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Database: UniProt
Entry: A0A495IWP1_9SPHI
LinkDB: A0A495IWP1_9SPHI
Original site: A0A495IWP1_9SPHI 
ID   A0A495IWP1_9SPHI        Unreviewed;      1116 AA.
AC   A0A495IWP1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=BDD43_1301 {ECO:0000313|EMBL:RKR81157.1};
OS   Mucilaginibacter gracilis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=423350 {ECO:0000313|EMBL:RKR81157.1, ECO:0000313|Proteomes:UP000268007};
RN   [1] {ECO:0000313|EMBL:RKR81157.1, ECO:0000313|Proteomes:UP000268007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18602 {ECO:0000313|EMBL:RKR81157.1,
RC   ECO:0000313|Proteomes:UP000268007};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) 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:RKR81157.1}.
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DR   EMBL; RBKU01000001; RKR81157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495IWP1; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000268007; 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; 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:UP000268007}.
FT   DOMAIN          575..736
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          757..911
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1116 AA;  127290 MW;  72FAF480851516AC CRC64;
     MNIREILERY KADERIQTLA TALNGAKNPR IQLRGLVGSS DAAMAIALYF LKHSHMLFIL
     PDREEAGYFQ SDLESLLDKE ILLFPSSYRK PFEFTQPDSS NVLARAEVLN ELNHTSEYGQ
     LIVTYPEALA EKVIDRASLE KNTLEIAVGN KLGLDFINEF LIEYDFERVD FVYSPGQFSI
     RGGIVDIFSF SHDLPYRVEF FGDFIESIRT FEIESQLSVE QVKTITIVPN VQSKFLTESN
     ISLLEYIDPS TQIWIRDVQF TLDIVQTGFK KATALWKALS AEEKNANPDW IDPKFAFTDE
     KMIADQLHDF SLIEFGKQFF YTPTSSIQFD IRPQPSFNKD FSLLIHNFKN NEAEKVENCI
     FTDSSRQLER LYAIFEDLDK TIKFTPVNIS IREGFIDHAQ KIACYTDHQI FDRYYKYKLK
     KGYQRSQAIT LKELRELKPG DYITHIDHGI GKYAGLEKVE VGGKMQEMIR LLYADNDLLY
     VNINSLNRIS KYSGKEGTVP KMNKLGTDTW EKLKKTTKKK VKDIARDLIK LYAVRKAQSG
     NAFSPDSYLQ TELEASFIYE DTPDQEKATI DFKKDMESPH PMDRLICGDV GFGKTEVAIR
     AAFKAVADSK QVAVLVPTTI LAAQHYKTFT ERLKGFPCNI DYVNRFKTSK QIKDTLQNLA
     DGKLDIIIGT HRLVSKDVKF KDLGLMIIDE EQKFGVSTKE KLKAMRINVD TLTLTATPIP
     RTLHFSLMGA RDLSIISTPP PNRQPVVTEL HVFNDKLIKE AVEFEIDRNG QLFFIHNRVA
     DLPQLGGMIK KLVPKARIGI AHGQLEGDDL EDVMLKFVNN DYDVLVATTI IEAGLDIPNA
     NTIIINYAHM FGLSDLHQMR GRVGRSNKKA YCYLLSPPLS TLTSEARKRL SAIEEFSDLG
     SGFNVAMRDL DIRGSGNLLG AEQSGFIAEI GFEMYHKILD EAIQELKDDE FKGLFDDKPR
     PFVSFTQIDT DLEILIPDEY VTSIPERYNL YTELSKLENE TELAAFAQQL HDRFGPVPPQ
     VHDLLNTMRL QWLGKAIGFE KLSIKKNVLR GYFITNQQSP YFETAQFRQV LNFMQANPRR
     CNMKEVKSTL RISIENVRGI DEAVAILEEM AEPVGV
//
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