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Database: UniProt
Entry: A0A0X8JAY8_9FLAO
LinkDB: A0A0X8JAY8_9FLAO
Original site: A0A0X8JAY8_9FLAO 
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
//
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