ID A0A2P8CIQ4_9BACT Unreviewed; 1121 AA.
AC A0A2P8CIQ4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CLV93_102613 {ECO:0000313|EMBL:PSK84822.1};
OS Prolixibacter denitrificans.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Prolixibacter.
OX NCBI_TaxID=1541063 {ECO:0000313|EMBL:PSK84822.1, ECO:0000313|Proteomes:UP000240621};
RN [1] {ECO:0000313|EMBL:PSK84822.1, ECO:0000313|Proteomes:UP000240621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27267 {ECO:0000313|EMBL:PSK84822.1,
RC ECO:0000313|Proteomes:UP000240621};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PSK84822.1}.
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DR EMBL; PYGC01000002; PSK84822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8CIQ4; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000240621; 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; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PSK84822.1};
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 564..725
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 745..900
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1121 AA; 127852 MW; 6360C2E485719754 CRC64;
MKREQLIDFY AQHPGVQALA GQLATPFGQK LHAKGLNGSA PSVAMAALFQ KKPFGALMLL
SDREEAAYFY DDLQTLGLEE HVLFFPSSYK RSVQYEKIES ENIILRTDVL NQLVEAEERF
IVVSYPEAVM EKVISGKGLE KHTLTVRVGE KLSISFVNEV LFEYGFERVD FVYEPGQYSI
RGSIVDIFSF AHEDPYRIDF FGDEVETIRT FDIENQISKD ALKKISIIPN IQEGLQEEER
ISFFEFLKDD TLLITDDLRF SAERMTEMYK SAREKNLETD LLVDDLVISG NALLERAEAL
TCIEIGPKAH FKSEEIPFHI KPQPVFNKNF NLLGDNLREN SQLGYINIIL SSSEKQVERL
HAIFEDKGDP QEFDHLPFAL KEGFIDHDLK LCCYTDHQIF ERYHRFKLRS KKSARQAITL
KELAKLHPGD YVVHVDHGIG KFAGLVRTEE DGKTQEAIRL IYRDNDSLLV SIHSLHRISK
YKGKDGTEPK INKLGTAAWQ NLKNKTKKKV KDIARELIGL YAHRKAEDGF AFARDSYLQQ
ELEASFIYED TPDQLKATVA TKEDMEKTMP MDRLICGDVG FGKTEVAIRA AFKAVTDSKQ
VAVLVPTTIL AFQHFKTFNE RLSDFPCRIE YISRLRKPAE VRHILKEVAE GKVDIVIGTH
RLVGKDVKFK DLGLLVIDEE QKFGVSVKEK LKHLKVNVDT LTLTATPIPR TLQFSLMGAR
DLSIINTPPP NRFPINTEVH GFNEDIIREA ITYEVARGGQ VFFINNRVQN IYEVEALIKR
IVPGVRTVVG HGQMEGSQLE KVMLDFINGE FDVLIATTII ESGLDIPNAN TIIINQAHNF
GLSELHQLRG RVGRSNKKAF CYLLAPPMTS MTPEARRRLQ AIEEFSDLGS GFSIAMQDLD
IRGAGNLLGA EQSGFIADIG FETYHRILNE AIQELKHEEF QQLYKEEESR EANEAFLNLR
FVNDCQVDTD LELLFPESYI SSISERMLLY RELDNIEDND ALEQFRAQLI DRFGKLPDST
IELLEVVRLR WTAIELNLEK IILKNKKMIC YFPSDQQSPF YQTGLFGNIL QWLQTHPKKC
RIKESKGKLS IIFSEVTSIQ HAVTLLSEIA ESVIPERVKA N
//
