ID A0A0X8JAY8_9FLAO Unreviewed; 1104 AA.
AC A0A0X8JAY8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=AXF12_08625 {ECO:0000313|EMBL:AMD85569.1};
OS Capnocytophaga haemolytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD85569.1, ECO:0000313|Proteomes:UP000065822};
RN [1] {ECO:0000313|Proteomes:UP000065822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-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; CP014227; AMD85569.1; -; Genomic_DNA.
DR RefSeq; WP_066430285.1; NZ_LT906449.1.
DR AlphaFoldDB; A0A0X8JAY8; -.
DR STRING; 45243.AXF12_08625; -.
DR KEGG; chg:AXF12_08625; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000065822; 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; 3.40.50.11180; -; 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 563..724
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 733..899
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1104 AA; 126213 MW; 8F2E7B02B70C5648 CRC64;
MKELLQQFAT RNSYKSLINN IEEGKNTAVK GVAGAAFSFL IANIFQRKAR PTFVMLNDKE
ESAYILNDLE RLLGEQCVLF YPDSYRRPYQ IEQTDNANVL LRAEVLNRFS QNKNTIVVTY
PEALFEKVIT QGQLEKNTLS IAKGEQISLD FLNEILFSYQ FIRTDFVTEP GEFSIRGGIV
DVFSFSNNEP YRIEFFGNEI ESIRTFDVET QLSTAQLSQI SIIPNVENKH SNEIRQTFLD
YLPDDTLIFA KDMDTFGEKI DKLFKKASET YQTLPNEVKH ITPEALFCQK EELLSRIDTL
QHIFTGFSTS SLPQIDFHTV PQPSFGKQFG LLVNYFNEKH DQGYVNYLLC ASEQQEKRFR
DIFEELQQSV HYKTFVLSLH AGFIDLENHC NIFTDHQFFE RYHKFSLKNG YAKKQAITIK
ELLQLQVGDY VTHIDHGIGK FAGLQKIDVG GKMQEAIKLI YGDRDVLFVS IHALHKITKY
NGKDGAPPKI YKLGSNAWKA LKQKTKARVK EIAFNLIQLY AKRKEAKGFA FSQDSYLQNE
LEASFLYEDT PDQSKTTEEV KNDMQSDRPM DRLICGDVGF GKTEVAIRAA FKAVDNGKQV
AVLVPTTVLA FQHYKTFTSR LKDLPVRVEY LNRFRTLKKK SQILKDLASG QIDILIGTHQ
IVGEKVIYKD LGLLIVDEEQ KFGVNTKDKL KTLKENLDVL TLTATPIPRT LQFSLMAARD
LSVINTPPPN RYPIDSQLIN FDEETIRDAI VYEIQRGGQV FFMHNRVENI QELAGILSRL
VPEAKIAVGH GQMDGKKLEE TMLRFMDGTY DVLVATTIIE SGLDVPNANT IFINNAHNFG
LSDLHQMRGR VGRSNKKAFC YFITPPLSSM SEDARRRMEA ISQYTDLGSG LNIALKDLEI
RGAGDLLGGE QSGFINEIGF DTYQKILQEA ITELKEQDFA DIYGVEEENY RTDTQIDTDF
ELLFPDTYIN RVAERLNLYN ELSNLTDEVQ LQQYEHNLID RFGKLPPQAV DLLTSVRLKW
LASSLGMEKL VMKLGKMTAY FIFNPESKFY QGSVFQNILQ YAQHHPSVCH IQEKETRGGL
RLLMIFDHIK SVQQALSVMQ AIKK
//