ID U1FQC7_TRESO Unreviewed; 1269 AA.
AC U1FQC7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:ERF61681.1};
GN ORFNames=HMPREF1325_0357 {ECO:0000313|EMBL:ERF61681.1};
OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF61681.1, ECO:0000313|Proteomes:UP000016412};
RN [1] {ECO:0000313|EMBL:ERF61681.1, ECO:0000313|Proteomes:UP000016412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF61681.1,
RC ECO:0000313|Proteomes:UP000016412};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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:ERF61681.1}.
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DR EMBL; AUZJ01000007; ERF61681.1; -; Genomic_DNA.
DR AlphaFoldDB; U1FQC7; -.
DR STRING; 1125725.HMPREF1325_0357; -.
DR PATRIC; fig|1125725.3.peg.308; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000016412; 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; 3.40.50.300; 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}.
FT DOMAIN 743..904
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 913..1079
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 276..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 142425 MW; 70B1A8ECB7992D12 CRC64;
MRDAVFRLTD ASCRFPFSVR GLHGSLSAYF TAEYCERIQS LAFKKSVSGG VSFDSRSSDI
VIVTPGENEA IDIRTDLTSI FPEAEIIDIP WWGMIPYRPV SRGAAVFGER AAALAKLAGA
GREGFSQKPR IFIVSERVFL SPLPPPESVK SRSFSISRGA HVDTVKTAER LSSLGYTRAP
RVYVQGEFSL RGEVLDVFVP QSTAPCRIIF DFDTVAQIKT FDTDTQTTTG SLESVFISPM
REVIWDDALL TDLKNAIEAY EATAVSAEDE MRLSDAASQN GETPFCNVDR HSDTADNTSA
GEIPSSDEDE FSDAGAPKDG EPPLRKSCRA HLPFTKEAKA ALSNMLSELE TAKSCEGEEL
LYPVLWKKRY TISDYIGERT TVFFFDYDRL VNAEETIVRE YGGMYRKARL SFPAFPPEQI
LSDFQKNLKI VSRSILFHTV SRADTPSTDE SPSDIAFPCE VSRSFFGNIP FLKEEIGKLQ
DAGWKIAVFA DGENQERRIA QLLSDFTEER GNEIALNGRN AKIHERDAKP HEERTHEHRT
LERSSAPIEK RCALAVFPEA ISEGFSIPDL KLIVIQENEI FGRRRAVPKS LKKAKSAAID
TFVELTPGDY VVHVQYGIGI FCGIERVKAG GNERDYIKLE YADKEVAFVP IEQVNMVQRY
IGSEGDAPKL DKIGSKSWEN RKRKVQKAVE DLAKKLIDLY SRRKASRGFP FPKDTEWQTS
FEAAFPYEDT KDQAIVTEDV KRDMEKPVPM DRLICGDVGY GKTEIAMRAA FKAVMGGKQV
VFLAPTTILA EQHYETCVER FANFPVKIAV LSRFVPHAEQ KKTLTLLASG DIDILIGTHR
VIQKDVVFKN LGLMIIDEEQ RFGVKDKEKL KEMKANIDCL ALSATPIPRT LHMSLLKIRD
MSLLATPPQN RQMIETAIEP YSDERVATAI RRETERGGQV FFLHNRVDSL FEVRRKIERL
VPEMLVDVAH GQMMSAELED IFRRFKLGGF HVLVSTTIIE NGIDIPNVNT IIIDRADMYG
VSQLYQLRGR VGRSDRKAYA YLLYPENTSL SEVAMKRLQV ISDFTELGSG FKIAMKDMEI
RGAGNLLGRD QSGDVYAVGF ELYLKLLNEA VERLTASENY KAQSEVLMEL EYTGFIPDAY
VRSAETKMEI YKKIASVQTD DELIAVMNEI EDRFGPVPDE VASLLSLAEI RILCKKLSVS
ALKESKGVVE IEFAKVSDIS VDRVLQLIKE SSGSVWLDAA KPNMLFLKLG KIGLKEKSEF
IRERLEKLA
//
