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Database: UniProt
Entry: A0A2A2EDG3_9BIFI
LinkDB: A0A2A2EDG3_9BIFI
Original site: A0A2A2EDG3_9BIFI 
ID   A0A2A2EDG3_9BIFI        Unreviewed;      1183 AA.
AC   A0A2A2EDG3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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   ORFNames=B1526_1349 {ECO:0000313|EMBL:PAU67264.1};
OS   Bifidobacterium criceti.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1960969 {ECO:0000313|EMBL:PAU67264.1, ECO:0000313|Proteomes:UP000218399};
RN   [1] {ECO:0000313|EMBL:PAU67264.1, ECO:0000313|Proteomes:UP000218399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71 {ECO:0000313|EMBL:PAU67264.1,
RC   ECO:0000313|Proteomes:UP000218399};
RX   PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA   Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA   Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT   "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT   tree of life.";
RL   ISME J. 11:2834-2847(2017).
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:PAU67264.1}.
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DR   EMBL; MVOH01000015; PAU67264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2EDG3; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000218399; 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}.
FT   DOMAIN          648..809
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          834..984
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1183 AA;  131082 MW;  F6A9DF8EF70298CB CRC64;
     MPADMNEHEL HHGSLAALRA ALDADPTFHD LAHGLADTPD AAGDPSLVIG APDGIRPALA
     AARAALDPIV IVVPSGREAE ELVDDVRSWY DGDPAAVAQL EAWETLPHER LSPRADTVAN
     RMEVFRRLCH PEPGNAMFGP IRILVMPVRS LIQPVVAGIG DVEPLVFTVG EEVALDEASA
     ALVRNAYTRV DLVMDRGEFA VRGGLIDVFP PTLPHPVRIE FFGDEIESIR EFHASDQRTY
     GGTIETVWAT PCRELQLTPE VRERARSLIG RIPNADDMLE SIAQAIPVEG MESLMPALID
     DMCPVSSMLP RRSVVMLCDP EKLRRAVDDL AKTANEFLAT SWHVAASGHG AGAPITFDGA
     NFLAYDEVVS SLAYSERELW KVSGFTVDTS MPGHLQIDAQ TPREFRGDER RTEQGVRTLL
     ADGYAVTLTA AAQGTLHRLT RMLNAVGVTD VTPVRSQARD GFIEHRAKVA LLTERDITGR
     ESAAGGPKTP RKRRKSIDLM ELKPGDFVVH EQHGIGRFIE MRQRTTGSGR NRTTREYLVI
     EYAPGKRNAP PDKLFIPTDQ LDLVSKYIGA EIPKLNKLGG SDWAATKAKA RKHVHEIAQN
     LIKLYSARQR TKGFAFSKDT PWQKELEDAF PYQETADQLT TIDDVKADME KPLPMDRLIC
     GDVGFGKTEI AVRAAFKAVQ DSKQVAVLVP TTLLVQQHYE TFTERFEGFP VNVAAMSRFQ
     STKQINETIK GLADGSVDVV IGTHKLLNPK ITFKDLGLVI IDEEQRFGVE AKEALKAIRT
     NVDVLSLSAT PIPRTLEMAV TGIREMSTLA TPPEDRLPVL TYVGAYEDAQ VTAAIRRELL
     RGGQVFYIHN RVEDIDKKAA KLHELVPEAR IGIAHGKMGR KQLDQVIRDF WHRDIDVLLC
     TTIVETGLDI SNANTLIVDH ADRFGLSQLH QLRGRVGRGR ERAYAYFLYD PGKPMTEQSH
     ERLVTIAQNT ALGSGFDVAM KDLELRGTGN LLGDEQSGHI EGVGFDLYVR MVSEAIEDYK
     EPDRTEPPVV SIDLPIEASI PVDYIDADKL RLEAYRKLAE ARDDDDLEEL REELTDRYGK
     PPQVFTSLFD IARLRERARG LGITEIVGQG GKLRVGGIDP PESVRMRIER IYKGAQYRPL
     THTYMIPTPF EGTLGSGPMS SDDVIKWTEQ LLDDLAWTPK PRT
//
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