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Database: UniProt
Entry: A0A1V2QE21_9PSEU
LinkDB: A0A1V2QE21_9PSEU
Original site: A0A1V2QE21_9PSEU 
ID   A0A1V2QE21_9PSEU        Unreviewed;      1187 AA.
AC   A0A1V2QE21;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ALI22I_26335 {ECO:0000313|EMBL:ONI86219.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI86219.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI86219.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI86219.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(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:ONI86219.1}.
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DR   EMBL; MTQP01000064; ONI86219.1; -; Genomic_DNA.
DR   RefSeq; WP_077008210.1; NZ_MTQP01000064.1.
DR   AlphaFoldDB; A0A1V2QE21; -.
DR   STRING; 1933778.ALI22I_26335; -.
DR   Proteomes; UP000188617; 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; 4.
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:UP000188617}.
FT   DOMAIN          639..800
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          818..975
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1187 AA;  129314 MW;  01EC67BD9A358F25 CRC64;
     MPQPGPLSGL LTAVLPDKAL RALADSVGVP DLELEGPPAA RPLVAAALAN SAPVLAVTAT
     GREADDLKAV LCDLIGPEQV ALFPSWETLP HERLSPRADT VGARLEVLRR LAHPDGHPLK
     VVITTVRSLI QPMAPGLGDL KPVHLTVGGE HDFEALLVNL TEIAYTRVDM VEKRGEFAVR
     GGILDVFPPT AEHPLRVEFW GDEVSEIRPF AVADQRSLPQ EISEFIAPPC RELLLTESVK
     GKAAVLAEEH AADAHLHELL DKIANGIPAE GMEALIPALC EGELQLLTDV VPEGTHVVLN
     DPEKIRARAQ DLVRTGQEFL EASWMAAAGG GQSPIDLDSS AYHSLADVAR AAKAKNRPWW
     TLSQLTTEGG DVIRLELKHV EAYQGDIDRA FADLRAHTVS GGTAVLVVPG AGTAQRATEQ
     LREADVNVVL RDTLDTAPKP GAVTVVRGAL EDGFSLPELA LVVLTETDLT GGRHGTSTKD
     MRRMPSRRRN AVDPLALKAG DYVVHEQHGI GKYVEMVQRT VAGATREYLV LEYGSSKRGQ
     PGDRLFVPTD QLDEVSRYVG GELPTLNKLG GSDWKNTKAK AKKAVKQIAA ELVQLYAARQ
     AAPGHAFASD TPWQRELEDA FPFTETIDQM AAIDEVKSDM ERTVPMDRVI CGDVGYGKTE
     IAVRAAFKAV QDGKQVVVLV PTTLLAQQHL NTFTERMRAF PVNIKGLSRF TDALEAEQTI
     TGLAEGDVDI VIGTHRLLQK SLRYKDLGLV IVDEEQRFGV EHKEHIKALR THVDVLTMSA
     TPIPRTLEMS LAGIREMSTI LTPPEERHPI LTYVGGYDDK QVGAAIRREL LRDGQVFYVH
     NRVSSIERAA RHIRELVPEA RVITAHGQMN EDKLEKIIQG FWENEYDVLV CTTIVETGLD
     ISNANTLIVE RGDLLGLAQL HQLRGRVGRG RERGYAYFLY PPEAPLTETA HDRLATIAQN
     TELGAGMAVA MKDLEIRGAG NILGAEQSGH IAGVGFDLYV RLVGEAVEAF RKHAGADGEL
     EEDLAEVRVD LPVDAHIPHD YVPGERLRLE AYRKIAAAGD AESLQSVWDE LKDRYGTPPL
     PVERLLAVAR FRQTCRAHGV TEVATQGATI RFAPLELKDS QLVRLRRLFP KALYKQANGT
     VSVPRPTEGA AGGRMGAPQL RDQELLDWCA QFLASLAGTP VSGVTRS
//
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