ID A0A1X1RPX8_MYCCE Unreviewed; 1207 AA.
AC A0A1X1RPX8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:PIB77995.1};
GN ORFNames=AWB95_14655 {ECO:0000313|EMBL:ORV11077.1}, CQY23_16090
GN {ECO:0000313|EMBL:PIB77995.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV11077.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV11077.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV11077.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PIB77995.1, ECO:0000313|Proteomes:UP000230971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12882 {ECO:0000313|EMBL:PIB77995.1,
RC ECO:0000313|Proteomes:UP000230971};
RX PubMed=29030295; DOI=10.1016/j.meegid.2017.10.013;
RA Tortoli E., Fedrizzi T., Meehan C.J., Trovato A., Grottola A.,
RA Giacobazzi E., Serpini G.F., Tagliazucchi S., Fabio A., Bettua C.,
RA Bertorelli R., Frascaro F., De Sanctis V., Pecorari M., Jousson O.,
RA Segata N., Cirillo D.M.;
RT "The new phylogeny of the genus Mycobacterium: The old and the news.";
RL Infect. Genet. Evol. 56:19-25(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:ORV11077.1}.
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DR EMBL; LQOM01000031; ORV11077.1; -; Genomic_DNA.
DR EMBL; PDKV01000021; PIB77995.1; -; Genomic_DNA.
DR STRING; 28045.AWB95_14655; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR Proteomes; UP000230971; 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 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 651..812
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 830..987
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1207 AA; 130199 MW; 8E05537745EFF2F5 CRC64;
MTETPIAGLV ELALSAPTFQ QLIEQSADRP AELALVGPAS SRLFVAAALA RQGPLLVVTA
TGREADDLTA ELRGVFGDAA ATFPSWETLP HERLSPGVDT VGARLMLLRR LAHPDDARLG
PPLQVVVTAV RSLLQPMTPQ LGQLEPLTLA VGDEIAFEDV IARLVELAYT RVDMVGRRGE
FAVRGGILDV FPPTAEHPVR VEFWGDEVSE MRMFAVADQR SIPEIDVDTV VAVACRELLL
TDDVRRRAAE LSAQHPPTEN TVSGSVADML AKLAEGIPVD GMEALLPVLR PDDLALLTGQ
LAPGTPVLVC DPEKVRTRAA DLIETGREFL EASWSVAAVG GDAPIDVEQL GGSGFRELDE
VRQAARSSGH PWWTLSQLSD EAAIELDVRA APSARGHQRD IDEIFAMLRG HVATGGCAAV
VAPGTGTAHR VVEQLAESDT PATMLESGAT PKPGVVGVLK GPLHDGVVIP GAALVIITET
DLTGNRVTAT DGKRLAAKRR NVVDPLALTA GDLVVHDQHG IGRFVEMTER IVGGARREYL
VLEYASSKRG QSDTDKLYVP MDSLDQLSRY VGGQAPALSR LGGSDWANTK TKARRAVREI
AGELVSLYAK RQAAPGYAFG PDTPWQAEME DAFGFTETVD QLTAITEVKA DMEKPVPMDR
VICGDVGYGK TEIAVRAAFK AVQDGKQVAV LVPTTLLADQ HLETFRERMA GFPVTVKGLS
RFTDPAESRA VIDGMADGSV DIVIGTHRLL QTGVRWKDLG LVVVDEEQRF GVEHKEHIKS
LRTHVDVLTM SATPIPRTLE MSLAGIREMS TILTPPEERY PVLTYVGPHD DKQIAAALRR
ELLREGQAFY VHNRVSSIDQ AAARVRALVP EARVAVAHGQ MPEDLLESTV QGFWNRDYDI
LVCTTIVETG LDISNANTLI VERADTFGLS QLHQLRGRVG RSRERGYAYF LYPQHAPLTE
TAYDRLATIA QNNELGAGMA VAMKDLEIRG AGNVLGVEQS GHVAGVGFDL YVRLVGEAVE
AYRAAADGKT VTGPEEPKEV RIDLPVDAHL PPDYIPSDRL RLEGYRRLAA AGSDDEIAAV
VEELTDRYGA LPEPAQRLVA VARLRLLCRE VGITEVSAPS EATVRLAPMT LPDSAQVRLK
RLYPAARYRA TSATVQVPIP RAGGVGAPRI RDLELVQMVA DLVSALDGKP QADLGITKAV
TSERQAR
//
