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Database: UniProt
Entry: E4KMU1_9LACT
LinkDB: E4KMU1_9LACT
Original site: E4KMU1_9LACT 
ID   E4KMU1_9LACT            Unreviewed;      1181 AA.
AC   E4KMU1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, 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   ECO:0000313|EMBL:EFR31790.1};
GN   ORFNames=HMPREF9257_0154 {ECO:0000313|EMBL:EFR31790.1};
OS   Eremococcus coleocola ACS-139-V-Col8.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX   NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR31790.1, ECO:0000313|Proteomes:UP000005990};
RN   [1] {ECO:0000313|EMBL:EFR31790.1, ECO:0000313|Proteomes:UP000005990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR31790.1,
RC   ECO:0000313|Proteomes:UP000005990};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFR31790.1}.
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DR   EMBL; AENN01000006; EFR31790.1; -; Genomic_DNA.
DR   RefSeq; WP_006417922.1; NZ_AENN01000006.1.
DR   AlphaFoldDB; E4KMU1; -.
DR   STRING; 908337.HMPREF9257_0154; -.
DR   eggNOG; COG1197; Bacteria.
DR   Proteomes; UP000005990; 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:UP000005990}.
FT   DOMAIN          639..800
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          821..975
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1181 AA;  134438 MW;  DC88EE1D4D2A7EA6 CRC64;
     MQVELNRNAF QESIQQINAD KKRKLPYLIT GLDGSARAIY LAQLFQARPT TILIVESSDL
     QMQELSQDLA HILPEVPVLT YPADDNLAIE YAQASMDFAS QRVAALNFLA QGQPGFVLTT
     LAGLRQKLNP VDQWVAYNKI IQVGQELDRQ ALLDTLIALS YKSVNMVMTP GEFSVRGGIV
     DFYPLDSDYP VRLDFFDSEV DSIRYFNAET QESVEQIDEV ILSPVQELIF PNFMQLMVAD
     ELKKRAKKYL DKVKDPAIKN NLQINLLGDL KNLADHNEPL KYASAFFGLI PETSSLLDYL
     RYDGHLVIND YAKLQQEQVQ QIEQNHYWIE QEIEKGQLIP NLPIKWDFED LVKNFSGSTL
     HFSVLQRGYV AMALAGLFNY KYQTMTPYFS QMPMIIDDLQ TWLKQGYVVQ VALPSKKQVL
     NFRQALADHG FDKVYLQDEQ PIQANRVNLV TLDLSKGFVL SEQAWALVTH HDLFKEVNRP
     RGRVRQPHLS NAEKIKSYNE LSVGDYVVHL NHGVGRYTGM ETLEMNGVHR DMLAIEYQNN
     ARVLIPVDKI HLIQKYVSSE SKTPKINKLG GTEWAKTKQK VQATVEDIAD DLIKLYAKRE
     AEKGYRFSPD TPEQSEFEQA FGFVETPDQL TSSQEIKADM EKSRPMDRLL VGDVGYGKTE
     VAMRAIFKAV MDGKQVAFLV PTTVLAQQHY NTLQARFNDW PFEIGLLSRF VSRVQQKETI
     AKLKSGAVSI VVGTHRILSK DIVFNDLGLL IVDEEQRFGV KHKERLKQLK AQVDVLTLTA
     TPIPRTLHMS MIGIRDLSVI ETPPNNRFPV QTYIMERNEG AIKTAIEREM ARGGQCFYLY
     NRVATIYQRA DEISQLVPQA RVAVAHGQMS ETELETVLVD FIQGLYDVLV TTTIIETGVD
     IPNANTLFVD HADKMGLSTL YQLRGRVGRT HRVAYAYLMY EPFKQLSEVS EKRLKAIREF
     TDLGSGFKIA MRDLSIRGAG NLLGKQQSGF IDSVGYDLYT QMLKEAVDQR KGIKKKQSQY
     ESQAIEWNVD VDAYLPKDYI QDERQKINMY KAIQQIDSEE AYRSIQDQLI DRFGEFPDQV
     ADLLDIALIK YYGLKSGIEE IKQDRQRIVV TYNERASMKL KGPNIFQALQ EVPLKAEVTV
     NGGKLAIRLL VQGKVSYQWL PALKALAKES MSIVNQGEEQ E
//
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