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Database: UniProt
Entry: A0A076H1C7_9SYNE
LinkDB: A0A076H1C7_9SYNE
Original site: A0A076H1C7_9SYNE 
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
//
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