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Database: UniProt
Entry: A0A0M0FZ93_9BACI
LinkDB: A0A0M0FZ93_9BACI
Original site: A0A0M0FZ93_9BACI 
ID   A0A0M0FZ93_9BACI        Unreviewed;      1177 AA.
AC   A0A0M0FZ93;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=AF331_21550 {ECO:0000313|EMBL:KON82697.1};
OS   Rossellomorea marisflavi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189381 {ECO:0000313|EMBL:KON82697.1, ECO:0000313|Proteomes:UP000037405};
RN   [1] {ECO:0000313|Proteomes:UP000037405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14235 jcm11544.";
RL   Submitted (JUL-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:KON82697.1}.
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DR   EMBL; LGUE01000010; KON82697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0FZ93; -.
DR   STRING; 189381.GCA_900166615_04432; -.
DR   PATRIC; fig|189381.12.peg.3991; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000037405; 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   CDD; cd18810; SF2_C_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; 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:UP000037405}.
FT   DOMAIN          638..799
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          820..974
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1177 AA;  134010 MW;  86AFF3C992AB6378 CRC64;
     MKGILTYVHQ SEEVQSLITG IEERLSEQLV AGLSGSSRSA YIADVYLQTK RSTIVVTHNL
     FQAQKIYEDL VQFLSEDEVY LYSANELIAA ELSVASPELR AQRIEVLNKL SQRQNGVYIV
     PVSGLRKILP PMDLWIKNQI RFNVGEDIDL DEVLNQLVQM GYQRAGMVST PGEFSLRGGI
     VDIFPLTSQH PVRIELFDTE IDSIRMFSVE DQRSIDKLKT VDIGPATEVL LTYQNIERLI
     GEINKGLSKS LKKIKSAGVK EKMTEYIGHE VEQLENGQVP EQIFKYLSLA YETPASLLDY
     LPEDGVLFFD EYSRVQEMSE SLEKEEAEWY TSLLSEGQII HDMVVSHPFA SLVSNAKRSK
     VYFSLFLRQI PNTSPQNIFN VSTKPMQNFH GQMNVLKAEL DRWKKGKYTV VLLGPDEERV
     KKLQRVLDDY QIEIAFVKDG GSLLNGKVQM INGSLTNGFE LPLQKLAVIT EEELFNKRTQ
     KKPRRQKMSN AERIKSYSEL KVGDLVVHVN HGIGKYLGIE TLEINGVHKD YLHLKYQGSD
     KLYVPVDQID LVQKYVASEN KDPKLYKLGG NEWKKVKSKV ASSVQDIADD LIKLYAEREA
     AKGYAFSPDG DMQREFEIAF PYEETEDQLR SIHEIKLDME RERPMDRLLC GDVGYGKTEV
     AIRAAFKAIA DGKQVALLVP TTILAQQHYE TIKERFQDFP VEISLLSRFR TRKQQQETTK
     GLKDGTVDIV VGTHRLLSKD IQYRDLGLLI IDEEQRFGVT HKEKIKQLKT NIDVLTLTAT
     PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVMEYNGAL IKEAIEREMA RNGQVYFLYN
     RVEDIERKAD EISMLVPDAR VAYAHGQMSE NELEAVILGF LAGEYDVLVT TTIIETGVDI
     PNVNTLIVFD ADRMGLSQLY QLRGRVGRSN RVAYSYFTYR KDKVLTEVAE KRLQAIKEFT
     ELGSGFKIAM RDLTIRGAGN LLGAQQHGFI DSVGFDLYSQ MLKEAIEERK GDRPKQPEAS
     LEVDLDLDAY IPDTYIKDGH QKIEMYKRFR ALSSLKEVEE LEEEILDRFG EYPEEVGYLF
     LISEMKVYAR NTRLDSVKQD KKSVNIFMSP EGTAAIDGSK VFDICSKHGR VVGLGMEGSK
     LKISINTTRL KADKWFNMAY DIVKNLDQAL KTEVHEA
//
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