ID A0A328BNC6_9CAUL Unreviewed; 1149 AA.
AC A0A328BNC6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:RAK68860.1};
GN ORFNames=DJ019_02265 {ECO:0000313|EMBL:RAK68860.1};
OS Phenylobacterium kunshanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1445034 {ECO:0000313|EMBL:RAK68860.1, ECO:0000313|Proteomes:UP000249524};
RN [1] {ECO:0000313|EMBL:RAK68860.1, ECO:0000313|Proteomes:UP000249524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUT-10 {ECO:0000313|EMBL:RAK68860.1,
RC ECO:0000313|Proteomes:UP000249524};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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:RAK68860.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QFYS01000001; RAK68860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328BNC6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000249524; 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:UP000249524}.
FT DOMAIN 616..777
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 798..952
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1149 AA; 126713 MW; C5560562D7882C53 CRC64;
MRRVADDPGR LDLVGAPEGF DALVVADIVR ARKNLVVFVA RDGARLSAFT EAFRFFGQGV
EVLTFPSWDC LPYDRVGPSA GVAAQRMATL SRLAEGLDAK PRLLVTTVPA LIQRVPPIKA
VKRASYSAKA GNSVEIADLE AYFAVNGYSR ASTVSEKGEF AIRGGVIDVF PPGAEEPVRL
DLFGDTLESI RAFDPETQRS TKQLKDVSLL PVSEALLDKE AISRFRTGYL ETFGAPGDDP
LYAAISEGGR RAGMEHYLPL FYPELASLFD YLPQDTVVAL DHLARDARDE RLAMISDAYE
ARANTERRTH YHPLEPTRLY LDEAEWGEAL RVRPSRRFSA FNEAESEAVI DMGARAGRNF
SAERKLDSVN LFEATVDHAK ALSANGKRVL FASWSEGSSD RLGHMLADHG LNKLPLAPYW
DAAKAADPKT PQRVVLPLDA GFETETLAVV SETDILGDRL ARPRKRRRAS NFLAEASALT
PGDLVVHIDH GIGRYEGLKT LDVQGAPHDT LELQYGGEAK LYLPVENIDL LTRYGADSEG
VQLDRLGGAA WQARKARAKE RLREMADGLI RIAAERAMRQ TEAAEPPQGL FDEFCARFPY
EETDDQLAAI GDVLEDLGAG KPMDRLICGD VGFGKTEVAL RAAFVVAMSG KQVAIVAPTT
LLARQHYKTF SERFEGWPVK VRRLSRLVPA KEASETRDGL ANGEVEIVVG THAVLSKQVS
FKELGLVIVD EEQHFGVKHK EKLKELRADV HMLTLTATPI PRTLQMSLSG IREMSIIATP
PVDRLAVRTY ITPWDPVVIR EALLREKYRG GQAYFVCPRI NDLPELERFL REQVPEVKFV
VGHGQMAPTQ LEEVMTAFYD GQYDVLLSTT IVESGLDIPT ANTMIIHRAD MFGLAQMYQL
RGRVGRSKAR AYAYLTTPAE KQITLSAEKR LKVLQSLDSL GAGFQLASHD LDIRGGGNLL
GDEQSGHIKE IGVELYQQML EDAVNELKAR ADVDALVPDR GWSPQINTGA AVLIPDEYVP
DLNVRLALYR RISDAEKAQD REALAAELID RFGPLPPEAD QLLKVVAIKG LCRQANVAKI
DVGPKGAVVT FRNDDFKNPM GLVQFVGKNA VAWKLRPDHK VVVKGEWETP RQRLDAAEKV
LSELAKLAA
//
