ID A0A3S0MG79_9FLAO Unreviewed; 1122 AA.
AC A0A3S0MG79;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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:RTZ02413.1};
GN ORFNames=EKM02_02565 {ECO:0000313|EMBL:RTZ02413.1};
OS Flavobacterium sp. RSP49.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTZ02413.1, ECO:0000313|Proteomes:UP000272024};
RN [1] {ECO:0000313|EMBL:RTZ02413.1, ECO:0000313|Proteomes:UP000272024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSP49 {ECO:0000313|EMBL:RTZ02413.1,
RC ECO:0000313|Proteomes:UP000272024};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (DEC-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:RTZ02413.1}.
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DR EMBL; RYDN01000003; RTZ02413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0MG79; -.
DR Proteomes; UP000272024; 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; 3.
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 576..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 746..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1122 AA; 128580 MW; 5CB359BDBAF4AFBF CRC64;
MSKTALYNTY DNSPKTQQIV ARLLDNKQIK MQLSGLLGSA LSFVIRSVFK KAELPLLIVL
NNKEEAAYYL NDLEQMIGEQ DVLFYPGSFR RPYEIEDTDN ANVLLRAEVL NRINSRKKPA
VIVTYPEALF EKVVTRKELD KNTLKVAVGD KISIDFINEV LFEYEFKRVD FITEPGEFSV
RGGIVDVFSF SNDNPYRIEF FGDEVESIRT FDVATQLSMV QQKKITIIPN VENKIFQENR
ESFLDYISEK TVIFIQNTED FLSQLDKQFG KAEEAFAKLS QEIKRSSPEQ LFLNQAEFIK
RALNFSIVEL SSKPIFRTTK KFEFHIQPQP SFNKQFDLLL NNLNENHFNG YKNHLFCSND
AQAKRFHDIF KTLDEANSEN IRKQYHTVVF PLYQGFIDEE NQITCYTDHQ IFERYHKFNI
KNGYSKKQNI TLKELTTLSV GDYVTHIDHG IGRFGGLQKI QVEGKTQEAI KLVYADNDIV
YVSIHSLHKI SKYNGKDGTP PKIYKLGSNA WKILKQKTKA RVKHIAFNLI QLYAKRRLEK
GFQFAPDSYL QNELESSFIY EDTPDQTKST AEVKADMESD RPMDRLVCGD VGFGKTEVAI
RAAFKAVDNS KQVAILVPTT ILAYQHYRTF TERLKDMPVS VGYLNRFRTA KQKAETLKLL
AEGKLDIVIG THQLVSKNVV FKDLGLLIVD EEQKFGVNVK DKLKTIAANV DTLTLTATPI
PRTLQFSLMA ARDLSVITTP PPNRYPIETN VVGFSEELIR DAISYEIQRN GQVFFINNRI
ENIKEVAGMI QRLVPNAKVG IGHGQMEGRK LEELMLAFMN GEFDVLVATT IIESGLDVPN
ANTIFINNAN NFGLSDLHQM RGRVGRSNKK AFCYFICPPY SAMTDDARKR IQALEQFSDL
GSGFNIAMKD LEIRGAGDLL GGEQSGFINE IGFDTYQKIM NEAIDELKEN EFKDLYPEEN
NLETKEYVKD LQIDTDFELL FSDEYINNVS ERLSLYNELG AIKNEEELIV FQNKLIDRFG
PMPPRAKALM NSIRIKWIAT RLGIEKLVMK QGKMIGYFIS DQQSDYYQSK RFQDVLQFVQ
KHSSICKMKE KQTPAGLRLL LTFDNVKNTR TALELMEKLG GE
//