ID A0A087BCG7_9BIFI Unreviewed; 1201 AA.
AC A0A087BCG7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=BMAGN_0588 {ECO:0000313|EMBL:KFI68717.1};
OS Bifidobacterium magnum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI68717.1, ECO:0000313|Proteomes:UP000029052};
RN [1] {ECO:0000313|EMBL:KFI68717.1, ECO:0000313|Proteomes:UP000029052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI68717.1,
RC ECO:0000313|Proteomes:UP000029052};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI68717.1}.
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DR EMBL; JGZB01000003; KFI68717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BCG7; -.
DR STRING; 1692.BMAGN_0588; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000029052; 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}; 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:UP000029052}.
FT DOMAIN 665..826
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 844..1001
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 133169 MW; A30693BD55063C11 CRC64;
MTPEGEPTTT SAQPATSARS TETFQPKPCG ELADLLTDLE TDTALRDLVH GDITPDTAAS
AANLTVGAPE GIRPALAAAT AANRTVVVVV PSSRQSEEFV EAARSWYDGD PHDIAQLDAW
ETLPHERLSP RADTVANRMA VFRRLAHPQE GSDLFSPIRV LVMPVRSLIQ PVVAGIGDIT
PLVFERGESM DMFAAVAALV ENAYTRADLV MDRGEFAVRG GIIDVFPPTL PHPVRIEFFG
DEVDSIRAFH ASDQRTFGDE IARVWATPCR EMQMTDEVRN RARALIGSIA NADDMLESIA
NGVPVEGMES LVPALVDHMQ SVASLLPRHS VVMLCDPEKL RRSVDDLVTT AQEFLATSWH
VAASGHATSA PISFDQASFY DYEQTVEALD NSAHDVWNVT AFPVDSSLAG HVQIDAVPAE
NFRADEHKTA RGFEQMVSDG YKIVVTAVAH GILSRLSRML KTAGISGFDA IQSQMTDGFV
DKSARLAVLT ERDITGRSGA AAHQKTPKKR RKSIDLMELK PGDYVVHEQH GVGRFLEMRQ
RTTGKGVNET TREYLVIEYA PSKRNAPNDK LFIPTDQLDL VSKYIGSDAP KLNKLGGSDW
ATTKAKAKKH VHEVAEDLIK LYSARQRTKG FAFSPDTPWQ KELEDAFPYQ ETADQLTTID
DVKADMEKPL PMDRLICGDV GFGKTEIAVR AAFKAVQDGK QVVVLVPTTL LVQQHYETFT
ERFEGFPVVV KPMSRFQTTK EINETIRGLE DGTVDVVIGT HKLLNPKIKF KDLGLVIIDE
EQRFGVEHKE TLKALRTNVD VLSLSATPIP RTLEMAVTGI REMSTLATPP EDRLPVLTYV
GPYEDSQVVA AVRREMMRGG QVFYLHNRVE DISRTAAKLQ ELLPEAKIAI AHGKMGKKQL
DQVIRDFWHR DIDILVTTTI IETGLDISNA NTLIVDHADR FGLSQLHQLR GRVGRGHERA
YAYFLYDPTK PMTQQSHDRL VTIAQNTALG SGFDVAMKDL ELRGTGNLLG DEQSGHIEGV
GFDLYVRMVS EAIEEYKEPD RVEPVAVSID LPIEASIPVD YIDSDKLRLE VYRKLASARN
EDDLTQLQEE LTDRYGEPPE VFHALFDIAR LRERARLMGI TEIFAQGKTM RVAKVKPADS
VQIRISRIYR GAQYRPVTQT YVIPTPFAGS LGGKPMSSHE IIRWTQQLLD DLAWKPGAKQ
Q
//
