ID A0A1E4L6N5_9PROT Unreviewed; 1135 AA.
AC A0A1E4L6N5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ABS92_02785 {ECO:0000313|EMBL:ODU50548.1};
OS Thiobacillus sp. SCN 63-374.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU50548.1, ECO:0000313|Proteomes:UP000094238};
RN [1] {ECO:0000313|EMBL:ODU50548.1, ECO:0000313|Proteomes:UP000094238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU50548.1}.
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DR EMBL; MEFK01000020; ODU50548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4L6N5; -.
DR Proteomes; UP000094238; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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}.
FT DOMAIN 609..770
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 791..945
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1135 AA; 125880 MW; 259D3B45B2879026 CRC64;
MPFFSPSSPL SGHRQSGLAG AADALYLAEL ARHAAPLAVV CASAWDANRL AEELRWFDPA
LRVCAFPDWE TLPYDTFSPH PDLISERLAT LYQISRGEFD IAVVALSTAL YRLAPPAFLA
AHTFFLKQKD VLDEPAFRAQ MALGGYTHVN QVFAPGEFSI RGGLIDLFPM GSALPYRIDL
FDNEIETLRA FDVDTQRSIY PVNEVRLLPA REFPLDEAGI TRFRQNFRER FEGDPSKSKL
YKDVSNGLAP AGIEYYLPLF FDETATLFDY LPRHTRFVSH GALDPAGQAF WADAQGRHRL
LAGDKDRPLL PPAELFLPTD TFFSLAKAYA RLDVEQAGEG LTHPVPPISV DRREAHPVAK
LQGFIDGFQG TTLIVAPSAG RRETLHEYLA EHGLDASLCD GWADCQQAAG RILLSRVLLT
HGPLAEGFIT ADGALAVITE TELYAIPPKT RRAREARATQ IDNLLRDLSE LKPGDPVVHA
QYGVGQYLGL INMDLGDGDT EFLQLEYAKG DKLYVPVANL HLISRYSGAG EGAAPLHKLG
TDQWEKARRR AMQAARDTAA ELLNLYALRA AREGHAFKFS PHDYEAFAEG FGYEETPDQA
AAIAAVMADM QAGKPMDRLV CGDVGFGKTE VALRAAFMAV MGGYQVAVLV PTTLLAEQHF
NNFSDRFSAW PVKLAELSRF RTAKEQAEAL QALKNGKLDI VIGTHRLIQK DVKFARLGLV
IMDEEHRFGV RQKEQLKALR AEVDVLTLTA TPIPRTLAMS LEGIRDFSVI ATAPQKRLAI
KTFVHSFSGG LIREAVLREL KRGGQVYFLH NEVSTIEAMR ERLEKLLPEA RIRVGHGQMG
ERELEQVIRD FYQQRYDILL CTTIIETGID IPTANTILIN RADKFGLAQL HQLRGRVGRS
HHQAFAYLLV EEDRTLTPQA KKRLEAIQLM EELGSGFHLA MQDLEIRGAG EVLGEKQSGE
ILEVGFSLYN DMLAGAVSSL KAGKEPDMNQ PLGVVSEINL HLPALLPVDY CPDVHERLVL
YKRLASVHDA EALTQLQEEL VDRFGPLPDP ARALLDTHRL RLAARPLGIM KVDASADSIL
LQFVPQPPID PGRIIQLIQS RRDIKLAGEN RLRWTANSSV EARAANVITL FNLLK
//
