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Database: UniProt
Entry: A0A2M9HDV0_9BIFI
LinkDB: A0A2M9HDV0_9BIFI
Original site: A0A2M9HDV0_9BIFI 
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}.
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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
//
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