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Database: UniProt
Entry: A0A086BMX3_9FLAO
LinkDB: A0A086BMX3_9FLAO
Original site: A0A086BMX3_9FLAO 
ID   A0A086BMX3_9FLAO        Unreviewed;      1120 AA.
AC   A0A086BMX3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=IQ37_00455 {ECO:0000313|EMBL:KFF30287.1};
OS   Chryseobacterium piperi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=558152 {ECO:0000313|EMBL:KFF30287.1, ECO:0000313|Proteomes:UP000028709};
RN   [1] {ECO:0000313|EMBL:KFF30287.1, ECO:0000313|Proteomes:UP000028709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTM {ECO:0000313|EMBL:KFF30287.1,
RC   ECO:0000313|Proteomes:UP000028709};
RA   Pipes S.E., Stropko S.J., Newman J.D.;
RT   "Genome of Chryseobacterium piperi CTM.";
RL   Submitted (JUL-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:KFF30287.1}.
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DR   EMBL; JPRJ01000001; KFF30287.1; -; Genomic_DNA.
DR   RefSeq; WP_034680497.1; NZ_JPRJ01000001.1.
DR   AlphaFoldDB; A0A086BMX3; -.
DR   STRING; 558152.IQ37_00455; -.
DR   KEGG; cpip:CJF12_12860; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000028709; 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:UP000028709}.
FT   DOMAIN          572..733
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          742..908
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1120 AA;  127942 MW;  3572BA36ACA1E340 CRC64;
     MQLKAINEKF LPDLLQKEFG KEIFTQLEAH QHISVKGNAG SSSSVFVAEL FLTQKKNILY
     LIDDKEEALY ANTEIEDLLG KDKVLFFPAT HLEPYQVEKT QNANLVLRTE VLNKLNSSKS
     PKVIVAYAGA LSEKVLKKED FKAISHHIKV GDQLDFDFVD ELLSHYQFQQ ADFVSEPGEF
     SVRGGIVDVF SYSYEKPYRI TFFGNEVESI KTFDIETQLS IDKIKEFQLV SNMNFSVSAS
     RVSLLQLLPK ESFVVSKNAV VGLQKIKSFY EKALEKYETL SKDIAHRTPQ ELFISDQEFL
     FDYKKFKTID FSSVGIEELE TFNITIEQTA QPSFHKNFEL LIQDLEEKQS EGFDTWISFS
     TEKQKERLES IFEELEHEAF FKSFKSELHE GFVDYNHKLL VYTDHQIFDR YQRYKAKNTF
     AKSEQLTLKD LMSLKVGDYI AHIDHGIGKF MGLVKVNNDG KIQECFKLTY KNGDLLYVSI
     HSLHKISKYN GPDGKEIVLS KLGSPAWKSL KQKTKAKVKQ IAFDLIKLYA QRKTAQGFAF
     TPDSYLQNEL EASFIYEDTP DQEKATIDVK KDMESSTVMD RLVCGDVGFG KTEVAIRAAF
     KAATDGKQVA VLVPTTILAF QHYRSFKERL KDFPVNVSYV NRFRTAKQKS EALEGLKNGK
     VDIIIGTHQL ASASVKFKDL GLLIIDEEHK FGVSVKDKLK TLKSNVDTLT LTATPIPRTL
     QFSLMAARDL SVIKTPPPNR QPVDTQIVGF NEEIIRDAVS YELQRDGQVY FINNRIENLK
     DIAGLIQRLV PDARVITGHG QMEGKQLEKN VLDFMEGKYD VLVSTTIVES GVDVPNANTI
     FINDAQRFGM ADLHQMRGRV GRSNRKAFCY LITPPYDMMT SDARKRLEAI EQFSDLGSGF
     QIAMKDLEIR GAGDLLGAEQ SGFINEMGFE TYQKLMQEAL EELKDDEDFE NLFDNEEDRQ
     KLFKSVKDVN IDTDLELMLP DFYISNTEER LSLYQKIAEI DNEKDLQKFE NELIDRFGDL
     PKEAVNLLKS VSLKWLAADI GFEKIVMKNG VFLGYFPSNP QDKFYQTDKF KHIISYLTQN
     PSEAQLKEKI GKEGNNLMMR KDKVKNVDEV NLLLKSILAL
//
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