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Database: UniProt
Entry: A0A1L7F1U7_9PSEU
LinkDB: A0A1L7F1U7_9PSEU
Original site: A0A1L7F1U7_9PSEU 
ID   A0A1L7F1U7_9PSEU        Unreviewed;      1228 AA.
AC   A0A1L7F1U7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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=UA75_03775 {ECO:0000313|EMBL:APU18787.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU18787.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU18787.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU18787.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-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}.
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DR   EMBL; CP016077; APU18787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7F1U7; -.
DR   STRING; 1612551.UA75_03775; -.
DR   KEGG; acti:UA75_03775; -.
DR   Proteomes; UP000185506; Chromosome.
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   CDD; cd18810; SF2_C_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}.
FT   DOMAIN          661..822
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          840..997
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1228 AA;  132702 MW;  BF653A76370D5A82 CRC64;
     MSAPLAGLLT ALLGSKPFQN LVDAAGSATV ELGGPPALRT LVASALAAEQ GADRPVLLVT
     ATGREAEESA AVLGDLIGRD VVAELPSWET LPHERLSPRA DTVGRRLAVL RRLAHPEQDS
     PDTGPLRVVV TTVRSLIQPL APGLGEVAPV HLRVGEEHDF ASQVERLANL AYSRVDMVEK
     RGEFAVRGGI LDVFPPTCEH PLRVEFWGDE VSEIRAFAVA DQRSLPEPVA ELLAPPCREL
     LITASVRARA EALAADHRSD AQLSEMLDKI AAGIPVEGME ALIPALCEGE LALLPDLLPR
     SAHVLLADPE KIRGRAADLV RTGQEFLEAS WMAAAGGGGA PIDLGASAYR DLDEIEQHTT
     ASGRPWWTLS QLHLDAEDGD AGAEIDLVGG VRALQLDIRP VEAYRGEVER AFADLRAHTA
     AGGAAVLVFP GAGTASRAAE QLRDADIPVR LITDGLPEAP ATGLVTIVRG TMEDGFIAAD
     PLLVVLTEAD LTGGRGGTST RDMRRMPSRR RNAVDPLGLS AGDYVVHDKH GIGRYVEMSQ
     RTVAGATREY LVLEYASSKR GQPGDRLFVP TDQLDEVSRY VGGELPTLNR LGGSDWAKTK
     TRARKAVKEI AAELVQLYAA RQSAPGHAFG PDTPWQRELE DAFPYTETID QLAAIDEVKG
     DMRRPVPMDR VICGDVGYGK TEIAVRAAFK AVQDGKQVVV LVPTTLLAQQ HLNTFSERMR
     SFPVVVKGMS RFTDKMESDE VINGLAAGDV DVVIGTHRLL QTGIRYKDLG LVIVDEEQRF
     GVEHKEHIKA LRTHVDVLTM SATPIPRTLE MSLAGIREMS TILTPPEERH PVLTYVGQYD
     EKQTGAAIRR ELLRDGQVFY VHNRVSSIEK AAKRLRELVP EAKIVIAHGQ MNEDRLEKVI
     QGFWEREFDV LVCTTIVETG LDISNANTLI VERGDMLGLA QLHQLRGRVG RARERGYAYF
     LYPPEKPLTE TAHDRLATIA QNSELGSGMA VAMKDLEIRG AGNILGAEQS GHIAGVGFDL
     YVRLVGEAVA AFRKQAGSDA GGDAVEEPAE VRIDLPVTAH IPHDYVAGER LRLEAYRKIA
     SAAGDSPLDS RERVSADAEA LTAVRAELVD RYGPPPVEVD RLLAVSAFRQ LCRRYGVTEV
     TLQGNAVRFA PMELRDSQIV RLERLYPKAT YKPALRLVSL PRPTEGGAGG RIGAPPLRDE
     ALLSWAEGFL SAMAGVPAPA AASAGNRS
//
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