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Database: UniProt
Entry: A0A1I3LN16_9FLAO
LinkDB: A0A1I3LN16_9FLAO
Original site: A0A1I3LN16_9FLAO 
ID   A0A1I3LN16_9FLAO        Unreviewed;      1112 AA.
AC   A0A1I3LN16;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05443431_102495 {ECO:0000313|EMBL:SFI86092.1};
OS   Olleya namhaensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1144750 {ECO:0000313|EMBL:SFI86092.1, ECO:0000313|Proteomes:UP000199559};
RN   [1] {ECO:0000313|Proteomes:UP000199559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28881 {ECO:0000313|Proteomes:UP000199559};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FORM01000002; SFI86092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3LN16; -.
DR   STRING; 1144750.SAMN05443431_102495; -.
DR   Proteomes; UP000199559; 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; 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:UP000199559}.
FT   DOMAIN          569..730
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          739..905
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1112 AA;  127460 MW;  FF8A0644874FE20F CRC64;
     MSKTLISQTY LQSLQLQKLQ TAISQTQSKT HLKGLVGSSL SYIITQTFKN TQLPFLLIFN
     DKEEAAFYLN DLEQLINKTD VLFYPGSYRR PYQIEETDNA NVLLRAEVLN RINSRKKPAI
     IVTYPDALFE KVVTRKELER NTLKINVNDS LSIDFVNEIL FDYKFKRVDF VTEPGEFSVR
     GGIVDVFSFS HDEPYRIEFF GDEVDSIRTF DVETQLSTEQ IKKISVIPNV ANKLMDESRQ
     SFLNYIAQKT VVFGKNFDLT FDRVDDFFDK AITAFVKLNQ DIKHAKPSEL FCNAAELKKQ
     LLDFTIVEFG SSPVFNPTET IVHNTSPQPT FNKQFNLLID NLNSNHNNDY TNYIACVSEQ
     QAKRFHDIFD DVDQNVHYQT VTLSLYQGFV DHDNKIVVYT DHQIFERYHK FHVKNGYAKK
     QAITLKDLTN LDIGDYVTHI DHGIGKFGGL QKIDVEGKKQ EAIKLVYGER DVLYLSIHSL
     HKITKFNGKD GKPPKVYKLG SKAWKVLKEK TKSRVKHVAF NLIKLYAKRK LEKGYQYKPD
     SYLQHELEAS FLYEDTPDQI TATADIKVDM ESERPMDRLI CGDVGFGKTE VAIRAAFKAV
     DNGKQVAVLV PTTILAFQHH KTFTERLKDL PVTVDYVNRF RTAKQKKETL EKLEKGHVDI
     IIGTHQLASK NVKFKDLGLL IVDEEQKFGV AVKEKLKTLK DNVDVLTLTA TPIPRTLQFS
     LMAARDLSVI TTPPPNRYPI ESNVIRFTEE AIRDAVSYEI ERGGQIFFIH NRIENIKEVA
     GMIQRLVPDA KIGIGHGQLE GKKLESLMLG FMDGEFDVLV STTIIESGLD VPNANTIFIN
     NANNFGLSDL HQMRGRVGRS NKKAFCYFIT PEYSAMTDDA RKRIQALEQF TELGSGFNIA
     MKDLEIRGAG DLLGGEQSGF INEIGFDTYQ KILNEAIEEL KENEFKDLYN EPLENKEYVK
     DITIDTDFEL LFPDDYVNNI AERLNLYTQL NNFKTEAELA EFEKQLLDRF GELPIQVIDL
     IDSVRIKWIA TKLGMEKVIM KQGKLISYFI NDQQSSFYQS PNFTKLLKYV QTHPKSCKMK
     EKQTRNGLRL LLTFDNIKSV KKALNALKPI LE
//
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