISE RLSLYNRLDH MKNEAELQAF
LSEVTDRFGP APEEVRDLVD LVRVRWKAEQ IGFEKLTLKQ NTLKGTFVSG ENEAYFQSER
FGKVLDFVKA NPRKVVLKDV KGKLQLQAEN LRQVTELDQL LGQMVSSGEK VSVA
//
