ID A1A142_BIFAA Unreviewed; 1188 AA.
AC A1A142;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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:BAF39425.1};
GN OrderedLocusNames=BAD_0644 {ECO:0000313|EMBL:BAF39425.1};
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39425.1, ECO:0000313|Proteomes:UP000008702};
RN [1] {ECO:0000313|EMBL:BAF39425.1, ECO:0000313|Proteomes:UP000008702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC {ECO:0000313|Proteomes:UP000008702};
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; AP009256; BAF39425.1; -; Genomic_DNA.
DR RefSeq; WP_011743074.1; NC_008618.1.
DR AlphaFoldDB; A1A142; -.
DR STRING; 367928.BAD_0644; -.
DR PaxDb; 1680-BADO_0688; -.
DR KEGG; bad:BAD_0644; -.
DR HOGENOM; CLU_005122_1_3_11; -.
DR Proteomes; UP000008702; Chromosome.
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:UP000008702}.
FT DOMAIN 653..814
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 839..989
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1188 AA; 131302 MW; 8A64BF127346E404 CRC64;
MAAEPTSPAQ PPQLPTAGSL AGILDVLETD DDFRALIAGE IEEPESDIDP SITVGVPDGL
RPALAAGAAG KQPVVLVVAS SREAEETVES IRSWYDGDPN DVAQLEAWET LPHERLSPRA
DTVASRMAVF RRLKHPEEGS TLFGPIRILV MPVRSLIQPV VAGLGDVEPL VFSQGEELLL
DEASRKLVEN AYTRVDLVMD RGEFAVRGGI IDVFPPTLPH PVRIEFFGDE IDTIREFHAS
DQRTYGKDIS TVWATPCREL QLTDQIRQRA KSLIGSIPNA EDMLGSIANA IPVEGMESLL
PALVDDMEPV QGMLPKHALV MLSDPEKLRR AADDLAKTAN EFLAASWHVA ASGHGAGAPI
TFDQANFYDF EETISALVFS KHDVWKLTSF GVDATREGHI QLDATKPGEY RGDENKAASG
IEGLLDAGYA VTITAAAQGT LTRLKRAINE TGIANFDCVR SHAIDGFVDD AAKIALLTER
DLTGRTSAAG QAKTPKRRRK AIDLMELKTG DYVVHEQHGI GRFVEMRQRT IGKGENQTTR
EYLVIEYAPS KRGAPADKLF IPTDQLDQVS KYIGAETPKL NKLGGSDWAA TKAKARKHVH
EIAEDLVKLY SARQRTKGYA FSKDTPWQKE LEDAFPYQET ADQLTTIDEV KSDMEKPIPM
DRLICGDVGF GKTEIAVRAA FKAVQDSKQV AVLVPTTLLV QQHFETFTER FEGFPVNVAA
MSRFQTAKEI NETIKGLEDG SVDVVIGTHK LLNPKIKFKD LGLVIIDEEQ RFGVEHKETL
KALRTNVDVL SLSATPIPRT LEMAVTGIRE MSTLATPPED RLPVLTYVGA YEDAQVTAAI
RRELLRGGQV FYVHNRVQDI SSVAAKIHEL VPESHVGIAH GKMGEKQLDG VIRDFWHRDI
DVLVCTTIIE TGLDISNANT LIVDHADRFG LSQLHQLRGR VGRGRERAYA YFLYDPTKPM
TQQSHDRLAT IAQNTALGSG FDVAMKDLEL RGTGNLLGDE QSGHIEGVGF DLYVRMVSEA
VEQYKEPERK ESVAVTIDLP IEASIPVDYI DSDKLRLEAY QKLASARTED DLDELRDELT
DRYGKPPVDF EALFDVARLR FKARKLGISE IIAQGRNVRV SKFEPRESVQ MRMARIYKGI
QYRPLTKTYL VPAPFAGSLG SKPMSSDEVV GWTSQLLDDL DWKPTPRQ
//
