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
//