ID A0A1S2LPQ9_9BACI Unreviewed; 1174 AA.
AC A0A1S2LPQ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BKP35_06830 {ECO:0000313|EMBL:OIJ14461.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ14461.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ14461.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ14461.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) 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:OIJ14461.1}.
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DR EMBL; MLQQ01000007; OIJ14461.1; -; Genomic_DNA.
DR RefSeq; WP_071312629.1; NZ_MLQQ01000007.1.
DR AlphaFoldDB; A0A1S2LPQ9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000180098; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000180098}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 820..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1174 AA; 133869 MW; E9581C7628BC3B44 CRC64;
MLGLKKFFLQ DDDVRAVLDG IEAELSEQMI AGLTGSARTL LLASVFEQTK RPQLIVTNNL
FQAQKLYDDL IGLIGGQSVY LYPVNELISS EIAVASPEMR GQRIEVLNYW SEMQTGIVIT
PIAGLRRLLP PKEIWRQCQL HFKVGDEINV EEKLDKLVQA GFQRSEMVSS PGQFSLRGGI
IDIYPLTEEM PLRIELFDTE VDSIRFFDVD TQRSQKQLNE INIGPAQEVI MYEEHFRRGA
ENLKQGLSSS LAKINDSKVK ESLLEQISYE IELLSGKNSF EGMYKYMSLY YDEVTTLIDY
LPNNGVVFID EISRVQEMGV SLDKEEAEWQ TTLLGQGAVI SDLKMSKHLE EIIEETKVPF
LYFSLFLRHV PNTSPKNIIN FNCKTMQNFH GQLNLLKNEV ERWTKVQYKV AIVAQDKERA
KRIDHILEDY KIEALVVDSD TDLITGSCQI LIGQLSGGFE LPLQKLIVIT EEEVFTKKAK
RPKRKQKLSN AERIKNYSEL KVGDLVVHIN HGIGKYLGIK TLEINGIHKD YMHITYAGND
KLYVPVEQID QVQKYVGSED KEPKIYALGG SDWKKVKKKV QSSVEDIADD LIKLYAEREA
SVGYAFSEDG PEQREFETSF PYEETEDQIR CIEEIKEDME RERPMDRLLC GDVGYGKTEV
AIRAAFKAIM DGKQVAFLVP TTILAQQHYE TIRERFAEHP INIGLLSRFR TRKEQNETLK
GLKSGVVDIA IGTHRILSKD VQYKDLGLLI IDEEQRFGVT HKEKIKQLKA NVDVLTLTAT
PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEFNEAL VREAIERELS RGGQVYFLYN
RVEEIAQMAD RISMLVPDAK ISFAHGKMNE TELETVIIDF LEGNSDVLVT TTIIETGVDI
PNVNTLIVYN ADKMGLSQLY QLRGRVGRSN RVAYSYFTYQ KDKVLTEVAE KRLQAIKEFT
ELGSGFKIAM RDLSIRGAGN LLGAQQHGFI ASVGFDMYSQ MLKDAIEERK GNKTEQVKKN
EVEIDLNVDA YIPESYIVDS KQKIDMYKRF KSIQSEDDII DLQSEMIDRF GDFPKEVNYL
FKISAIKLLS SEEGIQSITE NNHQCSILLA EKESQTIDGM KLFELISKMS REIGVGTAGN
QIKITIKTKK FEPMKFLEVI EEILSKLWTV KKDT
//
