ID A0A2M9HDV0_9BIFI Unreviewed; 1210 AA.
AC A0A2M9HDV0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:PJM74990.1};
GN ORFNames=CSQ87_07115 {ECO:0000313|EMBL:PJM74990.1};
OS Bifidobacterium simiarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2045441 {ECO:0000313|EMBL:PJM74990.1, ECO:0000313|Proteomes:UP000231451};
RN [1] {ECO:0000313|EMBL:PJM74990.1, ECO:0000313|Proteomes:UP000231451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRI7 {ECO:0000313|Proteomes:UP000231451};
RA Mattarelli P., Modesto M., Puglisi E., Morelli L., Spezio C., Bonetti A.,
RA Sandri C.;
RT "Draft genome sequences of strains TRE 1, TRE 9, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (OCT-2017) 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:PJM74990.1}.
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; PEBK01000006; PJM74990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9HDV0; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000231451; 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:UP000231451}.
FT DOMAIN 670..831
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 856..1006
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1210 AA; 132445 MW; 1FE35730485D7D00 CRC64;
MADNSIADGR VRERGSADVE DVTLGDIRRR LSRDPAFASL LDGSAVRSSS TTEPQLTVGA
VEGIRPALAA ALAGDADTDR TETAGASGGM VTLVVPSGRD AEEIAGALAS WYDGDPADIA
VLKAWETLPH ERLSPRSDTV ASRMAVFRRL AHPEAGSAMF GPIRLLVMPI RSLIQPVAAG
LGDVEPLVLR VGEEIALDVA ASRLVEGAYT RTELVMDRGE FAVRGGILDV FPPTAAHPVR
IEFFGDEIDS IHEFHASDQR TYGDGLDGIW ATPCRELQFT DAVRERARSL IGRIPNADDM
LESIAGAIAV EGMESLMPAL VDDLVSVGSL LPKDARILLC DPQRLQRAAE DLNKTADEFL
AASWHVAASG HGAGAPISFD RASFLDYDDA VRALVASGRT VWNLTSFGVD PERDGHVQLG
AVPPEEFRGS EERASRGIDG LLDRGLNVTV TAAAKGTLSR LRRVLETATV TGVHYALSRA
ADGFVDESAG VALLTERDLT GRAGVAAQAK TPKRRRKAID LMELKEGDYI VHEQHGIGRF
VAMQQRMVGA GAAKSKREYL VVEYAPSKRG APPDRLYIPT DQLDKVSKYI GADVPKLNKL
GGSDWAATKA KARKHVKEIA QDLVRLYSAR QSAKGFAFSP DTPWQKELED AFPYQETADQ
LTTIDEVKAD MEKPVPMDRL ICGDVGFGKT EIAVRAAFKA VQDSKQVAVL VPTTLLVQQH
YETFTERFEG FPVNVAAMSR FQTTKQINET IKALADGTVD VVIGTHKLLN PKIKFKDLGL
VIIDEEQRFG VEHKETLKAL RTNVDVLSLS ATPIPRTLEM AITGIREMST LATPPEDRLP
VLTYVGAYED AQVTAAIRRE LLRGGQVFYV HNRVSGIDKL AAHLKELVPE ANIGVAHGKM
GEKQLDSVIR DFWHRDIDVL LCTTIIETGL DISNANTLIV DHADKFGLSQ LHQLRGRVGR
GRERAYAYFL YDPTKTMTQT AHDRLATIAQ NTALGSGYDV AMKDLELRGT GNLLGGEQSG
HIEGVGFDLY VRMVSEAVEQ VKEPDRQAEP VSVTIDIPVN ASIPERYIDS DKLRLEAYRK
LAAARTEDDF REIREELTDR YGRPPEQLDM LFEVARLRAR ARAIGLSELV MQGRNLRVGR
FDPRESVQMR IARIYKGVQY RPVTHQYLIP TPFQGSMGSG PMSGEEVLAW VNQLLDDLTW
TPKPRKGHAG
//