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Database: UniProt
Entry: A0A176TCA3_9FLAO
LinkDB: A0A176TCA3_9FLAO
Original site: A0A176TCA3_9FLAO 
ID   A0A176TCA3_9FLAO        Unreviewed;      1111 AA.
AC   A0A176TCA3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=LPB303_08330 {ECO:0000313|EMBL:OAD45389.1};
OS   Polaribacter atrinae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1333662 {ECO:0000313|EMBL:OAD45389.1, ECO:0000313|Proteomes:UP000076923};
RN   [1] {ECO:0000313|EMBL:OAD45389.1, ECO:0000313|Proteomes:UP000076923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 17473 {ECO:0000313|EMBL:OAD45389.1,
RC   ECO:0000313|Proteomes:UP000076923};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Polaribacter atrinae KACC17473.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAD45389.1}.
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DR   EMBL; LVWE01000029; OAD45389.1; -; Genomic_DNA.
DR   RefSeq; WP_068449566.1; NZ_LVWE01000029.1.
DR   AlphaFoldDB; A0A176TCA3; -.
DR   STRING; 1333662.LPB303_08330; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000076923; 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; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000076923}.
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   1111 AA;  127393 MW;  39AFA962C00909AA CRC64;
     MSKQNIVNQY QKSANVSQII NQLQQDKNHF QISNLVGSSL SFVISETFKK ADKPYLLIFN
     DKEEAAYYLN DLEQLLGEKN VLFYPGSYRR PYQIEETDNA NVLLRSEVLN RINSRKKPAI
     IVTYPTALFE KVVTKKELEK NTLKVAVGES LSLDFVNEVL FEYKFKRVDF VTEPGDFSVR
     GGIIDVFSFS NDEPYRVEFF GDEIDSIRSF DVETQLSKEK LKKISIMPNV ENKTLEENRE
     SFLKYISSKT VIFAKNTDLL VGNLDKFYQK AEEAFLSLSK EIKHAKPSEL FCDGNFIKNQ
     LHEFSLIEMS PKVQSKELLE IEFNTIAQPS FNKQFNLLID NLEEYHKAKF TSYIFCANDQ
     QAKRFHDIFD DAEQEVHYET VVFPLYQGFV DVDNRLVCYT DHEIFERYHK FRLKNGYAKK
     QAITLQDLNK LEIGDYVTHM DHGIGKFGGL QKIDVQGRKQ EAIKLVYGER DILYVSIHSL
     HKISKFNGKD GKAPKIYKLG SGAWKKIKQK TKARVKHVAF NLIQLYAKRK LQKGFSFGPD
     THIQHELEGS FMYEDTPDQF TATQAVKQDM EKEQPMDRLV CGDVGFGKTE VAVRAAFKAV
     DNGKQVAILV PTTILAFQHY KTFTERLKDF PVRIDYLNRF RTAKQKTEAI NGVNDGSVDI
     IIGTHQLTNK RLQFKDLGLL VIDEEQKFGV AVKDKLKTLK ENVDTLTLTA TPIPRTLQFS
     LMAARDLSVI KTPPPNRHPI ESNVIRFSEE TVRDAIAYEI SRGGQVFFIH NRIENIKEVA
     GLIQRLVPNA KVGIGHGQME GKKLEGLMLG FMNGDFDVLV STTIIESGLD VPNANTIFIN
     NANNFGLSDL HQMRGRVGRS NKKAFCYFIT PPYHMMTDDA RKRIEALVLF SDLGSGINIA
     MKDLEIRGAG DLLGGEQSGF INDIGFDTYQ KILQEAIEEL KENEFKELYP TNNSKPKEYV
     KEVTIDTDFE ILFPDDYINS ITERLALYNK LGELKSEEEL QVFETEIIDR FGEIPTQVED
     LLDSVRIKWL AKELGLEKVI LKQKRMMGYF VANQQSEFYQ TDAFTRMLKY VQQNPKSCVM
     KEKESKNGLR LLITFIRIDT VKTALGVLQK V
//
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