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Database: UniProt
Entry: A0A2N4XMW4_9RHOO
LinkDB: A0A2N4XMW4_9RHOO
Original site: A0A2N4XMW4_9RHOO 
ID   A0A2N4XMW4_9RHOO        Unreviewed;      1146 AA.
AC   A0A2N4XMW4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ECO:0000313|EMBL:PLK48238.1};
GN   ORFNames=C0V76_13500 {ECO:0000313|EMBL:PLK48238.1};
OS   Uliginosibacterium sp. TH139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Uliginosibacterium.
OX   NCBI_TaxID=2067453 {ECO:0000313|EMBL:PLK48238.1, ECO:0000313|Proteomes:UP000234247};
RN   [1] {ECO:0000313|EMBL:PLK48238.1, ECO:0000313|Proteomes:UP000234247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH139 {ECO:0000313|EMBL:PLK48238.1,
RC   ECO:0000313|Proteomes:UP000234247};
RA   Cai h.;
RT   "genomes of bacteria within cyanobacterial aggregates.";
RL   Submitted (DEC-2017) 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:PLK48238.1}.
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DR   EMBL; PKRR01000005; PLK48238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N4XMW4; -.
DR   InParanoid; A0A2N4XMW4; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000234247; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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; 4.
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:UP000234247}.
FT   DOMAIN          618..779
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          800..954
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1146 AA;  127476 MW;  85885C3574386D20 CRC64;
     MSSPALPPLQ PLAAFSLPKP GQRFDLPRLH GSADAAALAQ LAASGQKLIV ITANPLDAQR
     LVEEIAWFAQ GLRVHLLPDW ETLPYDNFSP HQDLISERLA TLYAIHKGES DITLLPATTA
     LYRMAPPQYL AGHTFFMKAK QVLDVEAFKL QMALAGYEHV TQVVRPGEFS VRGGLIDLFP
     MGVKLPYRID LFDDEIDTIR TFDPDTQRTV YPVPEIRLLP AREFPMDDKG RSHFRAAFRE
     AFEGDPTKSP IYKDVSNGVA SAGIEYYLPL FFDATASLFD YLPKNVLLVT HQDVPAAIEA
     FWVEANSRYR LMAGDRARPL LPPEQLFLPA EAFWLAAKGL PRVAMGEKNE GHALSSALPD
     LGVERKASDP LHKLKHYLAN FPWRVLVLAE SAGRAQTITE YFHEYDLKPA ASADLAGFLA
     TDARLGLASG PLSAGFVLPG ANIAILTENE LYAAQARPRG RGRDARKSTV EGWLKDLSEL
     KIGDPVVHQS HGIGRYLGLV HMDMGEGDTE FLHLEYAEDT KLYVPVSQLH VITRYAGADP
     ENIALHKLGS GQWEKAKRKA AQQVRDTAAE LLVLYAKRAA RPGHKFDFKQ HDLEAFAEGF
     GFEETPDQLA AINAVVDDMR SGRPMDRLVC GDVGFGKTEV ALRATFIAVA DGKQVAVLCP
     TTLLAEQHYQ TFADRFADWP IKVAEISRFK TAKEQAEAIE MLAQGKVDIL IGTHRLLQKD
     VEFKRLGLVI IDEEHRFGVR QKEALKNLRS EVDILTLTAT PIPRTLGMAM EGLREFSVIA
     TAPQKRLAIK TFVQGWSKGI VREAVLREFK RGGQVYFLHN EVDTIENMRN TLTELLPEAR
     IVVGHGQMNE RELERVMKDF TAQRANLLLC TTIIETGINI PTANTIVINR ADRFGLAQLH
     QLRGRVGRSH HQAYAYLLTD ANAKPSANAQ KRLEAITMME DLGSGFFLAM HDLEIRGAGE
     VLGDNQSGEI QQVGFAMYSQ MLNRAVKALQ NGKEVDLAQP LDVTSEINLH APALLPNAYC
     PDVQERLTLY KRMANCEDVD ELQAIQEELI DRFGELPAQG QALLETHRLR IAAKPLGIIK
     IDASEGRIHL HFEPNPPIEP IKIIKLIQNN RNWKLAGQDK LTISITADTF AERVNKVRNC
     LKQLSA
//
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