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Database: UniProt
Entry: A0A3S0MG79_9FLAO
LinkDB: A0A3S0MG79_9FLAO
Original site: A0A3S0MG79_9FLAO 
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
//
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