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Database: UniProt
Entry: A5FKM8_FLAJ1
LinkDB: A5FKM8_FLAJ1
Original site: A5FKM8_FLAJ1 
ID   A5FKM8_FLAJ1            Unreviewed;      1121 AA.
AC   A5FKM8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 110.
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   OrderedLocusNames=Fjoh_1202 {ECO:0000313|EMBL:ABQ04234.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ04234.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ04234.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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}.
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DR   EMBL; CP000685; ABQ04234.1; -; Genomic_DNA.
DR   RefSeq; WP_012023284.1; NZ_MUGZ01000003.1.
DR   AlphaFoldDB; A5FKM8; -.
DR   STRING; 376686.Fjoh_1202; -.
DR   KEGG; fjo:Fjoh_1202; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_10; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000006694; Chromosome.
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   1121 AA;  128390 MW;  EE8A766D88062999 CRC64;
     MSKNVLYTTY DNLPKAQQIA SGLLEGNQIK MNISGLLGSA VSFIIRSVFK KTELPFLIVL
     DNKEEAAYYL NDLEQMIGEQ DVLFYPVSFR RPYQVDETDN ANVLLRAEVL NRINSRKKPA
     VIVTYPEALF EKVVTRQQLD KNTLKVSLND KISIDFINEV LFEYEFKRVD FITEPGEFSV
     RGGIVDVFSF SNDHPYRIEF FGNEVDSIRT FDVETQLSVE THKKITIIPN VENKIFQENR
     ESFLDYIAEK TVLFIQNTEG LFSQLDKQFA RAEEAFEKLS KEIKHAAPEQ LFLNQASFIK
     RALDFSVVEL ASRPVFKTTK KFEFHIQPQP SFNKQFDLLL NNLSDNHFNG YVNYLFCSNE
     TQAKRFHDIF ESLDEANSEN IRKHYHTIVL PLYQGFIDEE NQITAYTDHQ IFERYHKFNI
     KNGYSKKQNI TLKELTALSV GDYVTHIDHG IGKFGGLQKI QVEGKTQEAI KLVYADNDIV
     YVSIHSLHKI SKYNGKDGTP PKIYKLGSNA WKVLKQKTKA RVKHIAFNLI QLYAKRRLEK
     GFQFAPDSYL QNELESSFIY EDTPDQMKST QEVKADMESD RPMDRLVCGD VGFGKTEVAI
     RAAFKAVDNS KQVAVLVPTT ILAYQHYRTF SERLKDMPVS IGYLNRFRTA KQKTQTLKDL
     AEGKLDIVIG THQLVNKNVV FKDLGLLIVD EEQKFGVNVK DKLKTIAANV DTLTLTATPI
     PRTLQFSLMA ARDLSVITTP PPNRYPIETN VVGFNEEIIR DAISYEIQRN GQVFFINNRI
     ENIKEVAGMI QRLVPNARVG IGHGQMDGAK LEELMLGFMN GDFDVLVATT IIESGLDVPN
     ANTIFINNAN NFGLSDLHQM RGRVGRSNKK AFCYFICPPY SSMTEDARKR IQALEQFSEL
     GSGFNIAMKD LEIRGAGDLL GGEQSGFINE IGFDTYQKIM NEAIEELKEN EFKDLYPEEN
     DIDTKEYVKD IQIDADFELL FPDEYINNVS ERLVLYNELG AIKDEAGLQE FERKLIDRFG
     PLPKQATALL NSIRIKWIAT KVGIEKLVLK QGKMIGYFVS DQQSDYYQSV KFRNVLNFVQ
     KHSSLCKMKE KQTVNGLRLL LTFENVKSIK RALELMELFE E
//
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