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Database: UniProt
Entry: A0A2U1JN56_9FLAO
LinkDB: A0A2U1JN56_9FLAO
Original site: A0A2U1JN56_9FLAO 
ID   A0A2U1JN56_9FLAO        Unreviewed;      1119 AA.
AC   A0A2U1JN56;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:PWA06562.1};
GN   ORFNames=DB895_03870 {ECO:0000313|EMBL:PWA06562.1};
OS   Flavobacterium psychrotolerans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2169410 {ECO:0000313|EMBL:PWA06562.1, ECO:0000313|Proteomes:UP000245449};
RN   [1] {ECO:0000313|EMBL:PWA06562.1, ECO:0000313|Proteomes:UP000245449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB1R5 {ECO:0000313|EMBL:PWA06562.1,
RC   ECO:0000313|Proteomes:UP000245449};
RA   Liu Q., Xin Y.-H.;
RT   "Flavobacterium sp. nov., isolated from glacier ice.";
RL   Submitted (APR-2018) 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:PWA06562.1}.
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DR   EMBL; QCZI01000003; PWA06562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1JN56; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000245449; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:UP000245449}.
FT   DOMAIN          575..736
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          745..911
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1119 AA;  128350 MW;  A602E0070AB17373 CRC64;
     MSKANLLNTY ANSPKVKQII DCLQTPEQKI HLNGLIGSSL SFVIQSLFTK TEKPFLVLLN
     DKEEAAYYLN DLEQLIGEQD VLFYPGSYRR PYQIEDTDNA NVLLRAEVLN RINSRKKPAV
     IVSYPEALFE KVVTKKELDK NTLKVAVGDK ISIEFINEVL FEYEFKRVDF ITEPGEFSVR
     GGIIDVFSFS NDNPYRIEFF GNEVDSIRSF DVETQLSIEK QNKITIIPNV ENKFFQENRE
     SFLEYISNKT ILCIQNTELL LSKLDKLFGK ADEIFKNLNA TVSHVEPGQL FVNQTEFVKK
     SLDFSILELS SKPIYRIQKT FEFHIQPQPS FNKQFDLLLN NLNDNHFNGY KNYLFCSNDA
     QAKRFHDIFE TLDEANHESI RKQYNTITLP LYQGFIDEEN QIACYTDHQI FERYHKFSIK
     NNYSKKQTIT LKELTTLSVG DYVTHIDHGI GRFGGLQKIQ VEGKTQEAIK LVYADNDIVY
     VSIHSLYKIS KYNGKDGTPP KIYKLGSNAW KVLKQKTKAR VKHIAFNLIQ LYAKRRLEKG
     FRYAPDSYLQ AELESSFIYE DTPDQTKSTA EVKSDMESDR PMDRLVCGDV GFGKTEVAIR
     AAFKAVDNGK QVAVLVPTTI LAYQHFRTFT ERLKEMPVSV GYLNRFRTAK QKAETLKQLA
     EGKLDIVIGT HQLVNKNVVF KDLGLLIVDE EQKFGVNVKD KLKTIAANVD TLTLTATPIP
     RTLQFSLMAA RDLSVITTPP PNRYPIETNV VGFSEELIRD AISYEIQRNG QVFFINNRIE
     NIKEVAGMIQ RLVPDARVGI GHGQMEGSKL EELMLAFMNG EFDVLVATTI IESGLDVPNA
     NTIFINNANN FGLSDLHQMR GRVGRSNKKA FCYFICPPYS AMTDDARKRI QALEQFSELG
     SGFNIAMKDL EIRGAGDLLG GEQSGFINEI GFDTYQKIMN EAIEELKENE FKELYADEEK
     PEKEYVKDLQ IDTDFELLFP DEYINNITER LNLYNELSLI KDEETLLAYE TKLIDRFGLL
     PKQAISLLNS IKIKWIATKL GVEKLVMKQG KMIYYFVSDQ QSNYYTSPQF HKVLQFVQKQ
     PQLCKMKEKQ TPNGLRLLLT FEHVKSIRKA LELMELMQG
//
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