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Database: UniProt
Entry: I3C2W5_9FLAO
LinkDB: I3C2W5_9FLAO
Original site: I3C2W5_9FLAO 
ID   I3C2W5_9FLAO            Unreviewed;      1126 AA.
AC   I3C2W5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=JoomaDRAFT_0935 {ECO:0000313|EMBL:EIJ37958.1};
OS   Galbibacter orientalis DSM 19592.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Galbibacter.
OX   NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ37958.1, ECO:0000313|Proteomes:UP000004690};
RN   [1] {ECO:0000313|EMBL:EIJ37958.1, ECO:0000313|Proteomes:UP000004690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ37958.1,
RC   ECO:0000313|Proteomes:UP000004690};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; JH651379; EIJ37958.1; -; Genomic_DNA.
DR   RefSeq; WP_008611036.1; NZ_JH651379.1.
DR   AlphaFoldDB; I3C2W5; -.
DR   STRING; 926559.JoomaDRAFT_0935; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_4_10; -.
DR   Proteomes; UP000004690; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004690}.
FT   DOMAIN          577..738
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          747..913
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1126 AA;  128942 MW;  881C56010D4E87C6 CRC64;
     MSNTITLAGL SQVITTYKES LQQQKLGRSI ANSKNNTYLK GLVGSSISIV IANAFRETEL
     PFLLVLNDKE EAAYHLNDLE QLIGEKDVLF YPGSYRRPYQ IEETDNANIL LRAEVLNRIN
     SRKKPAIIVT YPEALFEKVV TKKELERSTL KINLNDKLSI DFINETLFEY KFKRVDFVTE
     PGEFSVRGGI VDVFSFSNDE PYRIEFFGEE VDSIRTFDVE TQLSTEKLKK INIIPNVENK
     FLEEERESFL KYVSAKTVVF SRNSELLFSR IDGLFSKAEE AFTKLSKEIK HAPPKELFCD
     GALLKNQLKG FITIHLSAPK ANDIAYETIL FNTTPQPSFN KQFDLLIEDL NSNHEKGYKN
     YIYCVSEQQA KRFHDIFDDV ETEVHYQTVV FSMYQGFIDN EFKIACYTDH QIFERYHKFQ
     LKNGYSKKQA ITLKELTNLE IGDYVTHIDH GIGTFGGLQK IQVEGKLQEA IKLIYGERDI
     LYVSIHSLHK ITKFNGKDGK PPKIYKLGSA AWKNLKKKTK SKVKEIAFNL IKLYAKRKTE
     KGFQYGPDSY LQNELEASFL YEDTPDQSTA TEDVKRDMEN EQPMDRLVCG DVGFGKTEVA
     IRAAFKAVDN GKQVAILVPT TILAFQHHKT FSERLSDMPV TIDYLNRFRT AKEKRDTLER
     LEEGKVDIII GTHQLVNKNV KFKDLGLLIV DEEQKFGVAV KDKLKTIKEN VDVLTLTATP
     IPRTLQFSLM AARDLSVITT PPPNRYPIES NVIQLNEEII RDAVSYEIQR GGQIFFIHNR
     IENIKEVAGM VQRLVPDAKI GIGHGQMDGK KLEQLMLSFM NGDFDVLVAT SIIESGLDVP
     NANTIFINNA NNFGLSDLHQ MRGRVGRSNK KAFCYFITPP YSAMTDDARK RIQALEQFTE
     LGSGFNIAMK DLEIRGAGDI LGGEQSGFMN EIGFDTYQKI LQEAIEELKE NEFADLYETP
     KNEDKVYVKD TQIDTDFQLL FPDDYINAIT ERLNLYNELS TIKTEEALTL YETRLIDRFG
     ELPEEATDLL NSVRIKWIAT ELGLERIILK QGKMVGYFIA DQQSSFYQSN RFRNVLQYIQ
     THPNVGKIKE KQTRNGLRLL ITFENIKSIN KALNTLKPFL DRIYVA
//
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