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Database: UniProt
Entry: A0A0A5FSV3_9BACI
LinkDB: A0A0A5FSV3_9BACI
Original site: A0A0A5FSV3_9BACI 
ID   A0A0A5FSV3_9BACI        Unreviewed;      1175 AA.
AC   A0A0A5FSV3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-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=N783_20945 {ECO:0000313|EMBL:KGX83856.1};
OS   Pontibacillus marinus BH030004 = DSM 16465.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX83856.1, ECO:0000313|Proteomes:UP000030403};
RN   [1] {ECO:0000313|EMBL:KGX83856.1, ECO:0000313|Proteomes:UP000030403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030004 {ECO:0000313|EMBL:KGX83856.1,
RC   ECO:0000313|Proteomes:UP000030403};
RA   Huang J., Wang G.;
RL   Submitted (AUG-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}.
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:KGX83856.1}.
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DR   EMBL; AVPF01000079; KGX83856.1; -; Genomic_DNA.
DR   RefSeq; WP_027447161.1; NZ_AVPF01000079.1.
DR   AlphaFoldDB; A0A0A5FSV3; -.
DR   STRING; 1385511.GCA_000425225_03592; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000030403; 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; 3.40.50.11180; -; 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; 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:UP000030403}.
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   1175 AA;  134816 MW;  E9B06B89F6E37AB6 CRC64;
     MQGLKDFLKK QDDVHSIISG FSSGMQEQFA AGLSGSARSV LVSLLEESTK RPILLVTHQL
     MQAQQLYEDL LGISDAEHVH LYPVNELIAS EIAVASPELR SERIDALNHW AQEKSGILIA
     PVAALKRILP PPSYWEQYQL NFKVGEAIDL DAYLKGLINV GYERADMVSS PGEFSLRGGI
     LDIYPLTQPN PLRIELFDDE VDSIRYFDSE SQRSLEKLDQ VTIGPASELL LTDEDLTRGA
     HRLEEALAKT LQKMQSSELK EKVTETIEHD ISRLNNHERF EEMYKYISLY YENSASLLDY
     IPENGIVVLD EMSRIQETAN RLDEEEADWY SSLLESGQMV RDISISYNWP DVWHAIKQPR
     LYMSVFLRHI PNTQPQNIVN FSCRAMQQFH GQMNLLQNEM DRWKKSGYSV IIVAPNHERA
     QKIQNVLEDY DMEAVVSEHE PSLPVTTPTI VTEQMTSGFE LPMHKIAVLT ESELFKKQTT
     RPKRKKKISN AERIKSYQEL KVGDYVVHAN HGIGKYIGIE TLELNGIHKD YMLVKYSGDD
     KLYVPIDQID QVQKFVGSEG KEPKLYKLGG SEWKKVKSRV QSSVEDIADD LIQLYAEREA
     TKGYAFGEDT EMQKDFEAAF PYQETEDQIR CIQEIKTDME KIRPMDRLLC GDVGYGKTEV
     AIRAAFKAIA DGKQVAILVP TTILAQQHYE TVRERFQDFP INIGLLSRFR TQKQQKETKE
     GLKSGIVDIV IGTHRLLSKD IQVKDLGLLI VDEEQRFGVK HKEKIKQMKT NVDVLTLTAT
     PIPRTLHMSM LGVRDLSVIE TPPENRFPIQ TYVLEYNPVF MREAIEREMA RGGQVFFLFN
     RVENIERMAE EISALVEDAR VTFAHGQMNE TELENVMFSF LEGESDVLVS TTIIETGVDI
     PNVNTLIVYD ADRMGLSQLY QLRGRVGRSN RVAYAYFTYQ KDKVLTEVAE KRLQAIKEFT
     ELGSGFKIAM RDLSIRGAGN LLGAQQHGFI DSVGFDMYSQ MLKDAIEAKQ EGKTYEETKP
     FEPELTLNID AYIPDGYIDD EKQKIDMYKR FQAVDSQEDI HDLREELIDR FGDYPEEVEN
     LFQVSVLKLY AKRERIESIT EKNKKVELIM EEEASQQIDG AKLFELANQY GRMIQLGTEG
     KQLKVTFQFQ RDMYPRRYKV MEEVLQSLKD VKHDE
//
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