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Database: UniProt
Entry: A0A1I2BPV3_9FLAO
LinkDB: A0A1I2BPV3_9FLAO
Original site: A0A1I2BPV3_9FLAO 
ID   A0A1I2BPV3_9FLAO        Unreviewed;      1092 AA.
AC   A0A1I2BPV3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=SAMN04488131_102395 {ECO:0000313|EMBL:SFE57373.1};
OS   Flavobacterium xueshanense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=935223 {ECO:0000313|EMBL:SFE57373.1, ECO:0000313|Proteomes:UP000198596};
RN   [1] {ECO:0000313|EMBL:SFE57373.1, ECO:0000313|Proteomes:UP000198596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9227 {ECO:0000313|EMBL:SFE57373.1,
RC   ECO:0000313|Proteomes:UP000198596};
RA   de Groot N.N.;
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; FONQ01000002; SFE57373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2BPV3; -.
DR   STRING; 935223.SAMN04488131_102395; -.
DR   Proteomes; UP000198596; 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}.
FT   DOMAIN          546..707
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          716..882
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1092 AA;  125354 MW;  3D6720EAB95AFF61 CRC64;
     MQLSGLLGSA VSFIIRSVFK QSELPFLIVL NNKEEAAYYL NDLEQMIGEQ DVLFYPGSYR
     RPYQIEETDN ANVLLRAEVL NRINSRKKPA VIVTYPEALF EKVVTRKELD KNTLKVAVSD
     KISIDFINEV LFEYEFKRVD FITEPGEFSV RGGIVDVFSF SNDNPYRIEF FGDEVESIRT
     FDVATQLSIV TQKKITIIPN VENKVFQENR ESFLDYISEK TVIFIQNTED FLSQLDKQFG
     KAEEAFAKLS QEIKRSTPEQ LFLNQAEFIK RALDFSIVEL SSKAIFRTTK KFEFHIQPQP
     SFNKQFDLLL NNLNENHFNG YKNYLFCSNE AQAKRFHDIF ETLDEANSEN IRKQYNTIVL
     PLYQGFIDEE NQITCYTDHQ IFERYHKFNI KNGYSKKQNI TLKELTTLSV GDYVTHIDHG
     IGRFGGLQKI QVENKTQEAI KLVYADNDIV YVSIHSLHKI SKYNGKDGTP PKIYKLGSNA
     WKILKQKTKA RVKHIAFNLI QLYAKRRLEK GFQFAPDSYL QNELESSFIY EDTPDQTKST
     AEVKADMESD RPMDRLVCGD VGFGKTEVAI RAAFKAVDNS KQVAILVPTT ILAYQHYRTF
     TERLKDMPVS VGYLNRFRTA KQKAETLKQL AEGKLDIVIG THQLVNKNVV FKDLGLLIVD
     EEQKFGVNVK DKLKTIAANV DTLTLTATPI PRTLQFSLMA ARDLSVITTP PPNRYPIETN
     VVGFSEELIR DAISYEIQRN GQVFFINNRI ENIKEVAGMI QRLVPNARVG IGHGQMEGRK
     LEELMLAFMN GEFDVLVATT IIESGLDVPN ANTIFINNAN NFGLSDLHQM RGRVGRSNKK
     AFCYFICPPY SAMTDDARKR IQALEQFSEL GSGFNIAMKD LEIRGAGDLL GGEQSGFINE
     IGFDTYQKIM NEAIDELKEN EFKDLYPEEN NLETKEYVKD LQIDTDFELL FSDEYINNVS
     ERLSLYNELG AVKNEEELII FQNKLIDRFG PMPPRSKALM NSIRIKWIAT RIGIEKLVMK
     QGKMIGYFIS DQQSDYYQSK RFQDVLQFVQ KHSAICKMKE KQTPAGLRLL LTFDNVKNTR
     TALELMEMLG DE
//
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