ID R7K920_9FIRM Unreviewed; 1125 AA.
AC R7K920;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=BN810_01150 {ECO:0000313|EMBL:CDE72321.1};
OS Acidaminococcus sp. CAG:917.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=1262688 {ECO:0000313|EMBL:CDE72321.1, ECO:0000313|Proteomes:UP000018048};
RN [1] {ECO:0000313|EMBL:CDE72321.1, ECO:0000313|Proteomes:UP000018048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:917 {ECO:0000313|Proteomes:UP000018048};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE72321.1}.
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DR EMBL; CBJM010000031; CDE72321.1; -; Genomic_DNA.
DR AlphaFoldDB; R7K920; -.
DR STRING; 1262688.BN810_01150; -.
DR Proteomes; UP000018048; 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; 3.
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:UP000018048}.
FT DOMAIN 600..761
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 782..937
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1125 AA; 124840 MW; 1A85E9C804E4C4B1 CRC64;
MKFPFLALEN FPQLYDAVSG YNKTSLYSVS EGAKIHIAAS VPGKKLFVAS DLLLAKKYAF
ELKAYGVDAI VFPTREDVLL YRKSYSSATD MARAAAFSKI ARGDFDVICC SAENILEKIT
SLDVISDYTI CAEEGKTFNL VLLSEKLSEM GYTRVEQVYE AGDFSVRGDI VDVYAAGEEN
PVRISFFDNE IESVHIFNVA DGSKIKSVKR FYIPPVSDVI CTSGALKDIL EVNKTETGKV
KEILSELIGG LKSGALSGKY SYLLPYFETT SLTELDLTVI IDEPKVVAEK LSLVEKEFLN
RFKTLQMSTM VTFRHKKAKD GADDAIKKLG ERKQISVSSL TMSNPMFSPD KVLKLSSKAC
TKYCYDFNAL LRDIRDYQRE DFKIVIMSRD DTRGRTIQSS LLEEGISPIY DAEPVKGKTT
ILPCDVTQGF LYLSDKLLLV GSDEILGKGR AVGAAKKVKG FEPPKEGDYV VHSLHGVGIC
EGTAVFDAGE YKKEYLSIRY EGGDHLYVAI DQMDCVTKFI GETNPPLNKL GGKDFRREKE
KVKKSVKKLA INLLALYAVR EKIKGHKYAP DGENQRRFED AFEYEETDDQ LRAIAEIKKE
MESGKVIDRL ICGDVGFGKT EVALRIMFKT AMEGKQACLI APTTILCKQH YDTLSKRLEG
FNVNAKLLTR FQTASERAEI LKGLKSGEIS IVVASHRILS KEVQFCDLGL LVLDEEQRFG
VEHKETLKER NPSVNTLTLS ATPIPRTLNM SLSGVRDISL LETPPQGRLP VETSVIEYSD
ALIKDAVERE HSRGGQVFIL YNKVETIADF TAKVASIVGG DIKIRYAHGQ MHPRELENAI
EAFYEKQYDV LVATTIIENG IDLPDANTLI VIDSQNFGLS QLYQLRGRVG RRGALAKAYF
TIPPAVSFSE TAQKRFDALL ENTEIGSGFK ISLADLSIRG AGSILGAEQH GHIERVGYEM
YIEILEEAIK ELKTGETAKE ENIEFKIAAT TYIPSDYVSA RDKIKMYKRI SSLCGPKEKE
ALVAEFSESY GAVPIGLKNL MNIALIKNLV KGMGVKSVIV TKQGAGINFV GADVFKDERI
LKAVSENKDK VVLTTTIPPA LIFDVKNLSP EDKLETIANF LVQCD
//
