ID C6J5E9_9BACL Unreviewed; 1177 AA.
AC C6J5E9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 71.
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:EES71770.1};
GN ORFNames=POTG_03626 {ECO:0000313|EMBL:EES71770.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71770.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES71770.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES71770.1,
RC ECO:0000313|Proteomes:UP000003981};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Paenibacillus sp. D14.";
RL Submitted (MAR-2009) 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}.
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DR EMBL; GG695988; EES71770.1; -; Genomic_DNA.
DR AlphaFoldDB; C6J5E9; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_1_9; -.
DR Proteomes; UP000003981; 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:UP000003981}.
FT DOMAIN 630..791
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..966
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1177 AA; 133868 MW; 0961991885FBC991 CRC64;
MPHLLQALIE AFSRDTDFAS TVAGINSGMK EQLISGLSGS SRQVMLAALH QETKRPLLVV
THNMFSAQKM YEDLQEALSP DQVLMYPANE LVAAESAVSS PETLAQRIEV LLQCSRGFRG
IVVVPYSGIR RYIPTPEAMA EAGLTVRLGG TLELERFMAQ MVELGYERVE RVESRGEMSL
RGGIIDFYPL TASMAYRVEL FDDEVDSIRT FDPADQRSVD QIKEVFIPPC KELIATKERM
GQAAQALSEK LEIQLDKMTD RQAKNRLREE MYKEIEMLRE HVYFSEIYKY ISLIYPERKT
LYDYMPEDTL LLLDEPSRLL ETAKQLERDE AEWNLHLYQN GKSLPDLPLA VDVDHLIYHR
PFQTLFLSLF LRQVPHSQPQ NIVNFVTRAM QDFHGQMNVL KAEMERWKKS GAHVIMLAST
EERMDRMRRV LQDYGIDEPQ LLQGNLQSGF ELPSVHLVVI TEGEMFSQKQ RKARRVAKSM
DNAERIKSYT ELKVGDYVVH QNHGIGKYMG IGTLEVGGIH KDYMHILYAG GDKLSVPIEQ
IDMIQKYVGS EDKEPKIYKL GGNEWNRVKN KVRSSVQNIA DDLIKLYAER QAAPGYAFEK
DTPEQQEFEA MFPYEETPDQ LRAIEEIKRD MEQSRPMDRL LCGDVGYGKT EVAIRAAFKA
AIEGKQVAVL VPTTILAQQH YETFRERFAG YPINIQTLSR FRSRKEQNET IKGIRQGTVD
IVIGTHRILS QDLVFKDLGL LIVDEEQRFG VTHKEKLKKL KTNVDVLTLT ATPIPRTLHM
SMLGVRDLSV IETPPENRFP VQTYVVEYSQ SLVREAIERE MARGGQIYYL YNRVQGIHEM
AAQISMLVPE ARVVVGHGQM SEQELEKTIL DFLDGEYDVL VSTSIIETGV DIPNVNTLIV
HDADKMGLSQ LYQLRGRVGR SNRIAYAYFT YQKDKSLTEV AEKRLQSIKE FTELGSGFKI
AMRDLAIRGA GNLLGAEQHG FIASVGFDLY SQMLAEEIQK RKITMLGETP PAEATWNTTI
DLGIDAYLPS DYIYDSIQKI EIYKKTASVQ TFEDVAELED ELLDRFGELP DAVQNLLAVA
RVKLYGKQYG IESMTLRGEE VTIKFYEGQE QAIVPSKLAE VGNLFGRCVQ FSQGSVMLIR
INTKGMDDKE MMGLLEQFLG ALKDAFKVKG ELQNVSK
//