ID A0A0Q5VIK5_9ACTN Unreviewed; 1180 AA.
AC A0A0Q5VIK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ASG36_05085 {ECO:0000313|EMBL:KQS61076.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS61076.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS61076.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS61076.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS61076.1}.
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; LMQA01000001; KQS61076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5VIK5; -.
DR STRING; 1736354.ASG36_05085; -.
DR Proteomes; UP000051830; 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:UP000051830}.
FT DOMAIN 640..801
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 819..976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1180 AA; 128879 MW; F56454D8B5BFDFFA CRC64;
MRGVLDVVLS DPGLARVVEQ AGAADLTVTA PPSVQPLVAA ALAAPSPGAG VPVLVVTAGE
RDADRTADLL RCFLPDRRVE VFPAWETLPH ERLSPRPDTV GRRLAVLRDL THPEAATGRI
DVVVAPVRSL LQPLAPGLGD LVPVELAAGD SAELGEISKR LADAAYTRVE LVEKRGEFAV
RGGLLDVFPP TEPHPVRVEF WGDEVDELRY FSAADQRSLD ERPDRLWAPP CRELLLTPTV
RERARALTLE HPELAEVTDS LAEGIAVEGM EALTPALIGG EHMELLTDLV PRDTHVLVCD
PERVRSRAAD LVRTAEEFLA ASWQTAAEAG QAPIDLGASS FRDLEDVADD ARGRGLPWWT
TGAFTLQTED DDTHVTLTAT PVERFHGDQD AALGQLRDWG RDDWRVVLTF AGPGPAQRAA
DQLTEADLGV RLLPDLAAAP ESGLTHVTQA NLEAGFAFPG IKLALLTEHD LTGQRGTSMR
DAQKMPARRR NAVDLVQLQP GDVVVHEQHG VGRYVEMVSR TVHGGQRDYL IVEYAPGKKN
QPPDRLFVPT DALDQLTRYV GGDAPALSKL GGADWAKTKG QARKAVKQIA AELIRLYSAR
MASKGHAFGP DTVWQRELED AFPFQETPDQ LAAIDEVKAD MAQPVPMDRI ICGDVGYGKT
EIAIRAAFKA VQDGKQVGVL VPTTLLANQH FKTFSERMAQ FPVTVAVLSR FQSKTESDET
LRKLADGEVD ILVGTHRLLQ PTTRFKDLGL VIVDEEQRFG VEHKEYLKTM RTAVDVLSMS
ATPIPRTLEM SLTGIREMST ILTPPEERHP VLTYVGAWED KQMAAAIRRE LLRDGQVFVI
HNRVQSIDKA AATIRRLVPE ARVAVGHGQM KEHELEKIMV GFWEKEYDVL IATTIVESGL
DIPNANTLIV DRADTFGLSQ LHQIRGRVGR GRERAYAYFT YDPNRPLTET SVDRLTTIAN
NTDLGAGMAV AMKDLEIRGS GNLLGGEQSG HIAGVGFDLY VRLVGEAVSD YRAQATGESP
AVEPADVRVD LPVDAHLPHD YVPGERLRME AYRKVASVQD DDQAQAVLDE LTDRYGPAPA
PVLNLLAVAR FRAAMRQLGV TEVSMAGRNV RISPVDLRES QQMKLTRLAE GVSYKGTVNT
VSLKVPVGPD RRTPLRDVAL LEKLHALMTS VLEQPAGAAT
//