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Database: UniProt
Entry: C6J5E9_9BACL
LinkDB: C6J5E9_9BACL
Original site: C6J5E9_9BACL 
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
//
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