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Database: UniProt
Entry: A0A0C2Q4V1_9CYAN
LinkDB: A0A0C2Q4V1_9CYAN
Original site: A0A0C2Q4V1_9CYAN 
ID   A0A0C2Q4V1_9CYAN        Unreviewed;      1195 AA.
AC   A0A0C2Q4V1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=SD81_28365 {ECO:0000313|EMBL:KIJ73415.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ73415.1};
RN   [1] {ECO:0000313|EMBL:KIJ73415.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ73415.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-2015) 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:KIJ73415.1}.
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DR   EMBL; JXCB01000012; KIJ73415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2Q4V1; -.
DR   OrthoDB; 9804325at2; -.
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          661..823
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          848..1000
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          121..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  134087 MW;  8B988EBAF083CCE1 CRC64;
     MAFSSIVRAL GRSPLTTELL SKLNRQQELL LSGIPRLPKG LIASALAQTE GKNLFVVCAT
     LEEAGRWTTQ LEAMGWQTVH FYPTSEASPY EPFDPETEMT WGQMQVLADL VQFGRTRDEG
     DKQAKLSSSL PPSLPPSLPP SSPSPKMAIV ATVAALQPHL PPAEAFKPFC ITLKRGMEFD
     LDTFSEQITR LGYERVPLVE TEGQWSRRGD IVDVFPVSSE LPVRLDWFGD EIEQLREFDP
     ATQRSAALDK IDQLILTPTS FAPIVMAALE DNPQFPVLSE QLNDDSELRT TENSELLEGS
     RRFLGLAFDK PASLLDYLPE NTLITVDEPE QCHAHSDRWV ENAEEQWQLL ASREDEEIST
     SLPRVHRSFD ECLADTAEFK KLNLSELVEE NTGINLASRR LPVTPHQFAK IAETLRQERD
     RKFSVWLISA QPSRSVSLLQ EHDCPAQFIP NPRDYLAIDK QQLNHTPVAL KYSGLAELEG
     FILPTFRLVV VTDREFYGQH SLATPSYIRK RRKAASKQVD PNKLRPGDFV VHKNHGVGKF
     LKLESLTIND ETREYLVVQY ADGLLRVAAD QVGVLSRLRT ATDKPPELNK MTGKAWENTK
     NKVRKAIKKL AVDLLKLYAS RSQQKGNAYP QDTPWQQEME DSFPYQPTTD QLKATQDVKR
     DMESDRPMDR LVCGDVGFGK TEVAIRAIFK AVTSGGKQVA LLAPTTILTQ QHYHTLKERF
     APYPINVGLL NRFRSAEERR DILKRLATGE LDVVVGTHQL LGKGVTFRDL GLLVVDEEQR
     FGVNQKEKIK SLKTLVDVLT LSATPIPRTL YMSLSGIREM SLIATPPPSR RPIQTHLSPT
     NPESIRSAIR QELDRGGQVF YVVPRVEGIE EIAAELRQMI PGARIAIAHG QMEESELEST
     MLTFSNGEAD ILVCTTIIES GLDIPRVNTI LIEDAHRFGL SQLYQLRGRV GRAGIQAHAW
     LFYPKQRTLS DAARQRLRAI QEFAQLGSGY QLAVRDMEIR GVGNLLGAEQ SGQMEAIGFD
     LYMEMLEEAI REIRGQEIPK VDDTQIDLNL TAFVPADYIT DLDQKMSAYR AVAAAKSKEE
     LSQIAAEWND RYGAIPKPAT QLLRVMELKQ LAKKLGFSRI KPENKQHIVL ETQMEEPGWK
     NLAENLPESL RSRFVYSPGK VTVRGLGVMK ADQQLQTLID ALGKMQGAVV EEAIA
//
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