ID I0USW9_9MICC Unreviewed; 1249 AA.
AC I0USW9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:EID50972.1};
GN ORFNames=HMPREF1324_0515 {ECO:0000313|EMBL:EID50972.1};
OS Rothia aeria F0474.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=1125724 {ECO:0000313|EMBL:EID50972.1, ECO:0000313|Proteomes:UP000004863};
RN [1] {ECO:0000313|EMBL:EID50972.1, ECO:0000313|Proteomes:UP000004863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0474 {ECO:0000313|EMBL:EID50972.1,
RC ECO:0000313|Proteomes:UP000004863};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-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:EID50972.1}.
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DR EMBL; AJJQ01000032; EID50972.1; -; Genomic_DNA.
DR AlphaFoldDB; I0USW9; -.
DR PATRIC; fig|1125724.3.peg.1080; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000004863; 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}.
FT DOMAIN 704..865
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 890..1040
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1249 AA; 136421 MW; F80839E2F7302A3C CRC64;
MKLTGLSRTL LGYPSYRNVV AAAQLPATER SAQTLIGAVP GLHAPLIADI AAAIRNSTRR
EGVGKEPLTL VITPTERQAE DTAHALGAYL PDNDIALLPA WETLPHERLS PRSDTVGRRL
GVLRAITQAG ERTPLVLVAP VRAVIQPIVA GIEKLVPVTL TRGEEYSFKE VIKGLTNAAY
SRVDLVAKRG EYAVRGGIID VFSPTATNPV RLEFFGDELD EIRYFSAADQ RTLTGEGSQP
DRITLPPCRE LLITPEVMSR AARLVGDYPA ASAMLEKIAG GIYVEGMESL TPLLVERMNT
LISLLPSGSL ALSVEPERIA ARAEDLVATN EEFLTAAWDT AAEENSAAPI DLGQLRMSEA
GFRTITATRT EALDAGIGWW EITELIANAE LAASVPDDPA ETDTATEKTS AHCALADAVA
DGVDTLVVRA SAAASFTGSV QRMLEEVGAL VKDGWRVLAL TNGRGSTDRL IELFNDSEVP
ASRRDTLDKG IEPGIIEVCE APASAGFLLP QEQLAVFTEG EILGRRGTYA PRGVTGSKLK
ARRRRNAVDP LSLTPGDYVV HERHGIGRFI EMTSRSVAGV KPAAGQNVPM REYLVLEYAP
SKRGGAPDRL FVPSEQLDMI SHYVGSEKPT LSKMGGSDWA KTKSRARKAV KEIAADLIKL
YSARQASRGH AFTEDTPWQR ELEESFPYNE TPDQLNAIYE VKADMEKELP MDRLISGDVG
FGKTEVAVRA AFKAVQDGKQ VAVLVPTTLL AQQHYETFTE RFSGFPIKIK VLSRFQKPKE
SRQITEEIAS GAVDVVIGTH RILSESISFK DLGLVIIDEE QRFGVEHKEK LKQMRTNVDV
LAMSATPIPR TLEMSLTGIR ETSTLATAPE ERHPVLTFVG ARTDAQITAA IRRELMREGQ
VFFVHNRVAN IDNVAAELAK LVPEARIATA HGRMSEARLE QIIVDFWERR FDVLVCTTIV
ETGLDISNAN TLIVDNAQNY GLSQLHQLRG RVGRGRERAY AYFLYPPGKP LGEVALERLK
AVATHNELGA GLQLAMKDLE IRGAGNLLGG EQSGHIAGVG FDLYLRLVGE AVADFRGEKD
ERDVEVKVDL PVNAHIPHSY IDAERLRLQA YRQIAAADTE QKMAEAREEL TDRYGELPEP
VQNLLAVTAL RQRARAAGIR EIVVMGPKVR VVTDEQLPDS RQMRLGRVYP GSSHTQPKGL
QTWLTLLPRP KSSPVGGIEL VDAAMLEWCQ QLIDTIFADV PGASRSAPE
//