ID H6NSG6_9BACL Unreviewed; 1174 AA.
AC H6NSG6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=PM3016_7139 {ECO:0000313|EMBL:AFC33716.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC33716.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC33716.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC33716.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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; CP003235; AFC33716.1; -; Genomic_DNA.
DR RefSeq; WP_014372587.1; NC_016935.1.
DR AlphaFoldDB; H6NSG6; -.
DR STRING; 1116391.PM3016_7139; -.
DR KEGG; pmq:PM3016_7139; -.
DR HOGENOM; CLU_005122_1_0_9; -.
DR Proteomes; UP000007523; 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 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:UP000007523}.
FT DOMAIN 627..788
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 801..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1174 AA; 132256 MW; 5A39570F37399C1D CRC64;
MQALIQAFSA DNDFKSVVSG IRSGMREQLI AGLTGSSRQV MLASLFEELQ QPLFVVTHNM
FAAQKMFEDL AELLPPEKVL LFPAQELLAA EAAIASPEML AQRIDALARL AAGFRGLVVV
PYAGMRRLLP DQASIAAAQM TVSVGETLEL DQLVVRLVEL GYERVERVER KGEMSVRGGI
LDLFPLTSPH PFRIELFDVE VDSIRSFDAS DQRSIDKVQT LLIPPCREIV VDRKRLQSAA
QQVHELLQEQ IGKMTDRSAK DKLLEGIGHE IELLREGHSF QGMFKYVSLL FPDRQTLLDY
MPGDTILLVD EPARLLETAK QLEKDEAEWM TNSLQEGKSL PSLVLSKPYE TLLHRKPYPT
LYMSLFLRQV PQTTPQNIVN FMCRVMQSFH GQMNLLKSEM ERWKKAGAHV IMLASGSDRV
ERMKRVLADY DIEAPQIESG SLQTGFELPG IHLVVITEGE MFTQKQRKAR KVDKKIENAE
RIKNYQELKV GDYVVHVNHG IGKFVGIGTL EVGGIHKDYL HIMYAGGDKL SVPIDQIDQV
QKYVGAEEGK EPKIYKLGGT DWNRVKSKAR ASVQDIADDL IKLYAERQAT VGYAFNGDSN
YQQEFEGMFP YEETTDQLRA IEEIKKDMEK PRPMDRLLCG DVGYGKTEVA IRAAFKAAID
GKQVAVLVPT TILAQQHYET FRERFSGYPF NIQVLSRFRS KKEQTDTMKG VKAGTVDVVI
GTHRLLSKDV QFKDLGLLIV DEEQRFGVSH KEKLKRLKTN VDVLTLTATP IPRTLHMSML
GVRDLSVIET PPENRFPVQT YVVEYSTNLV REAIERELAR EGQVYYLYNR VQGITQMAEQ
ITALVPEARV TVAHGQMSEQ ELEKTILDFL DGEYDVLVST SIIETGVDIP NVNTLVVHDA
DKMGLSQLYQ LRGRVGRSNR IAYAYFTYQR DKVLTEVAEK RLQAIKEFTE LGSGFKIAMR
DLSIRGAGNL LGAEQSGFIA SVGFDLYSQM LGEEISKRKK EMGGEAVQET KAWSTQLDIQ
LDAYIPGDYI YDSVQKIEIY KKVAGIQTLE EAAELHDELV DRFGDLPEAV HNLLLAARLK
VYGAQYAIET ISQKGLDYEL KIHPDQNGNL DGQKLFELSA EFENRVKLIG GPQIIVELKG
KGLTPEQSIE TLERFLVQYK RALKSKGELQ DVAK
//
