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Database: UniProt
Entry: A0A180ELU2_9BACT
LinkDB: A0A180ELU2_9BACT
Original site: A0A180ELU2_9BACT 
ID   A0A180ELU2_9BACT        Unreviewed;      1137 AA.
AC   A0A180ELU2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=A3850_006595 {ECO:0000313|EMBL:OAV44183.1};
OS   Lewinella sp. 4G2.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Lewinella.
OX   NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV44183.1, ECO:0000313|Proteomes:UP000076582};
RN   [1] {ECO:0000313|EMBL:OAV44183.1, ECO:0000313|Proteomes:UP000076582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G2 {ECO:0000313|EMBL:OAV44183.1,
RC   ECO:0000313|Proteomes:UP000076582};
RA   Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT   "Lewinella sp. 4G2 Genome sequencing.";
RL   Submitted (MAY-2016) 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:OAV44183.1}.
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DR   EMBL; LVWJ02000014; OAV44183.1; -; Genomic_DNA.
DR   RefSeq; WP_068215612.1; NZ_LVWJ02000014.1.
DR   AlphaFoldDB; A0A180ELU2; -.
DR   STRING; 1803372.A3850_006595; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000076582; 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:UP000076582}.
FT   DOMAIN          580..741
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          754..916
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1137 AA;  129370 MW;  2673A0F9CA4CCFBF CRC64;
     MPVTDPTQAI LQRYADSPRV AEIVGHVAEN PTARLQLKGL AGALESFLIA GCYRKAGGHT
     LVVATDKEEA AYIQNTISAL LPKKQIRLLP DSFRRPLYFE VLDHTNVLLR TETINYLTHS
     KSKGEIIVTY PEALFEQVVA PAELTSARIE LNKGEDLDVD TIIELLVEYG FSRQEFVYEP
     GQFSIRGGIV DIFSYGNEYP YRIELFDEEI ESIRTFDPLE QLSKDNVEYV SIVPNINTKF
     GRDQKTSIFE VLPENTTIWM RDFQLLIDKL NEAFEKANAF AQNLTVVDDL ELKQLFNDRA
     FIRPGEVLQD VSGKPIVFFT DYKQTMKICK TIDCRAKPQP SFNKNMDLLI RNLLENTSGG
     LKNYIFAGNP KQIERFYSIF KDLEASVRFE PINTAIHAGF IDPEMQAAFY TDHQIFERYH
     RYRLKKGFTK DRALNLRMLR DLSPGDLVVH LDHGVGRFSG LEKLEVAGRT QESVRLIYKN
     NDVLYVSINS LHKLSKFTGK EGALPRLDKI GGDAWRNMKA RTKKKMKDMA GELIKLYAKR
     KASPGHAFPP DGHLQNEMEA NFMYEDTPDQ LKATNATKED MMKDHPMDRL ICGDVGFGKT
     EIALRAAFKA AENGKQVAVL VPTTILALQH YRTFKERLEE FGIVVDYVNR FRTAKEKTQI
     YKDLKEGKID IVIGTHAILS KRVGFKDLGL LVIDEEQKFG VKAKEKLRAM QVNVDTLTLT
     ATPIPRTLQF SLMNARDMSV LRTAPLNRQP IHTEVRQFNE EVIKEAIESE VFRGGQAFFV
     HNRVKSLNDM AVMLRKLCPE VQFAVAHGQM DPKNLEKTLI EFIDRKFEVL ICTNIIETGL
     DISNANTIII NNSHQFGLSD LHQLRGRVGR SNKKAYCYLI APPLSVLTPE ARKRLRTLEE
     HSDLGSGFDI AMKDLDIRGA GNLLGGEQSG FIADIGYETY QRILEEAVRE LKQGEFRDVF
     AEQVHDVSNF VTDVTIETDV EMHIPTLYVE STQERLRLYQ ELDNLSTEEE LEVFAAGLVD
     RFGKIPEEVE ELFDGLRLRW LCRELGFERL VLKNNKLICM FVEDAQSLYY ESPTFGALSE
     IIAKDGVLRG LKLKQSPRRL SLIKENVKSL DIAQKVLNGL VDKLRMVLAD EKSEALA
//
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