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Database: UniProt
Entry: A0A087A9W5_9BIFI
LinkDB: A0A087A9W5_9BIFI
Original site: A0A087A9W5_9BIFI 
ID   A0A087A9W5_9BIFI        Unreviewed;      1196 AA.
AC   A0A087A9W5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=BCAL_0822 {ECO:0000313|EMBL:KFI55565.1};
OS   Bifidobacterium callitrichos DSM 23973.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI55565.1, ECO:0000313|Proteomes:UP000029072};
RN   [1] {ECO:0000313|EMBL:KFI55565.1, ECO:0000313|Proteomes:UP000029072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI55565.1,
RC   ECO:0000313|Proteomes:UP000029072};
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:KFI55565.1}.
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DR   EMBL; JGYS01000005; KFI55565.1; -; Genomic_DNA.
DR   RefSeq; WP_052119092.1; NZ_JGYS01000005.1.
DR   AlphaFoldDB; A0A087A9W5; -.
DR   STRING; 1437609.BCAL_0822; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000029072; 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          655..816
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          841..991
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1196 AA;  131693 MW;  92B4FEC1421B43A9 CRC64;
     MAAESGITPE QTLVNGSLAG ILESLNRDPV FGKVVSGGID ETDDIDGSIV VGAPEGVRPA
     IAAAIAQGGA VKPRPVVLVV ASGREAEEMV GSLRSWYDGD PNDIAQLEAW ETLPHERLSP
     RADTVAGRMA VFRRLRHPSD TDPMFGPVRI LVMPVRSLIQ PVVSGLADVE PLVFTRGNDL
     PLDEAAKRLI ENAYTRVDLV MDRGEFAVRG GILDVFPPTA PHPVRIEFFG DEIDQIKEFH
     ASDQRTYGDG LKTIWATPCR ELQLTDKVRA RAKALIGSIP NAEDMLESIA NAIPVEGMES
     LMPALIDDME PVSAMLPGTA VILLSDPEKL RRAADDLTKT ANEFLAASWH VAASGHGAGA
     PISFDQASFL DFEETVRSLN LTGHDVIDLT SFTVDSTRPG HVQIDAKNPA EYRGDESKAA
     AGIEGLIDEG LKVVITAGAK GTLARLKRAI NETGITRFET IRSQALDGFV DRSAGVALLT
     ERDLTGRTSA VGVAKTPKRR RKAIDLMELK AGDYVVHEQH GIGRFVEMRQ RTIGTGANRT
     TREYLVIEYA PSKRGAPPDK LFIPTDQLDQ VSKYIGAETP KLNKLGGSDW AATKAKARKH
     VQEIADDLVK LYSARQRTPG FAFSPDTPWQ KELEDAFPYQ ETPDQLTTID EVKADMEKPR
     PMDRLICGDV GFGKTEIAVR AAFKAIQDGK QVAVLVPTTL LVQQHYETFT ERYEGFPVTV
     RAMSRFQKPK EIQETIDGLA SGGVDIVIGT HKLLNPKIKF KDLGLVIIDE EQRFGVEHKE
     TLKALRTNVD VLSLSATPIP RTLEMAVTGI REMSTLATPP EDRLPVLTYV GAYEDAQVTA
     AIRRELLRGG QVFYVHNRVE DIARVADRIH TLVPEARVSV AHGKMGEKQL DQVIRDFWHR
     DIDVLVCTTI IETGLDISNA NTLIVDHADR FGLSQLHQLR GRVGRGRERA YAYFLYDPSR
     TLTQQSHDRL ATIAQNTALG SGFDVAMKDL ELRGTGNLLG DQQSGHIEGV GFDLYVRMVS
     EAVEAYKEPD KASEPLNVSI DLPVEASIPV DYIDSDKLRL EAYRKLAAAR DEQDLKELAE
     ELTDRYGPLP EEFEMLFGVA RLKFKARKLG ISEILAQSNR LRVGRVDPPE SILMRMSRIY
     KGFQYRPVTH QMIIPTPFAG TLGGKPMPGE QVMDWVSDLL NDLAWTPASS KRQSRL
//
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