ID A0A076H1C7_9SYNE Unreviewed; 1192 AA.
AC A0A076H1C7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=KR100_09070 {ECO:0000313|EMBL:AII43510.1};
OS Synechococcus sp. KORDI-100.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII43510.1, ECO:0000313|Proteomes:UP000028591};
RN [1] {ECO:0000313|EMBL:AII43510.1, ECO:0000313|Proteomes:UP000028591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-100 {ECO:0000313|EMBL:AII43510.1,
RC ECO:0000313|Proteomes:UP000028591};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequence of Synechococcus sp. KORDI-100.";
RL Submitted (JUN-2013) 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; CP006269; AII43510.1; -; Genomic_DNA.
DR RefSeq; WP_038544784.1; NZ_CP006269.1.
DR AlphaFoldDB; A0A076H1C7; -.
DR STRING; 1280380.KR100_09070; -.
DR KEGG; synk:KR100_09070; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_3; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000028591; 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}; Reference proteome {ECO:0000313|Proteomes:UP000028591}.
FT DOMAIN 636..797
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 822..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1171..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 132450 MW; E092FABBAC681AAC CRC64;
MPLRSLVRQL QDSALSGELL DRSRRTDRLL MRGAGRCSRA LVASALARRD QRPLLIVVPT
LEEAGRWTAL LDLMGWDSVS LYPTSEGSPY EPFDPTSEII WGQLQVLSDL LGDPDGTNKA
MVATERCLQP HLPPPQALAD QCRSLKRGDE LDLEQLGEHL AHLGYERVSS IDQEGTWSRR
GDIVDIFPVS SELPVRLEFF GEELDKLREF DPASQRSLDA IEQLRLTPTG FSPLIADRLR
DEMPEGIERL LGDEATEALL EGGTPEGMRR LMGLAWNQPA SLLDYLPERC CVLIDERRHG
LAHGQQWLDH AADHHQEMAA ELGFSEDERD RLWPGVLHRD ISEAYQTAEA FDGFDLAELL
EEDAHPNSFD LASRPVPAYP NQFGKLGELI KGYQKDKTAV WLVSAQPSRA VALLEEHDCI
SRFVPNSGDA PAIERLIQQN TPVALKTRGS AELEGVQLPP WRVALVTDRE FFGQQTLTSS
GYVRRRRKAA SRTVDPNKMR PGDFVVHRNH GIGRFKTMEK LAVSGDIRDY LVVQYADGTL
RVAADQLGSL GRYRATSETP PQLSRMGGSA WNKAKERAKK AVRKVAMDLV KLYAERHQAN
GYAFPVDGPW QIELEESFPF EPTPDQLKAT ADVKRDMEKP EPMDRLVCGD VGFGKTEVAI
RAIFKAITAG KQVAMLAPTT VLAQQHWRTL SERFAPYPIK VALLNRFRTA SERKGILDGL
KAGTVDAVVG THQLLGKGAA FNQLGLLVVD EEQRFGVNQK EKIKVLRKDV DVLTLSATPI
PRTLYMSLSG VREMSLITTP PPLRRPIKTH LAALDPEAVR SAIRQELDRG GQVFYVVPRV
EGIEDVAAGL RGMLPGLKLL VAHGQMAEGE LESAMVAFNA GEADVMLCTT IVESGLDIPR
VNTILIEDAH RFGLAQLYQL RGRVGRSGIQ AHAWLFYPGN ASLSDNARQR LRAIQEFAQL
GSGYQLAMRD MEIRGVGNLL GVEQSGQMET IGFDLYMEML QESLAEIQGQ DIPSVEDTQV
DLQVTAFVPA DWITDPDEKI SAYRAAADCT SSEALVELAA GWADRYGALP GAVQSLLQLM
DLKLLAKRCG FSRIRPEKPN IALETPMEEP AFRMLRQGLP QHLHGRLIYQ SGSGIQHKVL
ARGLGVLPME KQLEQLMEWL KQMAAQIPDV NGRTASEMEA EQKRRNDQVL RV
//