ID A0A0A2EKI9_PORCN Unreviewed; 1126 AA.
AC A0A0A2EKI9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=HQ35_07840 {ECO:0000313|EMBL:KGN79458.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN79458.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN79458.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL Submitted (AUG-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:KGN79458.1}.
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; JQJD01000050; KGN79458.1; -; Genomic_DNA.
DR RefSeq; WP_036852270.1; NZ_JQJD01000050.1.
DR AlphaFoldDB; A0A0A2EKI9; -.
DR STRING; 36874.HQ34_02570; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000030125; 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; 3.
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:UP000030125}.
FT DOMAIN 571..732
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 752..907
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1126 AA; 127998 MW; 525BD113C8E24D70 CRC64;
MELSRLVSRL SSTKAATALI RLLSEGKQRL IHIDQVHGSA VALLFKGLSE KMSVPILCIA
SDEDEAGYLC SDLTALCEEE SAVSFFPSLY KRGIRFGQTD GANEILRSQL IEALRSGYTP
SFIVTYPEAL MEGIVHEEDF EKSRKIIAKG DVVDRKSLRE RLWEMGFEET DYVYNPGTFA
VRGSLIDIYS YAHERPVRID FFGDEVESIR SFDPESQLSH DSMPEVTILA SFSNQSRSHH
VSLLSLLSEQ SLLYVDQYTL LPISLSQVYD TPPVHKEENI HASLEDMRRC LIEPASLLDE
IRSFTLLSRT VPYGEKWKSV DFGQSPEPLF HKRFDHLSDA ILKHETEGIM TAIMSGQKSQ
IRRLESIFDD QGKGVKFEPI YPTLHKGFID RQARIACYTD HTIFERFHKY TLKSDRIRHN
DAVLTLKEIH KFEHGDYVVH INHGVGVFAG LFTIDRNGKQ QECVRINYKG GDSIYVSIHS
LHHISKYKSK DNDEPPQLSK LGTGAWEKLK ERTKKKVKDI ARDLIKIYAK RLEEKGFAFS
PDSFMQKELE ASFTYEDTPD QELATAQVKE DMERPVPMDR LICGDVGFGK TEIAVRAAFK
AVADSKQVAV LVPTTVLAYQ HYRTFRKRLA DFPCRVEYLS RAKTAKEQSQ LLADLAEGKI
DIIIGTHMLT AKRVKYKDLG LLVIDEEQKF GVSVKEKLRE YRTHIDTLTM TATPIPRTLQ
FSLMGARDMS NIQTPPPNRQ PVRTEQITFD AEIIAEVINY ELARDGQVFF VHNRIHNLND
IAVSIRNAVP GVKIAIGHGQ MDPKELETLL IDFVNHEYDV LLTTTIVENG IDVPNANTII
INDAHRFGLS DLHQLRGRVG RGDRKAYCYL ITPPLDILTQ DAKRRIRGIT TFSDLGSGIH
IAMQDLDIRG AGNLLGAEQS GFIADLGYET YRRILEEAVM ELKDEEFGDI FEEDEKEDTP
QKMPSGSERK SYVYETNIET DVEAYLPPTY VPGDDERIGL YRELDSITQL KAIEEFRYKL
EDRFGKLPVE AEELLKILHL KLLGKSIGVE RISLKRSLLR LQLVSDLNSA YYRSATFATI
LSNASTWSRN LTFNEEGGKR FITVREVKSI TQAYDILTQI SEKTLS
//
