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Database: UniProt
Entry: J6HIM2_9FIRM
LinkDB: J6HIM2_9FIRM
Original site: J6HIM2_9FIRM 
ID   J6HIM2_9FIRM            Unreviewed;      1122 AA.
AC   J6HIM2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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:EJU22488.1};
GN   ORFNames=HMPREF1152_1228 {ECO:0000313|EMBL:EJU22488.1};
OS   Mogibacterium sp. CM50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX   NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU22488.1, ECO:0000313|Proteomes:UP000003142};
RN   [1] {ECO:0000313|EMBL:EJU22488.1, ECO:0000313|Proteomes:UP000003142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM50 {ECO:0000313|EMBL:EJU22488.1,
RC   ECO:0000313|Proteomes:UP000003142};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-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:EJU22488.1}.
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DR   EMBL; ALNL01000017; EJU22488.1; -; Genomic_DNA.
DR   RefSeq; WP_009643566.1; NZ_ALNL01000017.1.
DR   AlphaFoldDB; J6HIM2; -.
DR   STRING; 936375.HMPREF1152_1228; -.
DR   PATRIC; fig|936375.3.peg.473; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000003142; 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:UP000003142}.
FT   DOMAIN          585..746
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          763..921
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1122 AA;  127193 MW;  18CCD87A60252D33 CRC64;
     MKTNITGISG SRIAYYAAKE IVKNNKTLII VSRANVAERL RDDISFFVHD RAIYVMPEED
     DLQIIYEAKD SNMLVQRIQA VDSLVSDDKT VVIAPVSAAL RPLQPVERFM ESVIELEMGV
     RVEPAELRQK LVSIGYSPAP VVEAPGEFSA RGGIIDIYSP NNSDPVRIEF FDDEIDSLRF
     FDPKSQLSFE NIDFVRVCPA AEFLPTAYER RRALSRITDE YDERLSRLKA ESGEGKLSDG
     RIDRIEELKG RISEMFENCT NVQIFANYLK YFDVTDERIW DYVIDPADAN MMIYDPNRVA
     AEIPEYQEQG DINKFYDKDI IAFTPFPEPI KGIDVFDKVV NVPSRQIASF NGQMELFGRE
     MRRLSKEGVE VHIVSADKER HDRIREYLED ARIFGHFRYD LGLLGSGMML DDEKLCYITD
     TDIFPNIRKS SKKRLRHRSG KQDFLDLHAG DYVVHEEHGI GRFEGIKTLE ADGEIKDYLK
     IHYSGTDVLY IPTEQMDIVQ RYIGSEGKAP KLSSLSGGDW RNTRARARKA IEEIAEDLVK
     LYAEREMKGG YAFQHDTVWQ REFEDSFLYQ ETDDQLQAIE EIKADMEKPL PMDRLLCGDV
     GYGKTEVAAR AIFKCVAEGK QAVFLAPTTL LANQHYNTLK ERFQDYPFNI EMLSRFVDET
     RQKRVLNDIA KGNVDLVIGT HRLLSDDVAY KDLGLLVIDE EQRFGVKHKE KLKMARQTID
     VLTLSATPIP RTLNMSLTGI KNISTIEEPP GDRYPVQTFV SAQDDELIRG AIERELARGG
     QLYVIYNRVN GINDIAKHIN KLVPEATVAV GHGRMNENTL ENVMLDFVEG DVDIFVTTTI
     IENGIDIPNA NTIIILNSDK LGLSQLYQLR GRVGRSNRLA YAYLLYKPER VLTEVATKRL
     AAIREFTEFG AGFKLAMRDL ELRGAGNVLG EAQHGNIAGI GYELYVKEID KAVRRLKGEK
     ITESREEISI EVDISARIPS EYIKDETLKL QAYKKIAQIT SHEEAEELIA ELIDRYGDLP
     DVTIDLVRIA EIKCLAAELG VKNISERGGR FVVEFNEDNN ADAFTLVVAK QKFGEGLIIS
     SGSNPYLSLQ KTKEKPAARI LDLMTVMKGA RLQGLAHSEM SN
//
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