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Database: UniProt
Entry: A0A420F5G9_9ACTN
LinkDB: A0A420F5G9_9ACTN
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ID   A0A420F5G9_9ACTN        Unreviewed;      1216 AA.
AC   A0A420F5G9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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:RKF28174.1};
GN   ORFNames=D7I43_07530 {ECO:0000313|EMBL:RKF28174.1};
OS   Micromonospora globbae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF28174.1, ECO:0000313|Proteomes:UP000285744};
RN   [1] {ECO:0000313|EMBL:RKF28174.1, ECO:0000313|Proteomes:UP000285744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF28174.1,
RC   ECO:0000313|Proteomes:UP000285744};
RX   PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA   Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT   "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT   roots of Globba winitii C. H. Wright.";
RL   Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
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:RKF28174.1}.
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DR   EMBL; RAQQ01000004; RKF28174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420F5G9; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000285744; 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:UP000285744}.
FT   DOMAIN          681..842
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          860..1017
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1216 AA;  133228 MW;  43A02EDFE3FF72E1 CRC64;
     MLTGLFSAAL ADPGLARARD LARSGAAQVD GLDITAPPAL RPFAVAAVAA DQGGAGADGG
     PAGGAGRPVL AVTATTREAD DLAAALGSLL PSEQVAVYPS WETLPHERLS PRSDTVGRRL
     AVLRRLAHPE AADAHGRTGP LRVVVAPVRS LLQPQLKGLG DLEPVQLAPG AEADLEEVAR
     RLTDMAYARV DLVTKRGEFA VRGGILDIFP PTDEHPSRIE FWGDEVEEIR TFAVADQRTI
     EQVDRLWAPP CRELLLTPDV RRRAAALAER HPELAEILDK LAEGIPVEGM ESLVPALLGS
     ESLELLLDVM PAGTHVLLCD PERIRTRAHD LVRTSEEFLQ ASWAAAAVGG QAPVDLGAAA
     FRSLAEVRAA AAKLGQPWWT LSPFGLAAEG EAAPERQPWE DEPEEVSVTP DDAIAVTLAA
     QPAPLYHGET ARVVDDLKRW SGEGWSIALV FEGHGPAQRA VEVLRDAGLG ARLTEQVPDA
     PAPGELLVTC GSLSAGFVDE ASRFVLLTGN DITGGRGAST RDMRRMPSRR RNTIDPLELK
     AGDYVVHEQH GIGRYIELVQ RTVNGASREY LVIEYAPSKR GQPGDRLFVP TDQLDQLSRY
     VGGEQPTLHK MGGSDWQKSK ARARKAVREI AAQLIQLYAA RKASKGHSFG PDTPWQRELE
     DAFPWQETPD QLAAIEEVKR DMEQSIPMDR LICGDVGYGK TEIAVRAAFK AVQDGKQVAV
     LVPTTLLVQQ HYNTFAERMS QFPVTIRQLS RFQTPKEAEQ TLAMAADGTA DIVIGTHRLL
     QSATRFKQLG LVIVDEEQRF GVEHKEHLKT MRASVDVLSM SATPIPRTLE MAITGIREMS
     TIATPPEERH PVLTAVGAYD DRQVAAAIHR ELLRDGQVFY VHNRVESIER AARRIRELVP
     EARVAVAHGQ MGEDALEKVM VGFWEKEFDV LVCTTIVESG IDIPNANTLI VERADLLGLA
     QLHQIRGRVG RGRERAYAYF LYPPDKPLTE QAHERLATIA QHTELGAGMY VAMKDLEIRG
     AGNLLGGEQS GHIEGVGFDL YVRMVGEAVQ AFKGEHAEEE TEVKVDLPVD AHLPHDYIGV
     ERLRLEMYRK LAEARDEERL REVVAEMTDR YGEPPAPVQN LVAVARFRLL ARRYGLTDVS
     MQGRHIRFSP LPLPDSKQMR LKRYHPDAVY KQATDQVSVP RPSTRRVGGE PLRDQALLEW
     CAQLLTDVLG EPALVG
//
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