ID A0A0Q8CQN0_9MICO Unreviewed; 1222 AA.
AC A0A0Q8CQN0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=ASD61_06910 {ECO:0000313|EMBL:KRA11762.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA11762.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA11762.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11762.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA11762.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11762.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRA11762.1}.
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DR EMBL; LMGR01000001; KRA11762.1; -; Genomic_DNA.
DR RefSeq; WP_055819993.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CQN0; -.
DR STRING; 1736567.ASD61_06910; -.
DR Proteomes; UP000051073; 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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 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:UP000051073}.
FT DOMAIN 671..832
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 857..1007
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1222 AA; 132847 MW; 502963178F026149 CRC64;
MMLQGLLTAL ERASTIESAL AQANRDADFS LPEGLNAPLI AALLARRGAQ RGAQAAFVIT
ATSREAEALE ASIAAYAPGA TVLDFPAWET LPHERLSPSA EIVGRRIQAL RTLREWSEAD
PAMRPPLIVV ASVRAALQPI ADNLADHPAV VLAQGGRGYD LSALAGELVD LAYTRVDMVT
RRGEFAVRGG ILDVFPPVAD HAYRVDFFGD EIDQLRAFSV SDQRSLPDAV ASVSLVPSRE
MLLSDSVRQR AREMRHEFPS LAQMLEKIAE GIPVEGMESL APALVDRLVP VTHYLPDDAV
VAVVGPERVS GRAQSLAETN REFLAAAWSA ATAGAEAPID LDSGDFLSLS ELRDSVRFSA
PGEKTQDHPW WTFSAFDAGD ADLLDYVRVA AYAVPSFAGN VEGALEHVGA RLADGWSMAI
VAAGHGLVER ARDVLADRGF AGRVADEFPE NPEPGVAYLL QAGVSRGFEV PSAKIGVLSE
GEFYGRTAGY DSRQIKKLAS RRKNVVDPLQ LKPGDYVVHQ THGIGRFVDM TQRTVASGAR
PTGPSRTAGI AQQPTIVREY LVLEYASSKR GQPADKLFVP TDQLDLLTRY VGGEAPALSK
MGGSDWSNAK SKARRAVRDI AVELVKLYSA RMASRGHAFG PDTPWQRELE EAFPYAETPD
QLQTIDEVKA DMERPIPMDR LLSGDVGFGK TEVAVRAAFK AVQDGKQVAM LVPTTLLVKQ
HVETFQERFA GFPVHLKALS RFQTDKEARE TLAGLTDGTV DVVIGTHRLL ADGVIFKDLG
LVIIDEEQRF GVEHKDKLKK LRTNVDFLAM SATPIPRTLE MAVTGIREMS TLATAPEDRH
PILTFVGPYS EKQVTAAIRR EMLREGQVFF VHNRVSSINR VAAQLAELVP EARIAVAHGK
LPESVLEQIV VDFWERKFDV LVSTTIIETG LDIANANTII IDRADKYGLS QLHQLRGRVG
RGRERAYAYF LYDENTPLSE TAHDRLSTIA ANNELGSGMQ VALKDLEIRG AGNLLGGEQA
GHIAGVGFDL YLRMIGEAVS TFRGDVAEGQ TELRLELPVD AHIPEDYVDS ERLRLEAYQK
LSTASSPAAK DGQIDSVLEE LTDRYGEPPQ AVLTLIAVSR LRRQAQRAGL GEVVAMGSNL
RVGPGTLPDS IQVRLQRMYP GSRYFTQTGV LSVPLPDKHG QPLEDAELIA WVTQLLTAIF
PAPVAEPAEP GAADADTVER AR
//
